# vtrsurvey

Viral_family: (none)
Species: Hepatitis delta virus
Name: S-HDAg
Aliases: HDAg, LHDAg, P24, Small delta antigen
UniProtID_Ref: P0C6L3
UniProt_Name_Ref: SHDAG_HDVD3
Binding_ligand: ssRNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(18653455)
EMSA: N
Other_assays: D(30153423, RNA-binding protein pull-down assay), D(18653455)
Human_infection_evidence: 24198831.0
UniProt_IDs_Orthologs:
A0A0P0KG82,A0A185QEB0,A0A185QEB2,A0A185QEV2,A0A185QEW3,A0A185QEX3,A0A190LCH6,A0A190LCI6,A0A190LCJ6,A0A190LCL2,A0A190LCM2,A0A190LCN4,A0A190LCP3,A0A221S7Z0,A0A221S7Z2,A0A221S7Z5,A0A221S872,A0A221S875,A4ZN24,A4ZN28,A4ZN30,A4ZN32,A4ZN33,A4ZN34,A4ZN37,A4ZN38,A4ZN41,A4ZN42,A4ZN43,A4ZN44,A4ZN52,A4ZN66,A4ZN69,A4ZN70,A4ZN71,A4ZN72,A4ZN77,A4ZN79,A4ZN80,A4ZN81,A4ZN85,A4ZN86,A4ZN91,A4ZN96,A4ZN97,A4ZN98,A4ZN99,A4ZNA0,A4ZNA3,A4ZNA5,A4ZNA6,A4ZNB1,A4ZNB3,A4ZNB8,A4ZNC1,A4ZNC4,A4ZNH4,A5A0U5,A5A0U6,A5A0U9,D7RA49,P06934,P25880,P25881,P25882,P25989,P29833,P29997,Q6DUC3,Q6QT49,Q71DP5,Q81835,Q9E925,Q9E926

Functional_annotation:
Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome (By similarity).


Viral_family: Adenoviridae
Species: Human adenovirus A
Name: E1A
Aliases: Early E1A 29.5 kDa protein, Early E1A protein
UniProtID_Ref: P03259
UniProt_Name_Ref: E1A_ADE12
UniProt_IDs_Orthologs: A0A3G1HCH6,D0Z5R8,Q6JGG5,Q6JGG8
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(19129215, 21715488)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(7951410)
EMSA: D(7951410)
Other_assays: D(7951410)
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).


Viral_family: Adenoviridae
Species: Human adenovirus A
Name: E2A
Aliases: DBP, DNA-binding protein, Early 2A protein, Early E2A DNA-binding protein
UniProtID_Ref: P04498
UniProt_Name_Ref: DNB2_ADE12
UniProt_IDs_Orthologs: A0A3G8WIW6,D0Z5T4,D3JIT2
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(11581372)
EMSA: I(12502807, 8039495)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its relese from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.


Viral_family: Adenoviridae
Species: Human adenovirus A
Name: E4
Aliases: E4 ORF6 protein, Early E4 34 kDa protein
UniProtID_Ref: P36710
UniProt_Name_Ref: E434_ADE12
UniProt_IDs_Orthologs: A0A3G8W3L7
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8633237, 1832724, 2137929)
EMSA: I(1832724, 2137929)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: P36710 is inferred from Human adenovirus C protein P03238
Functional_annotation:
Modulates viral and host transcriptional activity to promote viral genome replication. Stimulates viral E2a promoter activity by binding and inducing dimerization of host E2F. During viral infection E1A protein binds to cellular retinablastoma (RB) family members and disociates these repressors from a complex with E2F proteins. Free E2F is then bound to E4orf6/7 which leads to transactivation of viral E2 promoter, and cellular promoters such as E2F-1 promoter. Activation of cellular E2F targets promote cell cycle S phase and thereby possibly favorises viral DNA replication process.


Viral_family: Adenoviridae
Species: Human adenovirus A
Name: IVa2
Aliases: Packaging protein 1, Packaging protein IVa2
UniProtID_Ref: P12540
UniProt_Name_Ref: PKG1_ADE12
UniProt_IDs_Orthologs: A0A3G8WBN6,D0Z5S2,D3JIS0
Binding_ligand: dsDNA
Function: TR, NAP
Primary_secondary_vTR: S
ChIP: I(15681437)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8627656, 15327897)
EMSA: I(22884292, 8627656, 15681437)
Other_assays: I(15780869, DNA-binding protein pull-down assay)
Human_infection_evidence: Fields Virology
Functional_annotation:
Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 2 and 3, to the specific packaging sequence on the left end of viral genomic DNA and displays ATPase activity thereby providing the power stroke of the packaging machinery. The activity of packaging protein IVa2 is stimulated by protein 33K which acts as a terminase. May be the protein that pumps DNA into the capsid powered by ATP hydrolysis. Specifically binds to the 5'-CG-3' nucleotides of the repeats making up the packaging sequence. Component of the DEF-A and DEF-B transcription factors that bind downstream elements of the major late promoter (MLP), and stimulate transcription from the MLP after initiation of viral DNA replication. DEF-A is a heterodimer packaging proteins 1 and 2 and DEF-B is a homodimer of packaging protein 1.


Viral_family: Adenoviridae
Species: Human adenovirus A
Name: L2
UniProtID_Ref: D0Z5S8
UniProt_Name_Ref: D0Z5S8_ADE31
Binding_ligand: dsDNA
Function: TR, NAP
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(6828374, 27362237)
Other_assays: I(15780869, DNA-binding protein pull-down assay)
Human_infection_evidence: Fields Virology
Notes: D0Z5S8 is inferred from Human adenovirus C protein P68950
Aliases:
L2 protein pVII, L2 protein VII, Major core protein pVII, Pre-core protein VII, Pre-histone-like nucleoprotein, Protein VII, pVII, PVII

Functional_annotation:
Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Plays also a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.


Viral_family: Adenoviridae
Species: Human adenovirus B
Name: E1A
Aliases: Early E1A 28 kDa protein, Early E1A protein
UniProtID_Ref: P03256
UniProt_Name_Ref: E1A_ADE07
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(19129215, 21715488)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19129215, 10446138)
EMSA: I(10446138)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0A7DXW5,A0A0A7DY38,A0A1U9ALF8,A0A1U9ALG4,A0A219PC17,A0A386NAE6,A0A386NAK0,A0A386NCD8,A0A386NCU0,D2DM82,D6BP20,Q2KRU4,Q2KS74,Q2KS76,Q2KS77,Q2KSL5,Q2KSL6,Q4JEQ5,Q4JEQ6,Q5EY85,Q5EY86,Q5YKW5,Q5YKX2,Q6JGG9,Q6RK99,Q7T953,Q7T954,Q8JSK3,Q8JSK4,R4HLK4,R4HMJ7

Functional_annotation:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).


Viral_family: Adenoviridae
Species: Human adenovirus B
Name: E3
UniProtID_Ref: P11315
UniProt_Name_Ref: E3145_ADE03
UniProt_IDs_Orthologs: D2DMA9,P15135,Q2KSH2,Q2Y0F9,Q5EY47,Q67732,Q83121,Q91CJ8,Q9PX47,R4HML9
Binding_ligand: indirect/unknown
Function: TR, other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(16423054)
EMSA: I(16423054, 11991979)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: D2DMA9 is inferred from Human adenovirus C protein P68976
Functional_annotation: Protects virus-infected cells from TNF-induced cytolysis.
Aliases:
14 kDa protein, 14.7 kDa protein, 15.3 kDa protein, E3 14.7 kDa protein, E3B, Early E3 15.3 kDa protein, ORF 15.3 kDa


Viral_family: Adenoviridae
Species: Human adenovirus B
Name: E4
UniProtID_Ref: D0EF64
UniProt_Name_Ref: D0EF64_ADE07
UniProt_IDs_Orthologs: A0A096XFF7,D2DMB1,I1V198,K7SXT6,Q2KRV1,Q2KS47,Q2KSJ0,Q2Y0F6,Q4JEL5,Q5EY43,Q7T924,R4HLG5
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8633237, 1832724, 2137929)
EMSA: I(1832724, 2137929)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: D0EF64 is inferred from Human adenovirus C protein P03238
Aliases:
299 aa, 32 kDa protein, 33.2 kDa protein, 34 kDa protein, E4 33.2 kDa protein, E4 33 kDa protein, E4 ORF6 34.7 kDa protein, E4 ORF6/7, E4 ORF6 protein, E4 ORF (Fragment), ORF 6/7, Orf6/7 protein, ORF6/7

Functional_annotation:
Modulates viral and host transcriptional activity to promote viral genome replication. Stimulates viral E2a promoter activity by binding and inducing dimerization of host E2F. During viral infection E1A protein binds to cellular retinablastoma (RB) family members and disociates these repressors from a complex with E2F proteins. Free E2F is then bound to E4orf6/7 which leads to transactivation of viral E2 promoter, and cellular promoters such as E2F-1 promoter. Activation of cellular E2F targets promote cell cycle S phase and thereby possibly favorises viral DNA replication process.


Viral_family: Adenoviridae
Species: Human adenovirus C
Name: E1A
Aliases: Early E1A 32 kDa protein, Early E1A protein
UniProtID_Ref: P03255
UniProt_Name_Ref: E1A_ADE05
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(19129215, 21715488)
ChIP_seq: N
Structure_PDB_ID: 2KJE, 2R7G
Reporter_assay: D(19129215, 10446138)
EMSA: D(10446138)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A1U9ALK2,A0A3G1HBN7,E1U5L3,E1U5L4,E7DY80,P03254,P03254-2,P03255-2,Q2KS29,Q6JGH2,Q6JGH3,Q6VGV9,Q6VGW0,Q71BY7,Q71BY8,W8VTN3

Functional_annotation:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:26405230).


Viral_family: Adenoviridae
Species: Human adenovirus C
Name: E2A
UniProtID_Ref: P03264
UniProt_Name_Ref: DNB2_ADE02
UniProt_IDs_Orthologs: A0A0U5C455,A0A1U9ALL4,E1U5P2,E7DY93,P03265,Q2KS06,Q6VGU4,Q71BW6,W8VNG9
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(11581372)
EMSA: D(12502807, 8039495)
Other_assays: N
Human_infection_evidence: Fields Virology
Aliases:
DBP, DNA-binding protein, Early 2A protein, Early E2A DNA-binding protein, Early E2A DNA-binding protein,,E2a_1

Functional_annotation:
Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral pol, host NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the whole ssDNA genome during synthesis. The complementary strand synthesis induces its release from DNA template. May inhibit cellular transcription mediated by the interaction between host SRCAP and CBP.


Viral_family: Adenoviridae
Species: Human adenovirus C
Name: E3
Aliases: E3-14.7k, Early 3 14.7 kDa protein
UniProtID_Ref: P68976
UniProt_Name_Ref: E3145_ADE02
UniProt_IDs_Orthologs: A0A0U5BYW0,A0A127WKD0,A0A3G8W4Y8
Binding_ligand: indirect/unknown
Function: TR, other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(16423054)
EMSA: D(16423054, 11991979)
Other_assays: D(16423054)
Human_infection_evidence: Fields Virology
Functional_annotation:
May prevent Nf-kappaB activation by immune signals like Tumor necrosis factor, presumably by inhibiting NFKB1 dimer DNA-binding. May act directly at the TNF receptor to inhibit signaling.


Viral_family: Adenoviridae
Species: Human adenovirus C
Name: E4
Aliases: E4-ORF6/7, Early 4 ORF6/7 control protein, Early E4 17 kDa protein
UniProtID_Ref: P03238
UniProt_Name_Ref: E4RF5_ADE02
UniProt_IDs_Orthologs: A0A0U4XAB1,A0A0U5BPW3,A0A0U5CNF1,A0A127WK23,A0A1U9ALN2,A0A3G8WH84,E1U5Q6
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8633237, 1832724, 2137929)
EMSA: D(1832724, 2137929)
Other_assays: D(8035503)
Human_infection_evidence: Fields Virology
Functional_annotation:
Modulates viral and host transcriptional activity to promote viral genome replication. Stimulates viral E2a promoter activity by binding and inducing dimerization of host E2F. During viral infection E1A protein binds to cellular retinablastoma (RB) family members and dissociates these repressors from a complex with E2F proteins. Free E2F is then bound to E4orf6/7 which leads to transactivation of viral E2 promoter, and cellular promoters such as E2F-1 promoter. Activation of cellular E2F targets promote cell cycle S phase and thereby possibly favorises viral DNA replication process.


Viral_family: Adenoviridae
Species: Human adenovirus C
Name: L2
UniProtID_Ref: P68950
UniProt_Name_Ref: NP_ADE02
UniProt_IDs_Orthologs: A8D0L7,E1U5N6,P68951,Q71BX2
Binding_ligand: dsDNA
Function: TR, NAP
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(6828374, 27362237)
Other_assays: D(3743550, cross-linking), D(15163739, Immunofluorescence)
Human_infection_evidence: Fields Virology
Aliases:
L2 protein pVII, L2 protein VII, Major core protein pVII, ppVII, Pre-core protein VII, Pre-histone-like nucleoprotein, Protein VII, pro-VII, pVII, PVII

Functional_annotation:
Plays a role in the inhibition of host immune response within the nucleus. Interacts with cellular nucleosomes and immobilizes the host immune danger signal HMGB1 on chromatin. In turn, prevents HMGB1 release out of the cell and thus decreases inflammation. Plays also a role in the wrapping and condensation of the viral DNA. May also promote viral genome import into the nucleus.


Viral_family: Adenoviridae
Species: Human adenovirus D
Name: E1A
UniProtID_Ref: Q9YLA0
UniProt_Name_Ref: Q9YLA0_ADE09
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(19129215, 21715488)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19129215, 10446138)
EMSA: I(10446138)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle.
Aliases:
21 kDa protein, 21.2 kDa protein, E1A 12S, E1A 12S protein, Early E1A 12s, Early E1A 12S, Early E1A protein

UniProt_IDs_Orthologs:
A0A1B1W8K3,A0A1P7YXD4,A0A1P7YXL4,A0A1P7YY79,A0A1Y1C2A5,B2VQE2,B9A5A6,B9A5E2,B9A5H8,E1CII9,F1DT55,K7ZRT6,M0QU00,Q9YLA1


Viral_family: Adenoviridae
Species: Human adenovirus E
Name: E1A
Aliases: Early E1A 28 kDa protein, Early E1A protein
UniProtID_Ref: P10407
UniProt_Name_Ref: E1A_ADE04
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(19129215, 21715488)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19129215, 10446138)
EMSA: I(10446138)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A1U9AL55,A0A1W2KFI9,Q2KSG8,Q2KSH0,Q2KSH1,Q4JEV1,Q5GFD1,Q5VHC6,Q5YKX0,Q64835,Q64836,T1SQR0,T1SRS7,T1STJ3

Functional_annotation:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E1A protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1 by direct competition for the same binding site on RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes and of the E2 region of the adenoviral genome. Release of E2F1 leads to the ARF-mediated inhibition of MDM2 and causes TP53/p53 to accumulate because it is not targeted for degradation by MDM2-mediated ubiquitination anymore. This increase in TP53, in turn, would arrest the cell proliferation and direct its death but this effect is counteracted by the viral protein E1B-55K. Inactivation of the ability of RB1 to arrest the cell cycle is critical for cellular transformation, uncontrolled cellular growth and proliferation induced by viral infection. Interaction with RBX1 and CUL1 inhibits ubiquitination of the proteins targeted by SCF(FBXW7) ubiquitin ligase complex, and may be linked to unregulated host cell proliferation. The tumorigenesis-restraining activity of E1A may be related to the disruption of the host CtBP-CtIP complex through the CtBP binding motif. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).


Viral_family: Adenoviridae
Species: Human adenovirus F
Name: E2A
Aliases: DBP, DNA-binding protein, Early 2A protein, Early E2A DNA-binding protein
UniProtID_Ref: P11806
UniProt_Name_Ref: DNB2_ADE40
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(11581372)
EMSA: I(12502807, 8039495)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A060ILQ0,A0A060ILW5,A0A142G3K6,A0A1S6ELQ0,A0A1S6ELU3,A0A1S6ELX1,A0A3G4WEW3,A0A3G8W3Y9,B5SNS7,E2IJY9,P11807,W0RYE2


Viral_family: Adenoviridae
Species: Human adenovirus F
Name: E3
UniProtID_Ref: Q98817
UniProt_Name_Ref: Q98817_ADE41
Binding_ligand: indirect/unknown
Function: TR, other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(16423054)
EMSA: I(16423054, 11991979)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: Q98817 is inferred from Human adenovirus C protein P68976
Functional_annotation: mitigation of host defenses by virus
Aliases:
Control protein E3 14.7K, E3 14.0 kDa protein (Homologous to Ad2 E3 14.7 kDa protein), E3 14.0 kd protein, E3 14.7K, E3 14.7K protein


Viral_family: Arenaviridae
Species: Junin mammarenavirus
Name: N
Aliases: Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P14239
UniProt_Name_Ref: NCAP_JUNIN
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4K7E
Reporter_assay: I(21085117, 21262835)
EMSA: N
Other_assays: D(20007272), I(22084115, RNA complex structure)
Human_infection_evidence: 30123198.0
UniProt_IDs_Orthologs:
A0A0M4MQK9,C1K9K0,C1K9K4,C5MKK3,D1GI65,D2CFM2,D2CFM5,D2CFR6,D2CFR8,D2CFS0,D2CFS2,D2CFS4,D2CFS6,D2CFS8,D2CFT0,D2CFT2,O10431,O10432,O10433,Q2XP54,Q6IVU2,Q6UY72

Functional_annotation:
Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of host IRF3, a protein involved in interferon activation pathway, leading to the inhibition of interferon-beta and IRF3-dependent promoters activation. Encodes also a functional 3'-5' exoribonuclease that degrades preferentially dsRNA substrates and thereby participates in the suppression of interferon induction.


Viral_family: Arenaviridae
Species: Machupo virus
Name: N
Aliases: NP, Nucleocapsid protein, Nucleoprotein, Nucleoprotein (Fragment), Protein N
UniProtID_Ref: P26578
UniProt_Name_Ref: NCAP_MACHU
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(21085117, 21262835)
EMSA: N
Other_assays: D(20007272), I(22084115, RNA complex structure)
Human_infection_evidence: 22607481.0
UniProt_IDs_Orthologs:
A0A1U8ZS29,A0A1U8ZS66,A0A1U8ZS72,A0A1U8ZS90,A0A1U8ZSD0,A0A1U8ZSR6,A9JR11,A9JR13,A9JR15,A9JR19,A9JR21,C7AZ57,C7AZ59,C7AZ61,C7AZ63,C7AZ65,G9J1N3,Q6IUF6,Q6IVT4,Q6PXP5,Q8AZ68


Viral_family: Bornaviridae
Species: Borna disease virus 1
Name: P
Aliases: P protein, p23, p24, Phosphoprotein, P/X
UniProtID_Ref: P0C799
UniProt_Name_Ref: PHOSP_BDVV
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15509569, 14581561)
EMSA: N
Other_assays: D(14581561, 15509569)
Human_infection_evidence: 14581561.0
UniProt_IDs_Orthologs:
A4D837,A5A7J0,O10393,O10402,O10404,O10405,O10406,Q1HVJ9,Q1L311,Q53WV0,Q53WV1,Q5GLA5,Q5GLB1,Q5GLC9,Q5XWT9,Q5XWU0,Q5XWU1,Q5XWU2,Q5XWU3,Q65456,Q65457,Q65458,Q76RA4,Q774E4,Q80G14,Q80G15,Q9DRF2,Q9DRF3,Q9E7S5,Q9E7S8,Q9IV61,Q9IV62,Q9IW59,Q9JGP3,Q9Q4W4,X2D1D2,X2D1D5

Functional_annotation:
Essential component of the RNA polymerase transcription and replication complex. Acts as a scaffold which brings L in close proximity to the N-RNA complex. Plays a role in the segregation of the viral genome in host daughter cells during mitosis by interacting with host HMGB1, a host chromatin-remodeling DNA architectural protein, thereby stabilizing RNP on chromosomes. Interacts with host TBK1 and thus interferes with activation of cellular antiviral state. Inhibits cellular histone acetyltransferase activities.


Viral_family: Coronaviridae
Species: Human coronavirus 229E (HCoV-229E)
Name: E
Aliases: E protein, Envelope small membrane protein, sM, sM protein
UniProtID_Ref: P19741
UniProt_Name_Ref: VEMP_CVH22
UniProt_IDs_Orthologs: A0A059SEL9,A0A384L4F1,J9VDX2,S5YAG7,S5YGS8
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(https://www.biorxiv.org/content/10.1101/2020.03.22.002386v3.full.pdf)
Human_infection_evidence: 32006468.0
Functional_annotation:
Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.


Viral_family: Coronaviridae
Species: Human coronavirus 229E (HCoV-229E)
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P15130
UniProt_Name_Ref: NCAP_CVH22
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep, NAP
Primary_secondary_vTR: S
ChIP: I(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15890900)
EMSA: I(16546436;15759315;25700263)
Other_assays: I(14623261;29793506)
Human_infection_evidence: 32006468.0
Notes: P15130 is inferred from Human SARS coronavirus protein P59595
UniProt_IDs_Orthologs:
A0A059SGB0,A0A097ZMN8,A0A097ZMN9,A0A097ZMP1,A0A097ZMP2,A0A097ZMP3,A0A097ZMR3,A0A127ATI4,A0A127ATI5,A0A127ATI6,A0A127ATI8,A0A127ATJ0,A0A127ATJ4,A0A127ATJ5,A0A127ATJ6,A0A127ATJ8,A0A127ATM6,A0A127ATM8,A0A127ATP2,A0A127AU31,A0A127AU35,A0A127AUT5,A0A127AUU5,A0A127AWS1,A0A127AWT0,A0A193BL28,A0A1B3TN93,A0A1L7B914,A0A1L7B917,A0A1L7B932,A0A1L7B959,A0A1V0BZ85,A0A1V0E0Z0,A0A1W6DZN2,A0A1Z1R303,A0A223FUI1,A0A384QXL5,A0A384QXL7,A0A384QXY0,A0A384QZB4,A0A384R2K5,A0A384R2L0,A0A384RBS5,A0A384RBS7,A0A384RHP2,J9V7P0,J9V7P5,Q1HVM7,Q1HVM8,Q1HVM9,Q1HVN3,Q1HVN6,Q1HVN7,Q1HVN9,Q1HVP0,Q1HVP1,Q1HVP2,Q1HVP3,Q1HVP5,Q1HVP6,Q1HVP8,Q1HVP9,Q1HVQ0,S5YAG2,S5Z1H9,S5ZJ09,U3PTJ0,U3PUD7

Functional_annotation:
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.


Viral_family: Coronaviridae
Species: Human coronavirus HKU1
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: Q5MQC6
UniProt_Name_Ref: NCAP_CVHN1
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep, NAP
Primary_secondary_vTR: S
ChIP: I(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(16546436;14623261;18055455;17108024;15890900)
EMSA: I(16546436;15759315;25700263)
Other_assays: I(14623261;29793506)
Human_infection_evidence: 32006468.0
UniProt_IDs_Orthologs:
A0A0C5PN53,A0A0C5PWK5,A0A0C5PXY9,A0A0C5Q0N4,A0A0C5Q9E2,A0A127ASV7,A0A127ASV8,A0A127ASW6,A0A127ASW7,A0A127ASY7,A0A127ASZ8,A0A127AT27,A0A127AT34,A0A127AT49,A0A127AT59,A0A127AT66,A0A127AT73,A0A127ATF0,A0A127ATF4,A0A127ATT6,A0A127ATU5,A0A127ATV4,A0A127AUB1,A0A127AUC1,A0A127AW89,A0A127AWE0,A0A1Y0EV09,A0A3Q9JNH6,E0YJ48,Q0PRK0,Q0ZJD7,Q0ZJE5,Q0ZJH7,Q0ZME3,Q14EA6,Q19U24,Q19U25,Q19U26,Q19U29,Q19U34,Q19U36,S5ZBQ7,U3NAH8

Functional_annotation:
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.


Viral_family: Coronaviridae
Species: Human coronavirus NL63 (HCoV-NL63)
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: Q6Q1R8
UniProt_Name_Ref: NCAP_CVHNL
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep, NAP
Primary_secondary_vTR: S
ChIP: I(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: 5EPW
Reporter_assay: I(16546436;14623261;18055455;17108024;15890900)
EMSA: D(25700263)
Other_assays: I(14623261;29793506)
Human_infection_evidence: 32006468.0
UniProt_IDs_Orthologs:
A0A127ATP0,A0A127ATQ0,A0A127ATQ1,A0A127ATQ4,A0A127ATQ7,A0A127ATQ8,A0A127ATR0,A0A127ATR3,A0A127ATR6,A0A127ATR7,A0A127ATS0,A0A127ATS3,A0A127ATS5,A0A127ATS6,A0A127ATS9,A0A127ATT3,A0A127ATT5,A0A127ATT9,A0A127ATU8,A0A127ATV6,A0A127ATV7,A0A127ATW2,A0A127ATW4,A0A127ATX3,A0A127ATX8,A0A127ATY1,A0A127ATY7,A0A127ATY8,A0A127AU18,A0A127AU23,A0A127AU27,A0A127AU68,A0A127AU79,A0A127AU90,A0A127AUA1,A0A127AV25,A0A127AV38,A0A127AV50,A0A127AV68,A0A127AX00,A0A127AX15,A0A127AX50,A0A127AX58,A0A1Y0EV18,A0A2L0WQF7,A0A2P1E938,A0A2P1E945,A0A2P1E948,A0A2P1E959,A0A2P1E971,A0A2U8JDM2,A0A384R2N5,A0A384RBU9,A0A384RBV1,A0T2T5,H9EJ20,H9EJ69,H9EJ76,H9EJA4,I7DJE7,Q06XQ0,Q06XQ1,Q06XQ2,Q06XQ3,Q06XQ4,Q06XQ5,Q06XQ6,Q06XQ7,Q06XQ8,Q06Y12,Q0GMF2,U3M6A0,U3M7G3

Functional_annotation:
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.


Viral_family: Coronaviridae
Species: Human coronavirus OC43 (HCoV-OC43)
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P33469
UniProt_Name_Ref: NCAP_CVHOC
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep, NAP
Primary_secondary_vTR: S
ChIP: I(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(16546436;14623261;18055455;17108024;15890900)
EMSA: I(16546436;15759315;25700263)
Other_assays: I(14623261;29793506)
Human_infection_evidence: 32006468.0
UniProt_IDs_Orthologs:
A0A0A0YP48,A0A0B4N5U7,A0A0B4N5V5,A0A0B4N684,A0A0B4N6G5,A0A0B4N6G8,A0A0B4N6W6,A0A0B4N7F3,A0A0B4N7G3,A0A0B4N7G5,A0A0B4Q800,A0A0B4Q8L7,A0A0B4UEK7,A0A0B4UFS5,A0A0C5PN59,A0A0C5PN66,A0A0C5PN72,A0A0C5PWL1,A0A0C5PWL5,A0A0C5PWM1,A0A0C5PWM6,A0A0C5PXZ8,A0A0C5PY00,A0A0C5PY04,A0A0C5Q0P0,A0A0C5Q0P6,A0A0C5Q0Q2,A0A0C5Q9E8,A0A0C5Q9F4,A0A0C5Q9G1,A0A0G2RC60,A0A0G2RC64,A0A0G2RC66,A0A0G2RC68,A0A0G2RC70,A0A0G2RC83,A0A0G2RC86,A0A0G2RC94,A0A0G2RCA8,A0A0G2RCB5,A0A0G2RCY1,A0A0G2RCZ3,A0A0K0KPA1,A0A0K0KPA2,A0A0K0KPB1,A0A0K0KPQ5,A0A0K0KQ87,A0A0K0KQA8,A0A0K0L8G1,A0A0K0L9S6,A0A127AT13,A0A127AT23,A0A127AT26,A0A127AT35,A0A127AT45,A0A127AT53,A0A127AT99,A0A127ATA3,A0A127ATA6,A0A127ATA7,A0A127ATA9,A0A127ATB4,A0A127ATB6,A0A127ATC1,A0A127ATJ2,A0A127ATK0,A0A127ATZ8,A0A127AU02,A0A127AUL9,A0A127AUM9,A0A127AWJ2,A0A127AWK6,A0A127AWL7,A0A140E069,A0A1C8Z4S7,A0A1L7H9A3,A0A1S5VG93,A0A1S5VGD1,A0A1S5VGI5,A0A1S5VGJ0,A0A1V0BZ77,A0A1W6DZM9,A0A1W6DZV4,A0A1W6DZW0,A0A1W6DZX0,A0A1Y0EV19,A0A2D1CLX3,A0A2D1QW28,A0A385H5N1,A0A385H5Q3,A0A385H5U7,A0A385H5X1,A0A385H5Z4,A0A385H6E5,A0A385H6Q1,A0A385H6V0,G5CJB5,G5CJC3,Q4VID1,Q4VIE0,Q696P4,Q6SA23,U3M6V0,U3M6V7,U3M7I5,U3M7J7,U3M7K1,U3M7Z4,U3M7Z6,U3M7Z8,U3M804,U3M816,U3M820,U3M822,U3M826,U3M828


Viral_family: Coronaviridae
Species: Human SARS coronavirus
Name: 3b
Aliases: Accessory protein 3b, Non-structural protein 3b, ns3b, ORF3b,SARSCoVgp06, ORF4, Protein X2
UniProtID_Ref: P59633
UniProt_Name_Ref: NS3B_CVHSA
Binding_ligand: indirect/unknown
Function: TR, Rep, Other
Primary_secondary_vTR: S
ChIP: D(22253733)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(22253733)
EMSA: N
Other_assays: N
Human_infection_evidence: 27344959.0
Functional_annotation: Induces host cell G0/G1 arrest and apoptosis.
UniProt_IDs_Orthologs:
A0A0U2PTX6,A0A3G5BIZ2,B8Q8Q5,B8Q8R6,B8Q8S8,B8Q8T9,B8Q8V0,B8Q8W1,C4P6Q9,D2DJW6,D2E1D4,D2E1E9,D2E223,D2E252,D2E267,D2E2F4,D2E2T6,D3KDM7,J9T0L3,Q19QW8,Q1EFN0,Q1EFP3,Q1T6X4,Q3S2C3,Q3ZTC3,Q3ZTD8,Q4JDQ2,Q4JDR5,Q5DIC3,Q692E2,Q6GYQ9,Q6JH36,Q6JH44,Q6R7Y4,Q6RCW3,Q6RCX4,Q6RCY5,Q6RCZ6,Q6RD07,Q6RD18,Q6RD29,Q6RD40,Q6RD51,Q6RD62,Q6S8D5,Q6T1E1,Q6TPE6,Q6VA76,Q6VA87,Q6VA98,Q6WGN1,U5WHZ3,U5WI10,U5WLA7


Viral_family: Coronaviridae
Species: Human SARS coronavirus
Name: E
Aliases: E protein, Envelope small membrane protein, sM, sM protei, sM protein
UniProtID_Ref: P59637
UniProt_Name_Ref: VEMP_CVHSA
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(https://www.biorxiv.org/content/10.1101/2020.03.22.002386v3.full.pdf)
Human_infection_evidence: 27344959.0
UniProt_IDs_Orthologs:
A0A0K1Z002,A0A0K1Z029,A0A0U2PTJ4,A0A3G5BJ03,A2TGS2,B8Q8Q6,B8Q8R7,B8Q8S9,B8Q8U0,B8Q8V1,B8Q8W2,C4P6R0,D2DJW7,D2E1D5,D2E1F0,D2E224,D2E253,D2E268,D2E2J8,D2E2M8,D2E2S3,D2E2T7,D3KDM8,D3KDQ6,D5HJQ3,D5HJR4,D5HJS5,D5HJT6,D5HJW0,D5HJX1,D5HJY2,D5HJZ3,D5HK04,J9TE86,Q19QW7,Q1EFM9,Q1EFP2,Q1T6X3,Q3LZU0,Q3LZV1,Q3S2C2,Q3ZTC2,Q3ZTD7,Q4JDQ1,Q4JDR4,Q5DIC2,Q5Y298,Q692E1,Q6GYQ8,Q6JH35,Q6JH43,Q6QJ39,Q6R7Y3,Q6RCW2,Q6RCX3,Q6RCY4,Q6RCZ5,Q6RD06,Q6RD17,Q6RD28,Q6RD39,Q6RD50,Q6RD61,Q6S8D4,Q6SRI1,Q6SRI5,Q6SRI9,Q6SRJ3,Q6SRJ7,Q6SRK1,Q6SRK5,Q6SRK9,Q6SRL3,Q6SRL7,Q6SRM1,Q6SRM5,Q6SRM9,Q6SRN3,Q6SRN7,Q6SRP1,Q6SRP5,Q6SRP9,Q6T1D9,Q6TPE5,Q6VA75,Q6VA86,Q6VA97,Q6WGP2,U5WI28,U5WI54,U5WLL8

Functional_annotation:
Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.


Viral_family: Coronaviridae
Species: Human SARS coronavirus
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P59595
UniProt_Name_Ref: NCAP_CVHSA
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep,NAP
Primary_secondary_vTR: S
ChIP: D(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: 2OFZ
Reporter_assay: D(16546436;14623261;18055455;17108024)
EMSA: D(16546436;15759315)
Other_assays: D(14623261, TransFactor analysis assay)
Human_infection_evidence: 27344959.0
UniProt_IDs_Orthologs:
A0A0K1YZZ7,A0A0K1Z0P8,A0A0U2NR12,A0A3G5BJ14,A2TGS3,B8Q8R0,B8Q8S2,B8Q8T3,B8Q8U4,B8Q8V5,B8Q8W6,C4P6R7,D2DJX3,D2E1E2,D2E1F7,D2E216,D2E230,D2E275,D2E2E7,D2E2N5,D3KDN4,D5HJQ9,D5HJS0,D5HJT1,D5HJU2,D5HJV5,D5HJW6,D5HJX7,D5HJY8,D5HJZ9,D5HK10,Q19QW0,Q1EFM2,Q1EFN5,Q1T6X0,Q3I5K0,Q3I5K3,Q3LZU2,Q3LZV6,Q3S2B5,Q3ZTB6,Q3ZTD1,Q4JDP5,Q4JDQ8,Q5DIB8,Q692D7,Q6GYQ2,Q6JH33,Q6JH41,Q6QHB3,Q6QHB4,Q6QHB5,Q6QJ37,Q6R7X9,Q6RCV8,Q6RCW9,Q6RCY0,Q6RCZ1,Q6RD02,Q6RD13,Q6RD35,Q6RD46,Q6RD57,Q6S8C7,Q6S8E1,Q6T1D2,Q6TPE0,Q6UPD4,Q6UUW1,Q6UZE8,Q6UZF2,Q6V583,Q6VA71,Q6VA82,Q6VA93,U5WIP0,U5WLA2,U5WLN3


Viral_family: Coronaviridae
Species: Middle East respiratory syndrome-related coronavirus; Human coronavirus EMC
Name: E
Aliases: E protein, Envelope small membrane protein, M, sM protein
UniProtID_Ref: R9UQN1
UniProt_Name_Ref: R9UQN1_9BETC
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(https://www.biorxiv.org/content/10.1101/2020.03.22.002386v3.full.pdf)
Human_infection_evidence: 27344959.0
UniProt_IDs_Orthologs:
A0A075E1D8,A0A0G3VM72,A0A0G3VM78,A0A0S3IVQ1,A0A0U2GLG8,A0A0U2GP61,A0A1D6Y7S6,K0BRH1,K9N5R3,M4SQZ1,R9WYQ9,T2BBC7,T2BBI3


Viral_family: Coronaviridae
Species: Middle East respiratory syndrome-related coronavirus; Human coronavirus EMC
Name: N
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: K9N4V7
UniProt_Name_Ref: NCAP_CVEMC
Binding_ligand: ssRNA, dsDNA
Function: TR, Rep, NAP
Primary_secondary_vTR: S
ChIP: I(16546436;18055455)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(16546436;14623261;18055455;17108024;15890900)
EMSA: I(16546436;15759315;25700263)
Other_assays: D(29793506, Filter binding assay )
Human_infection_evidence: 27344959.0
Notes: K9N4V7 is inferred from Human SARS coronavirus protein P59595
UniProt_IDs_Orthologs:
A0A023NFV4,A0A023VZL1,A0A023VZM0,A0A024E1L1,A0A068FIZ3,A0A068FM93,A0A068FR27,A0A0A0QHI8,A0A0A7E7L7,A0A0A7KVQ1,A0A0D3MU51,A0A0D3MU65,A0A0G2UKT0,A0A0G3KE78,A0A0R7E423,A0A0U2GLA1,A0A0U2GM98,A0A0U2GMX8,A0A0U2GPN9,A0A0U2GQM3,A0A0U2GQX0,A0A0U4BQZ8,A0A140AZ32,A0A141LLD8,K0BVN3,M1S193,M4SRY6,R9UM87,T2B9H8,T2B9R0,T2BBB8,T2BBK0,V9TXP8,W5ZZJ8,W5ZZL9,W5ZZM7,W5ZZP8,W5ZZV0,W6A8J1,W8NMH3


Viral_family: Filoviridae
Species: Bundibugyo ebolavirus
Name: VP35
Aliases: Polymerase cofactor VP35, Polymerase complex protein
UniProtID_Ref: B8XCM8
UniProt_Name_Ref: B8XCM8_9MONO
UniProt_IDs_Orthologs: R4QGV8
Binding_ligand: dsRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(9971816, 11027311, 12829834, 19557165)
EMSA: I(27642076)
Other_assays: I(19557165)
Human_infection_evidence: 21987745.0
Notes: R4QGV8 is inferred from Zaire ebolavirus protein Q05127
Functional_annotation:
Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling.


Viral_family: Filoviridae
Species: Ebola virus
Name: NP
Aliases: Nucleocapsid protein, Nucleoprotein
UniProtID_Ref: A0A2Z2FMG9
UniProt_Name_Ref: A0A2Z2FMG9_9MONO
Binding_ligand: ssRNA
Function: NAP, TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(31952352; 9971816)
EMSA: I(28566377)
Other_assays: D(28593988)
Human_infection_evidence: Fields Virology
Functional_annotation: RNA binding,viral RNA genome packaging,helical viral capsid,host cell cytoplasm,viral nucleocapsid
UniProt_IDs_Orthologs:
A0A0E3H7K1,A0A0E3KX27,A0A141BR54,A0A1C4HD05,A0A2Z2FIR4,A0A2Z2FJ72,A0A2Z2FJB7,A0A2Z2FJH7,A0A2Z2FNR0,A0A2Z2FWI4


Viral_family: Filoviridae
Species: Ebola virus
Name: VP35
Aliases: Polymerase cofactor VP35
UniProtID_Ref: A0A1C4HDK9
UniProt_Name_Ref: A0A1C4HDK9_9MONO
UniProt_IDs_Orthologs: A0A0E3N983
Binding_ligand: dsRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9971816, 11027311, 12829834, 19557165)
EMSA: D(27642076)
Other_assays: D(19557165)
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays an essential role +U68:U85in viral RNA synthesis and also a role in suppressing innate immune signaling.


Viral_family: Filoviridae
Species: Lake Victoria marburgvirus
Name: NP
Aliases: NC, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P27588
UniProt_Name_Ref: NCAP_MABVM
UniProt_IDs_Orthologs: A9Q1G5,A9Q1H2,C0IT76,C0IT83,G9HWE2,P35263,Q1PD53,Q1PD74,Q1PDA9,Q1PDB6,Q1PDD0,Q6UY69
Binding_ligand: ssRNA
Function: NAP, TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 6APP
Reporter_assay: I(31952352; 9971816)
EMSA: I(28566377)
Other_assays: I(28593988)
Human_infection_evidence: 31131088.0
Functional_annotation:
Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. During replication, encapsidation by NP is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).


Viral_family: Filoviridae
Species: Lake Victoria marburgvirus
Name: VP30
Aliases: Minor nucleoprotein VP30, Transcription activator VP30
UniProtID_Ref: P35258
UniProt_Name_Ref: VP30_MABVM
UniProt_IDs_Orthologs: P41326,Q1PD49,Q1PD56,Q1PDA5,Q1PDB2,Q1PDB9,Q1PDC6,Q6UY65
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 5T3W
Reporter_assay: I(27279615, 23493393, 27755595)
EMSA: I(27279615)
Other_assays: I(12163572)
Human_infection_evidence: 31131088.0
Functional_annotation:
Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA secondary structure at the transcription start site of the first gene (By similarity).


Viral_family: Filoviridae
Species: Marburg marburgvirus
Name: NP
Aliases: Nucleocapsid protein, Nucleoprotein
UniProtID_Ref: C7B276
UniProt_Name_Ref: C7B276_9MONO
Binding_ligand: ssRNA
Function: NAP, TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9971816;9765419)
EMSA: D(28566377)
Other_assays: I(28593988)
Human_infection_evidence: 31146800.0
Functional_annotation: RNA binding,viral RNA genome packaging,helical viral capsid,host cell cytoplasm,viral nucleocapsid
UniProt_IDs_Orthologs:
A0A077D355,A0A0U2M3H8,A0A385L0K9,C7B248,C7B269,C7B283,E0X0Z7,E0X111,K4MQ25,K4MQC5,K4MQF4,K4MQY0,K4MR07,K4MR89,K4MRA8,K4MSQ7,K4MSZ0,K4MT16,K4N3C7,K4N3K2,K4N3V7


Viral_family: Filoviridae
Species: Marburg marburgvirus
Name: VP30
Aliases: Minor nucleoprotein VP30, Viral protein 30, VP30 minor nucleoprotein
UniProtID_Ref: C7B280
UniProt_Name_Ref: C7B280_9MONO
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9765419)
EMSA: I(27279615)
Other_assays: I(12163572)
Human_infection_evidence: 31146800.0
Functional_annotation: metal ion binding,viral nucleocapsid
UniProt_IDs_Orthologs:
A0A077CZD4,A0A1U8ZSA8,A0A385L0L3,C7B252,C7B273,E0X101,K4MQ93,K4MQB7,K4MQE5,K4MR00,K4MSM3,K4MSU4,K4MSY4,K4MSZ1,K4MT90,K4N3J5,K4N3M2


Viral_family: Filoviridae
Species: Reston ebolavirus
Name: NP
Aliases: Nucleocapsid protein, Nucleoprotein, Protein N, Reston NP, rNP
UniProtID_Ref: Q8JPY1
UniProt_Name_Ref: NCAP_EBORR
Binding_ligand: ssRNA
Function: NAP, TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 5W2B
Reporter_assay: I(31952352; 9971816)
EMSA: I(28566377)
Other_assays: I(28593988)
Human_infection_evidence: 28542463, 24699737
UniProt_IDs_Orthologs:
A0A1I9VT52,A0A1Y0K5B8,A0A1Y0K5E1,A0A1Y0K5E6,A0A343J1N2,A0A343J1P1,C6G8D3,C6G8E1,C6G8E9,L7RI74,Q91DE1

Functional_annotation:
Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response. VP35 binds to and stabilizes monomeric NP, keeping it soluble. Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released. The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm. Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid. Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription. Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1.


Viral_family: Filoviridae
Species: Reston ebolavirus
Name: VP30
UniProtID_Ref: Q8JPX6
UniProt_Name_Ref: VP30_EBORR
UniProt_IDs_Orthologs: A0A1I9VT58,A0A1Y0K5D8,A0A343J1N8,C6G8D8,C6G8E6,C6G8F4,L7RFD4,L7RI71,Q91DD6
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(27279615, 23493393, 27755595)
EMSA: I(27279615)
Other_assays: I(12163572)
Human_infection_evidence: 28542463, 24699737
Notes: Q8JPX6 is inferred from Zaire ebolavirus protein Q05323
Aliases:
Minor nucleoprotein VP30, Transcription activation factor VP30, Transcription activator VP30, Truncated transcription activation factor VP30

Functional_annotation:
Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA stem-loop at the transcription start site of the first gene. Binds to RNA (By similarity).


Viral_family: Filoviridae
Species: Reston ebolavirus
Name: VP35
Aliases: Polymerase cofactor VP35, Polymerase complex protein VP35
UniProtID_Ref: Q8JPY0
UniProt_Name_Ref: VP35_EBORR
UniProt_IDs_Orthologs: A0A1I9VT53,A0A343J1P2,C6G8D4,C6G8E2,C6G8F0,L7RF08,L7RFC8,Q91DE0
Binding_ligand: dsRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(9971816, 11027311, 12829834, 19557165)
EMSA: I(27642076)
Other_assays: I(19557165)
Human_infection_evidence: 28542463, 24699737
Notes: Q8JPY0 is inferred from Zaire ebolavirus protein Q05127
Functional_annotation:
Acts as a polymerase cofactor in the RNA polymerase transcription and replication complex. Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factor 3 (IRF3), a transcription factor critical for the induction of interferons alpha and beta. This blockage is produced through the interaction with and inhibition host IKBKE and TBK1 producing a strong inhibition of the phosphorylation and activation of IRF3. Also inhibits the antiviral effect mediated by the interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (By similarity).


Viral_family: Filoviridae
Species: Zaire ebolavirus
Name: NP
Aliases: Ebola NP, eNP, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P18272
UniProt_Name_Ref: NCAP_EBOZM
Binding_ligand: ssRNA
Function: NAP, TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4ZTA
Reporter_assay: D(31516086)
EMSA: I(28566377)
Other_assays: D(20421407)
Human_infection_evidence: 20957152.0
UniProt_IDs_Orthologs:
A0A068J945,A0A068J9B9,A0A075W933,A0A075WG99,A0A096YGX0,A0A0A7PCE0,A0A0D4D8I2,A0A0D5W848,A0A0D5W865,A0A0D5W876,A0A0D5W897,A0A0D5W8E5,A0A0D5W8K5,A0A0D5W8N2,A0A0D5W8N9,A0A0D5W8U8,A0A0D5W957,A0A0D5W989,A0A0D5W9A2,A0A0D5W9C4,A0A0E3GLU4,A0A0E3TL09,A0A0E3TL91,A0A0E3TLB3,A0A0E3TLI7,A0A0E3TLJ4,A0A0E3TLM0,A0A0E3TLN8,A0A0E3TLR4,A0A0E3TLU1,A0A0E3TLU2,A0A0E3TLW5,A0A0E3TLZ1,A0A0E3TM18,A0A0E3TM19,A0A0E3TMF2,A0A0E3TMH8,A0A0E3TMK2,A0A0E3TMK6,A0A0E3TMN6,A0A0E3TMR4,A0A0E3TMS8,A0A0E3TMW3,A0A0E3TMX8,A0A0E3TMZ7,A0A0E3TN27,A0A0E3TN97,A0A0E3TNH7,A0A0E3TNK0,A0A0E3TNX9,A0A0E3X8E1,A0A0E3XJA0,A0A0E3XJB4,A0A0E3XJS6,A0A0E3XJW0,A0A0E3XJY7,A0A0E3XJZ8,A0A0E3XK34,A0A0E3XK48,A0A0E3XK58,A0A0E3XKU6,A0A0E3XKW4,A0A0E3XL13,A0A0E3XL94,A0A0E3XLF1,A0A0E3XLG4,A0A0E3XLG8,A0A0E3XLL9,A0A0E3XLQ1,A0A0E3XLR5,A0A0E3XLX7,A0A0E3XM43,A0A0F6PCY0,A0A0F6PD20,A0A0F6PDL5,A0A0F6PDL7,A0A0F6PE43,A0A0F6PE50,A0A0F6PEB1,A0A0F6PFN6,A0A0F6PG50,A0A0F6PGB6,A0A0F6PGL9,A0A0F6PGT9,A0A0F6PHL7,A0A0F7DDS0,A0A0F7DDT8,A0A0F7DDX4,A0A0F7IMS2,A0A0F7IMW8,A0A0F7ING0,A0A0F7IQ00,A0A0F7IQT2,A0A0F7IRF1,A0A0G2Y8P8,A0A0G2Y8U2,A0A0G2Y8W8,A0A0G2YAC4,A0A0G2YAP4,A0A0G2YAR8,A0A0G2YAT2,A0A0G2YB39,A0A0G2YCG7,A0A0G2YD31,A0A0G2YDZ4,A0A0G2YEH7,A0A0G2YGJ1,A0A0G2YGK1,A0A0G2YHE2,A0A0G2YHH9,A0A0G2YIW8,A0A0H3VU44,A0A0H3VUH4,A0A0H3VV97,A0A0H3VVT3,A0A0H3VXA2,A0A0H3VYJ4,A0A0H3VYM0,A0A0H3VYM9,A0A0K1NXJ4,A0A0K1NXX0,A0A0K1NY14,A0A0K1NYC4,A0A0K1NYD3,A0A0K1NYE8,A0A0K1NYH3,A0A0K1NYT7,A0A0K1NZA3,A0A0M4RGV8,A0A0N9BE19,A0A0N9QXB6,A0A0N9QXW1,A0A0S0GAE9,A0A0S0GAT9,A0A0S0GBJ7,A0A0S0H198,A0A0S0H215,A0A0S0H2Q7,A0A0S0H2R5,A0A0S0H2S9,A0A0S0H383,A0A0S0H385,A0A0S0H3C5,A0A0S0H3D3,A0A0S0H430,A0A0S0H572,A0A0S0HC67,A0A0S0HDV6,A0A0S2RN13,A0A0U3MRZ4,A0A0U3V214,A0A0U3V2G4,A0A0U3V4C0,A0A0U3V6V7,A0A0U3VB98,A0A0U3VJA1,A0A0U4CUH6,A0A0U4D4X6,A0A0U4DB33,A0A0U4DBA8,A0A0U4DCH1,A0A0U4DD37,A0A0U4DGL1,A0A0U4DGS4,A0A0U4E4B3,A0A0U4E4X5,A0A0U4EBG4,A0A0U4EBR7,A0A0U4EBZ4,A0A0U4EES8,A0A0U4EGH6,A0A0U4EGX9,A0A0U4ENR9,A0A0U4EP82,A0A0U4EPI4,A0A0U4EPQ5,A0A0U4EQU8,A0A0U4ESJ8,A0A0U4ET89,A0A0U4ETP8,A0A0U4EW56,A0A0U4EWH3,A0A0U4EXV0,A0A0U4EYY3,A0A0U4F6D6,A0A141LL89,A0A165Q9F3,A0A172QC61,A0A172QC79,A0A172QC87,A0A1L2BID6,A0A1L2BIG9,A0A1L2BIR4,A0A1L2BIY4,A0A1L2BJ48,A0A1L2BJD9,A0A1L2BJG4,A0A1L7B882,A0A1L7B8E4,A0A1X9IXM9,A0A288QU69,A0A2I4PDK8,A0A2I4PDT9,A0A2I4PE21,A0A2I4PED3,A0A2I4Q526,A0A2I4Q545,A0A2I4SAN4,A0A2I4SAT9,A0A2I4SAU6,A0A2U8KL40,A0A2U9QPQ7,A0A345BF59,A0A345BF77,A0A345BFD1,A0A3G1S963,A0A3G1TWY2,A0A3G2LM13,A0A3G2LM48,A0A3G2LM81,A0A3G2XD84,A0A3G2XE25,A0A3G2XE33,A0A3G2XEF7,A0A3G2XEP4,A0A3G2XG98,A0A3G2XH51,A0A3Q8HGW6,A0A3Q8HHE4,A0A3Q8HHH5,A0A3Q8HHT0,A0A3Q8HI48,A0A3Q8HIF8,A0A3Q8HII1,A0A3Q8HIZ0,A0A3Q8HJA9,A0A3Q8HK17,A0A3Q8HQL2,A8TSK5,A8TSL1,A8TSL7,A8TSM3,A8TSM9,A8TSN5,A8TSP1,A8TSP9,A8TSQ5,A8TSR2,A8TSR7,A8TSS3,A9QPL6,G8DB37,I0DHA6,L7QHT6,L7QHU5,L7QI42,L7QI51,L7QIA8,O72142,Q913A5,Q9QCE9,X5GXS8,X5HMY5

Functional_annotation:
Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:26119732, PubMed:25865894, PubMed:30333622, PubMed:16719918). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:26119732, PubMed:25865894). Upon virus replication, NP is recruited to bind cooperatively viral genomic RNA and VP35 is released (PubMed:29144446). The encapsidated genomic RNA is termed the nucleocapsid and serves as template for transcription and replication. The nucleocapsid is helical with a pitch of 10.81 NP per turn and a diameter of about 22nm (PubMed:22247782). Each NP binds to six nucleotides of viral genomic RNA, three being exposed to the solvant and three hidden into the nucleocapsid (PubMed:30333622). Recruits also host PPP2R5C phosphatase to dephosphorylate VP30 and thereby promote viral transcription (PubMed:29290611, PubMed:27755595). Upon virion assembly and budding, NP binds to VP24 and possibly host STAU1 (PubMed:28794491, PubMed:30301857).


Viral_family: Filoviridae
Species: Zaire ebolavirus
Name: VP30
UniProtID_Ref: Q05323
UniProt_Name_Ref: VP30_EBOZM
Binding_ligand: ssRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 5DVW, 5T3T
Reporter_assay: D(18829754, 27279615, 9971816)
EMSA: D(27279615)
Other_assays: D(20421407)
Human_infection_evidence: 20957152.0
Aliases:
Ebola VP30, eVP30, Hexameric zinc-finger protein VP30, Minor nucleoprotein VP30, Transcription activator VP30

UniProt_IDs_Orthologs:
A0A0A7P6S7,A0A0D4D8P9,A0A0D5W867,A0A0D5W881,A0A0D5W8K4,A0A0D5W8L5,A0A0D5W8P3,A0A0D5W8Q0,A0A0D5W8S4,A0A0D5W9G0,A0A0E3TKV3,A0A0E3TLF2,A0A0E3TLT1,A0A0E3TNA7,A0A0E3XJ86,A0A0E3XKF2,A0A0E3XL58,A0A0F6PD42,A0A0F6PD98,A0A0F6PDF6,A0A0F6PE67,A0A0F6PGB0,A0A0F7IMJ5,A0A0F7IML9,A0A0F7IMR4,A0A0G2YEA1,A0A0G2YEX8,A0A0G2YGG0,A0A0K1NXF0,A0A0K1NY74,A0A0K1NY97,A0A0K1NYB8,A0A0K1NYX1,A0A0K1NZ17,A0A0N9BE47,A0A0S0G9Y9,A0A0S0H3V9,A0A0S0H5G2,A0A0S0H693,A0A0S0HCI9,A0A0S0HCX3,A0A0U3MQS2,A0A0U3MRQ2,A0A0U3V2Q4,A0A0U3V2T6,A0A0U3V4I1,A0A0U3V9C5,A0A0U3VJZ0,A0A0U4CS06,A0A0U4D596,A0A0U4D5B5,A0A0U4E233,A0A0U4E3T0,A0A0U4E6R5,A0A0U4EJT4,A0A0U4ENB6,A0A0U4F7Q3,A0A144INH8,A0A165Q6Y8,A0A165Q9K2,A0A1L2BIG8,A0A1X9ITK5,A0A1X9IWG5,A0A2I4PDJ3,A0A2I4PEA3,A0A2I4Q549,A0A2I4Q575,A0A3G2LMC4,A0A3Q8HH29,A0A3Q8HQ01,L7QHS4,L7QI14,L7QI23

Functional_annotation:
Multifunctional protein that acts as a viral transcriptional activator. Promotes read-through of an RNA hairpin in the NP open reading frame to enhance viral transcription. Mechanistically, nonphosphorylated VP30 hexamers form a ternary complex with the viral leader RNA. In turn, clamps the RNA template and the complex VP35-polymerase L together, thereby increasing the polymerase affinity for the RNA template to increase transcription initiation despite the presence of RNA secondary structures. Assists also stop-start transcription at gene junctions to promote transcription of downstream genes.


Viral_family: Filoviridae
Species: Zaire ebolavirus
Name: VP35
Aliases: Ebola VP35, eVP35, Polymerase cofactor VP35
UniProtID_Ref: Q05127
UniProt_Name_Ref: VP35_EBOZM
Binding_ligand: dsRNA
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Reporter_assay: D(9971816, 11027311, 12829834, 19557165)
EMSA: I(27642076)
Other_assays: D(20421407)
Human_infection_evidence: 20957152.0
UniProt_IDs_Orthologs:
A0A096YGW9,A0A0A0UG55,A0A0A7P6T2,A0A0D4D9D7,A0A0D5W860,A0A0D5W888,A0A0D5W8A6,A0A0D5W8D3,A0A0D5W8F8,A0A0D5W8I0,A0A0D5W8K1,A0A0D5W8L0,A0A0D5W8L3,A0A0D5W8P1,A0A0D5W8P9,A0A0D5W8S0,A0A0D5W8Y3,A0A0D5W907,A0A0D5W910,A0A0D5W932,A0A0D5W967,A0A0D5W9C3,A0A0D5W9F6,A0A0E3JNL8,A0A0E3TL62,A0A0E3TLJ9,A0A0E3TLL9,A0A0E3TN58,A0A0E3TND3,A0A0E3TP51,A0A0E3XJ79,A0A0E3XL17,A0A0E3XLC2,A0A0F6PCZ9,A0A0F6PD95,A0A0F6PDS1,A0A0F6PDT0,A0A0F6PE53,A0A0F6PEA2,A0A0F6PEB0,A0A0F6PEX9,A0A0F6PG67,A0A0F6PGM5,A0A0F6PGU9,A0A0F6PH54,A0A0F7IM75,A0A0F7IMK4,A0A0G2YA07,A0A0G2YB97,A0A0G2YCE4,A0A0G2YCW0,A0A0G2YD36,A0A0G2YFC9,A0A0G2YGH5,A0A0G2YGK9,A0A0G2YGN0,A0A0G2YH23,A0A0G2YI78,A0A0G2YIT8,A0A0K1NXW9,A0A0K1NY24,A0A0K1NY41,A0A0K1NY91,A0A0K1NY92,A0A0K1NYD4,A0A0K1NYD6,A0A0K1NYW6,A0A0K1NZ58,A0A0K1NZE7,A0A0N7E4U0,A0A0N7E4U2,A0A0S0GA68,A0A0S0GBT2,A0A0S0GCF5,A0A0S0H1F0,A0A0S0H2X8,A0A0S0H3D9,A0A0S0H3X8,A0A0S0H3Y5,A0A0S0H453,A0A0S0H4A9,A0A0S0H4M9,A0A0S0H4P4,A0A0S0H6B4,A0A0S0HAT4,A0A0S0HBA9,A0A0S0HCX5,A0A0S0HDX3,A0A0S0HEE4,A0A0S0HEH4,A0A0U3MI82,A0A0U3MLC1,A0A0U4D7K3,A0A0U4DBV4,A0A0U4E017,A0A0U4E4W0,A0A0U4EJL2,A0A0U4EJR8,A0A0U4EPG5,A0A0U4FDH1,A0A141LKX3,A0A165Q6T7,A0A165Q7K3,A0A172QC54,A0A172QC60,A0A1L2BI43,A0A1L2BIB3,A0A1L2BIE6,A0A1L7B886,A0A1L7B8N5,A0A2I4PDK5,A0A2I4PEH1,A0A2I4PEM7,A0A2I4SAM2,A0A2I4SAS7,A0A2I4SAT1,A0A2U9QPQ6,A0A345K436,A0A3G2LLZ4,A0A3G2LM16,A0A3G2XDA3,A0A3G2XDB5,A0A3G2XDD1,A0A3G2XDD3,A0A3G2XDY9,A0A3G2XGG3,A9QPL7,I0DHA7,L7QI13,L7QI22,L7QI35,V9TIA7

Structure_PDB_ID:
3FKE, 3L25, 3L26, 3L27, 3L28, 3L29, 4IBB, 4IBC, 4IBD, 4IBE, 4IBF, 4IBG, 4IBI, 4IBJ, 4IBK, 4IJE, 4IJF, 4YPI, 4ZTA, 4ZTG, 4ZTI, 6GBO, 6GBP

Functional_annotation:
Plays an essential role in viral RNA synthesis and also a role in suppressing innate immune signaling. Acts as a polymerase cofactor in the RNA polymerase transcription and replication complexes. Serves as nucleoprotein/NP monomer chaperone prior to the formation of the large oligomeric RNA-bound complexes. Prevents establishment of cellular antiviral state, thereby suppressing host DC maturation (PubMed:26962215). Acts by inhibiting host DDX58/RIG-I activation both by shielding dsRNA from detection and by preventing PRKRA binding to DDX58 (PubMed:23870315). Blocks virus-induced phosphorylation and activation of interferon regulatory factor 3/IRF3, a transcription factor critical for the induction of interferons alpha and beta. This blockage is produced through the interaction with and inhibition of host IKBKE and TBK1, producing a strong inhibition of the phosphorylation and activation of IRF3. Also inhibits the antiviral effect mediated by the host interferon-induced, double-stranded RNA-activated protein kinase EIF2AK2/PKR (PubMed:17065211).


Viral_family: Flaviviridae
Species: Hepatitis C virus
Name: Genome polyprotein
Aliases: Cleaved into the following 11 chains-Core protein p21
UniProtID_Ref: P27958
UniProt_Name_Ref: POLG_HCVH
Binding_ligand: dsRNA
Function: TR, NAP, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 1A1R, 1A1V, 1CWX, 1HEI, 1JR6, 1N1L
Reporter_assay: D(10544138)
EMSA: D(10924497)
Other_assays: D(10544138)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A1X9Q776,A0A1X9Q782,A0A1X9Q784,A0A1X9Q787,A0A1X9Q788,A0A1X9Q790,A0A1X9Q798,A0A1X9Q7A4,A0A1X9Q7A5,A0A1X9Q7A7,A0A1X9Q7A8,A0A1X9Q7B3,A0A1X9Q7B5,A0A1X9Q7B6,A0A1X9Q7F9,A0A1X9Q7G7,A0A1X9Q7G8,A0A1X9Q7H0,A0A1X9Q7H1,A0A1X9Q7H2,A0A1X9Q7H4,A0A1X9Q7H6,A0A1X9Q7I0,A0A1X9Q7I2,A0A1X9Q7I6,A0A1X9Q7I8,A0A1X9Q7M9,A0A1X9Q7N5,A0A1X9Q7P0,A0A1X9Q7P4,A0A1X9Q7P8,A0A1X9Q7T5,A0A1X9Q809,A0A1X9Q843,A0A1X9Q844,A0A1X9Q845,A0A1X9Q860,A0A1X9Q868,A6N8C5,A8DEQ3,A8DER9,A8DES5,A8DF52,A8DF65,A8DF80,A8DF92,A8DFA3,A8DFB2,A8DFB8,A8DFC4,A8DFD0,A8DFD6,A8DFE3,A8DFF0,A8DFF3,A8DFF5,A8DFG4,A8DFP3,A8DFQ2,A8DFR2,A8DFS1,A8DFT0,A8DFT8,A8DFU5,A8DFV3,A8DFW2,A8DFW9,A8DFX7,A8DFY4,A8DFY6,A8DFZ1,A8DG21,A8DG30,A8DG50,A8DG59,A8DG69,A8DG81,A8DG88,A8DG98,A8DGA7,A8DGB7,A8DGC9,A8DGD8,A8DGF9,A8DGH0,A8DGI0,A8DGN1,A8DGP0,A8DGP9,A8DGQ7,A8DGR6,A8DGS6,A8DGV7,A8DGW5,A8DGX1,A8DGX9,A8DH64,A8DH72,A8DH77,A8DH84,A8DH90,A8DH96,A8DHA2,A8DHB9,A8DHE5,A8DHE9,A8DHF6,A8DHH1,A8DHV8,A8DHW9,A8QIN1,A8QIN2,A8QIN3,A8QIN4,A8QIN5,A8QIN7,A8QIN8,A8QIP8,A8WE32,A8WE34,A8WE36,A8WEV8,A8WFA4,A8WFA6,A9LLG7,A9LLH0,A9LLH2,B1PPI0,B1PPI5,B1PPI7,B1PPI9,B1PPJ1,B1PPJ3,B1PPJ6,B1PPJ8,B1PPK0,B1PPK2,B1PPK6,B1PPL0,B1PPL2,B1PPL5,B1PPL7,B1PPL9,B1PPM3,B1PPM5,B1PPM9,B1PPN4,B1PPN6,B1PPN8,B1PPP0,B1PPP2,B1PPP4,B1PPP6,B1PPP8,B1PPQ0,B1PPQ2,B1PPQ4,B1PPQ8,B1PPR2,B1PPR5,B1PPS1,B1PPS4,B1PPT0,B2CNA8,B2CNB0,B2CNB4,B2CNB6,B2CNB8,B2D1G7,B2D1G9,B2LXT0,B2ZGC3,B2ZGC5,B2ZTK5,B2ZTK7,B2ZTK9,B3TKD8,B3TKE0,B3TKE4,B3TKE6,B3TKE8,B3TKF0,B3TKF2,B3TKF4,B3TKF8,B3TKG0,B3TKG2,B3TKG4,B3TKG6,B3TKG8,B3TKH2,B3TKH4,B3TKH6,B3TKI6,B3TKI8,B3TKJ4,B3TKJ5,B3TKJ7,B3TKJ9,B3TKK3,B3TKK5,B3TKK7,B3TKK9,B3TKL1,B3TKL3,B3TKL5,B3TKL7,B3TKM0,B3TKM2,B3TKM4,B3TKM6,B3TKM8,B3TKN0,B3TKN2,B3TKN4,B3TKN6,B3TKN8,B3TKP0,B3TKP2,B3TKP3,B3TKP5,B3TKP7,B3TKP9,B3TKQ1,B3TKQ3,B3TKQ5,B3TKQ7,B3TKQ9,B3TKR1,B3TKR7,B3TKR9,B3TKS1,B3TKS5,B3TKS7,B3TKS8,B3TKT0,B3TKT2,B3TKT6,B3TKT8,B3TKU0,B3TKU2,B3TKU4,B3TKU6,B3TKU8,B3TKV0,B3TKV2,B3TKV4,B3TKV6,B3TKV8,B3TKW0,B3TKW2,B3TKW4,B3TKW6,B3TKW8,B3TKX0,B3TKX2,B3TKX4,B3TKX6,B3TKX8,B3TKY0,B3TKY2,B3TKY4,B3TKY6,B3TKY8,B3TKZ0,B3TKZ2,B3TKZ4,B3TKZ6,B3TKZ8,B3TL00,B3TL02,B3TL05,B3TL07,B3TL10,B3TL12,B3TL14,B3TL16,B3TL18,B3TL20,B3TL22,B3TL27,B3TL29,B3TL31,B3TL33,B3TL36,B3TL43,B3TL49,B3TL51,B3TL53,B3TL56,B3TL69,B3TL71,B3TL79,B3TL81,B3TL83,B3TL85,B3TL93,B3TL95,B5M916,B5M920,B5M922,B5M925,B5M928,B5M930,B5M932,B5TBA9,B5TBB2,B5TBB4,B5U654,B5U658,B5U6M7,B5U6M9,B5U6N1,B6VGD0,B6VGD2,B6VGD7,B6VJ19,C4MR37,C4MR38,C4MR39,C4MR40,C4MR41,C4MR42,C4MR43,C4MR44,C4MR45,C4MR46,C4MR47,C4MR49,C4MR50,C4MR51,C4MR52,C4MR53,C4MR54,C4MR55,C4MR56,C4MR57,C4MR58,C4MR59,C4MR60,C4MR61,C4MR62,C4MR63,C4MR64,C4MR65,C4MR66,C4MR67,C4MR68,C4MR69,C4MR70,C4MR71,C4MR72,C4MR73,C4MR74,C4MR75,C4MR76,C4MR77,C4MR78,C4MR79,C4MR80,C4MR81,C4MR82,C4MR83,C4MR84,C4MR85,C4MR86,C4MR87,C4MR88,C4MR89,C4MR90,C4MR91,C4MR92,C4MR93,C4MR94,C4MR95,C4MR97,C4MR99,C4MRA0,C4MRA1,C4MRA2,C4MRA3,C4MRA4,C4MRA5,C4MRA6,C4MRA7,C4MRA8,C4MRA9,C4MRB0,C4MRB1,C4MRB2,C4MRB3,C4MRB4,C7G539,D2CVL5,H6TCE5,H6TCE7,H6TCE8,H6TCE9,H6TCF0,H6TCF1,Q03463,Q9ELS8,S4UXY5,S4UXY7,S4UXY9,S4UXZ3,S4UXZ6,S4UXZ8,S4UXZ9,S4UY00,S4UY01,S4UY02,S4UY03,S4UY04,S4UY05,S4UY06,S4UY08,S4UY10,S4UY14,S4UY17,S4UY19,S4UYB5,S4UYB9,S4UYC1,S4UYC2,S4UYC4,S4UYC6,S4UYC7,S4UYC8,S4UYD0,S4UYD2,S4UYD4,S4UYD5,S4UYD7,S4UYE1,S4UYE2,S4UYE4,S4UYE5,S4UYE9,S4UYF0,S4UYF1,S4UYQ2,S4UYQ7,S4UYQ9,S4UYR2,S4UYR5,S4UYR9,S4UYS2,S4UYS4,S4UYS6,S4UYS8,S4UYT0,S4UYT1,S4UYT2,S4UYT4,S4UYT5,S4UYT6,S4UYT8,S4UZ41,S4UZ44,S4UZ47,S4UZ50,S4UZ54,S4UZ58,S4UZ60,S4UZ61,S4UZ62,S4UZ63,S4UZ64,S4UZ67,S4UZ68,S4UZ69,S4UZ71,S4UZ73,S4UZ76,S4UZ78,S4UZ79,S4UZG4,S4UZG5,S4UZG6,S4UZG7,S4UZG9,S4UZH0,S4UZH2,S4UZH3,S4UZH5,S4UZH6,S4UZH7,S4UZH9,S4UZI0,S4UZI1,S4UZI2,S4UZI3,S4UZI4,S4UZI5,S4UZI6

Functional_annotation:
Core protein p21: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding. Modulates viral translation initiation by interacting with HCV IRES and 40S ribosomal subunit. Also regulates many host cellular functions such as signaling pathways and apoptosis. Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by inducing human STAT1 degradation (PubMed:23799612). Interacts with, and activates STAT3 leading to cellular transformation. Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation. Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NK-kappaB activation, and activates AP-1. Enhances TRAIL mediated apoptosis, suggesting that it might play a role in immune-mediated liver cell injury. Seric core protein is able to bind C1QR1 at the T-cell surface, resulting in down-regulation of T-lymphocytes proliferation (PubMed:11086025). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage. Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:14602201). Envelope glycoprotein E1: Forms a heterodimer with envelope glycoprotein E2 that mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to host LDLR, CD81 and SCARB1/SR-BI receptors (PubMed:12615904). However, additional liver specific cofactors may be required for entry. The fusion function is carried by E1 (PubMed:14990718, PubMed:15371595, PubMed:16894197, PubMed:16533059). Envelope glycoprotein E2: Forms a heterodimer with envelope glycoprotein E1 that mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane. E1/E2 heterodimer binds to host LDLR, CD81 and SCARB1/SR-BI receptors (PubMed:12615904), but additional liver specific cofactors may be required for entry. E2 inhibits human EIF2AK2/PKR activation, preventing the establishment of an antiviral state. E2 is a viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses. These interactions allow capture of circulating HCV particles by these cells and subsequent transmission to permissive cells. DCs act as sentinels in various tissues where they entrap pathogens and convey them to local lymphoid tissue or lymph node for establishment of immunity. Capture of circulating HCV particles by these SIGN+ cells may facilitate virus infection of proximal hepatocytes and lymphocyte subpopulations and may be essential for the establishment of persistent infection. Viroporin p7: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. Targets also host mitochondria and induces mitochondrial depolarization (PubMed:29039530). In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. In addition of its role as a viroporin, acts as a lipid raft adhesion factor (PubMed:27320856). Protease NS2-3: Cysteine protease responsible for the autocatalytic cleavage of NS2-NS3. Seems to undergo self-inactivation following maturation. Serine protease NS3: Displays three enzymatic activities: a serine protease with a chymotrypsin-like fold, a NTPase and a RNA helicase. NS3 serine protease, in association with NS4A, is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and NS5A-NS5B (PubMed:8189513). NS3/NS4A complex also prevents phosphorylation of host IRF3, thus preventing the establishment of dsRNA induced antiviral state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' direction, and likely RNA stable secondary structure in the template strand. Cleaves and inhibits the host antiviral protein MAVS (PubMed:16301520). Non-structural protein 4A: Peptide cofactor which forms a non-covalent complex with the N-terminal of NS3 serine protease. Non-structural protein 4B: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex. This membrane alteration gives rise to the so-called ER-derived membranous web that contains the replication complex. NS4B polymerization or in protein-protein interactions activity may contribute to its function in membranous web formation (PubMed:23868571). Plays also a role in the inhibition of host innate response by inhibiting host TLR3-mediated interferon signaling. Mechanistically, promotes host TRIF protein degradation in a caspase8-dependent manner (PubMed:29782532). Non-structural protein 5A: Component of the replication complex involved in RNA-binding. Its interaction with host VAPB may target the viral replication complex to vesicles. Down-regulates viral IRES translation initiation. Mediates interferon resistance, presumably by interacting with and inhibiting human EIF2AK2/PKR. The hyperphosphorylated form of NS5A is an inhibitor of viral replication. RNA-directed RNA polymerase: Plays an essential role in the virus replication.


Viral_family: Hepadnaviridae
Species: Hepatitis B virus
Name: HBx
Aliases: Peptide X, Protein X, Px, X
UniProtID_Ref: P0C686
UniProt_Name_Ref: X_HBVC1
Binding_ligand: dsDNA
Function: TR, Other
Primary_secondary_vTR: P
ChIP: D(27302019)
ChIP_seq: D(28212627, 29933745)
Structure_PDB_ID: N
Reporter_assay: D(11604508, 28102638)
EMSA: D(11604508)
Other_assays: D(1602534)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A060A215,A0A060A625,A0A060A691,A0A060A6W8,A0A060AAM5,A0A060AB18,A0A060AB60,A0A060CJH4,A0A060CNF3,A0A060CP25,A0A067YSC9,A0A067YSG3,A0A067YST1,A0A067YSX0,A0A067YSZ4,A0A067YTH8,A0A067YTM9,A0A067YTS0,A0A067YU08,A0A067YU73,A0A067YUA7,A0A067YUE2,A0A067YUG9,A0A067YUJ1,A0A067YUP6,A0A067YUR5,A0A067YUT6,A0A067YUT9,A0A067YUW7,A0A067YV23,A0A067YV25,A0A067YV34,A0A067YV61,A0A067YVH3,A0A067YVP5,A0A067YVT2,A0A067YVV0,A0A067YVW2,A0A067YVX6,A0A067YWL3,A0A067YWN2,A0A067YWQ7,A0A067YWT4,A0A067YWU4,A0A067YWV9,A0A067YWX6,A0A067YWZ6,A0A067YX24,A0A067YXB4,A0A067YXH9,A0A067YXU2,A0A067YY49,A0A067YYA1,A0A075D8X9,A0A075D922,A0A075D983,A0A075D9Y3,A0A075DA09,A0A075DA55,A0A075DA67,A0A075DA80,A0A075DAP3,A0A075DAT4,A0A075DAW9,A0A075DAZ2,A0A075DB43,A0A075DBT5,A0A075DBU1,A0A075T6J6,A0A077EQB3,A0A0A0V835,A0A0A0V8W4,A0A0G2QWQ5,A0A0G2QWY8,A0A0G3EXJ8,A0A0G3EYX8,A0A0G3EZ59,A0A0G3EZQ6,A0A0G3F0M2,A0A0G3F1C1,A0A0G3F1E9,A0A0G3F1V7,A0A0G3F256,A0A0G3F2A3,A0A0G3F2V3,A0A0G3F2W2,A0A0G3F311,A0A0G3F376,A0A0G3F3N8,A0A0G3F4D1,A0A0G3F4Y2,A0A0G3F549,A0A0G3F559,A0A0G3F5R7,A0A0G3F666,A0A0G3F6R7,A0A0K0K6H8,A0A0K0K6I8,A0A0K0K6J9,A0A0K0K6M2,A0A0K0K6M5,A0A0K0K6N2,A0A0K0K6R4,A0A0K0WRU8,A0A0K0WZ59,A0A0S1RTH5,A0A0U3LF26,A0A1B1LVD7,A0A1B3SNS0,A0A1W5XAX3,A0A249JRC5,A0A286QXF4,A0A290G3R8,A0A290G413,A0A2H4NKA4,A0A2H4NKH4,A0A2H4NL94,A0A2H4NLA4,A0A2H4NLA6,A0A2H4NLF6,A0A2H4NLF8,A0A2H4NLH4,A0A2H4NLL5,A0A2H4NLM7,A0A2H4NLP1,A0A2H4NM06,A0A2H4NM11,A0A2H4NM90,A0A2H4NMB6,A0A2H4NMD0,A0A2H4NMS1,A0A2H4NN58,A0A2H4NNA6,A0A2H4NNB2,A0A2H4NNE7,A0A2H4NNG5,A0A2H4NNI4,A0A2Z6DS46,A0A346RSZ9,A0A346RT27,A0A346RT31,A0A346RT35,A0A346RT39,A0A346RT99,A0A3Q9HHF8,A0A3S5ICN4,A0FDK1,A5GZG6,A5GZH1,A5GZI2,A5GZJ0,A5GZK1,A5GZK9,A5GZL6,A5GZN2,A5GZN6,A5HKP8,A5HKQ4,A5LG64,A5LG76,A5LG84,A5LG92,A5LGB6,A6MG24,A6MG36,A7M682,A7M686,A8J461,A8J478,A8J5I3,A8R7F4,B0FCC1,B0FD21,B0FD41,B0FD94,B1B5L8,B1Q2W8,B2CY06,B2CY33,B2CZW0,B2LWA4,B2LWD7,B3V3R9,B4YT99,B5A2H5,B5ASU1,B5ASW3,B5B482,B5B494,B5B4B1,B5B4C4,B5B4G1,B5B4H9,B5B4J0,B5B4J7,B5B4P8,B5BPH9,B5BPK7,B5BPN1,B5BPR3,B5BPS1,B5BPT6,B5BPU0,B5BPU4,B5BPV6,B5BPW5,B5BPX6,B5BPY8,B5M520,B5M573,B5M576,B5M582,B5M5A9,B5M5B2,B5M5J9,B5M5K2,B5M5K6,B5M5L7,B5M5P4,B5M5V6,B5M5V9,B5M5X4,B5TXI5,B5TXK2,B5TXL1,B5TY06,B5TY09,B6EUP5,B7TTN0,B7TU29,B7TU66,B7TUB0,B7TUB9,B7TUE5,B7TUW8,B9VK29,B9VK45,B9VKC0,B9VKD1,B9VKG2,B9VKK5,B9VKP0,B9VKQ5,B9VKY1,B9VL15,B9VL31,B9VL35,C0SVX4,C0SVX6,C1K177,C1K1B6,C1K1C8,C1K1G7,C1K1K6,C1K1N4,C1K1Z2,C1K1Z8,C1K220,C5WK20,C5WK24,C5WK28,C7G2Z1,D0E579,D0E590,D0E5A5,D0E5B5,D0E5D1,D0E5F5,D0E5G7,D0E5I4,D0E5K5,D0E5P0,D0E5Q1,D0E5W6,D0E5X0,D0E643,D0E677,D0E684,D0E696,D0E6A4,D0E6A8,D0ESR9,D0UDN6,D0UDP1,D0UDQ6,D0UDR1,D0UDT1,D0UDT6,D0UDX9,D0UDY9,D0UE09,D0UE46,D0UE60,D0UE84,D0UE93,D0UE97,D0UEA9,D0VXG7,D2CGU5,D2JMN8,D2JMT5,D3Y5S0,D6QVP4,D8VB84,D9U5A9,D9U5H4,E5RD27,E5RD43,E5RD55,F5C7K1,F5C7K8,F5C7Q7,G1EIE8,G1EIF2,G1EIF4,G1EIF8,G1EIG3,G3XGU2,G3XGU6,G3XLB5,G4XMC5,G4XMG5,G9HVE4,G9HZX0,G9HZX1,G9HZX2,G9HZX4,G9HZX5,G9HZY5,G9HZY7,G9HZZ2,G9HZZ9,G9I018,G9I019,G9I021,G9M9Q7,H1ACW6,H1ACY2,H1AE16,H1AE19,H1AE20,H1AE26,H1AE33,H1AE34,H1AE40,H1AE44,H1AE49,H1AE50,H1AE52,H1AE53,H1AE59,H1AE61,H1AE66,H1AE68,H1AE74,H1AE78,H1AE79,H2ERA7,H3K3E8,H3K3L8,I0DH59,I0DH70,I0DH71,I0DH81,I0DH84,I0DH85,I0DH87,I0DH90,I3RTG2,I6XQK3,I6YLZ5,I6YM12,J7IFV6,J7INA2,K0F4R2,K0F4Y6,K0FBC6,K0FBH3,K0FCI9,K0FGT3,K4N0Z4,K4N2P0,K4N2U9,K7QG64,K7QGH7,K7QGZ9,K7QH35,L0HAK4,L0HBS8,O42033,O42065,O91520,O91550,P12936,Q04288,Q06AN6,Q0PVA4,Q1XHE0,Q2EIE9,Q2V2L4,Q3V642,Q4FD63,Q4FD75,Q4FDH3,Q58W10,Q5DW04,Q5KR13,Q5KR29,Q5KR37,Q5KR41,Q5R2M1,Q5R2N7,Q5SDK3,Q5SDK7,Q5SDL4,Q69027,Q7TDA7,Q7TDA8,Q7TDA9,Q805R6,Q80GZ0,Q80IS2,Q80JB9,Q80JC0,Q80JC1,Q80JC2,Q80JC8,Q80MQ6,Q80MR2,Q81109,Q81133,Q8BCI3,Q8JVC7,Q8JXA9,Q8QY54,Q8V1I7,Q8V1J3,Q8V1M6,Q910W8,Q91IN9,Q91IP3,Q91R65,Q91S91,Q99HU6,Q99HV1,Q9DH55,Q9DKR3,Q9DKR4,Q9DKS7,Q9E935,Q9PX27,Q9PX52,Q9QMJ9,Q9QMK2,Q9QN50,Q9WMC0,Q9YZR0,Q9YZR1,Q9YZR6,Q9YZS5,Q9YZT6,Q9YZU4,Q9YZU7,Q9YZU9,Q9YZV1,S4WC30,S4WD77,S4WEV9,S4WIB4,S4WIH4,T1YVH2,V5LDL0,V9P3T8,V9P494,W8E0P8,X4YQZ5,X4YR22,X4YRB2,X4YSM4,X4YXY3,X4YY13,X4YY84,X4YYT9,X4YZ76,X4YZQ5,X4YZY0,X4Z047,X4Z061,X4Z170,X4Z1A9,X4ZCP4,X4ZCY8,X4ZE40,X4ZEJ8,X4ZEL4,X4ZEN0,X4ZES8,X4ZFE0,X4ZFX8

Functional_annotation:
Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT.


Viral_family: Herpesviridae
Species: Cercopithecine alphaherpesvirus 2
Name: RL2
Aliases: Immediate early protein ICP0
UniProtID_Ref: Q5Y0P4
UniProt_Name_Ref: Q5Y0P4_9ALPH
Binding_ligand: dsDNA
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(18539148, 15494213, 2552142, 2820720, 20686034)
EMSA: I(15494213)
Other_assays: I(6098466; 25497088)
Human_infection_evidence: 12603998.0
Notes: ICP0 homolog
Functional_annotation:
Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells. Interestingly, the E3 ubiquitin ligase activity associated with the RING finger domain does not seem to be directly required to inhibit the activation of IRF3 but instead plays a critical role in modulating the cellular localization of ICP0. Upon reactivation of latent genome, suppresses the silencing of viral DNA by dissociating either HDAC1 or HDAC2 from the HDAC-RCOR1-REST-KDM1A complex localized at the ND10 structures and causes their dispersal. Two cellular histone ubiquitin ligases RNF8 and RNF168 are also targeted by ICP0 for degradation, leading to a loss of ubiquitinated forms of H2A, a relief of transcriptional repression, and the activation of latent viral genomes. Enhances the localization of host CCND3 to ND10 bodies that serve as precursors of replication compartments to enable efficient viral replication. Like many RING-finger E3 ubiquitin ligases, ICP0 can induce its own ubiquitination, an activity that promotes its instability due to its targeting to the 26S proteasome for degradation. ICP0 restricts this process by recruiting the cellular ubiquitin-specific protease USP7 that cleaves the anchored ubiquitin chains from ICP0, thereby promoting its stabilization.


Viral_family: Herpesviridae
Species: Cercopithecine alphaherpesvirus 2
Name: UL29
Aliases: DBP, Major DNA-binding protein, Single-strand DNA-binding protein
UniProtID_Ref: Q5Y0S3
UniProt_Name_Ref: Q5Y0S3_9ALPH
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(20585571)
EMSA: I(26676794, 30598436)
Other_assays: I(2987527)
Human_infection_evidence: 12603998.0
Functional_annotation:
Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.


Viral_family: Herpesviridae
Species: Cercopithecine alphaherpesvirus 2
Name: US1
Aliases: Immediate early protein ICP22, Regulatory protein ICP22
UniProtID_Ref: Q5Y0P2
UniProt_Name_Ref: Q5Y0P2_9ALPH
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(25233083, 23029222)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(25712217, 30863402)
EMSA: N
Other_assays: I(25712217)
Human_infection_evidence: 12603998.0
Functional_annotation:
Functions as a general transcriptional regulator of cellular and viral mRNAs mainly by mediating changes on the host RNA polymerase II. One change, which is UL13 independent, is the rapid loss of Pol II forms bearing Ser-2 phosphorylation. A second change, which is UL13 dependent, is the appearance of an intermediate form of Pol II that differs from the normal hypo- and hyperphosphorylated forms. These Pol II modifications immediately inhibit host genome transcription, leading to cell cycle deregulation and loss of efficient antiviral response.


Viral_family: Herpesviridae
Species: Cercopithecine herpesvirus 1
Name: RS1
Aliases: ICP4, Immediate early protein ICP4
UniProtID_Ref: Q7T401
UniProt_Name_Ref: Q7T401_CHV1
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: I(26984403)
ChIP_seq: I(28611249)
Structure_PDB_ID: N
Reporter_assay: I(26984403)
EMSA: I(22496239, 26984403)
Other_assays: I(28505309)
Human_infection_evidence: 12603998.0
Functional_annotation: positive regulation of transcription, DNA-templated,host cell nucleus
UniProt_IDs_Orthologs:
A0A059WI86,A0A1X9WFW5,A0A1X9WG45,A0A1X9WG88,A0A1X9WG94,A0A1X9WHE3,A0A1X9WI28,A0A1X9WIB5,A0A1X9WIH6,A0A1X9WIL9,A0A1X9WIS4


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: ICP0
UniProtID_Ref: P08393
UniProt_Name_Ref: ICP0_HHV11
Binding_ligand: dsDNA
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 5C56
Reporter_assay: D(18539148, 15494213, 2552142, 2820720, 20686034)
EMSA: D(15494213)
Other_assays: D(6098466; 25497088)
Human_infection_evidence: Fields Virology
Aliases:
Alpha-0 protein, E3 ubiquitin-protein ligase ICP0, IE110, Immediate-early protein IE110, RING-type E3 ubiquitin transferase ICP0, Trans-acting transcriptional protein ICP0, Trans-acting transcriptional protein ICP0 , VMW110

UniProt_IDs_Orthologs:
A0A0F6TMA8,A0A0F7CWV0,A0A0F7CX66,A0A0F7CXM5,A0A0F7CXT2,A0A0F7CXW1,A0A0F7CY33,A0A0F7CY77,A0A0F7CYD5,A0A0F7GQZ5,A0A0F7GR62,A0A0F7GRM9,A0A0F7GS15,A0A0F7GSK5,A0A0F7GSQ3,A0A0F7GT05,A0A0F7GTF5,A0A0F7GTH7,A0A0F7GTR3,A0A0F7GU10,A0A0F7GU88,A0A0F7GV83,A0A0F7GVF0,A0A0F7GW03,A0A0F7GW86,A0A0F7GX28,A0A0F7GXE2,A0A0F7MZW1,A0A0S1TJG0,A0A0S1TJU7,A0A0S1TL48,A0A0S2I6L3,A0A181ZG35,A0A181ZG46,A0A193GSD7,A0A193GSS8,A0A193GT95,A0A193GTE7,A0A193GTH4,A0A193GTN4,A0A193GTW0,A0A193GTW3,A0A193GU35,A0A193GUI9,A0A193GUJ6,A0A193GUP1,A0A193GUR4,A0A193GUX0,A0A193GV30,A0A193GVR5,A0A193GW67,A0A193GW73,A0A193GWM3,A0A193GWV3,A0A193GXB0,A0A1C3J693,A0A1C3J6C6,A0A1C3J6E2,A0A1C3J6E4,A0A1C3J6N4,A0A1C3J716,A0A1C3J749,A0A1C3J7K9,A0A1C3J7Q4,A0A1C3J7X0,A0A1C3J7Z9,A0A1C3K9E0,A0A1D9CK31,A0A1V0E4Z7,A0A290Y1F5,A0A2U9A3L9,A0A2U9AAR9,A0A2U9ABP7,A0A2U9ABT1,A0A2Z4GZE1,A0A2Z4H0U7,A0A2Z4H1E3,A0A2Z4H1P0,A0A2Z4H1Y3,A0A2Z4H2C8,A0A2Z4H2N9,A0A2Z4H2V1,A0A2Z4H2V5,A0A2Z4H3G6,A0A2Z4H3U3,A0A2Z4H4P0,A0A2Z4H4X5,A0A2Z4H5E2,A0A2Z4H5P4,A0A2Z4H5W9,A0A2Z4H614,A0A2Z4H6U6,A0A2Z4H6Y6,A0A2Z4H8C0,A0A2Z4H9C0,A0A2Z4HAC0,A0A2Z4HAK7,A0A2Z4HAT8,A0A2Z4HAY7,A0A2Z4HBW8,A0A2Z4HBY4,A0A2Z4HCB2,A0A2Z4HCC6,A0A2Z4HE50,A0A2Z4HEE5,A0A2Z4HEQ7,A0A2Z4HFF6,A0A3G1LC33,B9VQC7,D3YPC2,D3YPF7,F8RCI7,F8RCS6,F8RDF7,F8RDN3,F8RE37,F8REB3,F8REI9,F8REZ2,F8RF66,F8RFE3,F8RFX1,F8RG89,G8H5J4,G8H854,G8H8C3,G8H8P9,G8H8X1,G8H8Y7,G8H957,G8HBH2,H9E965,I3TC55,I3TC56,J7GUK9,J7H0H8,Q09I79,U5TMT3

Functional_annotation:
Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells. Interestingly, the E3 ubiquitin ligase activity associated with the RING finger domain does not seem to be directly required to inhibit the activation of IRF3 but instead plays a critical role in modulating the cellular localization of ICP0. Upon reactivation of latent genome, suppresses the silencing of viral DNA by dissociating either HDAC1 or HDAC2 from the HDAC-RCOR1-REST-KDM1A complex localized at the ND10 structures and causes their dispersal. Two cellular histone ubiquitin ligases RNF8 and RNF168 are also targeted by ICP0 for degradation, leading to a loss of ubiquitinated forms of H2A, a relief of transcriptional repression, and the activation of latent viral genomes. Enhances the localization of host CCND3 to ND10 bodies that serve as precursors of replication compartments to enable efficient viral replication. Like many RING-finger E3 ubiquitin ligases, ICP0 can induce its own ubiquitination, an activity that promotes its instability due to its targeting to the 26S proteasome for degradation. ICP0 restricts this process by recruiting the cellular ubiquitin-specific protease USP7 that cleaves the anchored ubiquitin chains from ICP0, thereby promoting its stabilization.


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: RS1
UniProtID_Ref: P08392
UniProt_Name_Ref: ICP4_HHV11
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(26984403)
ChIP_seq: D(28611249)
Structure_PDB_ID: 5MHJ
Reporter_assay: D(26984403; 21998580; 18539148)
EMSA: D(22496239, 26984403; 21998580)
Other_assays: D(28505309)
Human_infection_evidence: Fields Virology
Aliases:
Alpha-4 protein, ICP4, IE175, Infected cell protein 4, Major viral transcription factor ICP4, Major viral transcription factor ICP4 RS1, RS1.2, Transcriptional activator IE175, Transcriptional regulator ICP4

UniProt_IDs_Orthologs:
A0A0B5E5S4,A0A0B5EBZ6,A0A0F6TMP9,A0A0F7CX08,A0A0F7CXB0,A0A0F7CXL0,A0A0F7CY62,A0A0F7GR69,A0A0F7GS44,A0A0F7GVD0,A0A0F7GVQ1,A0A0F7GWJ5,A0A0S1TJ69,A0A0S1TJB1,A0A0X8E9W1,A0A193GSU1,A0A193GT76,A0A193GTA0,A0A193GTY9,A0A193GUC1,A0A193GV99,A0A193GVK4,A0A193GW58,A0A193GWU4,A0A193GX28,A0A193GXR6,A0A1C3J777,A0A1C3J7A4,A0A1C3J7I7,A0A1C3J7R6,A0A1C3J7T6,A0A1C3J7V9,A0A1C3J807,A0A1C3J815,A0A1C3K9I9,A0A1D9CK53,A0A1V0E590,A0A290Y188,A0A290Y1F8,A0A2U9ABK0,A0A2Z4GZD9,A0A2Z4GZG8,A0A2Z4GZN3,A0A2Z4H0A9,A0A2Z4H0B3,A0A2Z4H1V7,A0A2Z4H250,A0A2Z4H2C3,A0A2Z4H2W5,A0A2Z4H2Y6,A0A2Z4H2Z8,A0A2Z4H4F0,A0A2Z4H4K9,A0A2Z4H4P5,A0A2Z4H559,A0A2Z4H5Q1,A0A2Z4H6S2,A0A2Z4H6V6,A0A2Z4H7F9,A0A2Z4H7P9,A0A2Z4H7U3,A0A2Z4H986,A0A2Z4HAX0,A0A2Z4HB37,A0A2Z4HB72,A0A2Z4HBC0,A0A2Z4HBK8,A0A2Z4HBR2,A0A2Z4HCI3,A0A2Z4HCS0,A0A2Z4HCS6,A0A2Z4HDY8,A0A2Z4HEG2,A0A2Z4HEH1,A0A2Z4HEZ5,A0A2Z4HFA5,A0A2Z4HFJ4,A0A2Z4LE53,A0A2Z4LFE8,B9VQC5,D3YPC4,D3YPL8,F8RCC6,F8RCI9,F8RCS9,F8RD83,F8RDF9,F8RDN6,F8RDW3,F8RE39,F8REJ2,F8RER9,F8REZ4,F8RF68,F8RFE5,F8RFL6,F8RG91,F8RGG8,G8H8J2,G8H943,G8HBH4,H9E981,I1UYM4,I3TCD6,J7GV28,Q09I77,U5TQG7

Functional_annotation:
Plays an essential role in the regulation of viral gene expression by both activating and repressing host RNA polymerase II-mediated transcription. Binds with high affinity to the sequence 5'-ATCGTC-3'. Activates transcription by recruiting a form of the host TFIID to promoters and stabilizing the pre-initiation complex formation. Negatively regulates its own transcription. This immediate early (IE) protein is absolutely necessary for the transition from IE transcription to later viral gene transcription.


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: UL29
Aliases: DBP, ICP8, Major DNA-binding protein
UniProtID_Ref: P04296
UniProt_Name_Ref: DNBI_HHV11
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 1URJ
Reporter_assay: I(20585571)
EMSA: D(26676794, 30598436)
Other_assays: D(2987527)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0B5E506,A0A0B5EAK3,A0A0B5ED26,A0A0S1TES2,A0A0S1TIP6,A0A181ZGK5,A0A181ZGT1,A0A181ZHM5,A0A290Y1C7,A0A2U9A559,A0A2U9A5G9,A0A2U9A5R4,A0A2U9A614,A0A2U9A670,A0A2U9A6Q7,A0A2U9A7J1,A0A2U9A994,A0A2U9A9S5,A0A2U9ABP2,A0A2Z2D682,A0A2Z4H192,A0A2Z4H1V4,A0A2Z4H2S6,A0A2Z4H493,A0A2Z4H5K9,A0A2Z4H6I9,A0A2Z4H705,A0A2Z4H7A8,A0A2Z4H7J3,A0A2Z4H8N3,A0A2Z4H9Z2,A0A2Z4HBR6,A0A2Z4HBU1,A0A2Z4HD21,A0A2Z4HED3,A0A2Z4HEQ2,G8H881,G8H8M0,G8H8U2,I3TC88,P17469,P17470,Q2MGU6,Q2MGU7,Q2MGV1

Functional_annotation:
Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: UL48
Aliases: Alpha trans-inducing protein, Alpha-TIF, ICP25, Tegument protein VP16, Vmw65, VP16
UniProtID_Ref: P06492
UniProt_Name_Ref: VP16_HHV11
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(19321615)
ChIP_seq: N
Structure_PDB_ID: 16VP, 2PHE, 2PHG
Reporter_assay: D(2538647)
EMSA: D(11416146, 2538647)
Other_assays: D(11416146)
Human_infection_evidence: Fields Virology
Notes: Binds to DNA with host TFs
UniProt_IDs_Orthologs:
A0A0B5EBV9,A0A0F7GRN8,A0A0X8EA31,A0A109R0Q6,A0A110AV46,A0A110AX28,A0A140GKG8,A0A181ZFV5,A0A181ZGY2,A0A181ZHC6,A0A193GUI5,A0A1C3J6Y6,A0A1C3J7F2,A0A1C3J7F6,A0A1D9CK22,A0A1V0E561,A0A2U9A5R5,A0A2U9A645,A0A2U9A6S4,A0A2U9A847,A0A2U9A8N0,A0A2U9ABI7,A0A2U9AC12,A0A2Z2D2L3,A0A2Z4H418,A0A2Z4H451,A0A2Z4H850,A0A2Z4HC21,A0A2Z4HC83,A0A2Z4HEG6,D3YPB2,D3YPK6,F8RCZ3,F8RDE7,F8REY2,F8RF56,F8RG79,G8H933,G8HBG2,I3TCA8,J7GUJ5,U5TMS3

Functional_annotation:
Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F 1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection.


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: UL54
Aliases: ICP27, Immediate-early protein IE63, Infected cell protein 27, mRNA export factor, VMW63
UniProtID_Ref: P10238
UniProt_Name_Ref: ICP27_HHV11
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 2KT5, 4YXP, 5BQK
Reporter_assay: D(18539148)
EMSA: D(19783816; 1853914)
Other_assays: D(19783816, Yeast three-hybrid analysis, NMR)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A076N1M8,A0A089WX37,A0A181ZFZ5,A0A181ZG53,A0A290Y181,A0A2U9A4C7,A0A2U9A6X5,A0A2U9A8Q3,A0A2U9A975,A0A2U9ABC8,A0A2Z4H1C0,A0A2Z4H2L7,A0A2Z4H3W4,A0A2Z4H4C4,A0A2Z4H541,A0A2Z4H661,A0A2Z4H7A3,A0A2Z4H805,A0A2Z4H871,A0A2Z4H937,A0A2Z4HBG5,A0A2Z4HCG4,A0A2Z4HEX6,A0A2Z4HF86,A0A2Z4HF92,A0A2Z4LF63,G8H8A5,G8H8P6,G8H8W8,G8H940,P36295

Functional_annotation:
Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may indirectly compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways (PubMed:22334672). Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis. Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus.


Viral_family: Herpesviridae
Species: Human herpesvirus 1; Herpes simplex virus 1
Name: US1
Aliases: ICP22, Immediate-early protein IE68, Infected cell protein 22, Transcriptional regulator ICP22
UniProtID_Ref: P04485
UniProt_Name_Ref: ICP22_HHV11
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(25233083, 23029222)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(19535441)
EMSA: N
Other_assays: I(25712217)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A089YQP5,A0A0B5E4A8,A0A0S1TKF2,A0A181ZFQ8,A0A181ZFX4,A0A181ZG17,A0A181ZH58,A0A181ZHB1,A0A181ZHL3,A0A290Y190,A0A2U9A3V9,A0A2U9A473,A0A2U9A612,A0A2U9A653,A0A2U9A738,A0A2U9A8A8,A0A2U9A8H3,A0A2U9A988,A0A2Z4GZP5,A0A2Z4GZY6,A0A2Z4H1M5,A0A2Z4H668,A0A2Z4H8Q8,A0A2Z4H9C8,A0A2Z4HAC1,A0A2Z4HBP6,A0A2Z4HBT9,A0A2Z4HCT0,A0A2Z4HCU3,A0A2Z4HCZ9,A0A2Z4HDW9,A0A2Z4HE75,A0A2Z4HF25,Q09I76

Functional_annotation:
Functions as a general transcriptional regulator of cellular and viral mRNAs mainly by mediating changes on the host RNA polymerase II. One change, which is UL13 independent, is the rapid loss of Pol II forms bearing Ser-2 phosphorylation. A second change, which is UL13 dependent, is the appearance of an intermediate form of Pol II that differs from the normal hypo- and hyperphosphorylated forms. These Pol II modifications immediately inhibit host genome transcription, leading to cell cycle deregulation and loss of efficient antiviral response.


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: RL2
Aliases: E3 ubiquitin-protein ligase ICP0, RING-type E3 ubiquitin transferaseICP0, VMW118 protein
UniProtID_Ref: P28284
UniProt_Name_Ref: ICP0_HHV2H
Binding_ligand: dsDNA
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25712217)
EMSA: I(15494213)
Other_assays: I(20106921, 11333917
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A290D0A4,A0A290DJM1,A0A290DPU6,A0A290DQ85,A0A290DQC7,A0A290Y3R4,A0A290Y3T1,A0A290Y453,A0A290Y4M0,A0A290Y4T0,A0A2U9DUX7,A0A2X0RYZ6,D6PUZ2,D6PUZ3,D6PUZ4,D6PUZ5,D6PUZ6,D6PUZ7,G9I221,G9I280,P89473,W0NW81

Functional_annotation:
Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100. Prevents antiviral response to viral DNA induced by IFI16 by degrading it. Additionally, inhibits host IRF3 nuclear signaling to prevent interferon production by the infected cells.


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: RS1
UniProtID_Ref: P90493
UniProt_Name_Ref: ICP4_HHV2H
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: I(26984403)
ChIP_seq: I(28611249)
Structure_PDB_ID: N
Reporter_assay: D(25712217, 25673716)
EMSA: I(22496239, 26984403)
Other_assays: I(28505309)
Human_infection_evidence: Fields Virology
Aliases:
Alpha-4 protein, ICP4, IE175, Infected cell protein 4, Major viral transcription factor ICP4 homolog, Transcriptional activator IE175

UniProt_IDs_Orthologs:
A0A290DJV7,A0A290DQ87,A0A290DQD8,A0A290Y3U5,A0A290Y4N5,A0A290Y4U9,A0A2H4PJL5,A0A2U9DVR1,A0A2U9DWA7,A0A2X0TFV2,G9I282

Functional_annotation:
Plays an essential role in the regulation of viral gene expression by both activating and repressing host RNA polymerase II-mediated transcription. Binds with high affinity to the sequence 5'-ATCGTC-3'. Activates transcription by recruiting a form of the host TFIID to promoters and stabilizing the pre-initiation complex formation. Negatively regulates its own transcription. This immediate early (IE) protein is absolutely necessary for the transition from IE transcription to later viral gene transcription.


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: UL29
Aliases: DBP, DNA binding protein ICP8, ICP8, Major DNA-binding protein, Single-stranded DNA-binding protein
UniProtID_Ref: P36384
UniProt_Name_Ref: DNBI_HHV2
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(20585571)
EMSA: I(26676794, 30598436)
Other_assays: I(2987527)
Human_infection_evidence: Fields Virology
Notes: Q69101 is inferred from Cercopithecine alphaherpesvirus 2 protein Q5Y0S3
Functional_annotation: Single-stranded DNA-binding protein required for DNA replication.
UniProt_IDs_Orthologs:
A0A0E3U2R9,A0A0E3Y6D1,A0A0Y0R3K0,A0A0Y0RPP0,A0A0Y0RQH2,A0A109R1L2,A0A1D8M9D0,A0A1U9ZCS9,A0A1U9ZD80,A0A1U9ZDS2,A0A1U9ZDY0,A0A1U9ZFU3,A0A1U9ZGK2,A0A1U9ZGZ7,A0A1U9ZHX5,A0A1U9ZJ89,A0A1U9ZJG3,A0A1U9ZK04,A0A1U9ZKU7,A0A1U9ZLW5,A0A1U9ZM30,A0A218KLT5,A0A218KLU4,A0A290D402,A0A290D687,A0A290Y3N1,A0A290Y3X5,A0A290Y4D4,A0A290Y4L1,A0A290Y4Y4,A0A2U9DUT8,A0A2U9DVR8,G9I251,I6U4X4,P89452,Q69101,W0NSF6


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: UL48
Aliases: Transactivating tegument protein VP16, VP16, VP16 protein
UniProtID_Ref: Q69113
UniProt_Name_Ref: Q69113_HHV2
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: I(19321615)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(2538647)
EMSA: I(11416146, 2538647)
Other_assays: I(11416146)
Human_infection_evidence: Fields Virology
Functional_annotation: DNA binding,regulation of transcription, DNA-templated
UniProt_IDs_Orthologs:
A0A0Y0QTX6,A0A0Y0RIG1,A0A0Y0RUC4,A0A109R1E4,A0A120I2I5,A0A1U9ZDH2,A0A1U9ZE81,A0A1U9ZEL1,A0A1U9ZFX0,A0A1U9ZJL0,A0A1U9ZK94,A0A1U9ZKX9,A0A1U9ZLF9,G9I270,I6TLV8


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: UL54
Aliases: ICP27, Immediate-early protein IE63, Infected cell protein 27, mRNA export factor, VMW63
UniProtID_Ref: P28276
UniProt_Name_Ref: ICP27_HHV2H
UniProt_IDs_Orthologs: A0A1D8M9A7,A0A290D5Z7,A0A290DPS4,A0A290Y4K6,A0A2U9DVV4
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR+J84, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25712217)
EMSA: I(19783816)
Other_assays: I(19783816, Yeast three-hybrid analysis, NMR)
Human_infection_evidence: Fields Virology
Notes: ICP27 homolog
Functional_annotation:
Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways. Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis (By similarity). Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus.


Viral_family: Herpesviridae
Species: Human herpesvirus 2; Herpes simplex virus 2
Name: US1
UniProtID_Ref: P89474
UniProt_Name_Ref: ICP22_HHV2H
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(25712217)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25712217, 30863402)
EMSA: N
Other_assays: D(25712217)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0E3U2V3,A0A0Y0R3N1,A0A0Y0RAR6,A0A0Y0RPR1,A0A0Y0RQK2,A0A0Y0RQR5,A0A109R0Y3,A0A110B8A0,A0A1U9ZDA4,A0A1U9ZDI2,A0A1U9ZDV1,A0A1U9ZEP9,A0A1U9ZF54,A0A1U9ZFY2,A0A1U9ZGL3,A0A1U9ZH77,A0A1U9ZH85,A0A1U9ZII6,A0A1U9ZJK5,A0A1U9ZJQ9,A0A1U9ZK70,A0A1U9ZLG9,A0A1U9ZLK1,A0A1U9ZLR4,A0A1U9ZM71,A0A1U9ZMI5,A0A290DCW2,A0A290Y3Z3,A0A290Y411,A0A290Y505,A0A2U9DVE6,A0A2U9DVM7,A0A2U9DX76,A0A2X0SBG7,G9I283


Viral_family: Herpesviridae
Species: Human herpesvirus 3; Varicella-zoster virus
Name: IE61
UniProtID_Ref: Q6QCJ5
UniProt_Name_Ref: Q6QCJ5_HHV3
UniProt_IDs_Orthologs: A0A0F7CWE3,A0A1B1JGJ2,G9IWI5,I7EJ31,Q0Q9A7,Q0Q9Q3,U5NTS2
Binding_ligand: dsDNA (20225013,table1)
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(19457996, 22090112)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: ICP0 homolog
Functional_annotation: ligase activity,metal ion binding
Aliases:
Immediate-early protein 61,E3 ubiquitin-protein ligase IE61, Modulator of cell state and gene expression, ORF61, ORF62-2, Ring-finger protein, Transactivator, Transcription regulator, Ubiquitin E3 ligase ICP0


Viral_family: Herpesviridae
Species: Human herpesvirus 3; Varicella-zoster virus
Name: IE62
Aliases: ICP4, Immediate-early protein 62, Major viral transcription factor ICP4 homolog, ORF62, ORF71
UniProtID_Ref: P09310
UniProt_Name_Ref: ICP4_VZVD
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: I(26984403)
ChIP_seq: I(28611249)
Structure_PDB_ID: N
Reporter_assay: D(20631144, 15936796, 2556848, 21937644, 8230477, 19457996)
EMSA: D(21937644)
Other_assays: I(28505309)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A076N2G9,A0A0F7CV41,A0A0F7CVI7,A0A0F7CW41,A0A0F7GJ31,A0A0F7GL21,A0A0F7GMV1,A0A1B1JEY7,A0A1B1JFB3,A0A1B1JFK7,A0A1B1JG10,A0A1B1JG79,A0A1B1JGD9,A0A1B1JGP6,A0A1B1JGU1,A0A1B1JGX5,A0A3G2KR87,G0ZLH3,I2CNT9,I7EJ42,Q6X674,Q80AB9,Q80AC0,Q80AC2,Q80AC4,Q8AZM1,Q993S8,Q99BU9,Q99BW7,Q9DK02,Q9DWX9,U5NPD5,U5NQ74,U5NQE5,U5NQJ5,U5NR65,U5NRF1,U5NS27,U5NSM0,U5NSM7,U5NTS8,U5NUT7,W5RSN1

Functional_annotation:
Transcriptional transactivator. May interact with and recruit specific components of the general transcription machinery to viral promoters and stabilize their formation for transcription initiation. Negatively regulates its own transcription. This immediate early (EI) protein may be necessary in virion for viral pathogenesis.


Viral_family: Herpesviridae
Species: Human herpesvirus 3; Varicella-zoster virus
Name: IE63
UniProtID_Ref: P09255
UniProt_Name_Ref: ICP22_VZVD
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15843171, 11912195, 1316489, 15936796, 15936796, 21937644, 19457996)
EMSA: N
Other_assays: D(15843171)
Human_infection_evidence: Fields Virology
Aliases:
Immediate-early protein 63, ORF63, ORF70, Transcriptional regulator ICP22 homolog, Transcriptional regulator IE63

UniProt_IDs_Orthologs:
A0A1B1JGF9,A0A1B1JGW2,A0A2Z5BRN6,A0A2Z5BRP5,A0A2Z5BRQ4,A0A2Z5BRQ9,A0A2Z5BRS1,A0A2Z5BRT2,A0A2Z5BSR7,A0A2Z5BSS5,A0A2Z5BTS0,A0A2Z5BTS7,A0A2Z5BUH2,A0A2Z5BUI1,A0A2Z5BUI9,A0A2Z5BUK8,A0A2Z5BUL5,A0A2Z5BV47,A0A2Z5BV56,A0A2Z5BV63,A0A2Z5BWY5,A0A2Z5BWY7,A0A2Z5BX41,A0A2Z5BX44,G3LF46,Q77NN7

Functional_annotation:
Immediate early (EI) protein that functions as a transcriptional regulator of cellular and viral mRNAs mainly by interacting with several general transcription factors thereby disorganizing the preinitiation complex at certain promoters. May additionally help to regulate levels of histones in virus-infected cells by interacting with host ASF1. By inhibiting host transcriptional program, IE63 plays a major role in the ability of VZV to overcome the innate immune response to the virus.


Viral_family: Herpesviridae
Species: Human herpesvirus 3; Varicella-zoster virus
Name: ORF10
UniProtID_Ref: P09265
UniProt_Name_Ref: VP16_VZVD
UniProt_IDs_Orthologs: A0A0F7CW89,A0A1B1JG98,Q2PJ54,Q4JQW5,Q6QCP5
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(19321615)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15522876, 8386275)
EMSA: I(11416146, 2538647)
Other_assays: I(11416146)
Human_infection_evidence: Fields Virology
Aliases:
Alpha trans-inducing protein, Alpha-TIF, ORF10 protein, ORF-10, Tegument protein 10, Tegument protein VP16 homolog, VP16

Functional_annotation:
Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection (By similarity).


Viral_family: Herpesviridae
Species: Human herpesvirus 3; Varicella-zoster virus
Name: ORF4
UniProtID_Ref: Q6QCQ2
UniProt_Name_Ref: Q6QCQ2_HHV3
UniProt_IDs_Orthologs: A0A075X2D8,A0A0F7CVL9,A0A0F7CWE6,A0A1B1JFU7,U5NPR6
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8389935, 9261438, 17634217, 2556848, 19457996)
EMSA: I(19783816)
Other_assays: I(19783816, Yeast three-hybrid analysis, NMR)
Human_infection_evidence: Fields Virology
Notes: ICP27 homolog
Functional_annotation: regulation of transcription, DNA-templated
Aliases:
Gene expression post-transcriptional regulator, ICP27, Multifunctional expression regulator, Post-transcriptional regulator, Post-transcriptional regulator of gene expression, Transactivator, UL54


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: BALF2
Aliases: DBP, Major DNA-binding protein, Major DNA-binding protein,DBP
UniProtID_Ref: P03227
UniProt_Name_Ref: DNBI_EBVB9
Binding_ligand: ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: D(9434720, 8806519)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0C7TMQ4,A0A0C7TUF9,A0A0C7U097,A0A0S2YRG9,A0A0U3K2Q9,A0A0U3TGP5,A0A0U3TMI4,A0A0U3U8D7,A0A120GXZ4,A0A191T7N2,A0A1W7HH80,A0A1W7HHM5,A0A2D1LY71,A0A2D1LYV2,A0A2D1LZI4,A0A2D1M0K1,A0A2D1M0T4,A0A2S1MKR8,A0A2S1MLV4,A0A2S1MNV2,A0A2S1MPZ1,A0A2S1MQH8,A0A2S1MSX2,A0A2S1MUL4,A0A2S1MUV4,A0A2S1MV65,A0A2S1MWF2,A0A2S1MWR1,A0A2S1MX72,A0A2S1MX94,A0A2S1MY55,A0A2S1MYS1,A0A2S1N124,A0A2S1N1E3,A0A2S1N1K4,A0A2S1N246,A0A2S1N3C7,A0A2S1N3Z9,A0A2S1N521,A0A385J8J4,A0A385J8S6,A0A385J9A1,A0A385J9M3,A0A385J9X3,A0A385JAK5,A0A385JAS1,A0A385JAX3,K9UTM4,Q1HVB8,Q3KSN9,R4R989,V5KTZ5


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: BDLF4
Aliases: Uncharacterized protein BDLF4
UniProtID_Ref: P0CK56
UniProt_Name_Ref: UL92_EBVB9
UniProt_IDs_Orthologs: G3CKS0,P0CK57
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: D(25165108)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation:
host cell nucleus;DNA binding;DNA-binding transcription factor activity;protein dimerization activity;sequence-specific DNA binding;modulation by virus of host G0/G1 transition checkpoint;positive regulation of transcription, DNA-templated;regulation of transcription, DNA-templated;release from viral latency;suppression by virus of host IRF7 activity


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: BGLF3
Aliases: Protein BGLF3
UniProtID_Ref: P03220
UniProt_Name_Ref: UL95_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: D(25165108)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation: viral tegument;viral process
UniProt_IDs_Orthologs:
A0A0B6VJ43,A0A0B6VMR4,A0A0C7NU37,A0A0C7SZ89,A0A0C7T510,A0A0C7T6N5,A0A0C7T892,A0A0C7T8Y5,A0A0C7TBC9,A0A1P7TZK4,A0A2D1LY20,A0A2S1MNR9,A0A2S1MR69,A0A2S1MRS3,A0A2S1MRX8,A0A2S1MUP2,A0A2S1MYJ5,A0A2S1N2D8,A0A2S1N2L3,A0A2S1N4W5,A0A385J8Q1,A0A385JAF2,A0A385JAM3,A0A3R5TNR6,A0A3R5U7A5,A0A3R5VQ48,A0A3R5WKF6,A0A3R5WKP5,A0A3R5XW44,A0A3R5YGK7,G3CKR7,K9USY2,Q3KSR4,V5KTY2


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: BMRF1
UniProtID_Ref: P03191
UniProt_Name_Ref: EAD_EBVB9
UniProt_IDs_Orthologs: K9UR48,P0C6Z0
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(31462557)
EMSA: D(31462557)
Other_assays: D(19801550, Nitrocellulose Filter Binding Assay)
Human_infection_evidence: Fields Virology
Aliases:
DNA polymerase processivity factor BMRF1, EA-D, Early antigen protein D, Polymerase accessory subunit

Functional_annotation:
Plays an essential role in the viral lytic DNA replication by acting as the polymerase accessory subunit. Stimulates the viral DNA polymerase activity and appears to function with it as a holoenzyme. Increases the processivity of the viral polymerase, probably by acting as a sliding clamp that prevents dissociation of the polymerase from the active template. In addition, BMRF1 transcriptionally activates the early BHLF1 promoter.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA1
Aliases: BKRF1, EBNA-1, EBV nuclear antigen 1, Epstein-Barr nuclear antigen 1
UniProtID_Ref: P03211
UniProt_Name_Ref: EBNA1_EBVB9
UniProt_IDs_Orthologs: A0A0U3AZS7,A0A2D1LZQ0,Q1HVF7
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: D(20929547)
ChIP_seq: D(20929547, 26468528,29142137)
Reporter_assay: D(10799567)
EMSA: D(20929547, 10799567)
Human_infection_evidence: Fields Virology
Structure_PDB_ID:
1B3T, 1VHI, 1YY6, 2FYY, 2FZ3, 3MV7, 3MV8, 3MV9, 4PRA, 4PRE, 4PRI, 4PRP, 5WMF, 5WUM, 5WUN, 6NPI, 6NPM, 6NPP, 6PW2

Functional_annotation:
Plays an essential role in replication and partitioning of viral genomic DNA during latent viral infection. During this phase, the circular double-stranded viral DNA undergoes replication once per cell cycle and is efficiently partitioned to the daughter cells. EBNA1 activates the initiation of viral DNA replication through binding to specific sites in the viral latent origin of replication, oriP. Additionally, it governs the segregation of viral episomes by mediating their attachment to host cell metaphase chromosomes. Also activates the transcription of several viral latency genes. Finally, it can counteract the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA2
Aliases: BYRF1, EBNA-2, EBV nuclear antigen 2, Epstein-Barr nuclear antigen 2
UniProtID_Ref: P12978
UniProt_Name_Ref: EBNA2_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(26845565, 24068937)
ChIP_seq: D(21746931, 24068937, 26883634)
Structure_PDB_ID: 2MKR, 2N2J, 5HDA
Reporter_assay: D(26845565)
EMSA: D(21710493, 9445037)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A075FCH9,A0A075FCI7,A0A075FDA7,A0A075FDG8,A0A075FFC3,A0A075FFL0,A0A075FFX2,A0A075FGL9,A0A0A8IKS3,A0A0B6VHM4,A0A0C7NTX7,A0A0C7SZP2,A0A0C7T066,A0A0C7T1F2,A0A0C7T2F0,A0A0C7T426,A0A0C7T5P8,A0A0C7T5T4,A0A0C7T687,A0A0C7TCF1,A0A0C7TCX1,A0A0C7TEL7,A0A0C7TI73,A0A0C7TIT1,A0A0C7TKT1,A0A0C7TL19,A0A0C7TLJ0,A0A0C7TMR9,A0A0C7TN88,A0A0C7TNR8,A0A0C7TSE2,A0A0C7TUG9,A0A0C7TV69,A0A0C7TX39,A0A0C7TYV8,A0A0C7TZP5,A0A0C7U0A2,A0A0C7U0N0,A0A0E4D790,A0A0E4HQQ5,A0A0F6QKC9,A0A0S2YQC3,A0A0S2YR23,A0A0U2VT93,A0A0U3J1F9,A0A0U3J5M7,A0A0U3K2E3,A0A0U3SB38,A0A0U3SCD4,A0A0U3TM83,A0A0U3TY67,A0A0U3UKE0,A0A0X8W0J3,A0A0X8W0W5,A0A0X8XBT9,A0A0X8Z1K9,A0A125T0U7,A0A125T130,A0A191T6S4,A0A191T710,A0A191T790,A0A191T7H0,A0A1W5LUS2,A0A2D1LXX3,A0A2D1LY86,A0A2D1LYD8,A0A2D1LYN4,A0A2D1LYW2,A0A2D1LZ30,A0A2D1LZB0,A0A2D1M071,A0A2D1M0L5,A0A3R5TN76,A0A3R5TNW6,A0A3R5TRP0,A0A3R5TTM1,A0A3R5TU90,A0A3R5TUU2,A0A3R5TV00,A0A3R5TVV4,A0A3R5U305,A0A3R5U329,A0A3R5U471,A0A3R5U4S0,A0A3R5U5P5,A0A3R5U808,A0A3R5UAV2,A0A3R5UBI8,A0A3R5UCF3,A0A3R5UCS0,A0A3R5UD40,A0A3R5UDT7,A0A3R5UGT2,A0A3R5VW62,A0A3R5VZT8,A0A3R5W0Z1,A0A3R5W616,A0A3R5W7U3,A0A3R5W866,A0A3R5WD22,A0A3R5WKC0,A0A3R5WQ14,A0A3R5WQP7,A0A3R5WU22,A0A3R5WUM5,A0A3R5WWB4,A0A3R5WWE7,A0A3R5WWI4,A0A3R5WX09,A0A3R5WXB8,A0A3R5WY79,A0A3R5WYI2,A0A3R5WYN4,A0A3R5WZW6,A0A3R5X0F9,A0A3R5X0S5,A0A3R5X1P2,A0A3R5X4D5,A0A3R5X6P1,A0A3R5X741,A0A3R5X8A5,A0A3R5X9K2,A0A3R5XD17,A0A3R5XDF6,A0A3R5XDK0,A0A3R5XFA1,A0A3R5XIC4,A0A3R5XMU8,A0A3R5XR67,A0A3R5YDU1,A0A3R5YEE6,A0A3R5ZGU7,A0A3R5ZZ51,A0A3R6A0M6,A0A3R6A337,A0A3R6A9X6,I1YNZ9,K9UR36,K9URA4,Q3KSV2,R4QYS0,U5YU33

Functional_annotation:
Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by up-regulating the expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as several host genes including CD21, CD23 and MYC. Activates transcription by acting as an adapter molecule that binds to cellular sequence-specific DNA-binding proteins such as host CBF1, SMARCB1 and SPI1. Once EBNA2 is near promoter sites, its acidic activating domain recruits basal and activation-associated transcription factors TFIIB, TAF40, TFIIH components ERCC2 and ERCC3, and CBP in order to promote transcription. Alternatively, EBNA2 can affect activities of cell cycle regulators and retard cell cycle progression at G2/M phase. It also induces chromosomal instability, by disrupting mitotic checkpoints, multi-nucleation and formation of micronuclei in infected cells.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA3A
UniProtID_Ref: P12977
UniProt_Name_Ref: EBNA3_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(26719268)
ChIP_seq: D(26719268, 27903901, 24068937)
Structure_PDB_ID: 1M05, 1XR8, 5WMO
Reporter_assay: D(12372828, 9499037, 8709211)
EMSA: D(8709211)
Other_assays: D(12372828, 9499037)
Human_infection_evidence: Fields Virology
Aliases:
BLRF3-BERF1, EBNA3, EBNA-3, EBNA-3A, EBV nuclear antigen 3, EBV nuclear antigen 3A, Epstein-Barr nuclear antigen 3, Epstein-Barr nuclear antigen 3A

UniProt_IDs_Orthologs:
A0A075FCV9,A0A075FCW4,A0A075FFK6,A0A075FGE2,A0A0A8IN05,A0A0B6VPX8,A0A0C7P0X9,A0A0C7SX58,A0A0C7SZG8,A0A0C7T019,A0A0C7T0J9,A0A0C7T1N7,A0A0C7T3A9,A0A0C7T3S7,A0A0C7T5I8,A0A0C7T6Q6,A0A0C7T6Z1,A0A0C7T8F1,A0A0C7T9C3,A0A0C7T9D1,A0A0C7TAY3,A0A0C7TBQ7,A0A0C7TD44,A0A0C7TFN4,A0A0C7TIG9,A0A0C7TKB3,A0A0C7TLT1,A0A0C7TLW3,A0A0C7TN30,A0A0C7TNK3,A0A0C7TPP7,A0A0C7TPQ7,A0A0C7TPS6,A0A0C7TQD5,A0A0C7TR83,A0A0C7TRR5,A0A0C7TSA1,A0A0C7TSL0,A0A0C7TSM3,A0A0C7TTD0,A0A0C7TU38,A0A0C7TUC1,A0A0C7TVT3,A0A0C7TVZ9,A0A0C7TWE5,A0A0C7TWV3,A0A0C7TYQ1,A0A0C7TZ60,A0A0C7TZJ3,A0A0C7U0I2,A0A0C7U378,A0A0F6QK09,A0A191T7B4,A0A191T7J2,A0A1W5LUA3,A0A1W5LUF8,A0A2D1LXZ8,A0A2D1LYG7,A0A2D1LYX5,A0A2D1LZ53,A0A2D1M0F9,A0A2S1MLI0,A0A3R5TLU3,A0A3R5TQC1,A0A3R5TU26,A0A3R5TUK3,A0A3R5TUX6,A0A3R5TX13,A0A3R5TXM2,A0A3R5TY93,A0A3R5TZE0,A0A3R5U0J0,A0A3R5U3V1,A0A3R5U4Q0,A0A3R5U5C4,A0A3R5U5V3,A0A3R5U6R9,A0A3R5U851,A0A3R5UBX8,A0A3R5UBZ5,A0A3R5UFL7,A0A3R5W1K4,A0A3R5W2D1,A0A3R5WDB0,A0A3R5WHZ1,A0A3R5WJQ0,A0A3R5WME6,A0A3R5WT39,A0A3R5WTU4,A0A3R5WXL4,A0A3R5WYV7,A0A3R5X5D7,A0A3R5XA97,A0A3R5XE13,A0A3R5XG85,A0A3R5XHM9,A0A3R5ZJQ4,A0A3R5ZMQ3,A0A3R6A954,A0A3R6ADF3,I1YP19,K9USU8,K9UT27,Q3KST2,Q69138,V5KUF0

Functional_annotation:
Plays an essential role for activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Since Cp is the promoter for all EBNA mRNAs, EBNA3A probably contributes to a negative autoregulatory control loop.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA3B
UniProtID_Ref: P03203
UniProt_Name_Ref: EBNA4_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(26719268)
ChIP_seq: D(26719268, 24068937, 27903901)
Structure_PDB_ID: N
Reporter_assay: D(7975264)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Aliases:
BERF2A-BERF2B, EBNA-3B, EBNA4, EBNA-4, EBV nuclear antigen 3B, EBV nuclear antigen 4, Epstein-Barr nuclear antigen 3B, Epstein-Barr nuclear antigen 4

UniProt_IDs_Orthologs:
A0A075FCS4,A0A075FDV6,A0A075FFW1,A0A075FGX8,A0A0B6VHN8,A0A0C7T689,A0A0F6QJ13,A0A0S2YQI6,A0A0S2YQL8,A0A0S2YQZ5,A0A0S2YR40,A0A0S2YRH7,A0A0S2YRK7,A0A0U3SNH2,A0A0U3SPQ3,A0A0U3TMR1,A0A0U3TXD3,A0A0U3U0Q9,A0A0U3UK97,A0A0X8WSM4,A0A0X8XBD6,A0A0X9A8U7,A0A0X9A9Q5,A0A109NQL8,A0A125T0X2,A0A125T156,A0A191T6V0,A0A191T735,A0A191T7J5,A0A2D1LY00,A0A2D1LYF8,A0A2D1LYQ0,A0A2D1LYY5,A0A2D1LZ71,A0A2D1LZD7,A0A2D1LZV8,A0A2D1M014,A0A2D1M0F4,A0A3R5TNF9,A0A3R5TP59,A0A3R5TPG0,A0A3R5TPS0,A0A3R5TQG9,A0A3R5TSJ0,A0A3R5TTM5,A0A3R5TUK0,A0A3R5TXL1,A0A3R5TZH9,A0A3R5TZN1,A0A3R5U7Y1,A0A3R5U9C9,A0A3R5UB62,A0A3R5UBE0,A0A3R5UBT5,A0A3R5UD37,A0A3R5UEB9,A0A3R5UF10,A0A3R5UFR7,A0A3R5VSI4,A0A3R5VTK1,A0A3R5W2X0,A0A3R5W7M9,A0A3R5WB92,A0A3R5WCP8,A0A3R5WLR6,A0A3R5WLT6,A0A3R5WPT2,A0A3R5WUM4,A0A3R5WUT6,A0A3R5WVA4,A0A3R5X152,A0A3R5X4L7,A0A3R5X4W3,A0A3R5X809,A0A3R5XAT0,A0A3R5XR04,A0A3R5XX02,A0A3R5XZ10,A0A3R5Y0F1,A0A3R5Y4K2,A0A3R5Y5B4,A0A3R5Y901,A0A3R5YB68,A0A3R5ZUB9,A0A3R5ZWY8,A0A3R5ZXN2,A0A3R6A7Y7,A0A3R6ACM8,G3CKQ8,I1YP20,K9URU7,K9US25,Q1HVG4,Q3KST1,Q69139,R4R679,U5YU54,V5KU13

Functional_annotation:
May be involved in transcriptional regulation of both viral and cellular genes by interacting with the host DNA-binding protein RBPJ.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA3C
UniProtID_Ref: P03204
UniProt_Name_Ref: EBNA6_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(24068937, 22357270, 26719268)
ChIP_seq: D(24068937, 22357270, 26719268, 24344258, 27903901)
Structure_PDB_ID: 1CG9, 2BSR, 3DX6, 3DX7, 3DX8, 3DXA
Reporter_assay: D(7745710, 11739688, 10799590)
EMSA: D(10799590, 8709211)
Other_assays: D(11739688)
Human_infection_evidence: Fields Virology
Aliases:
BERF3-BERF4, EBNA-3C, EBNA-4B, EBNA6, EBNA-6, EBV nuclear antigen 3C, EBV nuclear antigen 4B, EBV nuclear antigen 6, Epstein-Barr nuclear antigen 3C, Epstein-Barr nuclear antigen 4B, Epstein-Barr nuclear antigen 6

UniProt_IDs_Orthologs:
A0A0A8IMR0,A0A0B6VJ05,A0A0F6QLY8,A0A0S2YQE3,A0A0S2YQM8,A0A0S2YQU4,A0A0S2YR37,A0A0S2YRI8,A0A0U2IVT5,A0A0U3K2A9,A0A0U3SSI4,A0A0U3THE3,A0A0U3TY20,A0A0X8W0H0,A0A0X8W0R4,A0A0X8Z1G7,A0A109NNY9,A0A120GXX6,A0A120GY11,A0A125T0X3,A0A125T157,A0A191T6V5,A0A191T734,A0A191T7I9,A0A1W5LUG5,A0A1W5LUK3,A0A1W5LUQ5,A0A2D1LXZ6,A0A2D1LY82,A0A2D1LYF3,A0A2D1LYP4,A0A2D1LYY0,A0A2D1LZ65,A0A2D1LZD8,A0A2D1LZP5,A0A2D1LZW5,A0A2D1M0I0,Q3KST0,Q69140

Functional_annotation:
Plays an essential role for the activation and immortalization of human B-cells. Represses transcription of viral promoters TP1 and Cp through interaction with host RBPJ, and inhibits EBNA2-mediated activation of these promoters. Since Cp is the promoter for all EBNA mRNAs, EBNA6 probably contributes to a negative autoregulatory control loop. Alternatively, EBNA6 also regulates the transcription of the EBV oncogene LMP1 in a cell cycle-dependent manner. Modulates the activity of several host proteins involved in cell cycle regulation including host cyclin A, MYC, RB, p21 and p27 mainly through binding to the host SCF(SKP2) complex. Inhibits the promoter of host H2AX and targets H2AX to proteasomal degradation in order to promote latency and cell proliferation.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: EBNA-LP
UniProtID_Ref: Q8AZK7
UniProt_Name_Ref: EBNA5_EBVB9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: D(29467311, 24167291)
Structure_PDB_ID: 5X8N
Reporter_assay: D(29467311)
EMSA: N
Other_assays: D(29467311)
Human_infection_evidence: Fields Virology
Aliases:
EBNA5, EBNA-5, EBNALP, EBNA-LP protein, EBV nuclear antigen 5, EBV nuclear antigen leader protein, Epstein-Barr 62-kDa polypeptide RNA from clone IB4WY-1, Epstein-Barr nuclear antigen 5, Epstein-Barr nuclear antigen leader protein, Epstein-Barr virus Ir1/U2 region protein T1 (Fragment), Latency protein, Leader protein

UniProt_IDs_Orthologs:
A0A0A7DK99,A0A0S2YQH1,A0A0S2YQX5,A0A0S2YRB1,A0A0S2YRQ2,A0A0X8YIJ7,A0A125T0U6,A0A2D1LYW5,K9US68,K9USE8,P0C732,Q1HVI8,Q69125,Q69136,Q69147

Functional_annotation:
Plays an important role in the establishment of B-cell immortalization by acting as an EBNA2 coactivator. This transcriptional activation preferentially enhances the expression of the major viral protein LMP1. The interaction between EBNA-LP and host SP100 correlates with coactivation of EBNA2 and the relocalization of SP100 from PML nuclear bodies into nucleoplasm.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: Rta
Aliases: BRLF1, Immediate-early protein Rta, Replication and transcription activator, RTA
UniProtID_Ref: P03209
UniProt_Name_Ref: RTA_EBVB9
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(17301127, 22379087)
ChIP_seq: D(22379087)
Structure_PDB_ID: N
Reporter_assay: D(17301127, 22379087)
EMSA: D(17301127, 22379087)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A075FGE7,A0A0A8IL74,A0A0B6VHK7,A0A0B6VMK6,A0A0B6VP67,A0A0B6VPY0,A0A0C7SX63,A0A0C7SZH5,A0A0C7T024,A0A0C7T3T2,A0A0C7T5J1,A0A0C7T650,A0A0C7TFN7,A0A0C7TI29,A0A0C7TI76,A0A0C7TMI1,A0A0C7TN35,A0A0C7TNL3,A0A0C7TR86,A0A0C7TRS0,A0A0C7TS97,A0A0C7TZJ8,A0A0C7U0I6,A0A0U3J154,A0A0U3TX69,A0A1W7HHU5,A0A2D1LYE8,A0A2D1M0G7,A0A2D1M0N6,A0A2S1MKD6,A0A2S1MQS6,A0A2S1MR54,A0A2S1MRJ6,A0A2S1MSH1,A0A2S1MTZ3,A0A2S1MUD3,A0A2S1MUN1,A0A2S1MUU8,A0A2S1MUY5,A0A2S1MVQ3,A0A2S1MVZ5,A0A2S1MXG7,A0A2S1MZE3,A0A2S1MZL7,A0A2S1N122,A0A2S1N1H8,A0A2S1N1T8,A0A2S1N2Q2,A0A2S1N3I5,A0A2S1N441,A0A2S1N4M4,A0A385J7S9,G3CKR1,K9UT49,Q1HVG0,Q3KSS7,V5KU06

Functional_annotation:
Immediate-early transcription factor that controls the initiation of viral lytic gene expression and lytic reactivation from latency. Triggers lytic replication, and initiates a cellular senescence program in epithelial cells. Upregulates human DCR3/TNFRSF6B by directly binding to its receptor.


Viral_family: Herpesviridae
Species: Human herpesvirus 4; Epstein-Barr virus
Name: Zta
Aliases: BZLF1, EB1, Trans-activator protein BZLF1, Z, Zebra, ZEBRA, ZTA
UniProtID_Ref: P03206
UniProt_Name_Ref: BZLF1_EBVB9
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(23015699)
ChIP_seq: D(23015699, 25779048, 29142137)
Structure_PDB_ID: 1ZSD, 2AK4, 2AXF, 2AXG, 2C9L, 2C9N, 2NX5, 3KWW, 3KXF, 3SPV, 3VFN, 3VFO, 3VFP, 3VFR, 5SZX
Reporter_assay: D(2157874)
EMSA: D(2157874, 2159531)
Other_assays: D(2157874, 2159531)
Human_infection_evidence: Fields Virology
Notes: ICP0 homolog
UniProt_IDs_Orthologs:
A0A060A1H7,A0A060A1R5,A0A060A624,A0A060A629,A0A0B6VMG6,A0A0C7T7Z0,A0A0C7TGZ2,A0A0C7TIV5,A0A0C7TJ79,A0A0C7TJC8,A0A0C7TLE1,A0A0C7TNH9,A0A0C7TP04,A0A0C7TST0,A0A0C7TUL0,A0A0U3K1L7,A0A0U3SKG1,A0A1W5LUA9,A0A2D1LYB2,A0A2D1M030,A0A2D1M0N0,A0A3R5TL42,A0A3R5TWW0,A0A3R5U420,A0A3R5VRE2,A0A3R5W4V8,A0A3R5WXE1,A0A3R5X5L7,A0A3R5X6C8,A0A3R5XWF5,G3CKR0,K9URC5,Q1HVG1,Q3KSS8,Q69115,Q69123,V5KU67

Functional_annotation:
Plays a key role in the switch from latent infection to lytic cycle producing new virions. Acts as a transcription factor, inducing early lytic cycle genes, and as a origin binding protein for genome replication. BZLF1 activates the promoter of another EBV gene (BSLF2+BMLF1).


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: IE1
Aliases: 55 kDa immediate-early protein 1, UL123
UniProtID_Ref: P03169
UniProt_Name_Ref: VIE1_HCMVT
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(27733551)
ChIP_seq: N
Structure_PDB_ID: 4QRU, 5E5A
Reporter_assay: D(19776115, 27733551)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: ICP0 homolog
UniProt_IDs_Orthologs:
A0A0A7CGH8,A0A0A7CH45,A0A0G2T6P9,A0A0G2T717,A0A0G2T934,A0A0G2T9V0,A0A0G2TB17,A0A0G2TCU8,A0A0G2TFI8,A0A0G2TFM5,A0A0G2TIG1,A0A0G2TJG7,A0A0G2TKF7,A0A0G2TMB8,A0A0G2TQM8,A0A0G2TR65,A0A0G2TT45,A0A0G2TTN7,A0A0G2TTY5,A0A0G2TUY9,A0A0G2TVN3,A0A0G2TVV8,A0A0G2TWD2,A0A0G2TZN5,A0A0G2U0L5,A0A0G2U0P4,A0A0G2U107,A0A0G2U5F3,A0A0G2U6D3,A0A0G2U775,A0A0G2U789,A0A0G2U9Y0,A0A0G2UA46,A0A0G2UB54,A0A0G2UB64,A0A0G2UBY0,A0A0G2UCW7,A0A0G2UF68,A0A0G2UFS7,A0A0G2UGT4,A0A0R5E2Q2,A0A0R5E3W7,A0A0R5E6M7,A0A0R5E7P5,A0A0R5E9Q8,A0A0R5E9Z2,A0A0R5EB18,A0A0R5EGD5,A0A126N8Q0,A0A126N954,A0A126N9K7,A0A126NAR7,A0A126NBL2,A0A126NC20,A0A126NCL1,A0A126NCY3,A0A126NDE2,A0A126NIT2,A0A140D1E4,A0A140IIR2,A0A140IJ80,A0A159B136,A0A159B2R2,A0A159B4L6,A0A159B5S3,A0A161C1V5,A0A191SCH8,A0A1L3IX30,A0A1L3IYI0,A0A2H4GFT1,A0A2H4GJ43,A0A2H4GK92,A0A2H4GLV7,A0A2H4GNL9,A0A2I2MMP9,B8YED9,C5MKW0,C8BLJ1,C8CFF3,C8CFW8,D2K3S2,D2K507,D2W9F5,D2W9H9,D2W9M7,D2W9Q1,D2W9S5,D2W9X3,D2W9Z7,E7DVQ4,P13202,Q6RXC2,Q6SWJ1,Q6SWL8,Q6SWP6,Q6SWS4,Q6SWV2,Q6SX10,Q6SX39,R4S3N7,V9LM41,V9LMP3,V9LP50,V9LPA5,V9LPS2,V9LRP7,V9LS79,V9PU14,V9PU19,V9PV04,X4YAG1

Functional_annotation:
Plays an important role in transactivating viral early genes as well as activating its own promoter. Targets and disrupts host PML/nuclear domain 10 (ND10). Promotes efficient viral growth by interacting with and directing host SP100 to degradation, leading to enhanced acetylation level of histones. In addition, functions in counteracting the host innate antiviral response. Inhibits the type I interferon pathway by directly interacting with and sequestrating host STAT2. Alters host cell cycle progression, probably through its interaction with host E2F1 or RB1 that overcomes the RB1-mediated repression of E2F-responsive promoters.


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: IE2
Aliases: Protein UL122, UL122, Viral transcription factor IE2
UniProtID_Ref: P19893
UniProt_Name_Ref: VIE2_HCMVA
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(27733551, 15479808)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9875333, 27733551, 15479808, 28161581)
EMSA: D(10225210, 9875333)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0A0PU13,A0A0A7CFM1,A0A0A7CHB3,A0A0G2T7B8,A0A0G2T8I7,A0A0G2T9H8,A0A0G2T9P9,A0A0G2TAW2,A0A0G2TC19,A0A0G2TD78,A0A0G2TE28,A0A0G2TGN0,A0A0G2TI14,A0A0G2TIF9,A0A0G2TJ39,A0A0G2TLE4,A0A0G2TN04,A0A0G2TN92,A0A0G2TNS1,A0A0G2TPC1,A0A0G2TR93,A0A0G2TTK4,A0A0G2TVE6,A0A0G2TXS8,A0A0G2TYR3,A0A0G2TZ60,A0A0G2U2J8,A0A0G2U314,A0A0G2U3E1,A0A0G2U3Y8,A0A0G2U7G8,A0A0G2U7T0,A0A0G2UAC5,A0A0G2UC28,A0A0G2UCV3,A0A0G2UD10,A0A0G2UDJ2,A0A0G2UEQ5,A0A0G2UID8,A0A0G2UJ44,A0A0R5E660,A0A0R5E733,A0A0R5EB52,A0A0R5ECK4,A0A0R5ECZ5,A0A0R5EHA7,A0A126N9K6,A0A126NDW2,A0A126NF63,A0A126NGT3,A0A140D1E3,A0A140IIR1,A0A159AZC8,A0A159B0U1,A0A162DRE1,A0A191SBK7,A0A1L3IX19,A0A2H4GFS6,A0A2H4GHA4,A0A2H4GHN8,A0A2H4GL85,A0A2H4GP31,A0A2H4GQK7,B8YED8,C5MKV9,C8BLJ0,C8CFF2,D2IG93,D2K4M9,D2K506,D2K5K9,D2W9M6,D2W9S4,D2W9X2,D2W9Z6,D5LXA9,E7DVQ3,F5HE22,Q6RXC5,Q6SW29,Q6SWJ2,Q6SWL9,Q6SWP7,Q6SWS5,Q6SWV3,Q6SWY2,Q6SX11,Q6SX40,R4SHW1,V9LNF7,V9LQ15,V9LRJ7,V9LSG0,V9PUG0,V9PUQ9

Functional_annotation:
Stimulates viral early and late gene expression and thus play a crucial role in the regulation of productive infection. In addition, activates quiescent cells to reenter the cell cycle and upregulates several E2F-responsive genes, which are responsible for pushing the cell into S phase. In S-phase, inhibits cellular DNA synthesis and blocks further cell cycle progression.


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL29
Aliases: Protein UL29/UL28
UniProtID_Ref: C0H677
UniProt_Name_Ref: UL298_HCMVA
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(20585571)
EMSA: I(26676794, 30598436)
Other_assays: I(2987527)
Human_infection_evidence: Fields Virology
Functional_annotation: Contributes to activation of immediate-early gene expression.
UniProt_IDs_Orthologs:
A0A0A7CFZ0,A0A0A7CGC5,A0A0G2T6M0,A0A0G2T800,A0A0G2TD10,A0A0G2TJD6,A0A0G2TLM9,A0A0G2TPJ7,A0A0G2TQE9,A0A0G2TSX7,A0A0G2TZ11,A0A0G2U0G4,A0A0G2U0K1,A0A0G2U0V6,A0A0G2U2S6,A0A0G2U5N3,A0A0G2U760,A0A0G2UFK8,A0A0G2UGK9,A0A0G2UHH1,A0A0R5E240,A0A0R5E2Z4,A0A0R5E4G4,A0A0R5E6C3,A0A0R5EA67,A0A0R5EC46,A0A0R5EDP6,A0A0U2Q734,A0A126N9C9,A0A126NDN5,A0A126NFE8,A0A140III8,A0A159B0Q9,A0A159B4J9,A0A162DUP8,A0A2H4GFP4,A0A2H4GH35,A0A2H4GI26,A0A2H4GJW2,A0A2H4GKT9,A0A2H4GPE8,A8T794,B8YE64,B9VXJ9,D2K5D5,D3YRW8,D5LX41,E7DVH9,F5HIG2,P16764,Q6SWA3,Q6XNK8,S5FXY3,V9LME7,V9LN39,V9LQ33,V9LS16,V9LSI1,V9PSW3,V9PUS9,V9PV83


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL34
Aliases: Transcriptional regulator UL34
UniProtID_Ref: P16812
UniProt_Name_Ref: UL34_HCMVA
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: D(29626748)
Structure_PDB_ID: N
Reporter_assay: D(11390608)
EMSA: D(11390608)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0A7CFS9,A0A0A7CFU8,A0A0A7CFZ2,A0A0A7CGD1,A0A0G2T6M2,A0A0G2T6X8,A0A0G2T8U9,A0A0G2T9R9,A0A0G2T9V2,A0A0G2TAW7,A0A0G2TBG1,A0A0G2TD15,A0A0G2TJE0,A0A0G2TK87,A0A0G2TKN5,A0A0G2TKP7,A0A0G2TM42,A0A0G2TTS1,A0A0G2TV84,A0A0G2TW58,A0A0G2TZ16,A0A0G2TZG7,A0A0G2U0E2,A0A0G2U0H0,A0A0G2U700,A0A0G2U9Y1,A0A0G2UAW6,A0A0G2UCD9,A0A0G2UCR1,A0A0G2UD52,A0A0G2UDU7,A0A0G2UGL3,A0A0G2UHH5,A0A0R5E3K5,A0A0R5E3P5,A0A0R5E443,A0A0R5E5U6,A0A0R5E6Z8,A0A0R5E8J6,A0A0R5E9J3,A0A126N8Y5,A0A126N9E3,A0A140D0Q8,A0A159AZ79,A0A159B019,A0A159B132,A0A191SBA6,A0A1I9XCP6,A0A1I9XDE2,A0A1L3IXT5,A0A2H4GDQ8,A0A2H4GG19,A0A2H4GKH8,A0A2H4GLN9,A0A2H4GNF1,A0A2I2MMI6,A0A3G6XL13,A8T7A1,B8YE70,C8BKY8,C8BLC1,C8CF83,C8CFP8,C8CPD5,D2K5A2,D3YRX3,D5LX46,E7DVI4,F5HC16,Q6VNV0,R4S5N4,V9LMF4,V9LMN6,V9LN29,V9PTQ8,V9PUT4,X4YA79

Functional_annotation:
Acts as a transcriptional repressor of the US3 gene expression through a specific DNA sequence named the transcriptional repressive element (tre).


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL49
Aliases: Protein HFLF5, Uncharacterized protein UL49, Uncharacterized protein UL49,Protein HFLF5
UniProtID_Ref: P16786
UniProt_Name_Ref: UL49_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation: viral process,viral tegument
UniProt_IDs_Orthologs:
A0A0A0PIG0,A0A0A7CFW2,A0A0G2T6Y6,A0A0G2T7U5,A0A0G2TAX3,A0A0G2TD27,A0A0G2TFD1,A0A0G2TKA2,A0A0G2TPR1,A0A0G2TR21,A0A0G2TUT5,A0A0G2TW75,A0A0G2TXM7,A0A0G2TZY1,A0A0G2U0G0,A0A0G2U0V5,A0A0G2U4N6,A0A0G2U5C7,A0A0G2U5Q4,A0A0G2U679,A0A0G2U779,A0A0G2UAY1,A0A0G2UCF0,A0A0G2UD66,A0A0G2UFM8,A0A0G2UFN4,A0A0G2UG25,A0A0R5EA71,A0A0R5EC84,A0A0U2JPK2,A0A126NBX2,A0A126NCU9,A0A126ND93,A0A140D0S3,A0A159B0S4,A0A159B4B2,A0A162DZ71,A0A1L3IYU1,A0A2H4GDS4,A0A2H4GFN2,A0A2H4GIN6,A8T7C6,B8YE85,B9VXL8,C5MKQ5,C8BKK6,C8BLD6,C8CFR3,C8CPF0,D2K5F5,D3YRY8,D5LX61,E7DVJ9,F5HEF7,Q6RXG9,Q6SW82,R4S5P9,V9HX93,V9LMH3,V9LNW1,V9LQW8,V9LSI8,V9PSX2,V9PTS4


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL57
Aliases: DBP, Major DNA-binding protein
UniProtID_Ref: P17147
UniProt_Name_Ref: DNBI_HCMVA
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: D(9426445)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0R5EAX5,A0A1L3IXF9,A0A1L3IXW0,A0A1L3IYC5,A0A2H4GDT7,A0A2H4GET4,A0A2H4GKC4,A0A2H4GP02,A0A2S0DCR9,A0A3G6XKQ2,A8T7D7,A9YU24,A9YU25,A9YU26,A9YU27,A9YU31,Q6RXG4,Q80MY8,V9LM77

Functional_annotation:
Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein (PubMed:8230421). May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL69
Aliases: mRNA export factor ICP27 homolog
UniProtID_Ref: Q6SW73
UniProt_Name_Ref: ICP27_HCMVM
UniProt_IDs_Orthologs: A0A3G6XL32
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8189530, 16478985)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: ICP27 homolog
Functional_annotation:
Immediate early (EI) protein that plays many roles during productive infection including regulation of host cell cycle progression, regulation of viral gene expression or nuclear export of intronless viral RNAs. Acts as a transcriptional transactivator via interaction with the cellular transcription elongation factor SUPT6H and as a nuclear RNA export factor via interaction with UAP56, a component of the cellular mRNA export machinery (By similarity).


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL79
Aliases: Protein UL79
UniProtID_Ref: P16752
UniProt_Name_Ref: UL79_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: D(21367901)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
UniProt_IDs_Orthologs:
A0A0A0PKK4,A0A0A7CF34,A0A0A7CGG1,A0A0G2T6N3,A0A0G2T910,A0A0G2T9T2,A0A0G2TAY7,A0A0G2TBJ1,A0A0G2U0K7,A0A0G2U5D9,A0A0G2UB12,A0A0G2UG47,A0A0R5E690,A0A0R5E943,A0A126NDS7,A0A126NEP6,A0A159B014,A0A159B138,A0A1I9XCS0,A0A1L3IWY8,A0A2H4GK38,A0A2H4GN24,A0A2H4GNQ9,A0A2H4GPI2,A0A2I2MML7,A0A3G6XL37,A8T7F6,B8YEA4,B9VXN7,C5MKS5,C8BLF6,C8CFB8,C8CFT3,D2K5H5,D3YS03,D5LX75,F5HFM1,Q6SW63,V9LM10,V9LQ09,V9LQM3,V9LS53,V9PTX7,V9PTY8,V9PUX0

Functional_annotation:
Plays a role in the expression of late transcripts bridging viral DNA replication and late gene expression during infection.


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL82
UniProtID_Ref: P06726
UniProt_Name_Ref: PP71_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(28132838, 1318413)
EMSA: N
Other_assays: D(12610120)
Human_infection_evidence: Fields Virology
Aliases:
71 kDa upper matrix phosphoprotein, Phosphoprotein UL82, pp71, ppUL82, Protein pp71, Tegument protein UL82

UniProt_IDs_Orthologs:
A0A0A7CGS9,A0A0G2TA12,A0A0G2TE35,A0A0G2TFG8,A0A0G2TLV2,A0A0G2TVB4,A0A0G2U825,A0A0G2U8I2,A0A0G2U9L4,A0A0G2UA33,A0A0G2UAJ0,A0A0G2UKQ3,A0A0R5E8M4,A0A140D1B2,A0A140D1S9,A0A159B0K5,A0A1L3IYE9,A0A2H4GFA1,A0A2H4GJN7,A0A2H4GK52,A0A2I2MM68,A0A3G6XKT7,A8T7G0,B8YEA7,B9VXP0,C8BKM9,C8BL26,C8CFC1,C8CPH3,D3YS06,R4SH92,V9LLY2,V9LNL7,V9LQC3,V9PTH3,V9PTY5,V9PUF9

Functional_annotation:
Stimulates viral immediate-early (IE) transcription. Plays a role in the inhibition of the host innate repsonse by targeting STING and thus the cGAS-STING pathway (PubMed:28132838). Counteracts also the DAXX-mediated repression of viral transcription. Displaces a DAXX-binding protein, ATRX, from nuclear domain 10 sites (ND10) shortly after infection. Increases the basal level of SUMOylated DAXX in infected cells. May also play a role in the progression of the host cell cycle through the G1 phase.


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL84
Aliases: Initiator protein, Protein UL84, UL84 protein
UniProtID_Ref: P29839
UniProt_Name_Ref: UL84_HCMVT
Binding_ligand: ssRNA
Function: Rep, TNA, TR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9261435)
EMSA: N
Other_assays: D(20573826)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A076JUV4,A0A0A0PKK9,A0A0A7CGG2,A0A0A7CH25,A0A0G2T6N5,A0A0G2T701,A0A0G2T913,A0A0G2TA27,A0A0G2TAZ0,A0A0G2TBJ3,A0A0G2TCR6,A0A0G2TD50,A0A0G2TG34,A0A0G2TH07,A0A0G2TI36,A0A0G2TJB4,A0A0G2TJD7,A0A0G2TJH9,A0A0G2TJI0,A0A0G2TN73,A0A0G2TQJ7,A0A0G2TR45,A0A0G2TRN3,A0A0G2TS06,A0A0G2TXQ2,A0A0G2TZ57,A0A0G2U0L2,A0A0G2U0P1,A0A0G2U105,A0A0G2U3Z0,A0A0G2U6A5,A0A0G2U960,A0A0G2UA21,A0A0G2UBV3,A0A0G2UCH0,A0A0G2UCU0,A0A0G2UD93,A0A0G2UFP7,A0A0G2UFQ2,A0A0G2UG52,A0A0G2UGQ0,A0A0R5E867,A0A0R5E9Q2,A0A0R5EA57,A0A0R5EAZ3,A0A0R5ECN0,A0A0R5EDV8,A0A126N924,A0A126NBJ0,A0A126NBZ0,A0A126NIL7,A0A140D0U8,A0A140D1B4,A0A159B2N6,A0A159B4L0,A0A161BXL4,A0A1I9XC23,A0A1L3IXH8,A0A2H4GEC9,A0A2H4GJ14,A0A2H4GJ70,A0A2H4GKM2,A0A2H4GQ12,A0A2H4GQI0,A8T7G3,A9YU44,A9YU45,A9YU46,A9YU47,A9YU48,A9YU49,A9YU51,B8YEA9,B9VXP2,C5MKT0,C8BLG1,C8CFC3,C8CPH5,D2K4K0,D2K4X7,D2K5I0,D3YS08,D5LX80,E7DVM4,P16727,Q6RXF3,R4S3J6,V9LM14,V9LMH2,V9LML4,V9LP17,V9LP67,V9LPN9,V9LRM2,V9LRU9,V9LS58,V9PTZ2,V9PUX5

Functional_annotation:
Plays an essential role in viral DNA replication. May participate in the DNA replication initiation by interacting with the origin of lytic replication, oriLyt and subsequently recruiting other viral/cellular factors. Additionally, interacts with and shuttles IRS1 viral mRNA from the host nucleus to the cytoplasm (By similarity).


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL87
Aliases: Protein UL87
UniProtID_Ref: P16730
UniProt_Name_Ref: UL87_HCMVA
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: I(24403583)
Other_assays: D(21507978)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation: Not annotated
UniProt_IDs_Orthologs:
A0A0A7CGT1,A0A0A7CH46,A0A0G2T6S1,A0A0G2T7C6,A0A0G2T8L6,A0A0G2TA16,A0A0G2TA67,A0A0G2TAE2,A0A0G2TBC7,A0A0G2TCR3,A0A0G2TDF1,A0A0G2TE40,A0A0G2TE80,A0A0G2TFH3,A0A0G2TIF5,A0A0G2TJT9,A0A0G2TN44,A0A0G2TNU9,A0A0G2TQ45,A0A0G2TQ79,A0A0G2TY67,A0A0G2TZN0,A0A0G2U036,A0A0G2U4U8,A0A0G2U8A3,A0A0G2U9J7,A0A0G2UAJ6,A0A0G2UB23,A0A0G2UC04,A0A0G2UDG5,A0A0G2UKQ8,A0A0R5E2I0,A0A0R5E8Z4,A0A0R5ECI5,A0A0R5EFR1,A0A126N941,A0A126NAB8,A0A126NAM9,A0A126NBX7,A0A126NDT6,A0A140D1T4,A0A159B023,A0A159B0T6,A0A159B283,A0A159B4A0,A0A159B5D5,A0A191SC79,A0A1I9XC25,A0A1I9XEZ1,A0A1L3IXY1,A0A1L3IYY9,A0A2H4GMD9,A0A2H4GPJ5,A0A2H4GRL2,B8YEB2,B9VXP5,C8BKN4,C8BLG4,C8CFC6,C8CFU1,D2K4K3,D3YS11,D5LX83,F5HIL1,Q6SW55,S5ZY95,V9LLY7,V9LMW9,V9PUG3,V9PV44


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL91
Aliases: Protein UL91
UniProtID_Ref: P16797
UniProt_Name_Ref: UL91_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: D(23720731)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation: Not annotated
UniProt_IDs_Orthologs:
A0A076JQV0,A0A0G2TFZ4,A0A0G2TTF4,A0A0G2TVC5,A0A0G2TYZ8,A0A0G2U7V6,A0A0G2UEE4,A0A0R5E5N9,A0A0R5E608,A0A159B1K2,A0A2H4GKW5,A8T7H4,B8YEB5,B9VXP8,C8CFU4,D2K4K6,D2K5V2,D5LX86,E7DVN0,F5HFJ8,S6A6A7,V9LML0,V9LSJ5,V9PUH7


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL92
Aliases: Protein UL92
UniProtID_Ref: P16798
UniProt_Name_Ref: UL92_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: D(24131715)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
Functional_annotation: Not annotated
UniProt_IDs_Orthologs:
A0A076JW34,A0A0A7CFH5,A0A0G2TF71,A0A0G2U868,A0A1L3IXZ5,A0A2H4GQI1,B9VXP9,C8CFU5,D3YS15,E7DVN1,F5HAS7,Q6RXE7,S5ZAG0,V9LLV3


Viral_family: Herpesviridae
Species: Human herpesvirus 5; Human cytomegalovirus
Name: UL95
Aliases: Protein UL95
UniProtID_Ref: P16801
UniProt_Name_Ref: UL95_HCMVA
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(25165108)
EMSA: N
Other_assays: D(21507978)
Human_infection_evidence: Fields Virology
Notes: vPIC homologs
UniProt_IDs_Orthologs:
A0A0A0PKL9,A0A0A7CG46,A0A0G2T6N9,A0A0G2T707,A0A0G2T826,A0A0G2T9T8,A0A0G2TAZ9,A0A0G2TBK3,A0A0G2TCS8,A0A0G2TFG7,A0A0G2TG53,A0A0G2TI46,A0A0G2TJE7,A0A0G2TJI8,A0A0G2TKT4,A0A0G2TLT4,A0A0G2TLT6,A0A0G2TM98,A0A0G2TMC3,A0A0G2TQK8,A0A0G2TR53,A0A0G2TUX1,A0A0G2TVC3,A0A0G2TVL3,A0A0G2TVT4,A0A0G2TXR1,A0A0G2TZ69,A0A0G2U0Y6,A0A0G2U2Y6,A0A0G2U3Z5,A0A0G2U4S4,A0A0G2U5T9,A0A0G2U6B4,A0A0G2UA30,A0A0G2UFQ6,A0A0G2UH47,A0A0G2UHL8,A0A0R5E486,A0A0R5E5G7,A0A0R5E5I6,A0A0R5E8J7,A0A0R5E8V4,A0A0R5EC08,A0A126NAD0,A0A126NC00,A0A126NE98,A0A140D1C4,A0A140D1U1,A0A140IIP2,A0A159AZJ9,A0A159AZP6,A0A159B123,A0A159B4K0,A0A162DTW9,A0A1L3IX11,A0A2H4GG66,A0A2H4GJ23,A0A2H4GKN2,A0A2H4GM46,A0A2H4GQ22,A0A2H4GQI7,B8YEB9,C8BLH1,C8CFD3,C8CPI5,D2K4L0,D2K4Y7,D2K5V6,D5LX90,F5HB20,R4S3K7,S5ZGL2,V9LM21,V9LMI2,V9LP79,V9LPP8,V9LQN8,V9LRV9,V9PSZ3,V9PU01,V9PUY4,V9PVC5,X4YAD5

Functional_annotation:
Participates in the expression of late viral mRNAs. Expressed before viral DNA replication, UL95 assembles at the viral pre-replication complexes (pre-RCs) containing the early viral protein UL44.


Viral_family: Herpesviridae
Species: Human herpesvirus 6A
Name: U42
Aliases: ICP27, mRNA export factor ICP27 homolog, UL69
UniProtID_Ref: P52354
UniProt_Name_Ref: ICP27_HHV6U
UniProt_IDs_Orthologs: A0A0A7RNQ1
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8189530, 16478985)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: ICP27 homolog
Functional_annotation:
Immediate early (EI) protein that plays many roles during productive infection including regulation of viral gene expression and nuclear export of intronless viral RNAs.


Viral_family: Herpesviridae
Species: Human herpesvirus 6A
Name: IE1
Aliases: Immediate-early protein 1, pRF2/pRF3/pRF4, RF4, U90/U89
UniProtID_Ref: Q69567
UniProt_Name_Ref: IE1_HHV6U
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(17376932)
EMSA: D(17376932)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
host cell cytoplasm;host cell nucleus;viral tegument;metal ion binding;regulation of transcription, DNA-templated


Viral_family: Herpesviridae
Species: Human herpesvirus 6B
Name: IE2
Aliases: Immediate-early protein 2, U86, U90/U86
UniProtID_Ref: Q9QJ16
UniProt_Name_Ref: IE2_HHV6Z
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(17005699, 12068008, 16884756)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation: Transcriptional transactivator.
UniProt_IDs_Orthologs:
A0A219XVN1,A0A219XW25,A0A219XWE5,A0A219XWM9,A0A219XWU0,A0A219XXA5,A0A219XXU4,A0A219XY21,A0A219XYM7,A0A219XYW1,A0A219XZ48,A0A219Y0C1,A0A219Y0K1


Viral_family: Herpesviridae
Species: Human herpesvirus 6B
Name: U41
UniProtID_Ref: Q785N4
UniProt_Name_Ref: Q785N4_HHV6H
UniProt_IDs_Orthologs: A0A219XV25,P52538
Binding_ligand: dsDNA, ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(20585571)
EMSA: I(26676794, 30598436)
Other_assays: I(30469324)
Human_infection_evidence: Fields Virology
Notes: U41 is an ortholog of HSV-1 ICP8 (30469324)
Aliases:
DBP, Major DNA binding protein, Major DNA-binding protein, Single-stranded DNA-binding protein, U41 protein


Viral_family: Herpesviridae
Species: Human herpesvirus 6B
Name: IE1
Aliases: IE1 Protein, Immediate-early protein 1, U90
UniProtID_Ref: Q6XA69
UniProt_Name_Ref: Q6XA69_HHV6H
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(17376932)
EMSA: D(17376932)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation: host cell nucleus;DNA binding;regulation of transcription, DNA-templated;viral process
UniProt_IDs_Orthologs:
A0A291ID66,A0A291ID67,A0A291ID73,A0A291ID74,A0A291ID75,A0A291ID93,A0A291IDA0,A0A291IDC1,Q6XA64,Q6XA65,Q6XA66,Q6XA67,Q6XA68,Q6XA70,Q6XA72,Q6XA73,Q77PU6,Q9QJ15


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: K8
Aliases: E3 SUMO-protein ligase K-bZIP, E3 SUMO-protein transferase K-bZIP, KIE-1, RAP
UniProtID_Ref: Q2HR82
UniProt_Name_Ref: KBZIP_HHV8P
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(12885907, 30998737)
ChIP_seq: D(30998737)
Structure_PDB_ID: N
Reporter_assay: D(12885907, 30998737)
EMSA: D(12885907, 30998737)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0N9RNL1,A0A0N9RP86,A0A0N9RPS7,A0A0N9S314,A0A0N9S4U8,A0A0N9SDG5,A0A0N9SDK7,A0A0N9SDQ8,A0A0N9SFS2,A0A0N9SFT9,A0A193PN17,A0A2Z5TGL2,A0A2Z5TGX0,A0A2Z5TK66,D0UZR3,E5LBX3,K0FC23,O92597,P88939,Q77UV1,Q9WRJ7

Functional_annotation:
Plays a role in viral gene regulation and seems to be essential for KSHV reactivation. Disrupts host G1 cell cycle control thus allowing viral transcription and translation to proceed at the early stages of infection. Catalyzes its own SUMO modification as well as that of its interacting partners such as host TP53 AND RB1.


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: LANA
Aliases: ORF73
UniProtID_Ref: E5LC01
UniProt_Name_Ref: E5LC01_HHV8
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(30682185, 24696474, 22419807)
ChIP_seq: D(24696474, 22419807, 25033463)
Structure_PDB_ID: 4UZC, 4UZB
Reporter_assay: D(30682185)
EMSA: D(25947153, 22419807, 12015325)
Other_assays: D(25947153, 12015325)
Human_infection_evidence: Fields Virology
Functional_annotation: DNA binding,nucleosome binding,host cell nucleus
UniProt_IDs_Orthologs:
A0A0N9S387,A0A0N9S3L8,A0A0N9SCV1,A0A0N9SCV5,A0A0N9SEW3,A0A0N9SF30,A0A0N9SF93,A0A0N9SNQ9,A0A193PND8,A0A2Z5THC2,A0A2Z5TRA4,D0UZU1,Q91LX9


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: ORF18
Aliases: Protein UL79 homolog, UL79
UniProtID_Ref: Q2HRB4
UniProt_Name_Ref: UL79_HHV8P
UniProt_IDs_Orthologs: A0A0N9RN23,A0A0N9S3E8,A0A0N9SD38,A0A0N9SGT1,D0UZN0,J9QSB8
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(30305361;26468530)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Notes:
 A specialized complex of viral transcriptional activators (vTAs) coordinate to direct expression of virus-encoded late genes. The vTAs in Kaposi’s sarcoma-associated herpesvirus (KSHV) are ORF18, ORF24, ORF30, ORF31, ORF34, and ORF66. 

Functional_annotation:
Plays a role in the expression of late transcripts bridging viral DNA replication and late gene expression during infection.


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: ORF34
Aliases: Protein UL95 homolog, UL95
UniProtID_Ref: Q2HR98
UniProt_Name_Ref: UL95_HHV8P
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(31095645)
ChIP_seq: D(31095645)
Structure_PDB_ID: N
Reporter_assay: D(30305361;26468530; 31095645)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Participates in the expression of late viral mRNAs. Expressed before viral DNA replication, protein ORF34 assembles at the viral pre-replication complexes (pre-RCs) (By similarity).


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: ORF49
Aliases: ORF49 Protein, Protein ORF49
UniProtID_Ref: Q2HR83
UniProt_Name_Ref: ORF49_HHV8P
UniProt_IDs_Orthologs: A0A0N9SE29,A0A0N9SF04,E5LBX2
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(16501115)
EMSA: N
Other_assays: D(16501115)
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in the activation the host JNK/p38 pathways necessary for KSHV reactivation from latency and for viral replication. Induces transcriptional activation through host JUN of several ORF50-responsive promoters.


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: ORF6
Aliases: Core gene UL29 family protein, DBP, Major DNA-binding protein, ORF 6
UniProtID_Ref: K0FHU3
UniProt_Name_Ref: K0FHU3_HHV8
Binding_ligand: ssDNA
Function: TR, Rep, DR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(24850743)
Other_assays: D(24850743, Fluorescence polarization analysis)
Human_infection_evidence: Fields Virology
Functional_annotation: single-stranded DNA binding,DNA replication,host cell nucleus
UniProt_IDs_Orthologs:
A0A0N9RNY3,A0A0N9RUK2,A0A0N9RV39,A0A0N9S3V6,A0A0N9SC72,A0A0N9SDM5,A0A0N9SFW6,A0A0N9SHS5,A0A2Z5TGV3,O40913


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: Rta
Aliases: ORF50, Putative transcription activator ORF50
UniProtID_Ref: F5HCV3
UniProt_Name_Ref: ORF50_HHV8P
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(19233445)
ChIP_seq: D(19233445, 29302027, 30541837)
Structure_PDB_ID: N
Reporter_assay: D(12154127, 11435569, 19233445)
EMSA: D(12154127, 11435569, 19233445)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation: Transcription activation.
UniProt_IDs_Orthologs:
A0A0N7GF04,A0A0N9RUU4,A0A0N9RVD9,A0A0N9RX80,A0A0N9S418,A0A0N9SDX6,A0A0N9SE53,A0A0N9SEG4,A0A193PN21,A0A2Z5TKP1,E5LBX1,K0FCG0,O92608


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: vIRF-1
UniProtID_Ref: Q77Q82
UniProt_Name_Ref: Q77Q82_HHV8
UniProt_IDs_Orthologs: A0A0N9RX90,A0A0N9SEG2,A0A0N9SGV7,P88946
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4HLX, 4YSI
Reporter_assay: D(9365244, 11027294, 10438822)
EMSA: D(10438822, 17855527)
Other_assays: D(23435230)
Human_infection_evidence: Fields Virology
Functional_annotation: DNA-binding transcription factor activity,transcription regulatory region DNA binding
Aliases:
K9, Latent viral interferon regulatory factor, Lytic viral interferon regulatory factor, ORF K9, vIRF, VIRF-1, VIRF-1 protein


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: vIRF-2
Aliases: K11, ORF K11, Viral IRF2-like protein, VIRF2
UniProtID_Ref: Q2HR71
UniProt_Name_Ref: VIRF2_HHV8P
UniProt_IDs_Orthologs: A0A193PN34,A0A2Z5TUW0,F5H9G3,O40941,P88948
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(26537687)
ChIP_seq: D(26537687)
Structure_PDB_ID: 4P55
Reporter_assay: D(26537687)
EMSA: D(26537687)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in the inhibition of host immune response. Acts by interacting with host EIF2AK2/PKR and inhibiting its activation. In turn, EIF2AK2/PKR substrates including EIF2S1 or histone H2A are not phosphorylated.


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: vIRF-3
UniProtID_Ref: Q9DUN1
UniProt_Name_Ref: Q9DUN1_HHV8
UniProt_IDs_Orthologs: D0UZS3,K0FCD9,O40940,Q99AM3
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(17728244, 19129183)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(22453922, 17728244, 19129183, 10933732, 17522209)
EMSA: D(17522209)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation: DNA-binding transcription factor activity,transcription regulatory region DNA binding
Aliases:
B-cell specific latent nuclear protein, Interferon regulatory factor 3, K10.5, ORF K10.5, Viral IRF3-like protein, VIRF-3 protein, VIRF-3 Viral IRF3-like protein


Viral_family: Herpesviridae
Species: Human herpesvirus 8; Kaposi sarcoma-associated herpesvirus
Name: vIRF-4
Aliases: K10, Viral IRF4-like protein
UniProtID_Ref: Q2HR73
UniProt_Name_Ref: VIRF4_HHV8P
UniProt_IDs_Orthologs: A0A193PN61,F5H9D8,O40939,P88947
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: D(24335298)
ChIP_seq: N
Structure_PDB_ID: 2XXN
Reporter_assay: D(28342865, 20861242)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in host cell apoptosis modulation by promoting TP53/p53 ubiquitination and subsequent degradation and thus downregulating TP53/p53-mediated apoptosis.


Viral_family: Herpesviridae
Species: Pseudorabies virus
Name: EP0
UniProtID_Ref: P29129
UniProt_Name_Ref: ICP0_SUHVF
Binding_ligand: dsDNA
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(10426211, 9850990, 7595399)
EMSA: I(15494213)
Other_assays: D(10426211)
Human_infection_evidence: Fields Virology
Aliases:
E3 ubiquitin-protein ligase ICP0, Early protein 0, Early Protein EP0, ICP0, RING-type E3 ubiquitin transferase ICP0, RL2

UniProt_IDs_Orthologs:
A0A0B4ZUF5,A0A0S2MM93,A0A142I9X0,A0A172XDT2,A0A1B2G2G1,B0FL91,B8Y463,G3G917,G3G997,I1WX43,Q5PPD2,Q9DYB6,T2FKB8

Functional_annotation:
Evades nuclear antiviral defenses triggered by dsDNA viruses. Acts during the initial stages of lytic infection and the reactivation of latent viral genome. Prevents the antiviral effect of nuclear bodies by degrading host PML and SP100.


Viral_family: Herpesviridae
Species: Pseudorabies virus
Name: IE180
Aliases: ICP4, IE, Immediate-early protein IE180, RS1
UniProtID_Ref: G3G929
UniProt_Name_Ref: G3G929_9ALPH
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(12881636, 9850990)
EMSA: D(12881636)
Other_assays: D(2539489)
Human_infection_evidence: Fields Virology
Functional_annotation: positive regulation of transcription, DNA-templated,host cell nucleus
UniProt_IDs_Orthologs:
A0A097I4Q1,A0A0B4ZXC3,A0A0B4ZXD4,A0A0D5C710,A0A0H4M3P1,A0A0S2MM72,A0A0X7ZX98,A0A140FAV4,A0A140FB14,A0A141B6X8,A0A172XDL4,A0A172XDM4,A0A1B2G2G2,B6UV86,G3G8V9,G3G918,P33479,Q5PP75,Q8JL63


Viral_family: Herpesviridae
Species: Pseudorabies virus
Name: RSP40
UniProtID_Ref: P24827
UniProt_Name_Ref: ICP22_SUHVK
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: I(25233083, 23029222)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19535441)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
Aliases:
Transcriptional regulator ICP22 homolog, Transcriptional regulator ICP22 homologï¼Œ Immediate-early protein RSP40

Functional_annotation:
host cell nucleus;DNA binding;DNA-templated viral transcription;positive regulation of transcription, DNA-templated


Viral_family: Herpesviridae
Species: Pseudorabies virus
Name: UL48
Aliases: UL48 tegument protein
UniProtID_Ref: Q8QXN6
UniProt_Name_Ref: Q8QXN6_SUHVK
UniProt_IDs_Orthologs: G3G8W8,Q5PP87,Q80KJ3
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: I(19321615)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(2538647)
EMSA: I(11416146, 2538647)
Other_assays: I(11416146)
Human_infection_evidence: Fields Virology
Functional_annotation:
host cell cytoplasm;host cell nucleus;metal ion binding;RNA binding;regulation of transcription, DNA-templated;viral process


Viral_family: Herpesviridae
Species: Pseudorabies virus
Name: UL54
Aliases: Early regulation protein UL54, ICP27, mRNA export factor ICP27 homolog, Protein UL54
UniProtID_Ref: Q85232
UniProt_Name_Ref: ICP27_SUHVK
UniProt_IDs_Orthologs: A0A0D5C668,Q6K1M1,Q9DL70,T2FL56
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: TR, TNA
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(25712217)
EMSA: I(19783816)
Other_assays: I(19783816, Yeast three-hybrid analysis, NMR)
Human_infection_evidence: Fields Virology
Notes: ICP27 homolog
Functional_annotation:
Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).


Viral_family: Orthomyxoviridae
Species: Influenza A
Name: NS1
Aliases: Nonstructural Protein 1, Non-structural protein 1, NS, NS1A
UniProtID_Ref: P03496
UniProt_Name_Ref: NS1_I34A1
Binding_ligand: ssRNA
Function: TR, other
Primary_secondary_vTR: S
ChIP: D(29259342;23283961)
ChIP_seq: N
Structure_PDB_ID: 5NT2
Reporter_assay: D(23283961;11090154;11773396)
EMSA: D(23093596;21085662;11090154;29782795)
Human_infection_evidence: 27486731.0
UniProt_IDs_Orthologs:
A0A075ETP1,A0A075ETS1,A0A075ETV2,A0A075EU06,A0A075EU11,A0A075EU57,A0A075EUA6,A0A075EUD3,A0A075EUU4,A0A075EV20,A0A075EV61,A0A075EVF3,A0A075EWN4,A0A075EWW8,A0A075EXF8,A0A075EXX0,A0A089H8R8,A0A0A7E4T1,A0A0A7E4W7,A0A0A7E4X0,A0A0A7E4Z7,A0A0A7E560,A0A0A7E699,A0A0A7E6A8,A0A0A7E6E6,A0A0C6DX30,A0A0D3RZY3,A0A0M3YVZ6,A0A1C9ZU70,A0A1D8EMU4,A0A1D8EMY9,A0A1L5LBA5,A0A1U9W4W5,A0A2I6B733,A0A2R4QPM2,A0A343VTP4,A0A343VTQ9,A0A343VTR4,A0A343VTR9,A0A385P538,A0A3G1GLA5,A0M7Z1,A0M802,A0M813,A0M824,A0M835,A0M846,A0M857,A0M868,A0RSE2,A0RSL9,A0RSN0,A0RSP1,A1BL03,A1BL14,A2CGG4,A2CGH5,A2CGI6,A3DRG9,A3DRJ1,A3DRK2,A3DRL3,A3DRM4,A3DSA5,A3DSB6,A3DSC7,A3DSD8,A4D6R9,A4D6T0,A4D6U1,A4D6V2,A4D6W3,A4D6X4,A4D6Y5,A4D6Z6,A4D707,A4GBF7,A4GBG8,A4GBH9,A4GBJ0,A4GBQ6,A4GBX2,A4GBY3,A4GC16,A4GC93,A4GCA4,A4GCJ2,A4GCK3,A4GCM5,A4GCN6,A4GCP7,A4JZ56,A4JZ89,A4JZA0,A4K0Z4,A4K116,A4K127,A4K149,A4K171,A4U6U7,A4U6V8,A4U6Y0,A4U6Z1,A4U768,A4U779,A4U790,A4U7A1,A4U7B2,A4Z3W0,A4Z3X1,A4Z404,A4ZNQ3,A4ZNR3,A5GX47,A5GX69,A5GXC3,A5GXD4,A6M5K9,A6N9H7,A6ZIX6,A6ZIY5,A9C4V7,A9C995,B0KVE4,B2VMN7,B2VMP8,B2VMS0,B3EUU5,B3EUW7,B3EUX8,B3EUY9,B3EV00,B3EV11,B3RDQ2,B4UPB2,B4UPD4,B4UPI5,B4UQV5,B4UR32,B4UR43,B4UR54,B4UR65,B4UR76,B4URE2,B6A6G5,B6A6Q3,B6A6S5,B6A6T6,B6A6V8,B6A723,B6A767,B6A778,B6A7B1,B7NZ26,B8K0Q2,B8K0R3,C0RSJ6,C3PQG2,C3PQH3,C4LP16,C7RWF6,C7RWK0,C7RWL1,C7RWM2,C7S1W6,C7S1X7,C7S1Y8,C7S221,C7S243,C7S254,C7S276,C7S287,C7S298,C8XP22,C8XP33,C9S2A3,C9S2C9,C9S2D8,C9S2E7,C9S2F7,C9S2G6,C9S2H4,C9S2J1,C9S2K0,D3J182,D5F1T6,D5F1U6,D5F1V6,D6R8P6,D8KQS4,E1AFU6,E4UFQ5,E4UFQ7,E5FF42,E6XTN1,E6XTN8,E6XTP9,E6XTR0,E6XTS0,E6XTT1,E6XTU2,E6XTV2,E6XTW3,E6XTX3,E6XTY4,E6XUC0,E6XUD1,E6XUE2,E6XUF2,E8Z3P7,E8Z4Y8,E8Z4Z0,F0TTA7,F0TTB8,F0TTC9,F0TTE0,F0TTF1,F0TTG2,F0TTH3,F0TTI4,F0TTJ5,F0TTK6,F0TTL7,F0TTM8,F0TTN9,F0TTQ0,F0TTR1,F0TTS2,F0TTT3,F0TTU4,F0TTV5,F0TTW6,F0TTX7,F0TTY8,F0TTZ9,F0TU10,F0TU21,F0TU32,F0TU43,F0TU54,F0TU65,F0TU76,F2P1A3,F2P1B4,F4MDL2,F5CGM8,F5CGN9,F5CGQ0,F5CU09,F6GLF7,G0KR79,G0KTU8,G0KTX4,G0KU08,G2TU06,G7WW33,G7WW47,G7X3X3,G7X407,G7X431,G7X486,G8JBY2,H2KIX8,H2KIZ8,H2KJ09,H6QNR4,H8PHK7,H8XZS5,H8XZT1,H8XZV5,H8XZW5,H9XI03,H9XJP7,I6S4N8,I6S507,I6S561,I6S5I7,I6S5K2,I6S5R7,I6S699,I6S6S7,I6S8B7,I6S8Z3,I6S927,I6S938,I6SGN6,I6SH48,I6SHB2,I6SHJ5,I6SI16,I6SIC0,I6SIT8,I6SJ14,I6SJ90,I6SK95,I6SKG6,I6SUD6,I6T2Q4,I6T342,I6T3J6,I6T444,I6T513,I6T525,I6T535,I6T550,I6T6Z8,I6TAB5,I6TAG8,I6TAN1,I6TB35,I6TBJ3,I6TBT2,I6TBV0,I6TC02,I6TCC8,I6TCJ2,I6TCQ6,I6TCX4,I6TDL1,I6TDV0,I6TE19,I6TEC5,I6TEG7,I6TEL7,I6TEZ1,I6TF77,I6TFJ0,I6TFV0,I6TG01,I6TG75,I6TGD2,I6TGJ1,I6TH83,I6THH9,I6THP0,I6THU6,I6TWM9,I7CY76,I7DBQ0,J7GXI7,K4P0X9,K4P1A0,K4P381,K4P399,M9Q862,M9Q876,M9Q888,M9Q974,M9Q982,M9QA98,M9QAA7,M9QAB7,M9QBB0,M9QBB4,M9QBB8,M9QBQ4,M9QBQ6,M9V1A0,M9V1A1,P03498,P11618,P17042,P69272,P69273,P69274,P69279,Q0A108,Q0A2W7,Q0HCS2,Q0HD44,Q0HD54,Q0PDM0,Q0R7K8,Q0R7L9,Q0R9C4,Q15ME2,Q15MF3,Q15MG4,Q194T2,Q194T3,Q1G0M3,Q1G0M5,Q1G0M6,Q1I1J9,Q1I1L0,Q1I1M1,Q1I1N2,Q1I1P3,Q1I1Q4,Q1I1R5,Q1I1S6,Q1I1T7,Q1I1U8,Q1I1V9,Q1I1X0,Q1I1Y1,Q1I1Z2,Q1I203,Q1I2B3,Q1K9K7,Q1K9P7,Q1WP03,Q1WP14,Q20MF1,Q20MG2,Q20MH3,Q20TN7,Q288T5,Q288U6,Q288V7,Q289A1,Q289B2,Q289C3,Q2IBH5,Q2Y206,Q30N15,Q4ZH89,Q67249,Q6LD08,Q6XSV8,Q6XSW8,Q6XSX2,Q6XSX4,Q6XSX6,Q6XSX8,Q6XSY2,Q6XSY4,Q6XSY6,Q6XSZ2,Q6XSZ4,Q6XTC4,Q6XTC6,Q6XTC8,Q6XTD0,Q6XTD6,Q6XTE2,Q6XTE4,Q6XTE6,Q6XTE8,Q6XTF2,Q6XTF4,Q6XTF6,Q6XTF8,Q6XTG2,Q6XTG4,Q6XTG8,Q6XTH0,Q6XTH2,Q6XTH4,Q6XTH6,Q6XTH8,Q6XTI0,Q6XTI2,Q6XTI4,Q6XTI6,Q6XTI8,Q6XTJ0,Q6XTJ2,Q6XTJ4,Q6XTJ6,Q6XTJ8,Q76MT8,Q82505,Q82506,Q84068,Q99AU3,Q9DUT8,R4PCK4,R9WJE6,R9WJT7,R9WK02,R9WKA5,R9WKG0,R9WKL2,R9WKN0,R9WKW2,R9WL34,R9WME5,R9WMK2,R9WND6,R9WNJ7,R9WNR4,S5FQH9,S5FR40,S5FRA4,S5FS10,S5FSD4,S5FSQ5,S5FT23,S5FTA2,S5FTD5,S5FTK0,S5FTR8,S5FZI2,S5G093,S5G297,S5G2D0,S5G2L6,S5G2T0,V5J5C4

Other_assays:
D(23093596;Fluorescence anisotropy), D(17376915;RNA-binding assay), D(29782795, Fluorescence anisotropy;RNA-binding assay;In Vitro Transcription)

Functional_annotation:
Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated DDX58 ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Prevents human EIF2AK2/PKR activation, either by binding double-strand RNA, or by interacting directly with EIF2AK2/PKR. This function may be important at the very beginning of the infection, when NS1 is mainly present in the cytoplasm. Also binds poly(A) and U6 snRNA.


Viral_family: Papillomaviridae
Species: Human papillomavirus type 116
Name: E2
Aliases: Regulatory protein E2
UniProtID_Ref: C7B7D5
UniProt_Name_Ref: C7B7D5_9PAPI
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: I(14643661, 22031941, 12019268, 29142126)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(22210627, 7957111)
EMSA: I(14643661, 21482558, 7957111, 12239214)
Other_assays: I(14643661, binding assay, DNA complex, footprinting)
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.


Viral_family: Papillomaviridae
Species: Human papillomavirus type 116
Name: E6
Aliases: Protein E6
UniProtID_Ref: C7B7D2
UniProt_Name_Ref: C7B7D2_9PAPI
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: I(15664194)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(31002735, 11275986, 22210627)
EMSA: I(11275986)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase and modulates its activity. Protects host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response.


Viral_family: Papillomaviridae
Species: Human papillomavirus type 16
Name: E2
Aliases: Regulatory protein E2
UniProtID_Ref: P03120
UniProt_Name_Ref: VE2_HPV16
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: D(14643661, 22031941, 12019268, 29142126)
ChIP_seq: N
Structure_PDB_ID: 1BY9, 1DTO, 1R8P, 1ZZF, 2NNU, 2Q79, 3MI7
Reporter_assay: D(22210627, 7957111)
EMSA: D(14643661, 21482558, 7957111, 12239214)
Other_assays: D(14643661, binding assay, DNA complex, footprinting)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0M4B738,A0A0M5I1R5,A0A140FB34,A0A141E6C6,A0A159DYJ1,A0A220NLS7,A0A220NM82,A0A220NM85,A0A220NMY5,A0A220NNA3,A0A220NNP4,A0A220NPB2,A0A220NPJ9,A0A220NPW4,A0A220NQ18,A0A291L508,A0A291L599,A0A291L5B6,A0A2P1HAL8,A0A2P1HAX9,A0A2P1HAZ0,A0A2P1HBJ1,A0A2P1HBK7,A0A2P1HBZ1,A0A2P1HC20,A0A2P1HCQ0,A0A2P1HCR3,A0A2P1HCR4,A0A2P1HCS0,A0A2P1HCX2,A0A2P1HCY1,A0A2P1HD20,A0A2P1HD25,A0A2P1HD43,A0A2P1HDC2,A0A2P1HDD2,A0A2P1HDS5,A0A2P1HDU8,A0A2P1HDW9,A0A2P1HE27,A0A2P1HE44,A0A2P1HEL7,A0A2P1HEM6,A0A2P1HES9,A0A2P1HEX6,A0A2P1HFE1,A0A2P1HFY5,A0A2P1HGA0,A0A2P1HGC9,A0A2P1HGE1,A0A2P1HGK3,A0A2P1HGQ9,A0A2P1HGV5,A0A2P1HH37,A0A2P1HH86,A0A2P1HH94,A0A2P1HHW6,A0A2P1HI17,A0A2P1HI38,A0A2P1HI44,A0A2P1HI84,A0A2P1HI91,A0A2P1HIA7,A0A2P1HIE3,A0A2P1HII1,A0A2P1HIQ3,A0A2P1HIV5,A0A2P1HIW5,A0A2P1HIY0,A0A2P1HJ67,A0A2P1HJA3,A0A2P1HJB1,A0A2P1HJB8,A0A2P1HJD0,A0A2P1HJG6,A0A2P1HJP9,A0A2P1HJS2,A0A2P1HK00,A0A2P1HK97,A0A2P1HKD8,A0A2P1HKI2,A0A2P1HKJ9,A0A2P1HKK3,A0A2P1HKL1,A0A2P1HKR6,A0A2P1HKT0,A0A2P1HL34,A0A2P1HLC9,A0A2P1HLK0,A0A2P1HLT4,A0A2P1HMF1,A0A2P1HMJ8,A0A2P1HMK4,A0A2P1HMP5,A0A2P1HMU0,A0A2P1HN06,A0A2P1HN27,A0A2P1HNB3,A0A2P1HND5,A0A2P1HNM5,A0A2P1HNU8,A0A2P1HNV4,A0A2P1HPG1,A0A2P1HPH7,A0A2P1HPS3,A0A2P1HPV0,A0A2P1HQ06,A0A2P1HQG6,A0A2P1HQR1,A0A2P1HQZ3,A0A2P1HQZ4,A0A2P1HQZ7,A0A2P1HR91,A0A2P1HRB4,A0A2P1HRL8,A0A2P1HRN8,A0A2P1HRP5,A0A2P1HRQ9,A0A2P1HRR6,A0A2P1HS03,A0A2P1HS26,A0A2P1HS42,A0A2P1HS76,A0A2P1HSA9,A0A2P1HSF4,A0A2P1HSP3,A0A2P1HSQ0,A0A2P1HSU6,A0A2P1HSW8,A0A2P1HSX8,A0A2P1HT05,A0A2P1HT52,A0A2P1HT60,A0A2P1HT76,A0A2P1HTC1,A0A2P1HTJ7,A0A2P1HTK2,A0A2P1HTK4,A0A2P1HTL0,A0A2P1HTN5,A0A2P1HTN8,A0A2P1HTZ3,A0A2P1HU04,A0A2P1HU15,A0A2P1HU23,A0A2P1HU81,A0A2P1HUG7,A0A2P1HUL7,A0A2P1HUN7,A0A2P1HUT3,A0A2P1HUV1,A0A2P1HV08,A0A2P1HV51,A0A2P1HV63,A0A2P1HVJ4,A0A2P1HVR1,A0A2P1HVU5,A0A2P1HW33,A0A2P1HW43,A0A2P1HW55,A0A2P1HW89,A0A2P1HWD2,A0A2P1HWF5,A0A2P1HWM1,A0A2P1HWR3,A0A2P1HWT1,A0A2P1HWT5,A0A2P1HWV9,A0A2P1HWW2,A0A2P1HWY5,A0A2P1HWY9,A0A2P1HX44,A0A2P1HX57,A0A2P1HX80,A0A2P1HXB2,A0A2P1HXJ6,A0A2P1HXJ8,A0A2P1HXK9,A0A2P1HXN5,A0A2P1HXT3,A0A2P1HXY6,A0A2P1HY15,A0A2P1HY36,A0A2P1HYS7,A0A2P1HZ11,A0A2P1HZ73,A0A2P1HZ74,A0A2P1HZF4,A0A2P1HZG3,A0A2P1HZH0,A0A2P1HZL0,A0A2P1HZS0,A0A2P1I011,A0A2P1I049,A0A2P1I080,A0A2P1I0E3,A0A2P1I0E5,A0A2P1I0J1,A0A2P1I0K7,A0A2P1I0M3,A0A2P1I0V9,A0A2P1I110,A0A2P1I114,A0A2P1I148,A0A2P1I176,A0A2P1I1A9,A0A2P1I1C0,A0A2P1I1C1,A0A2P1I1E1,A0A2P1I1G4,A0A2P1I1L0,A0A2P1I1N1,A0A2P1I1P3,A0A2P1I1R3,A0A2P1I1S1,A0A2P1I1U6,A0A2P1I1V2,A0A2P1I259,A0A2P1I2C0,A0A2P1I2D5,A0A2P1I2G5,A0A2P1I2K9,A0A2P1I2U5,A0A2P1I376,A0A2P1I3A1,A0A2P1I3A8,A0A2P1I3L7,A0A2P1I3P3,A0A2P1I3R0,A0A2P1I3R2,A0A2P1I3U6,A0A2P1I443,A0A2P1I444,A0A2P1I470,A0A2P1I4I8,A0A2P1I4M6,A0A2P1I4X1,A0A2P1I5I6,A0A2P1I5J7,A0A2P1I5N9,A0A2P1I5Q3,A0A2P1I5U4,A0A2P1I634,A0A2P1I655,A0A2P1I667,A0A2P1I686,A0A2P1I698,A0A2P1I6K3,A0A2P1I6K9,A0A2P1I6Q2,A0A2P1I6T7,A0A2P1I721,A0A2P1I744,A0A2P1I769,A0A2P1I773,A0A2P1I783,A0A2P1I7A6,A0A2P1I7D4,A0A2P1I7E7,A0A2P1I7H6,A0A2P1I7K2,A0A2P1I7M2,A0A2P1I7W3,A0A2P1I811,A0A2P1I872,A0A2P1I873,A0A2P1I878,A0A2P1I890,A0A2P1I894,A0A2P1I8I0,A0A2P1I8K4,A0A2P1I8M8,A0A2P1I8P0,A0A2P1I8T3,A0A2P1I950,A0A2P1I9C4,A0A2P1I9G8,A0A2P1I9J8,A0A2P1I9T0,A0A2P1I9X7,A0A2P1I9Y9,A0A2P1IAB5,A0A2P1IAK9,A0A2P1IAM9,A0A2P1IAU5,A0A2P1IAZ6,A0A2P1IB11,A0A2P1IB34,A0A2P1IB46,A0A2P1IB60,A0A2P1IB88,A0A2P1IBA1,A0A2P1IBF1,A0A2P1IBG1,A0A2P1IBH3,A0A2P1IBQ5,A0A2P1IBR3,A0A2P1IBV0,A0A2P1IBW3,A0A2P1IBZ1,A0A2P1ICD8,A0A2P1ICK7,A0A2P1ICM7,A0A2P1ICV0,A0A2P1ICX3,A0A2P1ID26,A0A2P1ID31,A0A2P1IDB5,A0A2P1IDD2,A0A2P1IDD9,A0A2P1IDG1,A0A2P1IDI0,A0A2P1IDJ2,A0A2P1IDK6,A0A2P1IDP1,A0A2P1IDT4,A0A2P1IDU6,A0A2P1IDW1,A0A2P1IE60,A0A2P1IE69,A0A2P1IEA0,A0A2P1IEI4,A0A2P1IEP9,A0A2P1IEQ8,A0A2P1IEY0,A0A2P1IEY4,A0A2P1IF70,A0A2P1IFB7,A0A2P1IFC5,A0A2P1IFQ2,A0A2P1IFT5,A0A2P1IFU1,A0A2P1IFY2,A0A2P1IG25,A0A2P1IG93,A0A2P1IGA1,A0A2P1IGE9,A0A2P1IGM0,A0A2P1IGM4,A0A2P1IGQ2,A0A2P1IGR6,A0A2P1IH19,A0A2P1IH21,A0A2P1IH35,A0A2P1IHA3,A0A2P1IHJ0,A0A2P1IHL9,A0A2P1IHN3,A0A2P1IHT0,A0A2P1IHW5,A0A2P1II20,A0A2P1II60,A0A2P1II66,A0A2P1IIF5,A0A2P1IIK4,A0A2P1IIW4,A0A2P1IJ92,A0A2P1IJ95,A0A2P1IJA7,A0A2P1IJH6,A0A2P1IJJ5,A0A2P1IJQ4,A0A2P1IJT5,A0A2P1IJY2,A0A2P1IKD0,A0A2P1IKE1,A0A2P1IKE7,A0A2P1IKL6,A0A2P1IKL7,A0A2P1IKR7,A0A2P1IKT3,A0A2P1IKV3,A0A2P1IKW8,A0A2P1IL29,A0A2P1IL50,A0A2P1IL94,A0A2P1ILC6,A0A2P1ILH3,A0A2P1ILI6,A0A2P1ILJ1,A0A2P1ILJ5,A0A2P1ILQ4,A0A2P1ILU5,A0A2Z5ZNE4,A0A2Z5ZNI2,A0A2Z5ZNJ8,A0A2Z5ZNL6,A0A2Z5ZNR3,A0A2Z5ZNU6,A0A2Z5ZNX6,A0A2Z5ZNY7,A0A2Z5ZP42,A0A2Z5ZP70,A0A2Z5ZP86,A0A2Z5ZPA8,A0A384K9A3,A0A384KLH2,A0A384KR39,A0A384L6H3,A0A384LBT8,A0A384LCN9,A0A384LIA5,A0A384LLD3,A0A384LN04,A0A384LPS7,B1A8W7,B1A8X5,B1A8Y3,B9UPB8,C6G868,C6G876,C6G884,D7RGN0,G0XRL3,I1SUZ8,I1SV00,J3SRD7,J3T1D1,J3T1F4,J3T1J6,J3T1Y4,J3UE95,J3XCG3,J3XCM3,J3XLP7,J3XLU0,J3XMC9,J7FME7,K4F2R3,K4F666,N0CFQ0,Q07D09,Q4VRP0,Q4VRP8,Q549Q0,Q71C70,Q8B5P3,Q8JQA8,Q918T0,Q918T5,Q918T8,Q918U1,Q918U3,Q918U5,Q918U7,Q9E839,Q9E840,Q9E841,Q9E842,Q9YIV0,Q9YV72,Q9YV73,Q9YV74,Q9YV75,Q9YV76,S4W1B0,S4W1C8,S4W1D1,S4W2B8,S4W2C7,S4W2D0,S4W2D4,S4W4I9,S4W4J3,S4W4J8,S4W4K3,S4W4K7,S4W7A5,S4W7A9,S4W7B3,S4W7B7,S4W7C0,S4W7C4,S4W8C4,S4W8C8,S4W8D0,S6AWR2,S6B2P1,S6BB15,S6BB53,S6BHC8

Functional_annotation:
Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.


Viral_family: Papillomaviridae
Species: Human papillomavirus type 16
Name: E6
Aliases: Protein E6
UniProtID_Ref: P03126
UniProt_Name_Ref: VE6_HPV16
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: D(15664194)
ChIP_seq: N
Structure_PDB_ID: 1VZN, 2FK4, 2KPL, 2LJX, 2LJY, 2LJZ, 4GIZ, 4JOP, 4XR8, 6HKS, 6SIV, 6SJA
Reporter_assay: D(31002735, 11275986, 22210627)
EMSA: D(11275986)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A059VIP8,A0A059VIQ1,A0A059VJK0,A0A059VNE0,A0A059VNE3,A0A059VNE7,A0A059VNM4,A0A059VNM8,A0A076G1E4,A0A076G284,A0A089N7R5,A0A089N7S9,A0A0C5FR62,A0A0C5FUK7,A0A0C5FUL8,A0A0C5G7Y2,A0A0C5G7Y5,A0A0D5CS67,A0A0D5ZYT6,A0A0M4AZY2,A0A0N9QU66,A0A0N9R7C8,A0A0S2E7X6,A0A0S2E831,A0A0U2QTF6,A0A0U2QTG8,A0A0U2QTK7,A0A0U2QTM0,A0A0U2YX27,A0A0U2YX58,A0A0U2ZNY5,A0A0U2ZPD7,A0A0U3AVN8,A0A0U3AVT2,A0A0U3I277,A0A0U3I8A2,A0A0U3IDX2,A0A0U3IE20,A0A0U3IE52,A0A0U3IE93,A0A0U3IEB5,A0A0U3IJH2,A0A0U3J8V8,A0A0U3J927,A0A0U3JAY8,A0A0U3JB52,A0A0U3JCG6,A0A0U3JCM7,A0A0U3JCQ7,A0A0U3JL94,A0A0U3JLC6,A0A0U3JLK2,A0A0U3JSW5,A0A0U3JWC6,A0A0U3JWG7,A0A0U3JWJ7,A0A0U3JWN1,A0A0U3K7C4,A0A0U3K7F7,A0A1B2AH91,A0A1B2AH95,A0A1B2AHB5,A0A1B2AHE3,A0A1B2AHE5,A0A1B2AHH7,A0A1C9HIX0,A0A1C9HIX9,A0A1D8V743,A0A1D8V772,A0A1D8V7D7,A0A1P8NVX0,A0A220NMJ5,A0A220NMS7,A0A220NMT0,A0A286LT27,A0A286LT38,A0A286R0Y2,A0A286R0Z6,A0A291L533,A0A291L5A1,A0A2D1LVN5,A0A2D1LVP3,A0A2D1LVP6,A0A2D1LVP7,A0A2D1LVP8,A0A2D1LVP9,A0A2D1LVQ0,A0A2D1LVQ5,A0A2D1LVQ7,A0A2D1LVR1,A0A2D1LVR3,A0A2D1LVR4,A0A2D1LVR6,A0A2D1LVR8,A0A2D1LVS2,A0A2D1LVS6,A0A2D1LVS8,A0A2D1LVT2,A0A2D1LVU2,A0A2D1LVU7,A0A2P0VG54,A0A2P0VGD5,A0A2P0VGY9,A0A2P0VHG1,A0A2P0VHX4,A0A2P0VIB7,A0A2P0VIU5,A0A2P0VIU9,A0A2P0VJB1,A0A2P0VJU1,A0A2P0VKB9,A0A2P0VKC2,A0A2P1HB01,A0A2P1HB02,A0A2P1HB15,A0A2P1HBA8,A0A2P1HBE1,A0A2P1HBH3,A0A2P1HBM3,A0A2P1HBR0,A0A2P1HBY2,A0A2P1HCG3,A0A2P1HCG9,A0A2P1HDE3,A0A2P1HE67,A0A2P1HEE5,A0A2P1HEF3,A0A2P1HEI2,A0A2P1HEJ9,A0A2P1HF36,A0A2P1HFT5,A0A2P1HFZ6,A0A2P1HG21,A0A2P1HGE7,A0A2P1HGM3,A0A2P1HGS9,A0A2P1HGX6,A0A2P1HHC8,A0A2P1HHQ0,A0A2P1HI11,A0A2P1HIG8,A0A2P1HIH1,A0A2P1HIR9,A0A2P1HJ72,A0A2P1HJF4,A0A2P1HJU7,A0A2P1HKA0,A0A2P1HKD0,A0A2P1HKP1,A0A2P1HKQ2,A0A2P1HKZ5,A0A2P1HL30,A0A2P1HL39,A0A2P1HL86,A0A2P1HLJ8,A0A2P1HLP0,A0A2P1HLP7,A0A2P1HM15,A0A2P1HM36,A0A2P1HM90,A0A2P1HME4,A0A2P1HMG4,A0A2P1HMG5,A0A2P1HMH9,A0A2P1HMJ0,A0A2P1HMQ1,A0A2P1HMT1,A0A2P1HMZ8,A0A2P1HN04,A0A2P1HN94,A0A2P1HNM9,A0A2P1HNV3,A0A2P1HNX7,A0A2P1HP96,A0A2P1HPQ3,A0A2P1HPX8,A0A2P1HQ86,A0A2P1HQE9,A0A2P1HQI1,A0A2P1HQJ9,A0A2P1HQK3,A0A2P1HQL5,A0A2P1HQL9,A0A2P1HR68,A0A2P1HRA2,A0A2P1HRC8,A0A2P1HRI0,A0A2P1HRR9,A0A2P1HS04,A0A2P1HS22,A0A2P1HS59,A0A2P1HSQ4,A0A2P1HSV1,A0A2P1HTP3,A0A2P1HTX2,A0A2P1HTZ5,A0A2P1HUS9,A0A2P1HUW9,A0A2P1HV39,A0A2P1HV98,A0A2P1HVX7,A0A2P1HW32,A0A2P1HX54,A0A2P1HXK4,A0A2P1HXQ6,A0A2P1HY06,A0A2P1HY11,A0A2P1HYJ5,A0A2P1HYN2,A0A2P1HZ06,A0A2P1HZ47,A0A2P1HZE4,A0A2P1HZX9,A0A2P1I0J5,A0A2P1I0M9,A0A2P1I102,A0A2P1I128,A0A2P1I1F2,A0A2P1I1I8,A0A2P1I1J9,A0A2P1I1X0,A0A2P1I1Z1,A0A2P1I1Z7,A0A2P1I2B1,A0A2P1I2B8,A0A2P1I2R1,A0A2P1I3F3,A0A2P1I3J7,A0A2P1I3Q5,A0A2P1I3X8,A0A2P1I3Z9,A0A2P1I419,A0A2P1I497,A0A2P1I4B0,A0A2P1I4E0,A0A2P1I4Z7,A0A2P1I4Z9,A0A2P1I543,A0A2P1I590,A0A2P1I5C9,A0A2P1I5D5,A0A2P1I5S2,A0A2P1I5X1,A0A2P1I643,A0A2P1I6U0,A0A2P1I704,A0A2P1I738,A0A2P1I741,A0A2P1I7I4,A0A2P1I7P4,A0A2P1I7P8,A0A2P1I7S1,A0A2P1I7Y6,A0A2P1I825,A0A2P1I830,A0A2P1I8M0,A0A2P1I8P9,A0A2P1I8Z1,A0A2P1I949,A0A2P1I9I0,A0A2P1I9T1,A0A2P1IA25,A0A2P1IA62,A0A2P1IA81,A0A2P1IAA7,A0A2P1IAG9,A0A2P1IB33,A0A2P1IB69,A0A2P1IBQ6,A0A2P1IBT0,A0A2P1IBW4,A0A2P1IBX1,A0A2P1IBY0,A0A2P1IC50,A0A2P1ICA0,A0A2P1ID20,A0A2P1IDC6,A0A2P1IDD8,A0A2P1IDN9,A0A2P1IDU8,A0A2P1IDV8,A0A2P1IDW3,A0A2P1IE23,A0A2P1IE68,A0A2P1IEA9,A0A2P1IEF5,A0A2P1IEX8,A0A2P1IFE8,A0A2P1IFG8,A0A2P1IFS0,A0A2P1IFV9,A0A2P1IFX6,A0A2P1IFY1,A0A2P1IG57,A0A2P1IG80,A0A2P1IG87,A0A2P1IGG0,A0A2P1IGW0,A0A2P1IGX6,A0A2P1IH24,A0A2P1IHC7,A0A2P1IHE2,A0A2P1IHI4,A0A2P1II23,A0A2P1IIF0,A0A2P1IIJ4,A0A2P1IIR6,A0A2P1IJK4,A0A2P1IJR0,A0A2P1IJR1,A0A2P1IK24,A0A2P1IK64,A0A2P1IK80,A0A2P1IK89,A0A2P1IKC0,A0A2P1IKF2,A0A2P1IKI0,A0A2P1IKJ2,A0A2P1IKU9,A0A2P1IL87,A0A2P1ILI8,A0A2P1ILK1,A0A2Z5DHD3,A0A2Z5DHF0,A0A384K9E7,A0A384K9Q3,A0A384KEH1,A0A384KKG5,A0A384KQK8,A0A384LDF5,A0A384LH07,A0A384LI46,A0A384LQE2,A0MPS4,A1YQC0,A1YT18,A1YT19,A3RM07,A3RM08,A4L2Z5,A4L2Z7,A4L313,A7LCD3,B1A8X8,B1N828,B1N831,B7T163,B7T167,B7T1G5,B7T1G7,B7T1H5,B7T1I2,B9UPB5,C0KXJ9,C0KXK0,C0KXK2,C0KXK3,C0KXK6,C0KXK7,C0KXK9,C0KXL0,C0KXL2,C0KXL4,C0KXL6,C0KXL9,C0KXM0,C0KXM1,C0KXM3,C0KXM5,C6G881,D5LNF2,D7RGM7,E1A4A4,G0WKQ5,G0WKQ6,G9HQC8,G9HQD8,G9HQE8,G9HQF1,H6VNE9,H6VNF0,H6VNF1,H6VNF2,H6VNF3,H6VNF4,H6VNF5,H6VNF6,H6VNF7,H6VNF8,H6VNF9,H6VNG0,H6VNG2,H6VNG4,H6VNG6,H6VNG7,H6VNG8,H6VNH0,H6VNH1,H6VNH2,H6VNH3,H6VNH4,H6VNH5,H6VNH7,H6VNH8,H6VNH9,H6VNI0,H6VNI2,H6VNI3,H6VNI4,H6VNI5,H6VNI6,H6VNI7,H6VNI8,H6VNI9,H6VNJ0,H6VNJ1,H6VNJ2,H6VNJ3,H6VNJ4,H6VNJ5,H6VNJ6,H6VNJ9,H6VNK0,H6VNK1,H6VNK3,H6VNK4,J3T208,J9ZYN7,J9ZYY5,J9ZZ15,J9ZZ21,K0A0D0,N0DLZ7,N0DM07,N0DRU0,N0DRU7,Q2PJN9,Q4VRN5,Q547J2,Q71BH9,Q778I6,Q77JC7,Q8JMU8,Q8QHN0,Q8QHP5,Q8QHT0,Q8QRD5,Q8QRD6,Q8QRD7,Q8QRD8,Q8QRD9,Q8QRE0,Q8QRE1,Q919A9,Q919B1,Q919C6,Q919D4,Q9QDH3,Q9QDH5,Q9QDH7,Q9QDH9,Q9W931,Q9WH13,S5TCK5,S5TDM3,S5TDR0,S5THQ0,S5THX6,S5TL73,S5TL98,S5TLA4,S5TQ97,S5U276,S5U2B7,S5U2Z7,S5U365,S5U371,S5U3B0,S5U3D5,S5U3E1,S5U7G7

Functional_annotation:
Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway.


Viral_family: Papillomaviridae
Species: Human papillomavirus type 16
Name: E7
Aliases: Protein E7
UniProtID_Ref: P03129
UniProt_Name_Ref: VE7_HPV16
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: D(22099967)
ChIP_seq: N
Structure_PDB_ID: 4YOZ, 6APN
Reporter_assay: D(22210627, 7933087, 9426463, 11039910)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A059PVS3,A0A059PVS5,A0A059PVS7,A0A059PVT2,A0A059PVT4,A0A059PVT6,A0A059PVU6,A0A059PVU7,A0A059PVU9,A0A059PVV2,A0A059PVW7,A0A059PVX1,A0A076G1E9,A0A076G292,A0A076G3A1,A0A076G7W8,A0A089N7T4,A0A0G2YFL8,A0A0G2YJI6,A0A0G2YL83,A0A0H4CN15,A0A0H4CQU3,A0A0M5I281,A0A159DWG2,A0A1B2AH93,A0A1B2AHI1,A0A1B2AHJ8,A0A289SF75,A0A289SFD2,A0A289SFF8,A0A289SFI7,A0A289SFR6,A0A289SFX4,A0A289SG08,A0A289SM88,A0A289SMC3,A0A289SME7,A0A289SMJ4,A0A289SMN5,A0A289SMS4,A0A289SMW3,A0A289SPS0,A0A289SPX7,A0A289SQ04,A0A289SQ43,A0A289SQA6,A0A289SQL8,A0A289SZM6,A0A289SZX7,A0A289T025,A0A289T0B9,A0A289T0E2,A0A289T0G1,A0A289TIL4,A0A289TIQ9,A0A289TIW2,A0A289TIZ2,A0A289TJ28,A0A289TJ61,A0A291S0D2,A0A291S0D3,A0A291S0D8,A0A291S0E0,A0A291S0E9,A0A291S0F0,A0A291S0F1,A0A291S0F3,A0A291S0F7,A0A291S0F8,A0A291S0G1,A0A291S0G3,A0A291S0G4,A0A291S0G5,A0A291S0G8,A0A291S0H0,A0A291S0H1,A0A291S0H3,A0A291S0H7,A0A291S0I0,A0A291S0I3,A0A2C9DJ22,A0A2C9DJ24,A0A2C9DJ25,A0A2C9DJ27,A0A2C9DJ29,A0A2C9DJ31,A0A2C9DJ33,A0A2C9DJ34,A0A2C9DJ36,A0A2C9DJ38,A0A2C9DJ40,A0A2C9DJ42,A0A2C9DJ43,A0A2C9DJ45,A0A2C9DJ47,A0A2C9DJ49,A0A2C9DJ51,A0A2C9DJ52,A0A2C9DJ54,A0A2C9DJ56,A0A2C9DJ58,A0A2C9DJ60,A0A2C9DJ61,A0A2C9DJ63,A0A2C9DJ65,A0A2C9DJ67,A0A2C9DJ69,A0A2C9DJ70,A0A2C9DJ72,A0A2C9DJ74,A0A2C9DJ76,A0A2C9DJ78,A0A2C9DJ79,A0A2C9DJ81,A0A2C9DJ83,A0A2C9DJ85,A0A2C9DJ87,A0A2C9DJ88,A0A2C9DJ90,A0A2C9DJ92,A0A2C9DJ94,A0A2C9DJ96,A0A2C9DJ97,A0A2C9DJ99,A0A2C9DJA1,A0A2C9DJA3,A0A2C9DJA5,A0A2C9DJA6,A0A2C9DJA8,A0A2C9DJB0,A0A2C9DJB2,A0A2C9DJB4,A0A2C9DJB5,A0A2C9DJB7,A0A2C9DJB9,A0A2C9DJC1,A0A2P0VGD6,A0A2P0VGD7,A0A2P0VGZ1,A0A2P0VHG2,A0A2P0VHG5,A0A2P0VHY0,A0A2P0VHY3,A0A2P0VIC2,A0A2P0VIV5,A0A2P0VJB3,A0A2P0VJU6,A0A2P0VKC6,A0A2P1HCE8,A0A2P1HF34,A0A2P1HG37,A0A2P1HIW7,A0A2P1HJR6,A0A2P1HJS5,A0A2P1HJZ9,A0A2P1HKE3,A0A2P1HKM2,A0A2P1HLI0,A0A2P1HME9,A0A2P1HMR8,A0A2P1HNA9,A0A2P1HNK2,A0A2P1HNX3,A0A2P1HPZ2,A0A2P1HRS5,A0A2P1HS38,A0A2P1HT93,A0A2P1HTU4,A0A2P1HTU6,A0A2P1HU85,A0A2P1HUE1,A0A2P1HUQ8,A0A2P1HV03,A0A2P1HV70,A0A2P1HWM3,A0A2P1HWX3,A0A2P1HXT8,A0A2P1HYA9,A0A2P1HYI5,A0A2P1HYV4,A0A2P1HZB6,A0A2P1HZJ7,A0A2P1HZQ7,A0A2P1HZY9,A0A2P1I050,A0A2P1I084,A0A2P1I1X1,A0A2P1I1Y2,A0A2P1I277,A0A2P1I2C5,A0A2P1I369,A0A2P1I3T1,A0A2P1I4H2,A0A2P1I589,A0A2P1I5V8,A0A2P1I5W2,A0A2P1I681,A0A2P1I752,A0A2P1I7N9,A0A2P1I898,A0A2P1I8U1,A0A2P1I8V3,A0A2P1I8Y6,A0A2P1I8Z6,A0A2P1I911,A0A2P1I9B3,A0A2P1I9B5,A0A2P1I9F6,A0A2P1I9K6,A0A2P1I9V6,A0A2P1IA20,A0A2P1IBS1,A0A2P1IBV2,A0A2P1ID77,A0A2P1IDR9,A0A2P1IDZ5,A0A2P1IE20,A0A2P1IE97,A0A2P1IHA0,A0A2P1IHZ3,A0A2P1II29,A0A2P1IJ05,A0A2P1IJ29,A0A2P1IJF7,A0A2P1IJW8,A0A2P1IK25,A0A2P1IKM7,A0A2P1ILF9,A0A2Z5DHM3,A0A384LCP1,A0A384LMA3,A0A384LNE6,A0MPS5,A0MPS6,A0MPS7,A1YQD4,A1YQD5,A1YQD6,A1YQD7,A1YQD8,A1YQD9,A1YQE0,A1YQE1,B7T164,B9UPB6,C0KXQ4,C0KXQ5,D7RGM8,G0WKQ8,J9Q2I8,J9Q2V6,J9Q2W0,J9Q391,J9Q3Y3,J9Q4N7,J9Q4P1,K0F2R1,K0F2S0,K0F2T0,K0F2T8,K0F2U7,K0F2V7,K0F2W6,K0F2X5,K0F2Y7,K0F300,K0F312,K0F9K7,K0F9L4,K0F9M5,K0F9N3,K0F9P2,K0F9Q2,K0F9Q8,K0F9Q9,K0F9R8,K0F9S1,K0F9S7,K0F9S9,K0F9T5,K0F9T8,K0F9U6,K0F9U7,K0F9V4,K0F9V8,K0F9W3,K0F9X1,K0F9X9,K0F9Y7,K0F9Z4,K0FA01,K0FAG8,K0FAH3,K0FAH8,K0FAI6,K0FAJ4,K0FAK5,K0FAL4,K0FAM6,K0FAN4,K0FAP2,K0FAQ5,K0FAR6,K0FFB1,K0FFC3,K0FFD3,K0FFE3,K0FFF2,K0FFG1,K0FFG8,K0FFH7,K0FFI7,K0FFJ6,K0FFK5,K0FFL4,O11650,O12337,O12338,Q2MJT4,Q547B8,Q778G4,Q778G6,Q778G8,Q778G9,Q778H1,Q778H2,Q778H3,Q778H5,Q778H7,Q778H9,Q778I0,Q778I1,Q778I3,Q778I5,Q77AI1,Q77GV7,Q8B5P6,Q8QRD2,Q8QRD3,Q8QRD4,Q8V1J0,Q9QDH2,Q9QDH4,Q9QDH6,Q9QDH8,R4UNR4,R4UNS0,R4UNS5,R4URG4,R4URH2,R4URH7,R4UZM3,R4UZM8,R4UZN4,R4V4T8,R4V4U3,R4V4U7,R4V4V0,R4V788,R4V795,R4V7A2,R9QVU4,S4S7U0,S4S7U2,S4S7U5,S4S7U9,S4S7V5,S4S7V7,S4S7V9,S4S7W1,S4S7W3,S4S7W5,S4S7W7,S4S7W9,S4S7X1,S4S7Y4,S4S868,S4S877,S4S884,S4S891,S4S895,S4S898,S4S8A1,S4S8A4,S4S8A6,S4S8A9,S4S8B1,S4S8B5,S4S8B8,S4S8M4,S4S8N2,S4S8N9,S4S8Q3,S4S8Q9,S4S8R3,S4S8R7,S4S8S1,S4S8S4,S4S8S8,S4S8T0,S4S8T4,S4S8T9,S4S8U0,S4S8U3,S4S8U4,S4S8V1,S4S8W3,S4S8X0,S4S8X6,S4S8Y0,S4S8Y3,S4S8Y7,S4S8Z1,S4S8Z4,S4S8Z7,S4S902,S4S9B2,S4S9B9,S4S9C6,S4S9D2,S4S9E0,S4S9E5,S4S9E8,S4S9F1,S4S9F4,S4S9F8,S4S9G0,S4S9G4,S4S9G8,S4S9H0,S4U723,S4U729,S4U736,S4U7T5,S4U7U0,S4U954,S4U959,S4UB75,S4UB84,S4UDF6,S4UDG0,T1R4E0,T1R4E3,T1R539

Functional_annotation:
Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Plays also a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).


Viral_family: Papillomaviridae
Species: Human papillomavirus type 5
Name: E6
Aliases: Protein E6
UniProtID_Ref: P06930
UniProt_Name_Ref: VE6_HPV05
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: I(15664194)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(31002735, 11275986, 22210627)
EMSA: I(11275986)
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A221SN86,A0A221SN96,A9XCP0,A9XCP7,A9XCQ4,A9XCR8,F8RC52,F8RC53,F8RC54,P24836,P26556,Q4PZJ4,Q4PZJ5,Q4PZJ6,Q4PZJ7,Q4PZJ8,Q4PZJ9,Q4PZK0,Q6LBH6,Q76WJ7,Q80927,Q81962,Q81985,Q81986,R9QCH1


Viral_family: Papillomaviridae
Species: Human papillomavirus type 5
Name: E7
Aliases: Protein E7
UniProtID_Ref: P06932
UniProt_Name_Ref: VE7_HPV05
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: I(22099967)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(22210627, 7933087, 9426463, 11039910)
EMSA: N
Other_assays: N
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A075LXE0,A0A075LYA7,A0A075LYB3,A0A075LYW2,A0A0N7I701,A0A0P0E4Z9,A0A0P0EBY8,A0A0P0EGY4,A0A0P0EME8,A0A140FA98,A0A140FAA6,A0A159DZX5,A0A192YER2,A0A192YG58,C7DYE0,C7DYE2,C7DYE4,C7DYE6,C7DYE8,C7DYF0,C7DYF2,C7DYF4,C7DYF6,C7DYF8,C7DYG0,C7DYG2,C7DYG4,C7DYG6,C7DYG8,C7DYH0,C7DYH2,C7DYH4,C7DYH6,C7DYH8,C7DYI0,C7DYI2,C7DYI4,C7DYI6,C7DYI8,C7DYJ0,C7DYJ2,C7DYJ4,C7DYJ6,C7DYJ8,C7DYK0,C7DYK2,C7DYK4,C7DYK6,C7DYK8,C7DYL0,C7DYL2,D0EDB6,F1AST1,F1AST2,F8S525,F8S541,F8S581,N0DP29,N0DQQ9,P26559,P36831,Q76WJ6,Q81019,Q8B5X6,R9QBR6


Viral_family: Paramyxoviridae
Species: Hendra virus
Name: Phosphoprotein
Aliases: Protein P, P/V/C
UniProtID_Ref: O55778
UniProt_Name_Ref: PHOSP_HENDH
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4HEO
Reporter_assay: I(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 25281398.0
Functional_annotation:
Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity).


Viral_family: Paramyxoviridae
Species: Human parainfluenza virus 1
Name: Phosphoprotein
Aliases: P, P/C, Protein P, P/V/C
UniProtID_Ref: P32530
UniProt_Name_Ref: PHOSP_PI1HB
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 12692097.0
Functional_annotation: This protein is probably a component of the active polymerase. It may function in template binding.
UniProt_IDs_Orthologs:
A0A059QA57,A0A059QA62,A0A059QA70,A0A059QA80,A0A059QAA8,A0A0G2R217,A0A1B2CW80,A0A1B2CW98,J7FNR1,J7FNT1,J7FNV2,J7FNW9,J7FNZ0,J7FP15,J7FP39,J7FP63,J7FQG2,J7FQI5,J7FQK8,J7FQL3,J7FQM7,J7FQP8,J7FQS6,J7FQV6,J7FQY2,J7FQY6,J7FSL2,J7FSN8,J7FSR7,J7FSU6,J7FSX6,J7FT03,J7FT30,J7FT61,J7FV05,J7FV29,J7FV56,J7FV78,J7FVA3,J7FVD2,J7FVG2,J7FVJ3,J7FXC5,J7FXE6,J7FXJ1,J7FXL5,J7FXN8,P28054,P32531,P32532,Q8QT31,T1UCF4,T1UCG6,T1UCH5,T1UF53,T1UF64,T1UF81,T1UF92,T1UFA1,T1UFB1


Viral_family: Paramyxoviridae
Species: Human parainfluenza virus 2
Name: Phosphoprotein
Aliases: Protein P, P/V
UniProtID_Ref: P23056
UniProt_Name_Ref: PHOSP_PI2HT
UniProt_IDs_Orthologs: P23055
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 12692097.0
Functional_annotation:
Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.


Viral_family: Paramyxoviridae
Species: Human parainfluenza virus 3
Name: Phosphoprotein
Aliases: P, Protein P, P/V/D
UniProtID_Ref: P06162
UniProt_Name_Ref: PHOSP_PI3H4
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 12692097.0
UniProt_IDs_Orthologs:
A0A023PFB4,A0A023PFG3,A0A023PFL0,A0A023PFQ5,A0A023PFZ5,A0A023PG51,A0A023PG69,A0A023PGA3,A0A023PGB4,A0A023PGD8,A0A023PGK3,A0A023PGS2,A0A023PGV1,A0A023PGY1,A0A023PGZ3,A0A023PH10,A0A023PH42,A0A023PH43,A0A023PH67,A0A023PH76,A0A023PH96,A0A023PHA5,A0A023PHD4,A0A023PHE7,A0A023PHF9,A0A023PHI5,A0A023PHI8,A0A023PHJ3,A0A023PHL9,A0A023PHN2,A0A023PHQ2,A0A023PHR4,A0A023PHS5,A0A023PHT7,A0A023PHX6,A0A023PI22,A0A023PI55,A0A023PI62,A0A023PI93,A0A023PIC6,A0A023PIJ5,A0A059Q9Z8,A0A059QA10,A0A059QA21,A0A059QA33,A0A059QA45,A0A059QA55,A0A059QA84,A0A059QAB7,A0A059QAB8,A0A059QAE1,A0A059QAF7,A0A059QAG4,A0A059QAH6,A0A059QAI0,A0A059QAJ6,A0A059QAM4,A0A059QBW4,A0A059QBZ1,A0A059QC16,A0A059QC39,A0A059QC70,A0A059QC91,A0A059QDV8,A0A059QDY9,A0A059QE20,A0A059QE50,A0A059QE92,A0A059QEF4,A0A0G2R241,A0A1C9FM37,A0A1C9FM46,A0A1C9FM56,A0A1C9FM77,A0A1C9FM79,A0A1C9FM80,A0A1C9FM90,A9Z0P3,B1A5Q1,B3GQS8,B8XXB5,O89234,Q81076,Q84742,R4X5Y3,T1UCU1,T1UCW0,T1UCY2,T1UD00,T1UD33,T1UD36,T1UD58,T1UD73,T1UE22,T1UE62,T1UEB9,T1UEG1,T1UFF6,T1UFJ6,T1UFQ1,U5L3E2

Functional_annotation:
Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.


Viral_family: Paramyxoviridae
Species: Measles virus
Name: Phosphoprotein
Aliases: C, P, Protein P, P/V
UniProtID_Ref: P35974
UniProt_Name_Ref: PHOSP_MEASA
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4BHV, 4C5Q
Reporter_assay: I(7491765)
EMSA: N
Other_assays: D(31381607, 8578862)
Human_infection_evidence: 25483511.0
UniProt_IDs_Orthologs:
A0A076FF09,A0A0A7DYR3,A0A0M3TG67,A0A0M3TG73,A0A0M3TG74,A0A0M3TG86,A0A0M3TG91,A0A0M3TGB0,A0A0M3TGC6,A0A0M4MCX4,A0A0M4MD66,A0A0M4MMI7,A0A0M4MQY5,A0A0M4N184,A0A0M4NEZ8,A0A0S1LL08,A0A0S1LL25,A0A140G963,A0A158UZJ4,A0A158V0F3,A0A158V2K3,A0A161UC10,A0A1C9U7M5,A0A1Z1ED88,A0A1Z1EDF0,A0A1Z1EDF8,A0A2R4LPH0,A0A2U7XVG9,A0A343LQ65,A0A3Q8BM42,A0A3Q8GW16,A0A3Q8GW50,A0A3Q8GW72,A0A3Q8GYD4,A0A3Q8GZ35,A0A3Q8H141,A0A3S5GNX2,A4URT3,A7XPM0,A7XPM1,A7XPM2,A7XPM3,A7XPM4,A7XPM5,A7XPM6,A7XPM7,A7XPM8,A7XPM9,A7XPN0,A7XPN1,A7XPN2,A7XPN3,A7XPN4,A7XPN5,A9YTL4,A9YTM2,B1AAA8,B1GX84,B1GX85,B1GX86,B1GX87,B1GX88,B1GX89,B1GX90,B1GX91,B1GX92,B1GX93,B1GX94,B1GX95,B1GX96,B1GX97,B1GX98,B1GX99,B1GXA0,B1GXA1,B2BML3,B2KPM4,B7TB11,B8PZQ7,B9A7E8,B9A7L7,C6L654,C8CAZ2,E2I6N2,E2I9Q7,E5RS81,E7DW48,E7DW50,E7DW52,E7DW54,E7DW62,E7DW64,E7DW68,E7DW70,E7DW72,E7DW76,E7DW78,E7DW80,E7DW84,E7DW86,E7DW92,E7DW94,E7DW96,E7DW98,E7DWA2,E7DWA8,E7DWB0,E7DWB2,E7DWB6,E7DWB8,E7DWC4,E7DWC6,E7DWC8,E7DWD0,E7DWD2,E7DWD4,E7DWD6,E7DWD8,E7DWF5,E7DWG1,E7DWG3,E7DWG5,E7DWG7,E7DWG9,E7DWH2,E7DWH4,E7DWH6,E7DWH8,E7DWI0,E7DWI4,E7DWI7,E7DWI9,E7DWJ1,E7DWJ3,E7DWJ7,E7DWJ9,E7DWK1,E7DWK3,E7DWK5,E7DWK7,E7DWL7,E7DWM1,E7DWM3,E7DWM5,E7DWM9,F1BCV1,F1BCV2,F1BCV3,F1BCV4,F1BCV5,F1BCV6,F1BCV7,F1BCV9,F1BCW3,F1BCW5,F1BCW6,F1BCW7,F1BCX0,F1BD28,F1BD31,F1BD34,F1BD35,F1BD37,F1BD45,F1BD46,F1BD53,F1BD54,F1BD55,F1BD57,F1BD59,F1BD61,F1BD62,F1BD64,F1BD65,F1BD67,F1BD69,F1BD71,F1BD77,F1BD78,F1BD79,F1BD80,F1BD84,F6I820,F6I821,F6I823,F6I825,F6I826,F6I828,F6I832,F6I833,F6I834,F8U897,G4XDT2,G5DD33,G5DD41,G5DD49,G5DD57,G5DD65,G5DD73,G5DD81,G5DD89,G5DD97,K9N4J4,K9N4K5,K9N5R1,P03422,P26033,P90485,Q00793,Q04159,Q2LJ39,Q2LJ47,Q2LJ55,Q2LJ63,Q76VZ7,Q77M20,Q77M25,Q77M31,Q77M42,Q783Q7,Q83320,Q83321,Q83623,Q8JQ52,Q8JT18,Q8JT21,Q9IC38,Q9IFK7,Q9WMB4,Q9YZZ2,Q9YZZ5,W8VRE9,X5D6I5,X5D6J1,X5D6J8,X5D6K5,X5D6L1,X5D6L7,X5D6M5,X5D6N2,X5D6Q1,X5D6Q9,X5D6R4,X5D6R7,X5D6S0,X5D6S4,X5D6S8,X5D6T1,X5D6T4,X5D6T9,X5DBD8,X5DBE2,X5DBE7,X5DBF3,X5DBF8,X5DBG3,X5DBG7,X5DBI4,X5DBJ2,X5DBJ6,X5DBJ9,X5DBK3,X5DBK6,X5DBL0,X5DBL3,X5DBL6,X5DBM0,X5DBM2,X5DBZ6,X5DD01,X5DD05,X5DD11,X5DD18,X5DD25,X5DD33,X5DD39,X5DD46,X5DD65,X5DD68,X5DD72,X5DD76,X5DD80,X5DD84,X5DD88,X5DD90,X5DD96,X5DDA1,X5DST0,X5DST5,X5DSU2,X5DSV0,X5DSV8,X5DSW3,X5DSW8,X5DSX2,X5DSZ1,X5DSZ4,X5DSZ8,X5DT03,X5DT07,X5DT10,X5DT14,X5DT19,X5DT23,X5DT28,X5DT32,X5DVE4,X5DVE9,X5DVF5,X5DVF9,X5DVG3,X5DVG9,X5DVH5,X5DVI1,X5DVK0,X5DVK9,X5DVL2,X5DVL5,X5DVL8,X5DVM1,X5DVM5,X5DVM9,X5DVN1,X5DVN3


Viral_family: Paramyxoviridae
Species: Nipah virus
Name: Phosphoprotein
Aliases: Non-structural protein V, P, Protein W, P/V/C, P/V/W/C, V protein, W protein
UniProtID_Ref: Q4VCQ1
UniProt_Name_Ref: Q4VCQ1_NIPAV
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4N5B
Reporter_assay: I(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 30647521.0
UniProt_IDs_Orthologs:
A0A1L7B8D0,A0A1L7B8D3,A0A3G1QY20,A0A3G1QY27,A0A3G1QY38,D2DEB8,E2II04,H6V847,H6V848,H6V860,H6V869,H6V870,H6V871,Q4VCP9,Q4VCQ0,Q997F2

Functional_annotation:
RNA binding;RNA-directed 5'-3' RNA polymerase activity;transcription, DNA-templated;viral genome replication


Viral_family: Parvoviridae
Species: Adeno-associated virus
Name: Rep52
Aliases: Protein Rep52
UniProtID_Ref: Q89270
UniProt_Name_Ref: REP52_AAV2S
Binding_ligand: indirect/unknown
Function: TR, NAP, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(16775308)
Other_assays: D(12824181)
Human_infection_evidence: 21212830.0
Functional_annotation:
Plays a critical role during packaging of viral DNA into empty capsids, where they are thought to be part of the packaging motor complex. The single stranded genomic DNA is packaged in a 3' to 5' direction and requires the association between viral DNA and Rep40. Regulates host PKA activity by interacting with host PRKX as a mechanism to interfere with helper virus propagation and to promote its own replication.


Viral_family: Parvoviridae
Species: Adeno-associated virus
Name: Rep68
Aliases: Protein Rep68
UniProtID_Ref: P03132
UniProt_Name_Ref: REP68_AAV2S
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 1S9H, 1U0J, 4ZO0, 4ZQ9, 5DCX
Reporter_assay: D(1845899)
EMSA: D(16775308, 15596798)
Other_assays: D(16775308, 15596798)
Human_infection_evidence: 21212830.0
Functional_annotation:
Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Plays also a role as transcriptional regulator, DNA helicase and as key factor in site-specific integration of the viral genome. Inhibits the host cell cycle G1/S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication.


Viral_family: Parvoviridae
Species: Adeno-associated virus
Name: Rep78
Aliases: Protein Rep78
UniProtID_Ref: Q89268
UniProt_Name_Ref: REP78_AAV2S
UniProt_IDs_Orthologs: A9RAH9,O56136,O56138,Q670Q9,Q670R1,Q670R3,Q670R5,Q670R7
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: D(15596798)
ChIP_seq: N
Structure_PDB_ID: 5BYG
Reporter_assay: D(10531369, 1845899)
EMSA: D(10531369, 10666281, 16775308)
Other_assays: N
Human_infection_evidence: 21212830.0
Functional_annotation:
Plays an essential role in the initiation of viral DNA synthesis. Binds specifically to an inverted terminal repeat element (ITR) on the 3' and 5' ends of the viral DNA, where it cleaves a site specifically to generate a priming site for initiation of the synthesis of a complementary strand. Plays also a role as transcriptional regulator, DNA helicase and as key factors in site-specific integration of the viral genome. Regulates host PKA activity by interacting with host PRKX as a mechanism of interfering with helper virus propagation and promoting its own replication. Inhibits the host cell cycle G1/S, S and G2/M transitions. These arrests may provide essential cellular factors for viral DNA replication.


Viral_family: Parvoviridae
Species: Human parvovirus 4
Name: NS1
UniProtID_Ref: F6KS47
UniProt_Name_Ref: F6KS47_9VIRU
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8970971)
EMSA: I(27809499, 24418564)
Other_assays: I(27809499, FA), I(11853402, Dnase I footprinting)
Human_infection_evidence: 22492853.0
Notes: F6KS47 is inferred from Adeno-associated virus protein Q89270
Functional_annotation: ATP binding,DNA replication,viral genome replication
Aliases:
Nonstructural protein, Nonstructural protein 1, Nonstructural protein 1,, Non-structural protein, ORF1

UniProt_IDs_Orthologs:
A0A0C4L654,A0A0C4L9E0,A7J3Q4,A7J3Q8,B0YZG4,B0YZG8,B0YZI4,D0FM80,D0FM90,D1M7U5,F6KS50,H9A241,H9A247,H9A250,H9A253,J9PN41,J9PNK6,J9PNL4,J9PPZ7


Viral_family: Parvoviridae
Species: Human parvovirus B19
Name: NS1
UniProtID_Ref: Q9PZT1
UniProt_Name_Ref: NS1_PAVHV
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8970971)
EMSA: D(27809499, 24418564)
Other_assays: D(27809499, FA), D(11853402, Dnase I footprinting)
Human_infection_evidence: 22492853.0
Aliases:
Initiator protein NS1, NCVP1, Non-capsid protein NS-1, Non-structural protein 1, Non-structural protein NS1

UniProt_IDs_Orthologs:
A0A076JV48,A0A076JZ43,A0A077B001,A0A097C0L5,A0A097C0M3,A0A097C0M7,A0A097C0N6,A0A0N9H666,A0A0N9H6S8,A0A0N9H8I9,A0A0N9H9D5,A0A0N9H9F8,A0A0S2Z242,A0A0S2Z256,A0A0S2Z2A0,A0A0S2Z2D7,A0A0S2Z2F9,A0A0S2Z2I2,A0A0S2Z2I4,A0A0S2Z2K1,A0A0S2Z2K5,A0A0S2Z2K8,A0A0S2Z2M3,A0A0S2Z2P9,A0A0S2Z2X0,A0A0S2Z356,A0A0X8XHP5,A0A223LL20,A0A3Q9D3C3,A0A3R5YZH1,A1A400,A1BML3,A1BML8,A3F778,B8YQ89,D2EBU8,D4AHY8,D6CHV0,E5L8C4,E5L8C6,I7BP20,J3SB70,J3SB73,J3SB76,J3SB79,J3SB82,J3SB85,J3SB88,J3SB91,J3SB94,J3SB97,J3SBA0,J3SBA3,J3SBA6,J3SET8,J3SEV0,J3SIA5,J3SIB2,J3SMR7,J3SMS1,J3SMS4,J3SMS7,J3SMT0,J3SMT3,J3SMT6,J3SMT9,J3SMU2,J3SMU5,J3SMU8,J3SMV1,J3SMV4,J3SN47,J3SN59,J3SN73,J3SN76,J3SN79,J3SN82,J3SN85,J3SN88,J3SN91,J3SN94,J3SN97,J3SNA0,J3SNA3,J7FCE3,J7FCE6,J7FCE9,J7FCF4,J7FCF7,J7FCQ7,J7FCR0,J7FCR7,J7FCS0,J7FD52,J7FD55,J7FD60,J7FD63,J7FDJ3,J7FDJ6,J7FDJ9,J7FDK2,J7FDZ9,J7FE02,J7FE05,J7FE08,J7FE11,Q206Z8,Q207A1,Q207A4,Q207A7,Q207B0,Q2I001,Q2I006,Q2MJ80,Q2MJ83,Q2MJ86,Q2PZ28,Q308H9,Q308I3,Q38IT5,Q38IU0,Q38IU5,Q38IV0,Q3KTM4,Q6DT44,Q6KBB7,Q6RCN2,Q6TV13,Q75U70,Q75U73,Q75U76,Q75U79,Q75U85,Q75U88,Q75U94,Q8JN58,Q913X2,Q9JGP9,Q9JGQ0,Q9JGS1,Q9PZT3,Q9PZT5,Q9PZT7,Q9PZT9,Q9PZU1,Q9WKM1,S5YS34,S5YS39,S5YS41,S5YS44,S5YSP7,S5YY54,S5YY89,S5YY94,S5YYA5,S5YYB0,S5YYB6,S5YYC7,S5YYD9,S5YYE2,S5YYF0,S5Z5M0,S5Z5U6,S5Z5V2,S5Z611,S5ZHB5,S5ZHF2,S5ZHP5,S5ZHQ1,S5ZHQ5,S5ZHQ9,S5ZXZ5,S5ZXZ7,S5ZY10,S5ZY14,S5ZY63,S5ZY70,S5ZY80,S5ZY87

Functional_annotation:
Multifunctional protein essential for viral DNA replication, which cooperatively interacts with the viral DNA origin of replication and transactivates several promoters including the viral p6 promoter (PubMed:27809499, PubMed:24418564, PubMed:11853402). Binds the origin of replication and performs an endonucleolytic nick within a conserved sequence in the viral genome, thereby initiating the rolling circle replication (RCR) (PubMed:27809499). Participates in the transcriptional regulation the viral p6 promoter that regulates all viral transcripts and the cellular CDN1A or IL6 promoters (PubMed:8970971, PubMed:11853402). Transactivates several host promoters some of which induce the S cell cycle phase for the production of host replicative proteins (PubMed:20890043, PubMed:15518826, PubMed:24049177). Upregulates the expression of host E2F4 and E2F5 and interacts with both these factors thereby inhibiting the host cell cycle G2/M transition (PubMed:20890043). This arrest promotes apoptosis for viral release (PubMed:20890043, PubMed:9525624).


Viral_family: Peribunyaviridae
Species: Bunyamwera virus
Name: N
Aliases: Non-structural protein NS-S, NS
UniProtID_Ref: P16494
UniProt_Name_Ref: NSS_BUNYW
UniProt_IDs_Orthologs: A0A0A7KU45,A0A0A7KY99,A0A0G2T176,A0A0G2T1F8,A0A0G2T1M9,A0A0G2T1U8,A0A0U2GIU0,G4Y821,Q8V617
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15150262)
EMSA: N
Other_assays: N
Human_infection_evidence: 29707545.0
Functional_annotation:
Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1.


Viral_family: Peribunyaviridae
Species: Bunyavirus La Crosse
Name: N
Aliases: Non-structural protein NS-S, NSs
UniProtID_Ref: P04874
UniProt_Name_Ref: NSS_BUNLC
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(15150262)
EMSA: N
Other_assays: N
Human_infection_evidence: 26375904.0
UniProt_IDs_Orthologs:
A5HC88,D3K4J5,D3K4J7,D3K4J9,D3K4K1,D3K4K3,D3K4K5,D3K4K7,D3K4K9,D3K4L1,D3K4L3,D3K4L5,D3K4L7,D3K4L9,D3K4M1,D3K4M3,D3K4M5,D3K4M7,D3K4M9,D3K4N1,D3K4N3,D3K4N5,D3K4N7,D3K4N9,D3K4P1,D3K4P3,D3K4P5,D3K4P7,D3K4P9,D3K4Q1,D3K4Q3,D3K4Q5,D3K4Q7,D3K4Q9,D3K4R1,D3K4R3,D3K4R5,D3K4R7,D3K4R9,D3K4S1,D3K4S3,D3K505,D3K507,D3K509,D3K511,D6NSL4,D6NSL8,F6JSE2,F6JSG2,F6JSH4,P09614,Q8JPQ9,Q917M9

Functional_annotation:
Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1 (By similarity).


Viral_family: Phenuiviridae
Species: Rift valley fever virus
Name: NSs
Aliases: Non-structural protein S
UniProtID_Ref: P21698
UniProt_Name_Ref: NSS_RVFVZ
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 2N0Y, 5OOO
Reporter_assay: D(22345363, 15331713)
EMSA: N
Other_assays: D(15331713)
Human_infection_evidence: 21188836.0
UniProt_IDs_Orthologs:
A0A3S5XDL9,A7KBW6,A7KBW7,O72702,O73535,O73536,O73537,O73538,O73539,O73540,O73541,O73542,O73543,O73544,O73545,O73546,O73547,O73548,O73549,Q7T6F4,Q7T6F5,Q8JUF9

Functional_annotation:
Plays a role in the escape of host innate immune response by promoting the degradation of host EIF2AK2/PKR and inhibiting host transcription. Cytoplasmic NSs interacts with host FBXW11 to degrade PKR whereas nuclear pool binds to host FBXO3 to target TFIIH subunit GTF2H1 for proteasomal degradation (PubMed:19197350, PubMed:19211744, PubMed:21543505, PubMed:23063407, PubMed:26837067). Forms filaments in the nucleus that may sequester NSs binding partners, causing cell cycle arrest (PubMed:28915104, PubMed:10233964).


Viral_family: Pneumoviridae
Species: Human metapneumovirus
Name: M2-1
Aliases: Envelope-associated 22 kDa protein, M2, Matrix M2-1
UniProtID_Ref: Q6WB97
UniProt_Name_Ref: M21_HMPVC
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 4CS9
Reporter_assay: I(22675274)
EMSA: I(22675274)
Other_assays: I(11024112)
Human_infection_evidence: 18820584.0
UniProt_IDs_Orthologs:
A0A2H4ZA70,C4B9I0,C5MRS8,F4YZY3,M9V764,M9V801,M9V8F9,M9V8I5,Q0GMS7,Q0GMT0,T1UEZ8,X4Y081,X4Y6I6,X4Y849,X4YLV7

Functional_annotation:
Acts as a transcriptional elongation factor to prevent premature termination during transcription thus allowing complete synthesis of viral mRNAs. Functions also as a processivity and antitermination factor to permit transit of the polymerase through intergenic regions to access promoter distal genes. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (By similarity).


Viral_family: Pneumoviridae
Species: Human metapneumovirus
Name: M2-2
Aliases: M2, Matrix protein M2-2
UniProtID_Ref: Q6WB96
UniProt_Name_Ref: M22_HMPVC
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(10500164)
EMSA: N
Other_assays: I(10500164)
Human_infection_evidence: 18820584.0
UniProt_IDs_Orthologs:
A0A1C9UMW8,A0A2H4ZA68,A0A2H4ZAG0,A0A2H4ZAL7,A0A2R4KPG0,B8X6L4,C4B9I1,G3KCK1,G3KCL0,M4QFJ4,M4QFL8,M4QJH5,M4QSN4,Q0GMS9,Q6QQH9,Q6WBA5,T1UCE1,X4XYU4,X4Y8N5,X4YM65

Functional_annotation:
Mediates the regulatory switch from transcription to RNA replication. Acts late in infection by inhibiting viral transcription and up-regulating RNA replication (By similarity). Plays a major role in antagonizing the type I IFN-mediated antiviral response. Interacts with host MAVS and prevents the interaction with its upstream partner DDX58/RIG-I in the signaling pathway leading to interferon production.


Viral_family: Pneumoviridae
Species: Human respiratory syncytial virus
Name: M2-1
Aliases: Envelope-associated 22 kDa protein, M2, Matrix M2-1
UniProtID_Ref: O42050
UniProt_Name_Ref: M21_HRSVB
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(22675274)
EMSA: D(22675274)
Other_assays: D(11024112)
Human_infection_evidence: 27486734.0
UniProt_IDs_Orthologs:
A0A023R760,A0A023R9H2,A0A023RAB4,A0A023RB46,A0A059TDC1,A0A059TDD0,A0A059TDD2,A0A059TDK0,A0A059TDS3,A0A059TDT2,A0A059TE43,A0A059TE80,A0A059TE92,A0A059TEB2,A0A059TED8,A0A076FRX0,A0A076FS08,A0A0A7NQY1,A0A0A7NR76,A0A0A7NS85,A0A0A7NSD8,A0A0A7NTH8,A0A0A7NTR2,A0A0A7NWI0,A0A0A7NWV7,A0A0E3JJE6,A0A0E3LZC2,A0A0X8CVT2,A0A0X8CW62,A0A0X9WN34,A0A0X9WNF5,A0A0X9WYQ7,A0A109QCV3,A0A109QF38,A0A109QF47,A0A109QFG0,A0A109QFU4,A0A120HQL9,A0A140H350,A0A140H3H1,A0A140H3I2,A0A142MLF2,A0A142MLU4,A0A142MME4,A0A142MMF8,A0A142MML9,A0A142MMY8,A0A142MN24,A0A142MN83,A0A142MNE0,A0A142MP28,A0A142MP67,A0A142MQE4,A0A142MQL3,A0A142MS12,A0A142MTE5,A0A142MTN4,A0A1B2VRY5,A0A1B2VTF5,A0A1B2VTV8,A0A1B2VU04,A0A1B2VUC4,A0A1B2VUQ6,A0A1B2VUR2,A0A1B2VV16,A0A1C9V116,A0A1C9V131,A0A1C9V1G1,A0A1C9V236,A0A1C9V2L7,A0A1C9V2L9,A0A1S5SHT2,A0A344X9C8,A0A384ZDG5,A0A384ZEL0,A0A384ZHM7,A0A384ZI92,A0A3Q8TDD0,G8EJ00,P04545,S5ZI93,T1UDB8,V5N720,V5N732,V5N764,V5N7P0,V5N7T2,V5N863,V5N8G0,V5N8M0,V5N9G7,X4Y2X6,X4Y354,X4Y4A9,X4Y4R1,X4Y5B0,X4Y9B5,X4YAG2,X4YBX8,X4YC51,X4YCE8,X4YCG8,X4YCK1,X4YRJ3,X4YRV8,X4YSL7,X4YT50

Functional_annotation:
Acts as a transcriptional elongation factor to prevent premature termination during transcription thus allowing complete synthesis of RSV mRNAs. Functions also as a processivity and antitermination factor to permit transit of the polymerase through intergenic regions to access promoter distal genes. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding. Also, can activate NF-kappa-B through association with host RELA (By similarity).


Viral_family: Pneumoviridae
Species: Human respiratory syncytial virus
Name: M2-2
Aliases: M2, Matrix M2-2, Matrix protein M2-2
UniProtID_Ref: O42047
UniProt_Name_Ref: M22_HRSVB
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(10500164)
EMSA: N
Other_assays: D(10500164)
Human_infection_evidence: 27486734.0
UniProt_IDs_Orthologs:
A0A023R862,A0A023RAK9,A0A023RAR0,A0A023RAW2,A0A059TD79,A0A059TD88,A0A059TD97,A0A059TDB9,A0A059TDL1,A0A059TDM2,A0A059TDN5,A0A059TDU3,A0A059TDW5,A0A059TE08,A0A059TE10,A0A059TE20,A0A059TE62,A0A059TE76,A0A059TE86,A0A059TEF7,A0A088S989,A0A088SBH4,A0A088STR4,A0A0A7NQN2,A0A0A7NRD7,A0A0A7NRW9,A0A0A7NRZ5,A0A0A7NSC6,A0A0A7NSS3,A0A0A7NSZ2,A0A0A7NTQ4,A0A0A7NW37,A0A0A7NWD7,A0A0C5BY14,A0A0U2X6D1,A0A0X8CUQ7,A0A0X8CV01,A0A0X8CVY3,A0A0X8CWA4,A0A0X8CWK3,A0A0X8CWL7,A0A0X8CX84,A0A0X8D1Y1,A0A0X9WEC3,A0A0X9WNJ9,A0A0X9WQ87,A0A0X9XCQ9,A0A0X9XSH9,A0A0X9XZP0,A0A109QF63,A0A120HQH2,A0A140H3H2,A0A142MLB5,A0A142MLT2,A0A142MLW9,A0A142MLZ4,A0A142MMA1,A0A142MND2,A0A142MNS2,A0A142MP32,A0A142MPS0,A0A142MQ01,A0A142MQ24,A0A142MQB9,A0A142MQQ3,A0A142MRP9,A0A142MRQ8,A0A142MRT1,A0A142MSE7,A0A142MSN4,A0A142MTD2,A0A1B2VRZ4,A0A1B2VT71,A0A1B2VTT6,A0A1C9V163,A0A1C9V1B2,A0A1C9V1B7,A0A1C9V1C5,A0A1C9V1K6,A0A1C9V273,A0A1C9V2D1,A0A1C9V2L4,A0A1C9V3M2,A0A1C9V3M4,A0A1P8L302,A0A1P8L312,A0A1P8L326,A0A1P8L340,A0A1P8L345,A0A1P8L3C1,A0A1P8L3J1,A0A1P8L3L8,A0A1P8L3L9,A0A1P8L3N1,A0A1P8L3R6,A0A1V0G3V1,A0A1V0G3V3,A0A1V0G3Y9,A0A219V069,A0A219V0B8,A0A219V1R2,A0A220QKK0,A0A240ESV1,A0A240ET90,A0A240ETA0,A0A2H4HTW4,A0A2H4WKD5,A0A2H4WKH4,A0A2H4WKI3,A0A2H4WKJ7,A0A2H4WKK7,A0A2H4WKM6,A0A2H4WKU2,A0A2H4WKZ5,A0A2H4WL43,A0A2H4WL88,A0A2H4WL89,A0A2H4WL96,A0A2H4WLC5,A0A2H4WLJ5,A0A2H4WLK0,A0A2H4WLK1,A0A2H4WLK4,A0A2H4WLR1,A0A2H4WLS0,A0A2H4WLW4,A0A2H4WM08,A0A2H4WM68,A0A2H4WM69,A0A2I6PIW0,A0A2Z4Z400,A0A344X9C9,A0A348FUX5,A0A348FUZ7,A0A348FV41,A0A384ZD99,A0A384ZDA6,A0A384ZDE7,A0A384ZDJ1,A0A384ZDP1,A0A384ZDQ6,A0A384ZE42,A0A384ZEB4,A0A384ZFD6,A0A384ZFQ7,A0A384ZGM2,A0A384ZHC5,A0A384ZIB7,A0A384ZIM0,A0A385MKF8,A0A385MKK5,A0A385MKM5,A0A385MKY3,A0A385MKY9,A0A385ML21,A0A385ML27,A0A385MLE1,A0A385MLJ5,A0A385MLV9,A0A385MLZ9,A0A385MM88,A0A385MMM9,A0A385MMY7,A0A385MNA9,A0A385MNH8,A0A385MP38,A0A385MPR2,G8EID1,G8EIF3,G8EIN0,G8EIP1,G8EIT4,G8EJ11,I1V243,I6TQU9,I6TQX6,K4G1T0,K4G1U1,K4G1X4,K4G267,K4G278,K4G291,K4G2E0,K4G2F1,K4G2G2,K4G8U6,K4G974,P88812,R9TBJ8,R9TBV7,R9TC35,R9TCE7,R9TCH9,R9TCV3,R9TD10,R9TDD3,R9TFD3,R9TGG7,R9TGM0,S5YT63,T1UDA9,T1UFV4,V5N6W9,V5N770,V5N7H4,V5N7S2,V5N7T7,V5N7T8,V5N800,V5N9B2,V5N9Q5,V9VEA7,X4Y2T5,X4Y2X0,X4Y459,X4YC44,X4YF41,X4YQG7,X4YRX7,X4YS61,X4YSE2,X4YUD1

Functional_annotation:
Mediates the regulatory switch from transcription to RNA replication. Acts late in infection by inhibiting viral transcription and up-regulating RNA replication (By similarity).


Viral_family: Pneumoviridae
Species: Human respiratory syncytial virus
Name: NS1
Aliases: 1C, Non-structural protein 1, Non-structural protein 1C
UniProtID_Ref: P0DOE9
UniProt_Name_Ref: NS1_HRSVA
Binding_ligand: indirect/unknown
Function: TR, Rep, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: D(unpublished)
Structure_PDB_ID: N
Reporter_assay: D(28665409, 15827150, 30558248)
EMSA: N
Other_assays: D(9445048)
Human_infection_evidence: 27486734.0
UniProt_IDs_Orthologs:
A0A023RAP1,A0A023RAP2,A0A059TDA4,A0A059TE30,A0A059TEA8,A0A059TEC6,A0A076FRG5,A0A076FRP0,A0A076FRZ6,A0A088S969,A0A088S9L5,A0A088S9Q0,A0A088SBF8,A0A0A7ESZ7,A0A0A7NQK8,A0A0A7NR06,A0A0A7NTB6,A0A0A7NW88,A0A0C5CHB8,A0A0E3JFY9,A0A0E3JJF0,A0A0N7AZB8,A0A0N7AZU8,A0A0N7AZW5,A0A0N7B004,A0A0X8CUX3,A0A0X8CV39,A0A0X8CV54,A0A0X8CVU3,A0A0X8D1H5,A0A0X9WFH4,A0A0X9WJP4,A0A0X9WNC3,A0A0X9YMG0,A0A109Q8Y4,A0A109QEZ3,A0A109QF81,A0A109QF99,A0A142MN86,A0A142MNL6,A0A142MR26,A0A142MR29,A0A142MS90,A0A142MSN6,A0A142MSP0,A0A142MTA9,A0A1B2VR66,A0A1B2VR76,A0A1B2VRC9,A0A1B2VRD0,A0A1B2VRG3,A0A1B2VRG9,A0A1B2VRK3,A0A1B2VRP7,A0A1B2VRQ7,A0A1B2VRV1,A0A1B2VRX1,A0A1B2VS19,A0A1B2VS39,A0A1B2VS48,A0A1B2VS52,A0A1B2VS65,A0A1B2VS80,A0A1B2VS84,A0A1B2VSA0,A0A1B2VSE3,A0A1B2VSH6,A0A1B2VSI1,A0A1B2VSM9,A0A1B2VST7,A0A1B2VSV0,A0A1B2VSV5,A0A1B2VSY0,A0A1B2VSY7,A0A1B2VT51,A0A1B2VT63,A0A1B2VT69,A0A1B2VT83,A0A1B2VT94,A0A1B2VT96,A0A1B2VTB8,A0A1B2VTC1,A0A1B2VTC4,A0A1B2VTD8,A0A1B2VTF8,A0A1B2VTG3,A0A1B2VTG4,A0A1B2VTK9,A0A1B2VTL3,A0A1B2VTM8,A0A1B2VTN0,A0A1B2VTN8,A0A1B2VTP7,A0A1B2VTQ3,A0A1B2VTS2,A0A1B2VTS4,A0A1B2VTT3,A0A1B2VTT4,A0A1B2VTV5,A0A1B2VTV9,A0A1B2VTW6,A0A1B2VU02,A0A1B2VU38,A0A1B2VU48,A0A1B2VU55,A0A1B2VU65,A0A1B2VU70,A0A1B2VU78,A0A1B2VU81,A0A1B2VU82,A0A1B2VU88,A0A1B2VU95,A0A1B2VUA4,A0A1B2VUE3,A0A1B2VUG6,A0A1B2VUJ1,A0A1B2VUJ9,A0A1B2VUK4,A0A1B2VUK6,A0A1B2VUL5,A0A1B2VUL7,A0A1B2VUM0,A0A1B2VUM4,A0A1B2VUN6,A0A1B2VUQ1,A0A1B2VUR4,A0A1B2VUS0,A0A1B2VUT2,A0A1B2VUW2,A0A1B2VUY0,A0A1B2VUZ1,A0A1B2VV04,A0A1B2VV13,A0A1B2VV32,A0A1B2VV64,A0A1C9V0V3,A0A1C9V0X8,A0A1C9V1C9,A0A1C9V1K2,A0A1C9V1N8,A0A1C9V3D2,A0A1C9V3K7,A0A1P8L3N0,A0A1P8L3T5,A0A219V0C0,A0A219V0N1,A0A219V114,A0A219V1P3,A0A220QKI1,A0A240ESZ3,A0A2H4WKM9,A0A2H4WKW4,A0A2H4WKZ0,A0A2H4WLA5,A0A2H4WLL9,A0A2H5BXT7,A0A348FUV5,A0A348FUY8,A0A384ZCX6,A0A384ZD04,A0A384ZD36,A0A384ZDB2,A0A384ZDB3,A0A384ZDI4,A0A384ZDK9,A0A384ZDY9,A0A384ZE34,A0A384ZE47,A0A384ZE63,A0A384ZE76,A0A384ZE81,A0A384ZER9,A0A384ZET1,A0A384ZEV2,A0A384ZEY9,A0A384ZF13,A0A384ZFF8,A0A384ZFM4,A0A384ZFU1,A0A384ZFW2,A0A384ZFX9,A0A384ZFY9,A0A384ZG16,A0A384ZG51,A0A384ZG82,A0A384ZGC2,A0A384ZGG9,A0A384ZGI6,A0A384ZGK2,A0A384ZGW1,A0A384ZGW2,A0A384ZH11,A0A384ZH71,A0A384ZHA1,A0A384ZHF7,A0A384ZHH1,A0A384ZHK6,A0A384ZHS5,A0A384ZHT3,A0A384ZHT8,A0A384ZI47,A0A384ZID6,A0A384ZJ47,D8L6X1,E0WLV8,E0WLW0,E0WLW8,E0WLX4,E0WLX8,E0WLZ0,E0WLZ2,E0WLZ6,E0WM00,E0WM08,E0WM12,E0WM16,E0WM18,E0WM26,E0WMQ1,G3C7U4,G8EIQ4,G8EIV8,I1V245,I6TFE5,K4G252,K4G274,K4G2M9,K4G8K1,K7QLZ3,K7QM45,K7QM88,K7QM91,K7QMA9,K7QMD7,K7QME5,K7QMZ2,K7QMZ6,O09716,O42083,P04544,P0DOE8,P24568,Q4KRX1,Q86306,R9TBY3,R9TCN8,R9TGK0,S5Z6Q7,V5N7F0,V5N7L4,V5N7V2,V5NA43,W8E1P4,X4Y4C8,X4YC42,X4YC71,X4YRG2,X4YSB5,X4YSJ2

Functional_annotation:
Plays a major role in antagonizing the type I IFN-mediated antiviral response. Acts cooperatively with NS2 to repress activation and nuclear translocation of host IFN-regulatory factor IRF-3. Interacts with host MAVS and prevents the interaction with its upstream partner DDX58/RIG-I in the signaling pathway leading to interferon production. Mediates the proteasomal degradation of host STAT2 with elongin-cullin E3 ligase. Suppresses premature apoptosis by an NF-kappa-B-dependent, interferon-independent mechanism and thus facilitates virus growth. Additionally, NS1 may serve some inhibitory role in viral transcription and RNA replication.


Viral_family: Pneumoviridae
Species: Human respiratory syncytial virus
Name: NS2
UniProtID_Ref: P04543
UniProt_Name_Ref: NS2_HRSVA
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(19193793, 15827150)
EMSA: N
Other_assays: D(19193793)
Human_infection_evidence: 27486734.0
Aliases:
1B, Non-structural protein 1B, Non-structural protein 2, Non-structural protein 2,Non-structural protein 1B

UniProt_IDs_Orthologs:
A0A023R830,A0A023R8E9,A0A023R8N9,A0A023R9I4,A0A023RA27,A0A023RA93,A0A059TE26,A0A059TE72,A0A059TEA2,A0A059TEF4,A0A060AG29,A0A060AHX0,A0A075D1R7,A0A075D1S8,A0A088S9K5,A0A088S9P1,A0A088SBF0,A0A088STT8,A0A0A7EB38,A0A0A7NQS6,A0A0A7NRK6,A0A0A7NRZ4,A0A0A7NT36,A0A0A7NTS5,A0A0A7NVS6,A0A0A7NVZ7,A0A0B5HHW4,A0A0B5HI09,A0A0B5HKC4,A0A0B5HPI0,A0A0E3GJT7,A0A0E3JJF2,A0A0E3LZC5,A0A0K0WTK1,A0A0N7ATI3,A0A0N7AUF0,A0A0X8CV14,A0A0X8CVP7,A0A0X8CVW4,A0A0X8CW71,A0A0X8D1A1,A0A0X9Y758,A0A0X9YM76,A0A109QA27,A0A109QF01,A0A120HQ64,A0A142MLQ4,A0A142MM12,A0A142MMA4,A0A142MNY1,A0A142MP94,A0A142MPB2,A0A142MQH2,A0A142MR38,A0A142MRB4,A0A142MRN0,A0A142MS94,A0A142MTJ5,A0A1B2VSE2,A0A1B2VUP9,A0A1B2VUS2,A0A1B2VV91,A0A1C9V187,A0A1C9V2R9,A0A1C9V385,A0A1C9V3K1,A0A1C9V3N0,A0A1P8L309,A0A1P8L388,A0A1P8L3F9,A0A1P8L3L5,A0A1V0BZ80,A0A1V0E2A8,A0A1Y0AVJ4,A0A219V0E0,A0A219V0P6,A0A219V1E6,A0A240ESZ4,A0A240ET33,A0A249Y6G1,A0A2H4N9A4,A0A2H4WKV6,A0A2H4WL58,A0A2H4WLD3,A0A2H4WLG6,A0A2H4WLM7,A0A2H4WLM8,A0A2H4WLW6,A0A2Z4Z441,A0A348FV22,A0A384ZEI2,A0A384ZEK3,A0A384ZFR9,A0A384ZG84,A0A384ZG97,A0A384ZH23,A0A384ZH48,A0A384ZHN3,A0A384ZHU2,A0A384ZHU8,A0A384ZIH2,A0A385ML73,A0A385ML91,A0A385MLX3,A0A385MMB0,A0A385MMC9,A0A385MN52,A0A385MN71,A0A385MNF0,A0A385MNM0,A0A385MNX2,A0A385MNZ9,A0A385MPD5,A0A386BXW1,A0A3G3NDU9,A0A3G3NFT1,A0A3G3NG18,A0A3Q8TDK8,A0A3Q8TEI7,C3UPA8,D8L6X2,E0WLV9,E0WLW5,E0WLW9,E0WLX5,E0WLY9,E0WLZ3,E0WLZ5,E0WM19,E0WM23,E0WMQ2,G8EIX0,G8FR15,G8FR70,I6TQX1,I6UJV8,K4G1V7,K4G272,K4G2D4,K4G905,K7QMY7,K7QMZ9,K7QN21,O12405,O42038,P24569,Q6V2F3,Q76TL1,Q86305,R9TCM6,R9TD28,R9TDF4,R9TF62,R9TFF7,R9TG22,V5N745,V5N794,V5N7E8,V5N7K8,V5N7Q9,V5N7U5,V5N858,V5N9I0,V5NA34,W8E0C3,X4Y3J0,X4Y5K9,X4Y5Y6,X4Y9H0,X4YCW8,X4YF64,X4YQI8,X4YQW8,X4YS53,X4YUK4,X5FNU1,X5FP42,X5FP72,X5FQ06,X5FQ21,X5FQ89,X5FQN9,X5FQS3

Functional_annotation:
Plays a major role in antagonizing the type I IFN-mediated antiviral response. Acts cooperatively with NS1 to repress activation and nuclear translocation of host IFN-regulatory factor IRF-3. Interacts with the host cytoplasmic sensor of viral nucleic acids DDX58/RIG-I and prevents the interaction with its downstream partner MAVS. Mediates the proteasomal degradation of host STAT2 with Elongin-Cullin E3 ligase. Induces activation of NF-kappa-B. Suppresses premature apoptosis by an NF-kappa-B-dependent, interferon-independent mechanism and thus facilitates virus growth. May also inhibit viral transcription and RNA replication.


Viral_family: Pneumoviridae
Species: Human respiratory syncytial virus
Name: Phosphoprotein
Aliases: P, Protein P
UniProtID_Ref: P03421
UniProt_Name_Ref: PHOSP_HRSVA
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(7491765)
EMSA: N
Other_assays: N
Human_infection_evidence: 27486734.0
UniProt_IDs_Orthologs:
A0A023R796,A0A023R931,A0A023R9H0,A0A023R9X3,A0A023RAW9,A0A023RB54,A0A059TD78,A0A059TDA9,A0A059TDC0,A0A059TDF6,A0A059TDK1,A0A059TDN4,A0A059TDP5,A0A059TDU4,A0A059TDW6,A0A059TDX7,A0A059TEE1,A0A059TEG5,A0A0A7NRI4,A0A0A7NTQ9,A0A0B5H8J4,A0A0B5HBQ7,A0A0B5HBR0,A0A0B5HBW0,A0A0B5HP07,A0A0B5HPA9,A0A0B5HPC5,A0A0B5HPR7,A0A0K0WTK9,A0A0N7ATJ7,A0A0N7ATT1,A0A0N7ATY2,A0A0N7AUS2,A0A0N7AV14,A0A0N7AZ16,A0A0N7AZE2,A0A0N7AZH2,A0A0N7AZI8,A0A0N7B002,A0A0X8CUQ8,A0A0X8CUV1,A0A0X8CV22,A0A0X8CW06,A0A0X8CX11,A0A0X9WMU9,A0A0X9WYK0,A0A0X9XGP1,A0A0X9XZG1,A0A0X9YMD9,A0A120HQ68,A0A120HQ74,A0A120HQF5,A0A120HQJ1,A0A120HQQ2,A0A140H334,A0A140H3G6,A0A140H3I8,A0A142MLZ0,A0A142MML1,A0A142MMQ9,A0A142MNC8,A0A142MNP1,A0A142MNY4,A0A142MPT4,A0A142MQK9,A0A142MR33,A0A142MRC6,A0A142MT43,A0A142MTU1,A0A1B2VSC7,A0A1B2VSP3,A0A1B2VSX6,A0A1B2VTC9,A0A1B2VTP2,A0A1B2VU10,A0A1B2VUZ0,A0A1C9V167,A0A1C9V175,A0A1C9V195,A0A1C9V1K3,A0A1C9V1M4,A0A1C9V2B2,A0A1C9V2G9,A0A1C9V2R8,A0A1C9V340,A0A1C9V367,A0A1C9V3B2,A0A1C9V3K6,A0A1C9V3Q0,A0A1P8J9Y5,A0A1V0G3P6,A0A1V0G3R8,A0A1V0G425,A0A1W6LX83,A0A1Y0AUC6,A0A1Y0AUD1,A0A1Y0AUU0,A0A1Y0AUW1,A0A1Y0AV62,A0A1Y0AVH6,A0A219V0G5,A0A219V0Y7,A0A219V1D0,A0A219V1P9,A0A240ESU6,A0A240ET35,A0A249Y6F2,A0A249Y6G5,A0A2H4N9D3,A0A2H4WKC9,A0A2H4WKS8,A0A2H4WKT4,A0A2H4WL41,A0A2H4WL85,A0A2H4WLA8,A0A2H4WLL5,A0A2H4WLQ9,A0A2H4WLR2,A0A2H4WLX1,A0A2H5BXX0,A0A2U9NKX0,A0A2Z4Z422,A0A344X9A1,A0A344X9D4,A0A348FV24,A0A384ZCY9,A0A384ZFT9,A0A384ZGS7,A0A384ZGZ3,A0A384ZH06,A0A384ZHN0,A0A384ZHV3,A0A384ZI22,A0A384ZIF5,A0A384ZII8,A0A384ZIU7,A0A385MKH7,A0A385MKI8,A0A385MKL1,A0A385MKU3,A0A385ML22,A0A385ML33,A0A385MLR4,A0A385MLT1,A0A385MM07,A0A385MM18,A0A385MMB4,A0A385MMP1,A0A385MMT6,A0A385MN26,A0A385MN46,A0A385MNI7,A0A385MNN3,A0A385MNW5,A0A385MPH8,A0A385MPW8,A0A3G3NDI3,A0A3G3NE50,A0A3G3NEL4,A0A3G3NFT0,A0A3G3NGN2,A0A3G3NH86,A0A3G3NHD3,A0A3Q8TBM7,G3C7R7,G8EIC5,G8EIJ1,G8EIL3,G8EIM4,G8EIR7,G8EIT9,G8EIV0,G8EIW1,I1V237,I6TFI2,O09633,O09717,O42062,P12579,P14156,P24567,Q04161,Q4KRW8,Q8UYD5,Q8V218,Q8V219,Q8V221,R9TG31,V5N740,V5N775,V5N7N3,V5N7N6,V5N7S5,V5N8A3,W8E4V8,X4Y3M5,X4Y679,X4YAF6,X4YBX5,X4YCE3,X4YCJ5,X4YCP4,X4YCT2,X4YD07,X4YD13,X4YF46,X4YQU8,X4YS93,X4YSD4,X4YSL4

Functional_annotation:
Acts as a cofactor that serves both to stabilize the protein L and to place the polymerase complex on the N:RNA template.


Viral_family: Polyomaviridae
Species: BK polyomavirus
Name: Agnoprotein
Aliases: Agno
UniProtID_Ref: P14998
UniProt_Name_Ref: AGNO_POVBA
Binding_ligand: dsDNA
Function: TR, DR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(11152520)
EMSA: I(22840425)
Other_assays: I(6262654)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A0G4CPA0,A0A1Q1MRD3,A0A223ZI77,A0A2H4Z6N5,A1IHW3,A1IHY7,A1IHZ9,A1II17,A1II41,A1II47,A1II83,A7BGR0,A7BH00,A7BH12,B6EXG3,B6VQB6,B9X1T9,B9X1V1,B9X1V7,B9X1W3,Q0PCM8,Q0PCN9,Q0PDF1,Q0PDG9,Q1ESU1,Q1ESU7,Q2PRN3,Q2WG17,Q65614,Q6GWH9,Q6GWN3,Q6GWQ7,Q89856

Functional_annotation:
Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins (By similarity).


Viral_family: Polyomaviridae
Species: BK polyomavirus
Name: Large T antigen
Aliases: LT, LT-AG
UniProtID_Ref: P03071
UniProt_Name_Ref: LT_POVBK
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: I(27462916; 15265983; 18642444)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8709258)
EMSA: I(22840425)
Other_assays: I(3003386, 168585, 6251241, 202398)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A1Q1MQ55,A0A1V0QSU1,A0A1V0QSU6,A0A2H4Z6M7,A0A2H4Z6P1,A7BGN4,P14999,Q068W4,Q0PCN5,Q0PDA5,Q6GWH5,Q6GWI1,Q6GWI7,Q6GWJ9,Q6GWK5,Q6GWL1,Q6GWL7,Q6GWM3,Q6GWN5,Q6GWQ3,U5NGJ3

Functional_annotation:
Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription (By similarity).


Viral_family: Polyomaviridae
Species: BK polyomavirus
Name: Small T antigen
Aliases: Small t antigen, ST, ST-AG
UniProtID_Ref: P15000
UniProt_Name_Ref: ST_POVBA
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: I(19282432)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19282432)
EMSA: I(19282432)
Other_assays: I(17158797)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A023SFN7,A0A2H4Z6N1,A0A2H4Z6P9,B2ZRH5,B2ZRI3,B2ZRI5,B2ZRI7,B2ZRJ1,B2ZRK4,B2ZRK6,B2ZRL0,B2ZRL2,B2ZRL6,B2ZRL8,B2ZRM0,B2ZRM2,B2ZRM6,B2ZRM8,B2ZRN0,B2ZRN5,B2ZRN7,B2ZRN9,B2ZRP1,B2ZRP3,B2ZRP7,B2ZRQ3,Q6GWH4,Q6GWI6,Q6GWJ8,Q6GWL0,Q6GWL6,Q6GWN4,Q6GWQ2

Functional_annotation:
Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters. Late during the infection cycle, ST may induce dephosphorylation of host MTOR, leading to the inhibition of cap-dependent translation. May establish and maintain high levels of viral genomes during persistent infection in cell culture.


Viral_family: Polyomaviridae
Species: JC polyomavirus
Name: Agnoprotein
Aliases: Agno, Agno protein, Agnogene, Agnoprotein (Fragment), Agnoprotein (LP1), Truncated agnoprotein
UniProtID_Ref: P03086
UniProt_Name_Ref: AGNO_POVJC
Binding_ligand: dsDNA
Function: TR, DR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(11152520)
EMSA: D(22840425)
Other_assays: I(6262654)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A173G677,A0A1E1FFS4,A0A1E1FFT6,A0A286R3X0,A0A286R3Z6,A0A286R3Z8,A0ZST9,C0SQA6,C0SQF4,C0SQH8,C0SQI4,J9XN85,K7QRQ6,K7QSR0,K7QW67,K7R6U0,O42075,O55863,O55870,O55873,O57296,P88896,P90499,Q4LFQ9,Q4LFW9,Q4W708,Q5YKE2,Q5YKE8,Q5YKP1,Q5YL44,Q679M8,Q679N4,Q679P0,Q69C52,Q6EH30,Q768G9,Q768H5,Q768I1,Q783F8,Q7T3Y5,Q7TDV5,Q82946,Q8AZ44,Q8B0K8,Q8BF42,Q8BF48,Q8BF50,Q8JJJ6,Q8JJJ8,Q8JUC0,Q8JUD7,Q8JWJ0,Q8JWJ1,Q8JWJ2,Q8JWJ6,Q8JWJ7,Q8JZI8,Q8JZJ0,Q8JZJ6,Q8JZJ7,Q8JZJ8,Q8JZJ9,Q8V6G0,Q8V6G2,Q8V6G5,Q8V6H5,Q910S4,Q910S7,Q91C18,Q91C19,Q91DE4,Q91DG4,Q91DH1,Q91DH5,Q91NM9,Q91NN5,Q91NN9,Q91NP8,Q91SI4,Q98Y35,Q993Y6,Q9DH65,Q9DPC8,Q9DUG2,Q9Q1G5,Q9Q1G6,W0LSY0,W6MEN0

Functional_annotation:
Alters the structure of the nuclear envelope by interacting with host CBX5 and disrupting CBX5 association with LBR. Involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. Plays an important role in the release of progeny virions from infected cells and in viral propagation, probably by acting as a viral ionic channel in the host plasma membrane. Allows influx of extracellular calcium ions in the host cell. May contribute to viral genome transcription and translation of viral late proteins.


Viral_family: Polyomaviridae
Species: JC polyomavirus
Name: Large T antigen
Aliases: LT, LT-AG
UniProtID_Ref: P03072
UniProt_Name_Ref: LT_POVJC
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: I(27462916; 15265983; 18642444)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8709258)
EMSA: D(22840425)
Other_assays: I(3003386, 168585, 6251241, 202398)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A0A0RHI4,A0A1E1FFU6,A0A286R3U4,A0A286R403,I0B5Z5,O55871,O55875,P88898,Q0MQN6,Q5YKC6,Q5YKD8,Q5YKL9,Q5YKN1,Q5YKN7,Q679N0,Q679N6,Q69C48,Q69F69,Q6EH26,Q7TDV3,Q7TDV4,Q8JJJ0,Q8JJK3,Q8JUB1,Q8JUB6,Q8JUB9,Q8JUC2,Q8JUC5,Q8JUC9,Q8JUD0,Q8JUD1,Q8JUD5,Q8JUD8,Q8JUE1,Q8JUE2,Q8JWI7,Q8JWJ3,Q8JWJ4,Q8JWJ5,Q8JZJ2,Q8JZK0,Q8V6F7,Q8V6F8,Q8V6G1,Q8V6G3,Q8V6G6,Q8V6G7,Q8V6H1,Q8V6H4,Q910D2,Q91C15,Q91C16,Q91DE5,Q91DE6,Q91DF4,Q91DF5,Q91DF8,Q91DG2,Q91DG3,Q91DH0,Q91DH2,Q91NL2,Q91NL5,Q91NL8,Q91NM2,Q91NM6,Q91NN1,Q91NP7,Q91NP9,Q993Y2,Q993Y4,Q993Y5,Q9DPC0,Q9DPC5,Q9DPC9,Q9DUG5,Q9WM07,Q9WM08,Q9WM10

Functional_annotation:
Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription.


Viral_family: Polyomaviridae
Species: JC polyomavirus
Name: Small T antigen
Aliases: Small t antigen, ST, ST-AG
UniProtID_Ref: P03083
UniProt_Name_Ref: ST_POVJC
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: D(19282432)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(19282432)
EMSA: D(19282432)
Other_assays: I(17158797)
Human_infection_evidence: 27381292.0
UniProt_IDs_Orthologs:
A0A286R3T1,A0A385NI07,A0A385NI69,O55876,Q69F68,Q8JUB5,Q8JUC1,Q8JUC8,Q8JUD4,Q8V6H0,Q8V6H3,Q910Q3,Q91DE7,Q91DE9,Q91NL4,Q91NL7,Q91NM7,Q91NN0,Q91NP3,Q9DPB9,Q9DPC4

Functional_annotation:
Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters. Late during the infection cycle, ST may induce dephosphorylation of host MTOR, leading to the inhibition of cap-dependent translation. May establish and maintain high levels of viral genomes during persistent infection in cell culture.


Viral_family: Polyomaviridae
Species: Merkel cell polyomavirus
Name: Small T antigen
Aliases: ST, STAg
UniProtID_Ref: U6C6B2
UniProt_Name_Ref: U6C6B2_9POLY
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: I(19282432)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(24067965; 24109239)
EMSA: I(19282432)
Other_assays: I(17158797)
Human_infection_evidence: 23217622.0
Functional_annotation: Not annotated
UniProt_IDs_Orthologs:
A0A2S1LV38,B0G0V7,B6DVX0,B6DVX6,B6DVY4,B8ZX49,B8ZX51,B8ZX57,C6KKZ9,C6KL03,C6KL05,C6KL07,D6QW80,D6QW84,D6QWD2,G8EHJ4,G8FT05,I0ISA5,T2HFI7,T2HFT7,T2HFZ4,U6C643,U6C665,U6C6W7,U6C7Y2,U6C841,U6C845,X2G6N5


Viral_family: Polyomaviridae
Species: Simian virus 40
Name: Large T antigen
Aliases: large, LT, LT-AG
UniProtID_Ref: P03070
UniProt_Name_Ref: LT_SV40
UniProt_IDs_Orthologs: A7XWJ9,A7XWL1,A7XWN5,Q0Z8T6,Q2I7F9,Q6QIR8,Q77PF5,Q8JMI9,Q98ZP7,Q9J7C9,Q9W8G8,Q9WND0
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: D(27462916; 15265983; 18642444)
ChIP_seq: N
Structure_PDB_ID: 1SVM
Reporter_assay: D(15265983; 18642444)
EMSA: D(14990710; 10438844; 10954561)
Other_assays: D(3003386, 168585, 6251241, 202398)
Human_infection_evidence: 9923853.0
Functional_annotation:
Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. May inactivate the growth-suppressing properties of the E3 ubiquitin ligase CUL7.


Viral_family: Polyomaviridae
Species: Simian virus 40
Name: Small T antigen
Aliases: small, Small t antigen, ST, ST-AG
UniProtID_Ref: P03081
UniProt_Name_Ref: ST_SV40
UniProt_IDs_Orthologs: Q2I7F8,Q77JR6
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 2PF4
Reporter_assay: D(15684382; 8917510)
EMSA: D(8917510)
Other_assays: D(17158797)
Human_infection_evidence: 9923853.0
Functional_annotation:
Promotes efficient viral genome replication by accelerating both G1 and S phase progression of the cell cycle. Inhibits host PP2A by binding to the A subunit, thereby displacing lower affinity regulatory B subunit. Inactivation of PP2A in turn results in the transactivation of cyclin A and cyclin D1 promoters. Late during the infection cycle, ST may induce dephosphorylation of host eIF4E-binding protein EIF4EBP1 leading to the inhibition of cap-dependent translation. May establish and maintain high levels of viral genomes during persistent infection in cell culture.


Viral_family: Polyomaviridae
Species: WU polyomavirus
Name: Large T antigen
Aliases: LT, LT-AG
UniProtID_Ref: A5HBG1
UniProt_Name_Ref: LT_POVWU
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: I(27462916; 15265983; 18642444)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8709258)
EMSA: I(22840425)
Other_assays: I(3003386, 168585, 6251241, 202398)
Human_infection_evidence: 21994565.0
Notes: A5HBG1 is inferred from JC polyomavirus protein P03083
UniProt_IDs_Orthologs:
A0A023IX55,A0A0F6PCE1,A0A1Z1RFH7,A0A1Z1RFJ4,A0A1Z1RFK4,A0A1Z1RGY2,A0A2S0DAE5,A0A2S0DAF7,A0A2S0DAG6,A0A2U3T9J1,A0A2U3T9M9,A0A2U3T9Q0,A0A346TQD9,A0A346TQF4,A0A346TQH9,A9YUH2,B3FQR5,B3V7B6,B3V7C1,B3V7C6,C3VQ34,C3VQ36,C3VQ41,C3VQ46,D0F055,D0F075,D0F080,D3XCG4,D3XCH4,D3XCP9,D3XCR4,D3XCT4,D3XCV4,D3XCV9,D3XCY4,D3XD04,D3XD19

Functional_annotation:
Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription.


Viral_family: Polyomaviridae
Species: WU polyomavirus
Name: Small T antigen
Aliases: Small t antigen, ST, ST-AG
UniProtID_Ref: A5HBD7
UniProt_Name_Ref: ST_POVWU
Binding_ligand: indirect/unknown
Function: TR, Other
Primary_secondary_vTR: S
ChIP: I(19282432)
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(19282432)
EMSA: I(19282432)
Other_assays: I(17158797)
Human_infection_evidence: 21994565.0
UniProt_IDs_Orthologs:
A0A023IWX3,A0A0F6PCF2,A0A2U3T9P7,A0A2U3T9T2,A0A346TQI0,A9YUH3,B3V7B7,B3V7C2,B3V7C7,B9VQY3,B9VQY4,C3VQ42,C3VQ47,D0F056,D0F066,D3XCF0,D3XCH0,D3XCL0,D3XCV5,D3XD10,E2FKL4,E2FKL5,E2FKL6,E2FKL7,E2FKL8,E2FKL9,E2FKM0


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: NPH-1
Aliases: BVTX09c1_072, Transcription termination factor NPH-I
UniProtID_Ref: Q6TVB6
UniProt_Name_Ref: Q6TVB6_9POXV
UniProt_IDs_Orthologs: A0A0E3XAG7
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 22362531.0
Notes: Inferred from Vaccinia virus NPH-1. Involved in transcription termination (27189950)
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Other_assays:
I(11279216, Transcription Termination Assay), I(27189950, Transcription Termination Assay), I(7829483)


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: ORF084
UniProtID_Ref: Q6TVA4
UniProt_Name_Ref: Q6TVA4_9POXV
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(10077573, Transcription Assay), I(15471883, Transcription Assay)
Human_infection_evidence: 22362531.0
Functional_annotation: Not annotated
Aliases:
BVTX09c1_084, BVTX09c15_084, BVTX09c5_084, Intermediate transcription factor VITF-3, ORF084 intermediate transcription factor VITF-3


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: Phosphoprotein
UniProtID_Ref: V5LTE9
UniProt_Name_Ref: V5LTE9_9POXV
UniProt_IDs_Orthologs: A0A0E3XBH8,Q6TVF6,V5LUD0
Binding_ligand: ssDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(9525612)
Other_assays: N
Human_infection_evidence: 22362531.0
Notes: V5LTE9 is inferred from Orf virus protein Q6TVT8. Ligand is based on prediction domains.
Functional_annotation: single-stranded DNA binding
Aliases:
BVTX09c1_032, DNA-binding phosphoprotein, ORF032 DNA-binding phosphoprotein, Putative DNA binding phosphoprotein


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: RAP94
UniProtID_Ref: Q6TVC8
UniProt_Name_Ref: Q6TVC8_9POXV
UniProt_IDs_Orthologs: A0A0E3XBV7
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(1565650)
EMSA: N
Other_assays: I(11279216, 18455214, 8125977)
Human_infection_evidence: 22362531.0
Notes: Q6TVC8 is inferred from Molluscum contagiosum virus protein Q98252
Functional_annotation: DNA-binding transcription factor activity
Aliases:
BVTX09c15_060, ORF060 RNA polymerase-associated protein RAP94, RNA polymerase-associated protein RAP94


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: VITF-3
UniProtID_Ref: Q6TV88
UniProt_Name_Ref: Q6TV88_9POXV
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(10077573, Transcription Assay), I(15471883, Transcription Assay)
Human_infection_evidence: 22362531.0
Functional_annotation: Not annotated
Aliases:
BVTX09c1_100, Intermediate transcription factor VITF-3, ORF100 intermediate transcription factor VITF-3


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: VLTF-2
UniProtID_Ref: Q6TVB2
UniProt_Name_Ref: Q6TVB2_9POXV
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8371339)
EMSA: I(9445047)
Other_assays: I(8371339)
Human_infection_evidence: 22362531.0
Functional_annotation: zinc ion binding
Aliases:
BVTX09c1_076, BVTX09c15_076, BVTX09c5_076, Late transcription factor VLTF-2, ORF076 late transcription factor VLTF-2


Viral_family: Poxviridae
Species: Bovine papular stomatitis virus
Name: VLTF-3
UniProtID_Ref: Q6TVB1
UniProt_Name_Ref: Q6TVB1_9POXV
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8371340)
EMSA: N
Other_assays: I(8676468, Transcription Assay), I(8523544, Transcription Assay)
Human_infection_evidence: 22362531.0
Functional_annotation: regulation of viral transcription
Aliases:
BVTX09c1_077, BVTX09c15_077, BVTX09c5_077, Late transcription factor VLTF-3, ORF077 late transcription factor VLTF-3


Viral_family: Poxviridae
Species: Cowpox virus
Name: ATPase
UniProtID_Ref: Q0NPW0
UniProt_Name_Ref: Q0NPW0_COWPX
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: N
Human_infection_evidence: Fields Virology
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Aliases:
CPXV128, CPXV128 protein, CPXV_GER91_3_120, CPXV_UK2000_K2984_121, E11L, Nucleoside triphosphate phosphohydrolase-I

UniProt_IDs_Orthologs:
A0A1X9T706,A0A212PN19,A0A212PXC4,A0A212Q0S7,A0A212QBP3,A0A212QF28,A0A290GQC0,A0A2R8F699,A0A2R8F8J3,G0XSL1,G0XX58,G0XXS0,Q80DX1,Q8QMV1,U5TA95,U5TH94,U5TL23

Other_assays:
I(11279216, Transcription Termination Assay), I(27189950, Transcription Termination Assay), I(7829483)

Notes:
Q0NPW0 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).


Viral_family: Poxviridae
Species: Cowpox virus
Name: CPXV082
UniProtID_Ref: Q8QMY7
UniProt_Name_Ref: Q8QMY7_COWPX
Binding_ligand: ssDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(9525612)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: Q8QMY7 is inferred from Orf virus protein Q6TVT8
Functional_annotation: single-stranded DNA binding
Aliases:
CPXV082 CDS, CPXV082 protein, CPXV_FIN2000_MAN_077, CPXV_GER1990_2_077, CPXV_GER1998_2_077, L3L, SsDNA-binding phosphoprotein

UniProt_IDs_Orthologs:
A0A1B5FLL2,A0A1X9T8A7,A0A1X9T9H7,A0A212PNL9,A0A212PWW6,A0A212Q1T2,A0A212Q3S3,A0A212QAR0,A0A290G6V1,A0A2R8F5R8,A0A3Q9TCS7,G0XSG7,G0XTD2,G0XTZ5,G0XUL0,G0XV73,G0XVT9,G0XWF3,G0XX14,G0XXM6,Q0NQ03,Q76QK8,U5T9P9,U5TAE0,U5TB25


Viral_family: Poxviridae
Species: Cowpox virus
Name: RAP94
UniProtID_Ref: Q0NPX4
UniProt_Name_Ref: Q0NPX4_COWPX
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(1565650)
EMSA: N
Other_assays: I(11279216, 18455214, 8125977)
Human_infection_evidence: Fields Virology
Notes: Q0NPX4 is inferred from Molluscum contagiosum virus protein Q98252
Functional_annotation: DNA-binding transcription factor activity
Aliases:
CPXV113, CPXV113 protein, CPXV_GER1990_2_107, CPXV_GER91_3_106, CPXV_NOR1994_MAN_107, J4L protein, RNA polymerase subunit RAP94

UniProt_IDs_Orthologs:
A0A1B5FLM3,A0A1S5WL33,A0A1V0FXA5,A0A1X9T7J1,A0A1X9TAC4,A0A1X9TB56,A0A212PQT9,A0A212PTE6,A0A212PU56,A0A212PWW4,A0A212Q3P6,A0A290G4Y9,A0A290G7N2,G0XSJ7,G0XTG2,G0XU25,G0XUP0,G0XVW9,G0XWI3,G0XXQ6,Q80DY0,Q8QMW3,U5TA80,U5TDQ9,U5TK54,U5TPC8


Viral_family: Poxviridae
Species: Cowpox virus
Name: VETFL
UniProtID_Ref: Q0NPV0
UniProt_Name_Ref: Q0NPV0_COWPX
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(1869571, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: Fields Virology
Notes: Q0NPV0 is inferred from Bovine papular stomatitis virus protein Q6TVA5
Functional_annotation: positive regulation of transcription, DNA-templated
Aliases:
82kDa large subunit of early gene transcription factor VETF, A8L, A8L protein, CPX139, CPXV139, CPXV139 protein, CPXV_GER91_3_130, CPXV_NOR1994_MAN_131, Early gene transcription factor VETF 82 kDa large subunit, Early gene transcription factor VETF 82kDa large subunit

UniProt_IDs_Orthologs:
A0A1X9T7I9,A0A212PNT3,A0A212PPV0,A0A212Q0X2,A0A212Q246,A0A212Q430,A0A290GA76,A0A290GLX5,A0A2R8F5T9,A0A3Q9TBA2,G0XSM1,G0XU49,G0XUR4,G0XVC7,G0XVZ3,G0XWK7,G0XX68,Q80DW4,Q8QMU3,U5TA85,U5TD88,U5TG43,U5TGS1


Viral_family: Poxviridae
Species: Cowpox virus
Name: VETFs
UniProtID_Ref: Q76QJ5
UniProt_Name_Ref: Q76QJ5_COWPX
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: Fields Virology
Notes: Q76QJ5 is inferred from Bovine papular stomatitis virus protein Q6TVB9
Functional_annotation: ATP binding,DNA binding,hydrolase activity,integral component of membrane
Aliases:
70 kDa VETF transcription factor small subunit, 70kDa small subunit of early transcription initiation factor VETF, CPXV123, CPXV123 protein, CPXV_FIN2000_MAN_116, E6R, E6R protein, Early gene transcription factor VETF 70 kDa small subunit, Early gene transcription factor VETF 70kDa small subunit

UniProt_IDs_Orthologs:
A0A212PQ86,A0A212Q0R7,A0A212Q433,A0A2R8F8M7,G0XSK6,G0XU34,G0XVB2,G0XVX8,G0XWJ2,Q0NPW5,Q8QMV4,U5T9K9,U5TAT0,U5TC84


Viral_family: Poxviridae
Species: Cowpox virus
Name: VITF-3
UniProtID_Ref: A0A0K2YTA9
UniProt_Name_Ref: A0A0K2YTA9_COWPX
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(10077573, Transcription Assay), I(15471883, Transcription Assay)
Human_infection_evidence: Fields Virology
Functional_annotation: Not annotated
Aliases:
32 kDa small subunit of transcription factor VITF-3, A9R, A9R protein, CPXV140 protein, Transcription factor VITF-3 32 kDa small subunit


Viral_family: Poxviridae
Species: Cowpox virus
Name: VLTF-4
UniProtID_Ref: Q0NPX3
UniProt_Name_Ref: Q0NPX3_COWPX
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(8794318, Transcription Assay)
Human_infection_evidence: Fields Virology
Notes: Q0NPX3 is inferred from Vaccinia virus protein Q76RC5
Functional_annotation: viral envelope
Aliases:
CPXV114, CPXV114 protein, CPXV_GER91_3_107, J5R, J5R protein, Morphogenesis-related substrate of B1R kinase, Substrate of B1R kinase, VLTF-4 viral late transcription factor

UniProt_IDs_Orthologs:
A0A1B5FLM5,A0A1S5WL30,A0A1X9T7T5,A0A1X9T8H8,A0A212PNP9,A0A212PQU1,A0A212Q403,A0A212QEI9,A0A212RA96,G0XSJ8,G0XTG3,G0XU26,G0XUP1,G0XVA4,G0XVX0,G0XWI4,G0XX45,G0XXQ7,Q80DX9,Q8QMW2,U5TDR6,U5TJX5,U5TK75


Viral_family: Poxviridae
Species: Molluscum contagiosum virus
Name: NPH-1
Aliases: NPH1, Nucleoside triphosphatase I, Nucleoside triphosphate phosphohydrolase I
UniProtID_Ref: Q98267
UniProt_Name_Ref: NTP1_MCV1
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 24558417.0
Other_assays:
I(11279216, Transcription Termination Assay), I(27189950, Transcription Termination Assay), I(7829483)

Notes:
Q98267 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).

Functional_annotation:
DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity).


Viral_family: Poxviridae
Species: Molluscum contagiosum virus
Name: NPH-II
Aliases: NPH2, NTPase II, Nucleoside triphosphatase II, RNA helicase NPH-II
UniProtID_Ref: Q98218
UniProt_Name_Ref: NPH2_MCV1
Binding_ligand: ssDNA, ssRNA
Function: TR, TNA, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(8505308)
Other_assays: I(20110368, 2839505, 4364422)
Human_infection_evidence: 24558417.0
Functional_annotation:
NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles (By similarity).


Viral_family: Poxviridae
Species: Molluscum contagiosum virus
Name: VETFL
Aliases: Early transcription factor 82 kDa subunit, ETF large subunit, MC110L
UniProtID_Ref: Q98277
UniProt_Name_Ref: ETF2_MCV1
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(1869571, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 24558417.0
Functional_annotation:
Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters (By similarity).


Viral_family: Poxviridae
Species: Molluscum contagiosum virus
Name: VETFs
UniProtID_Ref: Q98262
UniProt_Name_Ref: ETF1_MCV1
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 24558417.0
Aliases:
ATP-dependent helicase VETFS, Early transcription factor 70 kDa subunit, Early transcription factor 70 kDa subunit , ETF small subunit, MC095R

Functional_annotation:
Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters (By similarity).


Viral_family: Poxviridae
Species: Monkeypox virus
Name: A9R
UniProtID_Ref: Q3I8P5
UniProt_Name_Ref: Q3I8P5_MONPV
UniProt_IDs_Orthologs: F1DJH2,Q3I7J8,Q5IXQ6,Q8V4W7,V9NQ18
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(10077573, Transcription Assay), I(15471883, Transcription Assay)
Human_infection_evidence: 29927927.0
Aliases:
32 kDa small subunit of transcription factor VITF-3, 32kDa small subunit of transcription factor VITF-3 used for intermediate gene expression, Transcription factor VITF-3 32 kDa small subunit, VITF-3 34kDa subunit


Viral_family: Poxviridae
Species: Monkeypox virus
Name: E11L
Aliases: ATPase, Bifunctional ATPase/nucleoside triphosphate phosphohydrolase-I, NPH1
UniProtID_Ref: Q3I8Q6
UniProt_Name_Ref: Q3I8Q6_MONPV
UniProt_IDs_Orthologs: A0A0F6N8U0,Q5IXR7
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: N
Human_infection_evidence: 29927927.0
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Notes:
Q3I8Q6 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VETFL
UniProtID_Ref: Q3I8P6
UniProt_Name_Ref: Q3I8P6_MONPV
UniProt_IDs_Orthologs: Q5IXQ7,Q8V4W8
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(1869571, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 29927927.0
Notes: Q3I8P6 is inferred from Bovine papular stomatitis virus protein Q6TVA5
Functional_annotation: positive regulation of transcription, DNA-templated
Aliases:
82 kDa large subunit of early gene transcription factor VETF, A8L, Early gene transcription factor VETF 82 kDa large subunit, VETF-L (Early transcription factor large)


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VETFs
UniProtID_Ref: Q5IXS2
UniProt_Name_Ref: Q5IXS2_MONPV
UniProt_IDs_Orthologs: F1DIW0,Q3I8R1
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 29927927.0
Notes: Q5IXS2 is inferred from Bovine papular stomatitis virus protein Q6TVB9
Functional_annotation: ATP binding,DNA binding,hydrolase activity,integral component of membrane
Aliases:
70 kDa small subunit of early gene transcription factor VETF, E6R, Morphogenesis, MPXV-COP-097, MPXV-SL-097, MPXV-WRAIR097, VETF2, VETF-s (Early transcription factor small)


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VLTF-1
UniProtID_Ref: Q5IXU7
UniProt_Name_Ref: Q5IXU7_MONPV
UniProt_IDs_Orthologs: F1DJD1,Q77HN3
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(15471883, Transcription Assay), I(2041091, Transcription Assay), I(2476568, Transcription Assay)
Human_infection_evidence: 29927927.0
Notes: Q5IXU7 is inferred from Orf virus protein Q6TVS5
Functional_annotation: regulation of transcription, DNA-templated,integral component of membrane
Aliases:
G9R, Late gene transcription VLTF-1, Late transcription factor VLTF-1, MPXV-COP-072, MPXV-SL-072, MPXV-WRAIR072


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VLTF-2
UniProtID_Ref: Q5IXR4
UniProt_Name_Ref: Q5IXR4_MONPV
UniProt_IDs_Orthologs: Q77HM9
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8371339)
EMSA: I(9445047)
Other_assays: I(8371339)
Human_infection_evidence: 29927927.0
Notes: Q5IXR4 is inferred from Molluscum contagiosum virus protein Q98270
Functional_annotation: zinc ion binding
Aliases:
A1L, Late gene transcription factor VLTF-2, Late transcription factor VLTF-2, MPXV-COP-105, MPXV-SL-105, MPXV-WRAIR105, Viral late gene transcription factor 2


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VLTF-3
UniProtID_Ref: Q5IXR3
UniProt_Name_Ref: Q5IXR3_MONPV
UniProt_IDs_Orthologs: Q3I8Q2,Q8V4X4
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8371340)
EMSA: N
Other_assays: I(8676468, Transcription Assay), I(8523544, Transcription Assay)
Human_infection_evidence: 29927927.0
Notes: Q5IXR3 is inferred from Molluscum contagiosum virus protein Q98271
Functional_annotation: regulation of viral transcription
Aliases:
A2L, Late gene transcription factor VLTF-3, Late transcription factor VLTF-3, MPXV-COP-106, MPXV-SL-106, MPXV-WRAIR106, Viral late gene transcription factor 3


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VLTF-4
UniProtID_Ref: Q5IXT0
UniProt_Name_Ref: Q5IXT0_MONPV
UniProt_IDs_Orthologs: F1DIV2,F1DJE8,Q3I8R9
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(8794318, Transcription Assay)
Human_infection_evidence: 29927927.0
Notes: Q5IXT0 is inferred from Vaccinia virus protein Q76RC5
Functional_annotation: viral envelope
Aliases:
H5R, Late gene transcription factor VLTF-4, Late transcription factor VLTF-4, MPXV-COP-089, MPXV-SL-089, MPXV-WRAIR089


Viral_family: Poxviridae
Species: Monkeypox virus
Name: VP8
UniProtID_Ref: Q5IXU2
UniProt_Name_Ref: Q5IXU2_MONPV
UniProt_IDs_Orthologs: Q8V4Z9
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: NAP, TR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(9321647)
Other_assays: I(3201752, 9321647)
Human_infection_evidence: 29927927.0
Notes: Q5IXU2 is inferred from Orf virus protein Q6TVS0
Functional_annotation: DNA binding,structural molecule activity,viral capsid
Aliases:
Core protein vp8, DNA-binding virion core protein, L4R, M4R, MPXV-COP-077, MPXV-SL-077, MPXV-WRAIR077


Viral_family: Poxviridae
Species: Orf virus
Name: NPH-1
UniProtID_Ref: Q6TVP8
UniProt_Name_Ref: Q6TVP8_ORFSA
UniProt_IDs_Orthologs: A0A0R8HW06,A0A0R8IAB0,F1AX80,Q2F8A3,W5U9E8
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 25807056.0
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Aliases:
ORF072 transcription termination factor NPH-I, ORFV072, PP62, Transcription termination factor NPH-I

Notes:
Q6TVP8 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).


Viral_family: Poxviridae
Species: Orf virus
Name: ORF038
UniProtID_Ref: Q6TVT1
UniProt_Name_Ref: Q6TVT1_ORFSA
UniProt_IDs_Orthologs: A0A0R8IE54,F1AX11,Q2F8D6,Q80B06,W5U438
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: N
Human_infection_evidence: 25807056.0
Notes: Q6TVT1 is inferred from Bovine papular stomatitis virus protein Q6TVE9
Functional_annotation: translation elongation factor activity
Aliases:
G2R-like protein, Late transcription elongation factor, ORF038 late transcription elongation factor, ORFV038, PP176


Viral_family: Poxviridae
Species: Orf virus
Name: RAP94
UniProtID_Ref: Q6TVR0
UniProt_Name_Ref: Q6TVR0_ORFSA
UniProt_IDs_Orthologs: A0A0R8HSC6,A0A0R8HVU7,A0A0R8HW49,A0A0R8I9E8,F1AX49,F1AX50,Q86619,W5U3P9
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(1565650)
EMSA: N
Other_assays: I(11279216, 18455214, 8125977)
Human_infection_evidence: 25807056.0
Notes: Q6TVR0 is inferred from Molluscum contagiosum virus protein Q98252
Functional_annotation: DNA-binding transcription factor activity
Aliases:
F2L, ORF060 RNA polymerase-associated protein RAP94, ORFV060, PP81, PP82, RNA polymerase-associated protein RAP94, RNA-polymerase associated protein RAP94


Viral_family: Poxviridae
Species: Orf virus
Name: VETFL
UniProtID_Ref: Q6TVN7
UniProt_Name_Ref: Q6TVN7_ORFSA
UniProt_IDs_Orthologs: A0A0R8HJ22,A0A0R8I2G6,F1AXA1,Q2F892,Q6TW17,W5U3D9
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(1869571, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 25807056.0
Notes: Q6TVN7 is inferred from Bovine papular stomatitis virus protein Q6TVA5
Functional_annotation: positive regulation of transcription, DNA-templated
Aliases:
Early transcription factor, Early transcription factor VETFL, ORF083 early transcription factor VETFL, ORFV083, PP53


Viral_family: Poxviridae
Species: Orf virus
Name: VETFs
UniProtID_Ref: Q6TVQ1
UniProt_Name_Ref: Q6TVQ1_ORFSA
UniProt_IDs_Orthologs: A0A0F6N1P6,A0A0R8HK40,A0A0R8HYN4,F1AX73,Q2F8A6,Q6TW31,W5U458
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 25807056.0
Notes: Q6TVQ1 is inferred from Bovine papular stomatitis virus protein Q6TVB9
Functional_annotation: integral component of membrane
Aliases:
Early transcription factor, Early transcription factor VETFs, ORF069 early transcription factor VETFs, ORFV069, PP213


Viral_family: Poxviridae
Species: Orf virus
Name: VLTF-3
UniProtID_Ref: Q6TVP3
UniProt_Name_Ref: Q6TVP3_ORFSA
UniProt_IDs_Orthologs: A0A0R8I8Z6,F1AX92,Q6TW23
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8371340)
EMSA: N
Other_assays: I(8676468, Transcription Assay), I(8523544, Transcription Assay)
Human_infection_evidence: 25807056.0
Notes: Q6TVP3 is inferred from Molluscum contagiosum virus protein Q98271
Functional_annotation: regulation of viral transcription
Aliases:
Late transcription factor VLTF3, Late transcription factor VLTF-3, ORF077 late transcription factor VLTF-3, ORFV077, PP57


Viral_family: Poxviridae
Species: Pseudocowpox virus
Name: NPH-1
UniProtID_Ref: D3IZL9
UniProt_Name_Ref: D3IZL9_9POXV
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 25674608.0
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Notes:
D3IZL9 is inferred from Bovine papular stomatitis virus protein Q6TVB6.  Involved in transcription termination (27189950).


Viral_family: Poxviridae
Species: Tanapox virus
Name: NPH-1
Aliases: 88L, Transcription termination factor NPH-1
UniProtID_Ref: A7XCL5
UniProt_Name_Ref: A7XCL5_9POXV
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 25255815.0
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Notes:
A7XCL5 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).


Viral_family: Poxviridae
Species: Vaccinia virus
Name: NPH1
UniProtID_Ref: Q1PIT3
UniProt_Name_Ref: Q1PIT3_9POXV
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8230476)
EMSA: N
Other_assays: D(7829483)
Human_infection_evidence: Fields Virology
Functional_annotation: ATP binding,nucleoside-triphosphatase activity,transcription, DNA-templated
Aliases:
44.1rMVA_104, ATPase, CVA122, D11L, Early gene termination factor/Nucleoside triphosphatase I, Factor X, GL151, Nucleoside triphosphatase I, Nucleoside triphosphate phosphohydrolase-I, Putative uncharacterized protein, VACV112, VACV_BRZ_SERRO2_114, VACV-DUKE-124, VACV_IOC_B388_142, W86/88-1-112

UniProt_IDs_Orthologs:
A0A0A7A5M3,A0A0M4S9W7,A0A2I2MC53,A0A2I6J1B6,A4GDH1,A9J1V1,B9U1K8,L7QJK3,O57214,P05807,P20637,Q1PIT3,V5QZL6


Viral_family: Poxviridae
Species: Vaccinia virus
Name: I3L
UniProtID_Ref: P12923
UniProt_Name_Ref: I3_VACCW
Binding_ligand: ssDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(9525612)
Other_assays: N
Human_infection_evidence: Fields Virology
Aliases:
30k DNA binding phosphoprotein, DNA-binding phosphoprotein, GL094, MVA064L, Protein I3, SsDNA-binding phosphoprotein, TI3L, VAC_DPP12_083, VAC_TKT3_062, VACV_BRZ_SERRO2_070, VACV_IOC_B141_098, VACWR072, W86/88-1-068

UniProt_IDs_Orthologs:
A0A0A1CQQ4,A0A0A7A5D0,A0A0M4SA87,A0A0R5TUB6,A0A2I2MDT9,B9U1F0,H2DU26,O93118,P20499,Q1PIX7,Q49QJ4,Q9JFC7,V5R1E3

Functional_annotation:
Plays an essential role in viral DNA replication. Binds to ssDNA with high affinity and localizes to cytoplasmic factories where nascent viral genomes accumulate. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.


Viral_family: Poxviridae
Species: Vaccinia virus
Name: NPH-II
Aliases: I8R, NPH2, NTPase II, Nucleoside triphosphatase II, RNA helicase I8, RNA helicase NPH-II
UniProtID_Ref: P12927
UniProt_Name_Ref: NPH2_VACCW
Binding_ligand: ssDNA, ssRNA
Function: TR, TNA, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(8505308; 7609038)
Other_assays: D(20110368, 2839505, 4364422)
Human_infection_evidence: Fields Virology
Functional_annotation:
NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles.


Viral_family: Poxviridae
Species: Vaccinia virus
Name: RAP94
UniProtID_Ref: P68438
UniProt_Name_Ref: RAP94_VACCW
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(1565650)
EMSA: N
Other_assays: D(11279216, 18455214, 8125977)
Human_infection_evidence: Fields Virology
Aliases:
H4L, Protein H4, RNA polymerase-associated transcription-specificity factor RAP94, RPO-associated protein of 94 kDa, VACWR102

UniProt_IDs_Orthologs:
A0A0A1CQS7,A0A0A1CRL1,A0A0A1CUE4,A0A0A7A5E7,A0A0M5M2K1,A0A2I2MDW5,A0A2I6TDW8,A9J1S4,B9U1I7,M9WEP8,M9WGZ2,P68439,Q1PIU7

Functional_annotation:
DNA-directed RNA polymerase-associated factor required for the transcription of viral early genes as well as for transcription termination. Within minutes after virus entry, recruits the core RNA polymerase, the early transcription factor (ETF) and other enzymes needed for transcription initiation, elongation, and termination thereby allowing synthesis of early mRNAs which are extruded through pores in the core particle. Recruits the multifunctional J3 protein, with poly(A) polymerase-stimulatory, cap nucleoside-2'-O-methyltransferase, and transcription elongation activities. Interacts with NPH-I, a DNA-dependent ATPase required for the termination of early transcripts. Acts as a transcription termination factor by binding, together with the capping enzyme/VTF, to the termination motif 5'-UUUUUNU-3' in the nascent mRNA. Involved as well in the packaging of RNA polymerase and other components needed for early transcription in assembling virus particles.


Viral_family: Poxviridae
Species: Vaccinia virus
Name: VETFs
UniProtID_Ref: P04308
UniProt_Name_Ref: ETF1_VACCW
UniProt_IDs_Orthologs: A0A160NBD6,A0A2I6J267,A9J1U1,P20634,Q9JFA3
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8376362)
EMSA: D(7784215, 1869571, 8350421, 8376362)
Other_assays: D(1869571, 8428951, 2839505)
Human_infection_evidence: Fields Virology
Aliases:
ATP-dependent helicase VETFS, CVA117, D6R, Early transcription factor 70 kDa subunit, ETF small subunit, Vaccinia virus early transcription factor small subunit, VACWR111, VETF D6 subunit, VETF small subunit, VETFS

Functional_annotation:
Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters.


Viral_family: Poxviridae
Species: Vaccinia virus
Name: VLTF-3
UniProtID_Ref: P68319
UniProt_Name_Ref: VLTF3_VACCW
UniProt_IDs_Orthologs: A0A0A7A6B8,A0A0M5M2K3,A0A2I2MC78,A0A2I6J289,A9J0P1,B9U1L8,Q76ZR2
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8371340)
EMSA: N
Other_assays: I(8676468, Transcription Assay), I(8523544, Transcription Assay)
Human_infection_evidence: Fields Virology
Functional_annotation: Acts with RNA polymerase to initiate transcription from late gene promoters.
Aliases:
A2L, CVA126,GL161, Trans-activator protein A2, VACV_BRZ_SERRO2_118, VACV_IOC_B141_146,A2L, VACWR120, Viral late gene transcription factor 3, VLTF3


Viral_family: Poxviridae
Species: Vaccinia virus
Name: VLTF-4
UniProtID_Ref: Q76RC5
UniProt_Name_Ref: Q76RC5_9POXV
UniProt_IDs_Orthologs: A0A2I2MC42,A0A2I6J256,B9U1I8,H2DV26,M9WGD8,Q1PIU6
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: D(8794318, Transcription Assay)
Human_infection_evidence: Fields Virology
Functional_annotation: viral envelope
Aliases:
H5R,GL131,VAC_DPP13_114,VACV_BRZ_SERRO2_101, late transcription factor, Late gene transcription factor VLTF-4, MVA095R


Viral_family: Poxviridae
Species: Vaccinia virus
Name: VP8
UniProtID_Ref: P03295
UniProt_Name_Ref: VP8_VACCW
UniProt_IDs_Orthologs: A0A0A7A5K7,A0A2I6J178,A0A2I6J232,A0ERU0,B9U1H3,L7QJ25,P20981,Q1M1M8,Q49PP2,Q76RD0,Q77TK7
Binding_ligand: dsDNA, ssDNA, ssRNA, dsRNA
Function: NAP, TR
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: D(9321647)
Other_assays: D(3201752, 9321647)
Human_infection_evidence: Fields Virology
Functional_annotation: Major core structural protein.
Aliases:
25 kDa major core protein, Core protein VP8, DNA-binding virion core protein VP8, F5 polypeptide, L4 core protein, L4R, P25K, VACWR091


Viral_family: Poxviridae
Species: Variola virus
Name: I3L
UniProtID_Ref: P0DOP3
UniProt_Name_Ref: I3_VAR67
UniProt_IDs_Orthologs: A0A1U8QRX5,P33000,Q0N589,Q0N8Q3,Q0NAF4,Q0NCR4,Q0NG81,Q0NLZ6
Binding_ligand: ssDNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(9525612)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes: P33000 is inferred from Orf virus protein Q6TVT8
Aliases:
K3L, L3L, L3L protein, Protein I3, SsDNA-binding phosphoprotein, VARV_BRZ66_39_061, VARV_JAP46_yam_061, VARV_SAF65_102_061, VARV_SOM77_1252_061, VARV_SUM70_228_061

Functional_annotation:
Single-stranded DNA (ssDNA)-binding phosphoprotein which stimulates the enzymatic activity of vaccinia ribonucleotide reductase. In the absence of magnesium and at low I3 concentration, I3 forms beaded nucleosome-like structures on ssDNA. In the presence of magnesium and at high I3 concentration, I3 and DNA aggregate into large branched filamentous structures. Might be essential for viral parental DNA replication.


Viral_family: Poxviridae
Species: Variola virus
Name: NPH-1
UniProtID_Ref: P0DOQ3
UniProt_Name_Ref: NTP1_VAR67
UniProt_IDs_Orthologs: P0DOQ3,P33066,Q0N545,Q0N5Q2,Q0NBG5,Q0NCM0,Q0NG37,Q0NLV2
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: Fields Virology
Aliases:
ATPase, ATPase nucleoside triphosphate phosphohydrolase-I, D11L, N1L, NPH1, nucleoside triphosphate phosphohydrolase-I, Nucleoside triphosphatase I, Nucleoside triphosphate phosphohydrolase I, VARV_BEN68_59_105, VARV_BRZ66_39_105, VARV_JAP46_yam_105, VARV_SAF65_102_105, VARV_UNK52_but_105, VARV-VD21-UVic-107

Notes:
P33066 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).

Functional_annotation:
DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity).


Viral_family: Poxviridae
Species: Variola virus
Name: NPH-II
UniProtID_Ref: P0DSU5
UniProt_Name_Ref: NPH2_VAR67
UniProt_IDs_Orthologs: A0A1L6K3L4,P33051,Q0N584,Q0N5U1,Q0N848,Q0NAE9,Q0NCQ9,Q0NDB5,Q0NG76,Q0NLZ1
Binding_ligand: ssDNA, ssRNA
Function: TR, TNA, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: I(8505308)
Other_assays: I(20110368, 2839505, 4364422)
Human_infection_evidence: Fields Virology
Aliases:
I8R, NPH2, NTPase II, Nucleoside triphosphatase II, Nucleoside triphosphate phosphohydrolase II, RNA helicase I8, RNA helicase NPH-II

Functional_annotation:
NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles (By similarity).


Viral_family: Poxviridae
Species: Variola virus
Name: RAP94
UniProtID_Ref: P0DSR3
UniProt_Name_Ref: RAP94_VAR67
UniProt_IDs_Orthologs: A0A1U8QUB4,P33067,Q0N559,Q0N823,Q0NCN4,Q0NEZ8,Q0NG51,Q0NLW6,Q0NWC1,Q89218
Binding_ligand: ssRNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(1565650)
EMSA: N
Other_assays: I(11279216, 18455214, 8125977)
Human_infection_evidence: Fields Virology
Aliases:
H4L, Protein H4, RNA polymerase-associated transcription-specificity factor RAP94, RPO-associated protein of 94 kDa

Functional_annotation:
DNA-directed RNA polymerase-associated factor required for the transcription of viral early genes as well as for transcription termination. Within minutes after virus entry, recruits the core RNA polymerase, the early transcription factor (ETF) and other enzymes needed for transcription initiation, elongation, and termination thereby allowing synthesis of early mRNAs which are extruded through pores in the core particle. Recruits the multifunctional J3 protein, with poly(A) polymerase-stimulatory, cap nucleoside-2'-O-methyltransferase, and transcription elongation activities. Interacts with NPH-I, a DNA-dependent ATPase required for the termination of early transcripts. Acts as a transcription termination factor by binding, together with the capping enzyme/VTF, to the termination motif 5'-UUUUUNU-3' in the nascent mRNA. Involved as well in the packaging of RNA polymerase and other components needed for early transcription in assembling virus particles (By similarity).


Viral_family: Poxviridae
Species: Variola virus
Name: VETFs
UniProtID_Ref: P0DON9
UniProt_Name_Ref: ETF1_VAR67
UniProt_IDs_Orthologs: A0A1L6K3P8,P33056,Q0N550,Q0N5Q7,Q0N814,Q0NCM5,Q0NG42,Q0NLV7,Q0NS90
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: Fields Virology
Aliases:
ATP-dependent helicase VETFS, D6R, Early transcription factor 70 kDa subunit, ETF small subunit, VETF D6 subunit, VETFS


Viral_family: Poxviridae
Species: Variola virus
Name: VLTF-1
UniProtID_Ref: P32990
UniProt_Name_Ref: VLTF1_VAR67
UniProt_IDs_Orthologs: A0A1U8QUS9,Q0N575,Q0NG67,Q0NLY2,Q85380
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(15471883, Transcription Assay), I(2041091, Transcription Assay), I(2476568, Transcription Assay)
Human_infection_evidence: Fields Virology
Functional_annotation: Associates with RNA polymerase to initiate transcription from late gene promoters.
Aliases:
G8R, H8R, I9R, Late transcription factor 1, Trans-activator protein GK1, VARV_BRZ66_39_075, VARV_JAP46_yam_075, VLTF1


Viral_family: Poxviridae
Species: Variola virus
Name: VLTF-4
UniProtID_Ref: P33062
UniProt_Name_Ref: H5_VAR67
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: N
EMSA: N
Other_assays: I(8794318, Transcription Assay)
Human_infection_evidence: Fields Virology
Notes: P33062 is inferred from Vaccinia virus protein Q76RC5
Aliases:
H5R, H5R protein, I5R, J5R, Late transcription elongation factor H5, VLTF-4 viral late transcription factor

UniProt_IDs_Orthologs:
A0A1L6K3P0,A0A1U8QWZ4,Q0N558,Q0N5R5,Q0N6C0,Q0N6X0,Q0N8M2,Q0NBH8,Q0NCN3,Q0ND89,Q0NG50,Q0NGQ2,Q0NLW5,Q0NU07,Q85386,Q89219

Functional_annotation:
Involved in the co-transcriptional or post-transcriptional endoribonucleolytic cleavage that generates sequence-homogeneous 3' ends during late transcription. Involved in postreplicative transcription elongation on intermediate and late genes (Probable). Also involved in DNA replication and in multiple steps of virion morphogenesis. Required both for inclusion of virosoplasm into crescents as well as for maturation of immature virions (IV) into mature virions (MV) (By similarity).


Viral_family: Poxviridae
Species: Yaba monkey tumor virus
Name: NPH-1
Aliases: 88L, B5L, NPH I, Nucleoside triphosphatase I, Nucleoside triphosphate phosphohydrolase I
UniProtID_Ref: Q9QB93
UniProt_Name_Ref: NTP1_YMTV5
Binding_ligand: dsDNA, ssDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8230476)
EMSA: I(9472022)
Human_infection_evidence: 14645589.0
Notes:
Q9QB93 is inferred from Bovine papular stomatitis virus protein Q6TVB6. Involved in transcription termination (27189950).

Functional_annotation:
DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity).


Viral_family: Poxviridae
Species: Yaba monkey tumor virus
Name: VETFs
UniProtID_Ref: Q9QB97
UniProt_Name_Ref: ETF1_YMTV5
Binding_ligand: dsDNA
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8376362)
EMSA: I(7784215, 1869571, 8350421, 8376362)
Other_assays: I(1869571, 8428951)
Human_infection_evidence: 14645589.0
Aliases:
84R, ATP-dependent helicase VETFS, B1R, Early transcription factor 70 kDa subunit, VETF small subunit, VETFS

Functional_annotation:
Acts with RNA polymerase to initiate transcription from early gene promoters. A DNA-dependent ATPase activity is associated with VETF.


Viral_family: Retroviridae
Species: Human immunodeficiency virus 1
Name: Tat
Aliases: Protein tat, tat, Transactivating regulatory protein
UniProtID_Ref: P04608
UniProt_Name_Ref: TAT_HV1H2
Binding_ligand: dsDNA, ssRNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: D(26488441)
ChIP_seq: D(22073215, 26488441, 26468528)
Structure_PDB_ID: 3MI9, 3MIA, 4OR5, 5V61, 6CYT, 6MCE, 6MCF
Reporter_assay: D(11909874)
EMSA: D(15994812, 10428378, 14981150)
Other_assays: D(10428378)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A060KS15,A0A060KV49,A0A060KVI4,A0A076FNR3,A0A076V3Q8,A0A076V8N1,A0A076V943,A0A076V970,A0A089QCW2,A0A0K1RFJ0,A0A0K1RFL6,A0A0K1RFL8,A0A0S2CBE9,A0A0S2CBF6,A0A140GML0,A0A142J5A6,A0A142J5B5,A0A159C854,A0A159C9T1,A0A159C9V0,A0A159C9Z8,A0A159CAC9,A0A159CAP8,A0A161CFV2,A0A161CGQ6,A0A161CP30,A0A161CUQ5,A0A161CUV9,A0A161CV08,A0A161CVH7,A0A161CVX6,A0A161CW94,A0A161D3W4,A0A191CA08,A0A191CAI2,A0A191CAY4,A0A191CB60,A0A1L4AMD3,A0A1L5K0P5,A0A1L5K158,A0A1L5K1D0,A0A1L7DT27,A0A1L7DT44,A0A1L7DT47,A0A1L7DT66,A0A1L7DT91,A0A1L7DT95,A0A1L7DTB6,A0A1L7DTC9,A0A1L7DTF4,A0A1L7DTH0,A0A1L7E051,A0A1L7E086,A0A1L7E087,A0A1L7E088,A0A1L7E0C8,A0A1L7E0F9,A0A1L7E0G4,A0A1L7E0H2,A0A1L7E0J8,A0A1L7E0K6,A0A1L7E0K8,A0A1V0CPR5,A0A221SER0,A0A286LFT1,A0A2H4UM10,A0A2I6U5U1,A0A2I6U5W9,A0A2I6UA56,A0A2I6UAA8,A0A2I6UAP1,A0A2I6UAW6,A0A2I6UAX8,A0A2I6UB20,A0A2I6UB53,A0A2I6UB85,A0A2I6UBB9,A0A2I6UDU7,A0A2I6UE90,A0A2I6UEL9,A0A2I6UEW4,A0A2I6UEY9,A0A2L1KVE2,A0A2L1KVH1,A0A2L1KW66,A0A2L1KWQ3,A0A2L1KWR8,A0A2L1KX14,A0A2L1KXI4,A0A2L1KXX2,A0A2L1KXY1,A0A2L1KY88,A0A2P1IPK3,A0A2S1D2B0,A0A2S1J4U4,A0A346ARF5,A0A3G5NTJ6,A0A3G5NUD8,A0A3G5NVJ6,A0A3G5NWJ1,A0A3G5NXC4,A0A3G5NXJ3,A0A3G5NYA6,A0A3G5NYE3,A0A3G5NZ85,A0A3G5NZA5,A0A3G5NZA6,A0A3G5NZL3,A0A3G5NZN1,A0A3G5P091,A0A3G5P0G4,A0A3G5P116,A0A3G5P120,A0A3G5P1B7,A0A3G5P1C4,A0A3G5P1G0,A0A3G5P1I8,A0A3G5P1Y8,A0A3G5P1Z4,A0A3G5P267,A0A3G5P2F3,A0A3G5P2I3,A0A3G5P2J5,A0A3G5P2R2,A0A3G5P2Z0,A0A3G5P389,A0A3G5P3H0,A0A3G5P3Q1,A0A3G5P4H0,A0A3G8G526,A0ZVI9,A1DQV4,A1DQW3,A1DQW5,A1DQW7,A1DQW8,A1DQW9,A1DQX7,A1DQY0,A1DQY3,A1DQY5,A1DQY9,A1XFJ7,A1YAW1,A1YAX9,A3F992,A3F9A1,A3QVS4,A6MI20,A6MI21,A6MI22,A7YJW9,A8VGQ3,A8VGY9,A8VH75,A8VH95,A8VHA7,A8VHB4,A9U9H5,A9U9M0,A9U9M9,A9U9N8,A9U9S0,A9XCI1,B4YNJ3,B4YNL1,B4YNM3,B5AEQ4,B5AEU9,B7SWF0,B7TCC4,C4N7C1,C4N7J1,C5HA95,C5HAJ4,C5HAS7,C5HB94,C5HMU5,C5HN12,C5HNI8,C5HNW1,C5HNW7,C5HP06,C5HP90,C5HPB9,C5HR51,C5HS75,C7G256,C9E906,C9E908,C9E921,C9E988,D2CPM3,D2CPN7,D2CPN9,D2CPP0,D2CPR0,D2CPR1,D2CPS1,D2CPS6,D2CPS8,D2CPS9,D2CPU3,D2CPU4,D2K3B0,D3GG08,D3XND1,D3XND2,D3XND4,D4PC16,D4PC24,D4PE12,D5KEK7,D5KIN8,D5KIP6,D5KIS0,D5KIS8,D5KIY2,D5KIZ8,D5KJ06,D5KJ38,D5L1M9,D6NSX1,D6NVS0,D6NVS1,D6NVU0,D6NVU1,D6NVV2,D6NVW0,D6NVY1,D6NVY3,D6NVY7,D6NVY9,D6NVZ5,D6NW12,D6NW21,D6NW28,D6NW43,D6NW48,D6NW73,D6NW81,D6NW87,D6NW91,D6NW95,D6NW99,D6NWA0,D6NWA9,D6NWB6,D6NWC9,D6NWD4,D6NWE4,D6NWG1,D6NWH7,D6NWI8,D6NWI9,D6NWL1,D6NWM1,D6NWN0,D6NWN1,D6NWP0,D6NWP6,D6NWQ6,D6NWQ7,D6NWQ9,D6NWR0,D6NWR9,D6NWS1,D6NWV7,D6NWW8,D6NWY1,D6NWY7,D6NWZ8,D6NX04,D6NX09,D6NX22,D6NX24,D6NX29,D6NX32,D6NX42,D6NX46,D6NX50,D6NX58,D6NX59,D6NX60,D6NX61,D6NX65,D6NX72,D6NX88,D6R020,D6R056,E0A9Z8,E0AA13,E0AA18,E2CX23,E2CX68,F1B2A1,F1B2D3,F1B2G8,F1B2J4,F2YX68,F2YXK1,F2YXW5,F2YXX3,F5BD94,F5CFB7,G1FQH9,G9IQ96,H6CVW9,H6CW09,H6CW27,H6CWA4,H6CWD8,H6CX54,H6CX96,H6CXE0,H6CXE9,H6CXL2,I6N0A1,I6N0B0,I6N0B8,I6N0C6,I6N0D5,I6N0H9,I6QQN9,I6QTV7,I6R588,I6R5M0,I6R5Z2,I6R6E2,I6RBY5,I6RC25,I6RCG3,I6RG27,I6RGA6,I6RGK4,I6ZAD6,J3QYE6,J3QYF5,J3R262,J3R280,J3R298,J3R2A7,J3R8L1,J3R8M0,J3R8N0,J3R8N9,J3R8P8,J3RA22,J3RA49,J3RA58,J3RA67,J3RA77,J3RAX7,J3RB02,J3RB14,J3RB36,K4MKX3,K4MUI9,K4MYG3,M1KBE1,M1KBR3,M1LDW1,M4N2F6,M4N4H9,M4N943,M4N949,M4N966,M4NNN7,M4NRQ0,M4NRV8,M4PFA9,M4PHN2,M4PJ36,M4PJC5,M4PQG5,O42085,O92297,O92885,O92899,O93022,O93199,P90265,Q00EI6,Q0QL80,Q0QL89,Q1HGD2,Q1HGE1,Q1M0L8,Q1M0M7,Q1PAB4,Q1PAC0,Q2NMF7,Q2NMG6,Q2NMH5,Q2NMI4,Q2NMJ3,Q2NMM8,Q2NMP6,Q2NMS3,Q2NMT2,Q2NMU1,Q2NMV9,Q2NMW8,Q2NMX7,Q2NN30,Q2NN39,Q2NN65,Q2NN73,Q30BW0,Q30BX6,Q3SA27,Q462M7,Q462N6,Q4QXE2,Q4QXF9,Q507D6,Q507F1,Q52S52,Q52S62,Q5C9W8,Q5PYM7,Q5PYN4,Q5PYP0,Q5PYP7,Q5U882,Q5U8J9,Q672T0,Q672T8,Q673V9,Q6E6V7,Q6EFM4,Q6EG43,Q6EG88,Q6H1S1,Q6Q463,Q6RJ70,Q6RJ77,Q6RJ84,Q6RJ91,Q6RJ98,Q6RJA5,Q6RJC6,Q6RJD3,Q6RJE0,Q6RJE7,Q6RJG8,Q6RJH5,Q6Y0S7,Q6Y0T6,Q6Y0U6,Q6Y0V1,Q6Y0V2,Q74087,Q74810,Q76PP9,Q76W89,Q77688,Q7ZJC3,Q8AQT3,Q8AQV1,Q8AQW0,Q900A7,Q99BV6,Q99BV7,Q99BV8,Q99BV9,Q99BW0,Q99BW1,Q9DH20,Q9DHA9,Q9DQ29,Q9W9E3,Q9WJV2,Q9WJV9,Q9WJW7,Q9YP37,R9WY72,T2CGB4,T2CGG2,T2CHT3,T2CI19,U5YPQ4,U5YT43,U6BG48,W0FUJ1

Functional_annotation:
Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs.


Viral_family: Retroviridae
Species: Human immunodeficiency virus 1
Name: Vpr
Aliases: Protein Vpr, R ORF protein, Viral protein R
UniProtID_Ref: P05928
UniProt_Name_Ref: VPR_HV1BR
Binding_ligand: indirect/unknown
Function: TR, TNA, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(9560267)
EMSA: D(29042644)
Other_assays: D(9560267, 29042644)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A1L5K181,A0A1L7E075,A0A1L7E0E4,A0A1P8DFL4,A0A1P8DFQ6,A0A1S6Q1Y8,A0A1S7G5I7,A0A1V0CPS3,A0A1V0CQ70,A0A2I6U569,A0A2I6U5R3,A0A2I6U656,A0A2I6U705,A0A2I6U757,A0A2I6U762,A0A2I6U778,A0A2I6U7M6,A0A2I6U992,A0A2I6U9P4,A0A2I6UB19,A0A2I6UB27,A0A2I6UB41,A0A2I6UBA3,A0A2I6UE01,A0A2I6UEX6,A0A2L1KWL5,A0A2L1KWR7,A0A2L1KXB7,A0A2L1KXV9,A0A2L1KXY0,A0A2S1D2C4,A0A2S1J4Z9,A0A2Z2U098,A0A2Z2U294,A0A346ARF4,A0A346BLV9,A0A346BLY6,A0A3G5NS07,A0A3G5NSG1,A0A3G5P0U6,A0A3G5P2U2,A0A3G5P404,A0A3G8G4Y4,A0A3G8G516,A5YMI3,A5YMJ1,A5YML7,A5YML9,A5YMM6,A5YMN9,A5YMP1,B2CK75,B2CK78,B2CK80,O73404,O73405,O73406,O73411,O73412,O73418,O73425,O89601,O89603,O89604,O89605,O89606,O89608,O89609,O89610,O89611,O89612,O89613,O89614,O89615,O89616,O89617,O89618,O89619,O89620,O89622,O89624,O89626,O89627,O89629,O89630,O89631,O89632,O89633,O89634,O89636,O89639,O89641,O89644,O89645,O89647,O89648,O89649,O89650,O89651,O89652,O89655,O89656,O89659,O89660,O89661,O89662,O89663,O89664,O89665,O89667,O89671,O89672,O89674,O89676,O89680,O89684,O89687,O89697,Q3HP77,Q3HP85,Q3HP91,Q3HP95,Q3HPA1,Q3HPA5,Q3HPB5,Q3HPC4,Q3HPD4,Q3HPD5,Q3HPE1,Q3HPF2,Q3HPF6,Q3HPH8,Q3HPI1,Q3HPI8,Q3HPJ3,Q3HPK0,Q3HPL6,Q3HPL8,Q3HPM2,Q3HPM3,Q3HPM5,Q3HPP4,Q3HPP8,Q3HPR2,Q3HPS8,Q3HPU2,Q3HPU3,Q3HPU6,Q3HPU9,Q3HPW0,Q3HPW8,Q3HPX2,Q3HPX6,Q3HPX8,Q3HPZ0,Q3HPZ1,Q3HPZ4,Q3HPZ9,Q3HQ04,Q3HQ07,Q3HQ14,Q3HQ25,Q3HQ39,Q3HQ40,Q3HQ48,Q3HQ80,Q3HQ83,Q3HQ84,Q3HQA3,Q3HQA9,Q3HQB6,Q3HQC8,Q3HQC9,Q3HQD4,Q3HQD9,Q3HQE0,Q3HQE1,Q3HQH7,Q3HQI1,Q3HQI4,Q3HQI5,Q3HQI7,Q3HQJ1,Q3HQK4,Q3HQM8,Q3HQP6,Q3HQP7,Q3HQQ4,Q3HQR1,Q3HQR7,Q3HQR8,Q3HQS1,Q3HQS4,Q9E285,Q9E287,Q9E289,Q9E290,Q9E291,Q9E292,Q9E293,Q9E294,Q9E296,Q9E297

Functional_annotation:
During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.


Viral_family: Retroviridae
Species: Human immunodeficiency virus 2
Name: Tat
Aliases: Protein tat, Protein Tat, Transactivating regulatory protein
UniProtID_Ref: P18098
UniProt_Name_Ref: TAT_HV2BE
Binding_ligand: dsDNA, ssRNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: I(26488441)
ChIP_seq: I(22073215, 26488441)
Structure_PDB_ID: N
Reporter_assay: I(11909874)
EMSA: I(15994812, 10428378, 14981150)
Other_assays: I(10428378)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A0S3B0B1,A0A0U3VB96,A0A1L4CV17,A0A1L4CV23,A0A1L4CV30,A0A1L4CV41,A0A1L4CV44,A0A1L4CV58,A0A1L4CV62,A0A2D3HWP3,A0A2D3HWQ0,A0A2D3HWQ7,A0A2D3HWR8,A0A2D3HWS9,A0A2D3HWU1,A0A2D3HWU9,A0A2D3HWW0,A0A2D3HWW8,A0A2D3HWX9,A0A2D3HWY4,A0A2D3HWZ3,A0A2D3HX04,A0A385PLN6,A0A385PLS1,A0A385PSL7,A0A385PSQ4,B0YP97,B5TK20,B9VR79,C7G2W8,D7UPK3,D7UPL2,D7UPM1,L8AZ71,L8B2C8,L8B2J7,L8B2M8,L8B321,P88145,Q2PQT0,Q6R780,Q6R789,Q76625,Q7SNM0,Q8UTV3,Q9IBL5,Q9YTT6

Functional_annotation:
Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive (By similarity).


Viral_family: Retroviridae
Species: Human immunodeficiency virus 2
Name: Vpr
Aliases: Protein Vpr, R ORF protein, Viral protein R
UniProtID_Ref: P18100
UniProt_Name_Ref: VPR_HV2BE
Binding_ligand: indirect/unknown
Function: TR, TNA, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(9560267)
EMSA: I(29042644)
Other_assays: I(9560267, 29042644)
Human_infection_evidence: Fields Virology
UniProt_IDs_Orthologs:
A0A1L4CV18,A0A1L4CV25,A0A1L4CV28,A0A1L4CV35,A0A1L4CV43,A0A2D3HWN8,A0A2D3HWQ2,A0A2D3HWQ9,A0A2D3HWS0,A0A2D3HWT1,A0A2D3HWU2,A0A2D3HWV2,A0A2D3HWW2,A0A2D3HWX3,A0A2D3HWY8,A0A2D3HWZ9,A0A2D3HX07,A0A2D3HX19,A0A385PLN9,A0A385PM41,A0A385PMN5,A0A385PP22,Q9Q1T3

Functional_annotation:
Stimulates gene expression driven by the HIV-2 LTR. Prevents infected cells from undergoing mitosis and proliferating, by inducing arrest or delay in the G2 phase of the cell cycle. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity).


Viral_family: Retroviridae
Species: Human spumaretrovirus
Name: Bel-1
Aliases: Protein Bel-1, Tas, Transactivator of spumavirus, Transcriptional transactivator
UniProtID_Ref: P14353
UniProt_Name_Ref: BEL1_FOAMV
UniProt_IDs_Orthologs: Q9IHQ8,Q9IHR0,Q9QEJ6
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(8356798, 8648727, 9621006)
EMSA: I(8648727, 9420252, 9621006)
Other_assays: I(8648727, Footprinting), I(9420252, Footprinting)
Human_infection_evidence: Fields Virology
Functional_annotation:
Transcriptional transactivator that activates the viral internal promoter (IP), thereby enhancing its own expression. This transactivation is repressed by nuclear factor I. Also transactivates the long terminal repeat (LTR) promoter, thereby inducing structural gene expression, initiating the late phase of infection. It is therefore a key regulator of viral gene expression. It directly binds to and activates DNA target sites of viral promoters and those of distinct cellular genes. Required for viral replication.


Viral_family: Retroviridae
Species: Human T-cell leukemia virus 1; Human T-lymphotropic virus 1
Name: HBZ
Aliases: HTLV-1 basic zipper factor
UniProtID_Ref: P0C746
UniProt_Name_Ref: HBZ_HTL1A
UniProt_IDs_Orthologs: P0C747
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: D(17151132)
ChIP_seq: D(30057145)
Structure_PDB_ID: N
Reporter_assay: D(19064727, 12438606, 12937177, 17151132)
EMSA: D(17151132)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Contributes to the regulation of viral RNA transcription by interacting with host proteins involved in transcriptional activation such as ATF4, or CREB1, and by inhibiting their activity. Additionally, HBZ suppresses host NF-kappa-B-driven transcription mediated by host RELA as well as transcription of some classical NF-kappa-B target genes, including IL8, IL2RA, IRF4, VCAM1, and VEGFA.


Viral_family: Retroviridae
Species: Human T-cell leukemia virus 1; Human T-lymphotropic virus 1
Name: Tax
UniProtID_Ref: P14079
UniProt_Name_Ref: TAX_HTL1C
UniProt_IDs_Orthologs: P03409,P0C222
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15367606, 11861831)
EMSA: D(11861831)
Other_assays: N
Human_infection_evidence: Fields Virology
Aliases:
Protein PX, Protein Tax-1, Protein X-LOR, tax, Trans-activating transcriptional regulatory protein of HTLV-1

Functional_annotation:
Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Also induces chromatin remodeling of proviral LTR-mediated gene expression by recruiting the histone acetyl transferases CREBBP and EP300 to the chromatin, which results in histone acetylation. Via its interaction with IKK regulatory subunit IKBKG, Tax-1 persistently stimulates I-kappa-B kinase (IKK), resulting in constitutive activation of the transcription factor NF-kappa-B. Induction of the nuclear expression of members of the NFkB family of transcription factors, which leads to up-regulated expression of many gene promoters containing NFkB motifs. These genes include those encoding IL2, IL15, IL2RA and IL15RA, leading to autocrine IL2/IL2RA and IL15/IL15RA loops. The resulting T-cell proliferation leads to malignant transformation and to the development of adult T-cell leukemia (ATL). IL13, known to be linked to leukemogenesis, is also up-regulated by Tax-1. Interaction with PDZ domain-containing proteins induce IL2-independent growth, which may be a factor in multi-step leukemogenesis. Inhibits the action of at least three cellular tumor suppressors p53/TP53, RB1 and DLG1, and suppresses their abilities to dictate apoptosis in primary cells. Required for viral replication (By similarity).


Viral_family: Retroviridae
Species: Human T-cell leukemia virus 2
Name: Tax
Aliases: Protein Tax-2, Trans-activating transcriptional regulatory protein of HTLV-2
UniProtID_Ref: P03410
UniProt_Name_Ref: TAX_HTLV2
UniProt_IDs_Orthologs: A0A0U2S9I1
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(15367606, 11861831)
EMSA: D(11861831)
Other_assays: N
Human_infection_evidence: Fields Virology
Notes:
Tax does not directly bind DNA, but associates through its N-terminus with the CREB protein (16155604).

Functional_annotation:
Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Induces T-cell transformation, although much less efficiently than HTLV-1. Required for viral replication (By similarity).


Viral_family: Retroviridae
Species: Human T-cell leukemia virus 3
Name: Tax
Aliases: Protein Tax-3, Trans-activating transcriptional regulatory protein of HTLV-3
UniProtID_Ref: Q0R5R1
UniProt_Name_Ref: TAX_HTL32
UniProt_IDs_Orthologs: Q4U0X7
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(15367606, 11861831)
EMSA: I(11861831)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to two 21 bp repeat elements located within the LTRs, referred to as Tax-responsive element (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Activation of NF-kappa-B leads to up-regulation of the expression of gene promoters containing NFkB motifs like IL8 or BCL2L1. Inhibits the action of p53/TP53 and MYCB. All these functions could lead to the possible occurrence of lymphoproliferative disorders. Required for viral replication (By similarity).


Viral_family: Retroviridae
Species: Human T-cell leukemia virus 3
Name: Uncharacterized protein
UniProtID_Ref: Q6LDW4
UniProt_Name_Ref: Q6LDW4_HTLV3
Binding_ligand: ssRNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: I(26488441)
ChIP_seq: I(22073215, 26488441)
Structure_PDB_ID: N
Reporter_assay: I(11909874)
EMSA: I(15994812, 10428378, 14981150)
Other_assays: I(10428378)
Human_infection_evidence: Fields Virology
Notes: Q6LDW4 is inferred from Human immunodeficiency virus 1 protein P04608
Functional_annotation:
RNA-binding transcription regulator activity,positive regulation of viral transcription,host cell nucleus


Viral_family: Retroviridae
Species: Human T-lymphotropic virus 4
Name: Tax
Aliases: Tax protein
UniProtID_Ref: A0A193H3A4
UniProt_Name_Ref: A0A193H3A4_9DELA
UniProt_IDs_Orthologs: B8LHM2,Q50E57
Binding_ligand: indirect/unknown
Function: TR
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(15367606, 11861831)
EMSA: I(11861831)
Other_assays: N
Human_infection_evidence: Fields Virology
Functional_annotation:
2 iron, 2 sulfur cluster binding,oxidoreductase activity,positive regulation of transcription, DNA-templated


Viral_family: Retroviridae
Species: Simian foamy virus
Name: Bel-1
Aliases: bel1, Protein Bel-1, Taf, Tas, Transactivator of spumavirus, Transcriptional transactivator
UniProtID_Ref: Q87042
UniProt_Name_Ref: BEL1_SFVCP
UniProt_IDs_Orthologs: A0A1E1EMK5,A0A2H4PMA7,A0A2Z5HTX8,H6V7J1,K7YKU4,K7YKV0,K7YKV5,Q7SIS4,R9RVK5
Binding_ligand: dsDNA
Function: TR, Rep
Primary_secondary_vTR: P
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(8356798, 8648727, 9621006)
EMSA: D(8648727, 9420252, 9621006)
Other_assays: I(8648727, Footprinting), I(9420252, Footprinting)
Human_infection_evidence: 26446599.0
Functional_annotation:
Transcriptional transactivator that activates the viral internal promoter (IP), thereby enhancing its own expression. This transactivation is repressed by nuclear factor I. Also transactivates the long terminal repeat (LTR) promoter, thereby inducing structural gene expression, initiating the late phase of infection. It is therefore a key regulator of viral gene expression. It directly binds to and activates DNA target sites of viral promoters and those of distinct cellular genes. Required for viral replication (By similarity).


Viral_family: Rhabdoviridae
Species: Australian bat lyssavirus
Name: P
Aliases: Phosphoprotein, Protein M1, Protein P
UniProtID_Ref: Q9QSP3
UniProt_Name_Ref: PHOSP_ABLVB
UniProt_IDs_Orthologs: A0A088NJK8,A0A0S2VHH1,Q91RE3,Q91RE4,Q91RE5,Q91RE6,Q91RE7,Q9YZ23
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(26647356; 22740405; 27384657; 16973555)
EMSA: N
Other_assays: I(19369340), I(8676480, in vitro Transcription Assay), I(1309893, in vitro Transcription Assay)
Human_infection_evidence: 24556791.0
Notes: RNA polymerase cofactor
Functional_annotation:
Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity).


Viral_family: Rhabdoviridae
Species: Duvenhage lyssavirus
Name: N
Aliases: NP, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: Q66453
UniProt_Name_Ref: NCAP_DUVV
UniProt_IDs_Orthologs: A0A0F6MWF3,B2XXZ9,D2CRL8,D2CRM5,I3W9E2
Binding_ligand: ssRNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(11799201; 27384657; 31434934)
EMSA: I(15557246)
Other_assays: I(26957093; 9603315)
Human_infection_evidence: 17326954.0
Functional_annotation:
Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).


Viral_family: Rhabdoviridae
Species: Duvenhage lyssavirus
Name: P
UniProtID_Ref: B2XY05
UniProt_Name_Ref: B2XY05_DUVV
UniProt_IDs_Orthologs: B2XY00,D2CRL7,I3W9E3
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(26647356)
EMSA: N
Human_infection_evidence: 17326954.0
Notes: RNA polymerase cofactor
Aliases:
Isoform P2 of Phosphoprotein, Isoform P4 of Phosphoprotein, Phosphoprotein, Phosphoprotein Phosphoprotein, Protein M1, Protein P

Other_assays:
I(1848304, in vitro Transcription Assay), I(8676480, in vitro Transcription Assay), I(1309893, in vitro Transcription Assay)

Functional_annotation:
Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus.


Viral_family: Rhabdoviridae
Species: European bat lyssavirus 2
Name: P
UniProtID_Ref: A4UHQ4
UniProt_Name_Ref: PHOSP_EBLV2
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: I(26647356; 22740405; 27384657; 16973555)
EMSA: N
Human_infection_evidence: 29684025.0
Notes: RNA polymerase cofactor
Aliases:
Isoform P2 of Phosphoprotein, Isoform P3 of Phosphoprotein, Isoform P5 of Phosphoprotein, Phosphoprotein, Phosphoprotein Phosphoprotein, Protein M1, Protein P

Other_assays:
I(1848304, in vitro Transcription Assay), I(8676480, in vitro Transcription Assay), I(1309893, in vitro Transcription Assay)

Functional_annotation:
Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity).


Viral_family: Rhabdoviridae
Species: Mokola lyssavirus
Name: N
Aliases: NP, Nucleocapsid protein, Nucleoprotein, Protein N
UniProtID_Ref: P0C570
UniProt_Name_Ref: NCAP_MOKV
UniProt_IDs_Orthologs: B2XXY9,B2XXZ4,D6Q0P5,D6Q0P9,E4W5W4,E4W5W5,Q5VKP7,Q83544,Q86593,S5DHS6,S5DHT9
Binding_ligand: ssRNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(11799201)
EMSA: I(15557246)
Other_assays: I(26957093; 9603315)
Human_infection_evidence: 28143485.0
Functional_annotation:
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).


Viral_family: Rhabdoviridae
Species: Mokola lyssavirus
Name: P
Aliases: Phosphoprotein, Protein M1, Protein P
UniProtID_Ref: P0C569
UniProt_Name_Ref: PHOSP_MOKV
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 2WZL
Reporter_assay: D(26647356; 22740405)
EMSA: N
Human_infection_evidence: 28143485.0
Notes: RNA polymerase cofactor
UniProt_IDs_Orthologs:
A0A1L2C1Z1,A0A1L2C1Z5,A0A1L2C227,B2XXZ0,B2XXZ5,O56775,O56777,Q86594,Q910M0,Q91RE0,Q91RE1,Q91RE2,R9Q7B8,R9Q7N9,R9Q7P1,S4S267,S4S2C0,S4S2C5,S5DMU3,S5DMV1,S5DMV6,S5DMW2,U5L226


Viral_family: Rhabdoviridae
Species: Rabies virus
Name: N
Aliases: NP, Nucleoprotein, Protein N
UniProtID_Ref: P06025
UniProt_Name_Ref: NCAP_RABVP
Binding_ligand: ssRNA
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: N
Reporter_assay: D(27384657; 31434934)
EMSA: D(15557246)
Other_assays: D(26957093; 9603315)
Human_infection_evidence: 23602163.0
UniProt_IDs_Orthologs:
A0A024A0B8,A0A024A0W3,A0A024A1B4,A0A059TB69,A0A059TB70,A0A059TB87,A0A059TB89,A0A059TB90,A0A059TB93,A0A059TB94,A0A059TB96,A0A059TB98,A0A059TBC0,A0A059TBC2,A0A059TBC4,A0A059TBE0,A0A059TBE1,A0A059TBE2,A0A059V8W4,A0A060N356,A0A088AXQ2,A0A089N960,A0A097P8D2,A0A097P8G3,A0A0M6VAI4,A0A0N9HLM0,A0A0R5SAT5,A0A0R5SAT8,A0A0R5SAU1,A0A0R5SAU5,A0A0R5SAU7,A0A0R5SAV4,A0A0R5SAW1,A0A0R5SAX0,A0A0R5SAX7,A0A0R7EZ21,A0A0R7EZ32,A0A0R7EZ33,A0A0R7EZ56,A0A0R7EZ74,A0A0R7EZ77,A0A0R7EZ92,A0A0R7EZB5,A0A0R7EZB6,A0A0R7EZB8,A0A0U3SBI6,A0A0U3SBL4,A0A0U3SSS1,A0A0U4BAC4,A0A0U4BIP6,A0A0U4C038,A0A0U4C066,A0A0Y0FT50,A0A109QK65,A0A125QVS9,A0A142D6R1,A0A165DA56,A0A1B0THU0,A0A1B0THU8,A0A1B4WGP6,A0A1B4WGQ5,A0A1D8BP49,A0A1D8BP50,A0A1D8BP64,A0A1D8BP68,A0A1D8BP72,A0A1D8BP73,A0A1D8BP76,A0A1D8BP83,A0A1D8BP84,A0A1D8BP85,A0A1D8BP88,A0A1D8BP93,A0A1D8BP94,A0A1D8BPA1,A0A1D8BPA2,A0A1D8BPA6,A0A1D8BPB2,A0A1D8BPB6,A0A1D8BPC0,A0A1D8BPC5,A0A1D8BPD5,A0A1D8BPD8,A0A1D8BPD9,A0A1D8BPF6,A0A1D8BPG1,A0A1D8BPG5,A0A1D8BPG8,A0A1D8BPH6,A0A1D8BPI8,A0A1D8BPJ9,A0A1D8BPK9,A0A1D8BPL0,A0A1D8BPL3,A0A1D8BPL5,A0A1D8BPL6,A0A1D8BPL7,A0A1D8BPM3,A0A1D8BPN1,A0A1D8BPN2,A0A1D8BPP9,A0A1D8BPQ0,A0A1D8BPQ7,A0A1D8BPR3,A0A1D8BPR5,A0A1D8BPR7,A0A1D8BPS1,A0A1D8BPS6,A0A1D8BPT2,A0A1D8BPT6,A0A1D8BPT9,A0A1D8BPU4,A0A1D8BPU8,A0A1D8BPV0,A0A1D8BPV2,A0A1D8BPV4,A0A1D8BPV5,A0A1D8BPV7,A0A1D8BPW0,A0A1D8BPW3,A0A1D8BPX9,A0A1D8BPY2,A0A1D8BPZ0,A0A1D8BPZ5,A0A1I9WAC1,A0A1I9WAC6,A0A1I9WAD0,A0A1I9WAD2,A0A1I9WAD3,A0A1I9WAD6,A0A1J0RF46,A0A1J0RFS2,A0A1J0RGL4,A0A1J0RGM5,A0A1J0RH62,A0A1J0RH71,A0A1J0RHB0,A0A1J0RHR8,A0A1J0RHS7,A3F5M0,A3F5Q5,A3F5T0,A4D874,A4D875,A4D881,A4D883,A4D884,A4D885,A4D888,A4D889,A4D891,A4D8A5,A4D8A6,A4D8B1,A4D8B7,A4D8C0,A4D8C1,A4D8C4,A4D8C5,A4D8C7,A4D8C8,A4D8C9,A4D8D0,A4D8D4,A4D8D6,A4D8D8,A4D8E4,A4D8E5,A4D8F5,A4D8F7,A4D8G6,A4D8G9,A4D8H0,A4D8H1,A6MF76,A7LFL9,A8CEB8,A8VR20,A9QXE5,A9Y0H9,A9Y0I5,A9Y0I6,A9Y0J1,A9Y0J3,A9Y0J4,A9Y0J5,A9Y0J6,A9Y0K5,B0EYQ3,B0FPH5,B3GQF0,B3GQF1,B3GQF2,B3GQF4,B3GQF5,B3GQF6,B3GQF7,B3GQF8,B3GQG0,B3GQG1,B3GQG2,B3GQG3,B3GQG6,B3GQG7,B3GQG8,B3GQG9,B3GQH0,B3GQH5,B3GQH7,B3GQH8,B3GQI1,B3GQI2,B3GQI3,B3GQI5,B3GQI6,B3GQI7,B3GQI8,B3GQJ0,B3GQJ1,B3GQJ2,B3GQJ3,B3GQJ4,B3GQJ6,B3GQJ7,B3GQJ8,B3GQK0,B5AAR7,B5AXD4,B5KMJ7,B5KML5,B5KMN5,B9VS70,C0IQG0,C0IQG2,C0IQG7,C0IQG9,C0IQH0,C0IQH2,C0IQH3,C0IQH4,C0IQH6,C0IQH8,C0IQI0,C0IQI1,C0IQI2,C0IQI3,C0IQI4,C0IQI5,C0IQI7,C0IQI8,C0IQJ0,C0IQJ1,C0IQJ2,C0ITH9,C0ITI1,C0ITI2,C0ITI3,C0ITI4,C0ITI8,C0ITI9,C0J5B6,C0J5B7,C0J5B9,C0J5C2,C0J5P8,C0J5Q5,C0J5S4,C0J5V0,C0J5V3,C0J5V4,C0J5V9,C0J5X2,C0J5Y3,C0J5Y5,C0JJL4,C0JJL5,C0JJL8,C0JJM0,C0JJM1,C0JJM2,C0JJM3,C0JJM5,C0JJM7,C0JJM8,C0JJN1,C0JJN2,C0JJN4,C0JJN7,C0JJN8,C0JJN9,C0JJP1,C0JJP2,C0JJP6,C0JJP7,C0JJP9,C0JJQ1,C0JJQ3,C0JJQ4,C0JJQ6,C3VID6,C4MH53,C6ZD73,C6ZD88,C7ADP4,C9WLX2,C9WLX4,C9WLX6,D2D2A8,D2D2B3,D2D2B7,D3JZP8,D4P3X7,D6Q090,D6Q0A4,D6Q0Q6,D6Q0Q8,E0X4L5,E0X4M3,E0Y5E6,E0Y5F4,E0Y5I1,E0Y5I7,E0Y5M2,E0Y5M5,E0Y5M7,E0Y5M8,E0Y5N0,E0Y5N3,E0Y5N8,E5E232,E5E233,E5E234,E5E236,E5E237,E5E238,E5E239,E5E241,E5E243,E5E245,E5E246,E5E249,E5E250,E5E252,E5E254,E5E255,E5E256,E5E257,E5E260,E5E263,E5E264,E5E265,E5E267,E5E268,E5E269,E5E271,E5E272,E5E273,E5E274,E5E275,E5E276,E5E278,E5E280,E5E281,E5E282,E5E283,E5E284,E5E285,E5E287,E5E288,E5E289,E5E290,E5E291,E5E292,E5E293,E5E294,E5E295,E5E297,E5E298,E5E299,E5E2A1,E5E2A2,E5E2A3,E5E2A4,E5E2A6,E5E2A7,E5E2A8,E5E2A9,E5E2B0,E5E2B8,E5E2C0,E5E2C2,E5E2C6,E5E2C7,E5E2C8,E5E2D0,E5E2D3,E5E2D6,E5E2D9,E5E2E2,E5E2E3,E5E2E4,E5E2E6,E5E2E7,E5E2E9,E5E2F5,E5E2F6,E5E2F8,E5E2F9,E5E2G3,E5E2G4,E5E2G5,E5E2G6,E5E2H0,E5E2H1,E5E2H2,E5E2H3,E5E2H5,E5E2H6,E5E2H7,E5E2H8,E5E2H9,E5E2I0,E5E2I2,E5E2I4,E5E2I7,E5E2I8,E5E2I9,E5E2J0,E5E2J1,E5E2J2,E5E2J3,E5E2J4,E5E2J5,E5E2J6,E5E2J7,E5E2K0,E5E2K1,E5E2K2,E5E2K5,E5E2K6,E5E2K7,E5E2K9,E5E2L0,E5E2L1,E5E2L5,E5E2L6,E5E2L7,E5E2L8,E5E2L9,E5E2M0,E5E2M1,E5E2M2,E5E2M3,E5E2M4,E5E2M7,E5E2N1,E5E2N2,E5E2N3,E5E2N4,E5E2N6,E5E2N7,E5E2N8,E5E2N9,E5E2P0,E5E2P1,E5E2P2,E5E2P3,E5E2P4,E5E2P5,E5E2P6,E5E2P7,E5E2P8,E5E2Q0,E5E2Q1,E5E2Q3,E5E2Q4,E5E2Q6,E5E2Q7,E5E2Q8,E5E2Q9,E5E2R3,E5E2R5,E5E2R6,E5E2R7,E5E2R8,E5E2R9,E5E2S0,E5E2S1,E5E2S2,E5E2S3,E5E2S5,E5E2S6,E5E2T1,E5E2T2,E5E2T3,E5E2T5,E5E2T6,E5E2T7,E5E2U1,E5E2U3,E5E2U5,E5E2U6,E5E2U8,E5E2V0,E5E2V1,E5E2V2,E5E2V6,E5E2V8,E5E2V9,E5E2W1,E5E2W5,E5E2W6,E5E2W7,F8UZL2,F8UZL5,F8UZL9,F8UZM4,F8UZM5,F8UZM6,F8UZN5,F8UZP5,G8XR30,G8XR34,H9N3Z9,H9N400,H9N402,H9N404,H9N409,H9N411,H9N412,H9N413,H9N415,H9N416,H9N418,H9N421,H9N424,H9N425,H9N426,H9N428,H9N430,H9N431,H9N432,H9N433,I4CJZ0,I6WDF0,I6WDF7,I6WDI9,I6WDM1,I6WDM7,I6WDN8,I6WDS9,I6WDT4,I6WE51,I6WEI5,I6YLU0,I7F434,J9S3H1,K9LIJ7,K9MRV2,K9MRV9,K9MRW2,K9MS20,K9MT90,K9MTA4,K9MTB5,K9MTB9,K9NVT2,M1GND6,M1H0W2,M1PLG0,M4JCU8,M4JCV1,M4JCV3,M4JCV4,M4JCW5,M4JCW7,M4JCW9,M4JCX1,M4JCX3,M4JCX6,M4JCX8,M4JCZ3,M4JCZ6,M4JD07,M4JD09,M4JD15,M4JD23,M4JD25,M4JD33,M4JD35,M4JD37,M4JD40,M4JD43,M4JD44,M4JD46,M4JD50,M4JD53,M4JD64,M4JD66,M4JD79,M4JD80,M4JDI0,M4JDI4,M4JDI6,M4JDI8,M4JDJ0,M4JDJ3,M4JDJ5,M4JDK1,M4JDK3,M4JDK6,M4JDK8,M4JDL0,M4JDL4,M4JDL9,M4JDM0,M4JDM4,M4JDM5,M4JDM6,M4JE89,M4JE95,M4JE96,M4JEA4,M4JEA6,M4JEA9,M4JEB1,M4JEB7,M4JEC1,M4JEC4,M4JEC6,M4JED8,M4JEE1,M4JEF1,M4JEF2,M4JEF6,M4JEF9,M4JEG5,M4JF52,M4JF54,M4JF56,M4JF62,M4JF65,M4JF68,M4JF72,M4JF75,M4JF78,M4JF81,M4JFB3,M4JFC5,P15197,P16285,Q0PE64,Q0PE66,Q0PE68,Q0PE72,Q0PE74,Q0PNB8,Q0Q0C4,Q0Q0D4,Q0Q0D7,Q0QDH5,Q19NZ2,Q4F904,Q52YR0,Q52YR4,Q52YR8,Q52YS3,Q52YS5,Q52YS6,Q52YT7,Q52YV1,Q52YV4,Q52YW3,Q52YW5,Q52YW9,Q52YX4,Q52YX9,Q5L4F8,Q66T65,Q69DB2,Q86410,Q86411,Q86426,Q86430,Q86431,Q86438,Q86453,Q8B6J9,Q8JXF6,Q8UYC3,Q8V0H0,Q8V0H3,Q8V0H5,Q8V415,Q8V416,Q8V417,Q8V419,Q8V420,Q8V424,Q8V426,Q8V427,Q8V428,Q91SM2,Q91SM3,Q91SM4,Q91SM5,Q91SM7,Q91SN1,Q91SN3,Q91SU2,Q91SU7,Q91SU9,Q91SV0,Q91SV1,Q91SV4,Q91SV7,Q91SW1,Q91SW5,Q91SW7,Q91SW9,Q91SX2,Q9WJY7,Q9WLM8,S5FP98,S5FQI9,S6BCW3,T2DL99,U5KJ83,U5S5Z2,U5S8N2,W6JI73

Functional_annotation:
Encapsidates the genome in a ratio of one protein N per nine ribonucleotides, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, with protein N protecting the genome like a pearl necklace. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for viral transcription and replication. Protein N binds protein P in the NC through a different interaction, and can be phosphorylated. Subsequent viral replication is dependent on intracellular concentration of newly synthesized protein N. During replication, encapsidation by protein N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).


Viral_family: Rhabdoviridae
Species: Rabies virus
Name: P
Aliases: Phosphoprotein, Protein M1, Protein P
UniProtID_Ref: P06747
UniProt_Name_Ref: PHOSP_RABVP
UniProt_IDs_Orthologs: A3F5R6,P15198,P16286,P22363,P69479,P69480,Q0GBX8,Q0GBY3,Q8B6J8,Q9IPJ8
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 3OA1
Reporter_assay: D(27384657; 26647356)
EMSA: N
Other_assays: D(26957093)
Human_infection_evidence: 23602163.0
Notes: RNA polymerase cofactor
Functional_annotation:
Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity).


Viral_family: Rhabdoviridae
Species: Vesicular stomatitis Indiana virus
Name: P
Aliases: P Protein, Phosphoprotein, Protein M1
UniProtID_Ref: P03520
UniProt_Name_Ref: PHOSP_VSIVA
Binding_ligand: indirect/unknown
Function: TR, Rep
Primary_secondary_vTR: S
ChIP: N
ChIP_seq: N
Structure_PDB_ID: 2K47
Reporter_assay: D(16973555)
EMSA: N
Human_infection_evidence: 2845825.0
Notes: RNA polymerase cofactor
UniProt_IDs_Orthologs:
A0A140DCD4,A0A140DCD9,A0A3G1VCW6,P04879,P04880,Q89487,Q8B0H3,Q8B0H8,Q8B0I3,Q9IG72,Q9IG73,Q9IG74,Q9IG75,Q9IG76,Q9IG77,Q9IG78,Q9IG79,Q9IG80,Q9IG81,Q9IG82,W5U2W7

Other_assays:
D(3032453, in vitro Transcription Assay), D(1848304, in vitro Transcription Assay), D(8676480, in vitro Transcription Assay), D(1309893, in vitro Transcription Assay)

Functional_annotation:
Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly.


