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Q92985 (IRF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon regulatory factor 7

Short name=IRF-7
Gene names
Name:IRF7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages. Ref.6 Ref.9 Ref.18 Ref.23

Enzyme regulation

In the absence of viral infection, maintained as a monomer in an autoinhibited state and phosphorylation disrupts this autoinhibition leading to the liberation of the DNA-binding and dimerization activities and its nuclear localization where it can activate type I IFN and ISG genes.

Subunit structure

Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF3. Interacts with TICAM1 and TICAM2. Interacts with rotavirus A NSP1; this interaction leads to the proteasome-dependent degradation of IRF7. Interacts with Epstein-Barr virus LF2 and human herpes virus 8/HHV-8 proteins ORF45 and vIRF-1. Interacts with MYD88 AND TRAF6. Ref.6 Ref.8 Ref.11 Ref.12 Ref.14 Ref.17 Ref.18 Ref.24 Ref.25

Subcellular location

Nucleus. Cytoplasm. Note: The phosphorylated and active form accumulates selectively in the nucleus. Ref.6 Ref.17 Ref.18

Tissue specificity

Expressed predominantly in spleen, thymus and peripheral blood leukocytes.

Induction

By type I interferon (IFN) and viruses.

Post-translational modification

Acetylation inhibits its DNA-binding ability and activity. Ref.9

In response to a viral infection, phosphorylated on Ser-477 and Ser-479 by TBK1 and IKBKE1. Phosphorylation, and subsequent activation is inhibited by vaccinia virus protein E3. In TLR7- and TLR9-mediated signaling pathway, phosphorylated by IRAK1. Ref.6 Ref.7 Ref.9 Ref.16 Ref.19

TRAF6-mediated ubiquitination is required for IRF7 activation By similarity.

Sumoylated by TRIM28, which inhibits its transactivation activity. Ref.28

Sequence similarities

Belongs to the IRF family.

Contains 1 IRF tryptophan pentad repeat DNA-binding domain.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMDA-5 signaling pathway

Traceable author statement Ref.21. Source: UniProtKB

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Traceable author statement Ref.21. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

establishment of viral latency

Traceable author statement Ref.27. Source: UniProtKB

immunoglobulin mediated immune response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement Ref.23. Source: UniProtKB

interferon-alpha production

Inferred from sequence or structural similarity. Source: UniProtKB

interferon-beta production

Inferred from sequence or structural similarity. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

negative regulation of macrophage apoptotic process

Traceable author statement Ref.27. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

positive regulation of interferon-alpha production

Traceable author statement Ref.21. Source: UniProtKB

positive regulation of interferon-beta production

Traceable author statement Ref.21. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of type I interferon-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of MyD88-dependent toll-like receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of MyD88-independent toll-like receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of adaptive immune response

Inferred from direct assay Ref.23. Source: UniProtKB

regulation of immune response

Traceable author statement Ref.27. Source: UniProtKB

regulation of monocyte differentiation

Traceable author statement Ref.27. Source: UniProtKB

regulation of type I interferon production

Traceable author statement Ref.27. Source: UniProtKB

response to virus

Traceable author statement Ref.27. Source: UniProtKB

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

type I interferon biosynthetic process

Inferred from electronic annotation. Source: Ensembl

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement Ref.3. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.3. Source: ProtInc

   Molecular_functionDNA binding

Inferred from mutant phenotype Ref.9. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.23. Source: UniProtKB

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay Ref.23. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 17599067PubMed 18922877PubMed 21903422. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q92985-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q92985-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     228-256: Missing.
Isoform C (identifier: Q92985-3)

Also known as: Gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     152-164: GGPPGPFLAHTHA → AQGSLLGSCTGGQ
     165-503: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform D (identifier: Q92985-4)

Also known as: H;

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MALAPE → MPVPERPAAGPDSPRPGTR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Interferon regulatory factor 7
PRO_0000154562

Regions

DNA binding11 – 126116IRF tryptophan pentad repeat

Amino acid modifications

Modified residue921N6-acetyllysine; by KAT2A and KAT2B Ref.9
Modified residue4771Phosphoserine; by TBK1 and IKKE Ref.16
Modified residue4791Phosphoserine; by TBK1 and IKKE Ref.16
Cross-link444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
Cross-link446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28

Natural variations

Alternative sequence1 – 66MALAPE → MPVPERPAAGPDSPRPGTR in isoform D.
VSP_002757
Alternative sequence152 – 16413GGPPG…AHTHA → AQGSLLGSCTGGQ in isoform C.
VSP_002758
Alternative sequence165 – 503339Missing in isoform C.
VSP_002759
Alternative sequence228 – 25629Missing in isoform B.
VSP_002760
Natural variant1791K → E. Ref.1 Ref.3
Corresponds to variant rs1061502 [ dbSNP | Ensembl ].
VAR_027957
Natural variant2041D → N.
Corresponds to variant rs41313489 [ dbSNP | Ensembl ].
VAR_061273
Natural variant4121Q → R. Ref.3
Corresponds to variant rs1131665 [ dbSNP | Ensembl ].
VAR_034017

Experimental info

Mutagenesis901G → T: Loss of acetylation, increased DNA-binding and activity; when associated with R-93. Ref.9
Mutagenesis921K → R: Loss of acetylation, DNA-binding and activity. Ref.9
Mutagenesis931T → R: Loss of acetylation, increased DNA-binding and activity; when associated with T-90. Ref.9
Mutagenesis477 – 4793SLS → ALA: Complete loss of TBK1 and IKKE phosphorylation. Ref.16

Secondary structure

................ 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 9863C147514652DE

FASTA50354,278
        10         20         30         40         50         60 
MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK DLSEADARIF 

        70         80         90        100        110        120 
KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR STRRFVMLRD NSGDPADPHK 

       130        140        150        160        170        180 
VYALSRELCW REGPGTDQTE AEAPAAVPPP QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG 

       190        200        210        220        230        240 
DLLLQAVQQS CLADHLLTAS WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV 

       250        260        270        280        290        300 
ETTPSPGPQP AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV 

       310        320        330        340        350        360 
LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL RHVAPGLHLE 

       370        380        390        400        410        420 
LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC DTPIFDFRVF FQELVEFRAR 

       430        440        450        460        470        480 
QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL VKLEPWLCRV HLEGTQREGV SSLDSSSLSL 

       490        500 
CLSSANSLYD DIECFLMELE QPA 

« Hide

Isoform B (Beta) [UniParc].

Checksum: F98A7B630497BDD0
Show »

FASTA47451,459
Isoform C (Gamma) [UniParc].

Checksum: 6FC0146AD190006D
Show »

FASTA16418,036
Isoform D (H) [UniParc].

Checksum: 0A659B0BD1FE30F7
Show »

FASTA51655,635

References

« Hide 'large scale' references
[1]Grossman A., Nicholl J., Antonio L., Luethy R., Suggs S., Sutherland G.R., Mak T.W.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT GLU-179.
Tissue: Spleen.
[2]"IRF-7, a new interferon regulatory factor associated with Epstein-Barr virus latency."
Zhang L., Pagano J.S.
Mol. Cell. Biol. 17:5748-5757(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
[3]"Characterization of the interferon regulatory factor-7 and its potential role in the transcription activation of interferon A genes."
Au W.-C., Moore P.A., LaFleur D.W., Tombal B., Pitha P.M.
J. Biol. Chem. 273:29210-29217(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), VARIANTS GLU-179 AND ARG-412.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
[6]"Phosphorylation-induced dimerization of interferon regulatory factor 7 unmasks DNA binding and a bipartite transactivation domain."
Marie I.J., Smith E., Prakash A., Levy D.E.
Mol. Cell. Biol. 20:8803-8814(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, SUBUNIT.
[7]"IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein."
Smith E.J., Marie I.J., Prakash A., Garcia-Sastre A., Levy D.E.
J. Biol. Chem. 276:8951-8957(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION OF PHOSPHORYLATION BY VACCINIA VIRUS PROTEIN E3.
[8]"HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators."
Lin R., Genin P., Mamane Y., Sgarbanti M., Battistini A., Harrington W.J. Jr., Barber G.N., Hiscott J.
Oncogene 20:800-811(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-8 PROTEIN VIRF1.
[9]"Acetylation of interferon regulatory factor-7 by p300/CREB-binding protein (CBP)-associated factor (PCAF) impairs its DNA binding."
Caillaud A., Prakash A., Smith E., Masumi A., Hovanessian A.G., Levy D.E., Marie I.
J. Biol. Chem. 277:49417-49421(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-92, MUTAGENESIS OF GLY-90; LYS-92 AND THR-93, PHOSPHORYLATION.
[10]"Structure and function of IRF-7."
Zhang L., Pagano J.S.
J. Interferon Cytokine Res. 22:95-101(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[11]"A Kaposi's sarcoma-associated herpesviral protein inhibits virus-mediated induction of type I interferon by blocking IRF-7 phosphorylation and nuclear accumulation."
Zhu F.X., King S.M., Smith E.J., Levy D.E., Yuan Y.
Proc. Natl. Acad. Sci. U.S.A. 99:5573-5578(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-8 PROTEIN ORF45.
[12]"LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF."
Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T.
J. Exp. Med. 198:1043-1055(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TICAM2.
[13]Erratum
Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T.
J. Exp. Med. 198:1451-1451(2003)
[14]"Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TICAM1.
[15]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[16]"Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus infection and the role of viral ribonucleoprotein in the development of interferon antiviral immunity."
tenOever B.R., Sharma S., Zou W., Sun Q., Grandvaux N., Julkunen I., Hemmi H., Yamamoto M., Akira S., Yeh W.C., Lin R., Hiscott J.
J. Virol. 78:10636-10649(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-477 AND SER-479 BY TBK1 AND IKKE, MUTAGENESIS OF 477-SER--SER-479.
[17]"Role of a transductional-transcriptional processor complex involving MyD88 and IRF-7 in Toll-like receptor signaling."
Honda K., Yanai H., Mizutani T., Negishi H., Shimada N., Suzuki N., Ohba Y., Takaoka A., Yeh W.C., Taniguchi T.
Proc. Natl. Acad. Sci. U.S.A. 101:15416-15421(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MYD88.
[18]"Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6."
Kawai T., Sato S., Ishii K.J., Coban C., Hemmi H., Yamamoto M., Terai K., Matsuda M., Inoue J., Uematsu S., Takeuchi O., Akira S.
Nat. Immunol. 5:1061-1068(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYD88 AND TRAF6.
[19]"Interleukin-1 receptor-associated kinase-1 plays an essential role for Toll-like receptor (TLR)7- and TLR9-mediated interferon-{alpha} induction."
Uematsu S., Sato S., Yamamoto M., Hirotani T., Kato H., Takeshita F., Matsuda M., Coban C., Ishii K.J., Kawai T., Takeuchi O., Akira S.
J. Exp. Med. 201:915-923(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY IRAK1.
[20]"Distinct functions of IRF-3 and IRF-7 in IFN-alpha gene regulation and control of anti-tumor activity in primary macrophages."
Solis M., Goubau D., Romieu-Mourez R., Genin P., Civas A., Hiscott J.
Biochem. Pharmacol. 72:1469-1476(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[21]"Type I interferon gene induction by the interferon regulatory factor family of transcription factors."
Honda K., Takaoka A., Taniguchi T.
Immunity 25:349-360(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[22]Erratum
Honda K., Takaoka A., Taniguchi T.
Immunity 25:849-849(2006)
[23]"IRF-7: new role in the regulation of genes involved in adaptive immunity."
Sgarbanti M., Marsili G., Remoli A.L., Orsatti R., Battistini A.
Ann. N. Y. Acad. Sci. 1095:325-333(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Rotavirus NSP1 inhibits expression of type I interferon by antagonizing the function of interferon regulatory factors IRF3, IRF5, and IRF7."
Barro M., Patton J.T.
J. Virol. 81:4473-4481(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ROTAVIRUS A NSP1.
[25]"Epstein-Barr virus LF2: an antagonist to type I interferon."
Wu L., Fossum E., Joo C.H., Inn K.S., Shin Y.C., Johannsen E., Hutt-Fletcher L.M., Hass J., Jung J.U.
J. Virol. 83:1140-1146(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV LF2.
[26]"Regulation of immunity and oncogenesis by the IRF transcription factor family."
Savitsky D., Tamura T., Yanai H., Taniguchi T.
Cancer Immunol. Immunother. 59:489-510(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[27]"IRF7: activation, regulation, modification and function."
Ning S., Pagano J.S., Barber G.N.
Genes Immun. 12:399-414(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[28]"Tripartite motif-containing protein 28 is a small ubiquitin-related modifier E3 ligase and negative regulator of IFN regulatory factor 7."
Liang Q., Deng H., Li X., Wu X., Tang Q., Chang T.H., Peng H., Rauscher F.J. III, Ozato K., Zhu F.
J. Immunol. 187:4754-4763(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-444 AND LYS-446 BY TRIM28.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73036 mRNA. Translation: AAB17190.1.
U53830 mRNA. Translation: AAB80686.1.
U53831 mRNA. Translation: AAB80688.1.
U53832 mRNA. Translation: AAB80690.1.
U53832 mRNA. Translation: AAB80691.1.
AF076494 mRNA. Translation: AAC70999.1.
CH471158 Genomic DNA. Translation: EAX02360.1.
BC136555 mRNA. Translation: AAI36556.1.
CCDSCCDS7703.1. [Q92985-1]
CCDS7704.1. [Q92985-2]
CCDS7705.1. [Q92985-4]
RefSeqNP_001563.2. NM_001572.3. [Q92985-1]
NP_004020.1. NM_004029.2. [Q92985-2]
NP_004022.2. NM_004031.2. [Q92985-4]
XP_005252963.1. XM_005252906.1. [Q92985-4]
XP_006725200.1. XM_006725137.1. [Q92985-4]
UniGeneHs.166120.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O61X-ray2.80A8-125[»]
ProteinModelPortalQ92985.
SMRQ92985. Positions 8-123, 289-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109873. 42 interactions.
DIPDIP-34895N.
IntActQ92985. 24 interactions.
MINTMINT-1202972.
STRING9606.ENSP00000329411.

PTM databases

PhosphoSiteQ92985.

Polymorphism databases

DMDM116242593.

Proteomic databases

MaxQBQ92985.
PaxDbQ92985.
PRIDEQ92985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330243; ENSP00000329411; ENSG00000185507. [Q92985-4]
ENST00000348655; ENSP00000331803; ENSG00000185507. [Q92985-2]
ENST00000397566; ENSP00000380697; ENSG00000185507. [Q92985-4]
ENST00000397570; ENSP00000380700; ENSG00000185507. [Q92985-2]
ENST00000397574; ENSP00000380704; ENSG00000185507. [Q92985-1]
ENST00000469048; ENSP00000434607; ENSG00000185507. [Q92985-3]
ENST00000533182; ENSP00000433903; ENSG00000185507. [Q92985-3]
GeneID3665.
KEGGhsa:3665.
UCSCuc001lqg.3. human. [Q92985-4]
uc001lqh.3. human. [Q92985-1]
uc001lqi.3. human. [Q92985-2]

Organism-specific databases

CTD3665.
GeneCardsGC11M000602.
HGNCHGNC:6122. IRF7.
HPACAB017694.
MIM605047. gene.
neXtProtNX_Q92985.
PharmGKBPA29921.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39245.
HOGENOMHOG000111812.
HOVERGENHBG105600.
KOK09447.
OMAGWKTNFR.
PhylomeDBQ92985.
TreeFamTF328512.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ92985.

Gene expression databases

ArrayExpressQ92985.
BgeeQ92985.
CleanExHS_IRF7.
GenevestigatorQ92985.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProIPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR019471. Interferon_reg_factor-3.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSPR00267. INTFRNREGFCT.
SMARTSM00348. IRF. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
PROSITEPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIRF7. human.
GeneWikiIRF7.
GenomeRNAi3665.
NextBio14347.
PROQ92985.
SOURCESearch...

Entry information

Entry nameIRF7_HUMAN
AccessionPrimary (citable) accession number: Q92985
Secondary accession number(s): B9EGL3 expand/collapse secondary AC list , O00331, O00332, O00333, O75924, Q9UE79
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM