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Protein

Interferon regulatory factor 7

Gene

IRF7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Enzyme regulationi

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi11 – 126116IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: UniProtKB
  • transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • establishment of viral latency Source: UniProtKB
  • immunoglobulin mediated immune response Source: Ensembl
  • innate immune response Source: UniProtKB
  • interferon-alpha production Source: UniProtKB
  • interferon-beta production Source: UniProtKB
  • interferon-gamma-mediated signaling pathway Source: Reactome
  • MDA-5 signaling pathway Source: UniProtKB
  • negative regulation of macrophage apoptotic process Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • positive regulation of interferon-alpha production Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of type I interferon-mediated signaling pathway Source: Ensembl
  • positive regulation of type I interferon production Source: Reactome
  • regulation of adaptive immune response Source: UniProtKB
  • regulation of immune response Source: UniProtKB
  • regulation of monocyte differentiation Source: UniProtKB
  • regulation of MyD88-dependent toll-like receptor signaling pathway Source: UniProtKB
  • regulation of MyD88-independent toll-like receptor signaling pathway Source: UniProtKB
  • regulation of type I interferon production Source: UniProtKB
  • response to virus Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: ProtInc
  • TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  • type I interferon biosynthetic process Source: Ensembl
  • type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Antiviral defense, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ92985.
SIGNORiQ92985.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 7
Short name:
IRF-7
Gene namesi
Name:IRF7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:6122. IRF7.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: The phosphorylated and active form accumulates selectively in the nucleus.

GO - Cellular componenti

  • cytoplasm Source: AgBase
  • cytosol Source: Reactome
  • endosome membrane Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 39 (IMD39)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA primary immunodeficiency causing severe, life-threatening acute respiratory distress upon infection with H1N1 influenza A.
See also OMIM:616345
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti410 – 4101F → V in IMD39; loss of function mutation; shows abnormal localization to the cytoplasm rather than the nucleus. 1 Publication
Corresponds to variant rs786205223 [ dbSNP | Ensembl ].
VAR_073779

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901G → T: Loss of acetylation, increased DNA-binding and activity; when associated with R-93. 1 Publication
Mutagenesisi92 – 921K → R: Loss of acetylation, DNA-binding and activity. 1 Publication
Mutagenesisi93 – 931T → R: Loss of acetylation, increased DNA-binding and activity; when associated with T-90. 1 Publication
Mutagenesisi477 – 4793SLS → ALA: Complete loss of TBK1 and IKKE phosphorylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi616345. phenotype.
PharmGKBiPA29921.

Polymorphism and mutation databases

BioMutaiIRF7.
DMDMi116242593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Interferon regulatory factor 7PRO_0000154562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei92 – 921N6-acetyllysine; by KAT2A and KAT2B1 Publication
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Cross-linki446 – 446Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei477 – 4771Phosphoserine; by TBK1 and IKKE1 Publication
Modified residuei479 – 4791Phosphoserine; by TBK1 and IKKE1 Publication

Post-translational modificationi

Acetylation inhibits its DNA-binding ability and activity.1 Publication
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 IRAK1.4 Publications
TRAF6-mediated ubiquitination is required for IRF7 activation.By similarity
Sumoylated by TRIM28, which inhibits its transactivation activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ92985.
PaxDbiQ92985.
PeptideAtlasiQ92985.
PRIDEiQ92985.

PTM databases

iPTMnetiQ92985.
PhosphoSiteiQ92985.

Expressioni

Tissue specificityi

Expressed predominantly in spleen, thymus and peripheral blood leukocytes.

Inductioni

By type I interferon (IFN) and viruses.

Gene expression databases

BgeeiENSG00000185507.
CleanExiHS_IRF7.
ExpressionAtlasiQ92985. baseline and differential.
GenevisibleiQ92985. HS.

Organism-specific databases

HPAiCAB017694.
HPA052757.

Interactioni

Subunit structurei

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 LMP1 as well as human herpes virus 8/HHV-8 proteins ORF45 and vIRF-1. Interacts with MYD88 AND TRAF6.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIPO001702EBI-968267,EBI-704197
ARAFP103982EBI-968267,EBI-365961
BICP0P291285EBI-968267,EBI-11292028From a different organism.
CCDC47Q96A332EBI-968267,EBI-720151
CHUKO151114EBI-968267,EBI-81249
IRAK1P516172EBI-968267,EBI-358664
LTN1O948222EBI-968267,EBI-1044684
ORF45F5HDE43EBI-968267,EBI-8843990From a different organism.
PQ77M193EBI-968267,EBI-6149376From a different organism.
PALD1Q9ULE62EBI-968267,EBI-3957166
TBK1Q9UHD22EBI-968267,EBI-356402
TLK2Q86UE82EBI-968267,EBI-1047967
TRMT61BQ9BVS52EBI-968267,EBI-3197877

Protein-protein interaction databases

BioGridi109873. 42 interactions.
DIPiDIP-34895N.
IntActiQ92985. 26 interactions.
MINTiMINT-1202972.
STRINGi9606.ENSP00000329411.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 435Combined sources
Helixi55 – 573Combined sources
Helixi58 – 669Combined sources
Helixi84 – 929Combined sources
Beta strandi407 – 4137Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O61X-ray2.80A8-125[»]
ProteinModelPortaliQ92985.
SMRiQ92985. Positions 8-123, 289-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IRF family.PROSITE-ProRule annotation
Contains 1 IRF tryptophan pentad repeat DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IWNR. Eukaryota.
ENOG4111G85. LUCA.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000111812.
HOVERGENiHBG105600.
InParanoidiQ92985.
KOiK09447.
OMAiGWKTNFR.
OrthoDBiEOG091G067P.
PhylomeDBiQ92985.
TreeFamiTF328512.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProiIPR019817. 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]
PfamiPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
SM01243. IRF-3. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF49879. SSF49879. 1 hit.
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q92985-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALAPERAAP RVLFGEWLLG EISSGCYEGL QWLDEARTCF RVPWKHFARK
60 70 80 90 100
DLSEADARIF KAWAVARGRW PPSSRGGGPP PEAETAERAG WKTNFRCALR
110 120 130 140 150
STRRFVMLRD NSGDPADPHK VYALSRELCW REGPGTDQTE AEAPAAVPPP
160 170 180 190 200
QGGPPGPFLA HTHAGLQAPG PLPAPAGDKG DLLLQAVQQS CLADHLLTAS
210 220 230 240 250
WGADPVPTKA PGEGQEGLPL TGACAGGPGL PAGELYGWAV ETTPSPGPQP
260 270 280 290 300
AALTTGEAAA PESPHQAEPY LSPSPSACTA VQEPSPGALD VTIMYKGRTV
310 320 330 340 350
LQKVVGHPSC TFLYGPPDPA VRATDPQQVA FPSPAELPDQ KQLRYTEELL
360 370 380 390 400
RHVAPGLHLE LRGPQLWARR MGKCKVYWEV GGPPGSASPS TPACLLPRNC
410 420 430 440 450
DTPIFDFRVF FQELVEFRAR QRRGSPRYTI YLGFGQDLSA GRPKEKSLVL
460 470 480 490 500
VKLEPWLCRV HLEGTQREGV SSLDSSSLSL CLSSANSLYD DIECFLMELE

QPA
Length:503
Mass (Da):54,278
Last modified:October 17, 2006 - v2
Checksum:i9863C147514652DE
GO
Isoform B (identifier: Q92985-2) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     228-256: Missing.

Show »
Length:474
Mass (Da):51,459
Checksum:iF98A7B630497BDD0
GO
Isoform C (identifier: Q92985-3) [UniParc]FASTAAdd to basket
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.
Show »
Length:164
Mass (Da):18,036
Checksum:i6FC0146AD190006D
GO
Isoform D (identifier: Q92985-4) [UniParc]FASTAAdd to basket
Also known as: H

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

Show »
Length:516
Mass (Da):55,635
Checksum:i0A659B0BD1FE30F7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791K → E.2 Publications
Corresponds to variant rs1061502 [ dbSNP | Ensembl ].
VAR_027957
Natural varianti204 – 2041D → N.
Corresponds to variant rs41313489 [ dbSNP | Ensembl ].
VAR_061273
Natural varianti410 – 4101F → V in IMD39; loss of function mutation; shows abnormal localization to the cytoplasm rather than the nucleus. 1 Publication
Corresponds to variant rs786205223 [ dbSNP | Ensembl ].
VAR_073779
Natural varianti412 – 4121Q → R.1 Publication
Corresponds to variant rs1131665 [ dbSNP | Ensembl ].
VAR_034017

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MALAPE → MPVPERPAAGPDSPRPGTR in isoform D. 2 PublicationsVSP_002757
Alternative sequencei152 – 16413GGPPG…AHTHA → AQGSLLGSCTGGQ in isoform C. 1 PublicationVSP_002758Add
BLAST
Alternative sequencei165 – 503339Missing in isoform C. 1 PublicationVSP_002759Add
BLAST
Alternative sequencei228 – 25629Missing in isoform B. 1 PublicationVSP_002760Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7703.1. [Q92985-1]
CCDS7704.1. [Q92985-2]
CCDS7705.1. [Q92985-4]
RefSeqiNP_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_005252906.3. [Q92985-4]
UniGeneiHs.166120.

Genome annotation databases

EnsembliENST00000330243; ENSP00000329411; ENSG00000185507. [Q92985-4]
ENST00000348655; ENSP00000331803; ENSG00000185507. [Q92985-2]
ENST00000397566; ENSP00000380697; ENSG00000185507. [Q92985-4]
ENST00000397574; ENSP00000380704; ENSG00000185507. [Q92985-1]
ENST00000469048; ENSP00000434607; ENSG00000185507. [Q92985-3]
ENST00000533182; ENSP00000433903; ENSG00000185507. [Q92985-3]
ENST00000612534; ENSP00000479615; ENSG00000276561. [Q92985-4]
ENST00000621391; ENSP00000480358; ENSG00000276561. [Q92985-1]
ENST00000632827; ENSP00000488039; ENSG00000276561. [Q92985-4]
ENST00000633274; ENSP00000488591; ENSG00000276561. [Q92985-3]
ENST00000633943; ENSP00000488666; ENSG00000276561. [Q92985-2]
ENST00000634105; ENSP00000488581; ENSG00000276561. [Q92985-3]
GeneIDi3665.
KEGGihsa:3665.
UCSCiuc001lqg.3. human. [Q92985-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7703.1. [Q92985-1]
CCDS7704.1. [Q92985-2]
CCDS7705.1. [Q92985-4]
RefSeqiNP_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_005252906.3. [Q92985-4]
UniGeneiHs.166120.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O61X-ray2.80A8-125[»]
ProteinModelPortaliQ92985.
SMRiQ92985. Positions 8-123, 289-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109873. 42 interactions.
DIPiDIP-34895N.
IntActiQ92985. 26 interactions.
MINTiMINT-1202972.
STRINGi9606.ENSP00000329411.

PTM databases

iPTMnetiQ92985.
PhosphoSiteiQ92985.

Polymorphism and mutation databases

BioMutaiIRF7.
DMDMi116242593.

Proteomic databases

MaxQBiQ92985.
PaxDbiQ92985.
PeptideAtlasiQ92985.
PRIDEiQ92985.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330243; ENSP00000329411; ENSG00000185507. [Q92985-4]
ENST00000348655; ENSP00000331803; ENSG00000185507. [Q92985-2]
ENST00000397566; ENSP00000380697; ENSG00000185507. [Q92985-4]
ENST00000397574; ENSP00000380704; ENSG00000185507. [Q92985-1]
ENST00000469048; ENSP00000434607; ENSG00000185507. [Q92985-3]
ENST00000533182; ENSP00000433903; ENSG00000185507. [Q92985-3]
ENST00000612534; ENSP00000479615; ENSG00000276561. [Q92985-4]
ENST00000621391; ENSP00000480358; ENSG00000276561. [Q92985-1]
ENST00000632827; ENSP00000488039; ENSG00000276561. [Q92985-4]
ENST00000633274; ENSP00000488591; ENSG00000276561. [Q92985-3]
ENST00000633943; ENSP00000488666; ENSG00000276561. [Q92985-2]
ENST00000634105; ENSP00000488581; ENSG00000276561. [Q92985-3]
GeneIDi3665.
KEGGihsa:3665.
UCSCiuc001lqg.3. human. [Q92985-1]

Organism-specific databases

CTDi3665.
GeneCardsiIRF7.
HGNCiHGNC:6122. IRF7.
HPAiCAB017694.
HPA052757.
MIMi605047. gene.
616345. phenotype.
neXtProtiNX_Q92985.
PharmGKBiPA29921.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IWNR. Eukaryota.
ENOG4111G85. LUCA.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000111812.
HOVERGENiHBG105600.
InParanoidiQ92985.
KOiK09447.
OMAiGWKTNFR.
OrthoDBiEOG091G067P.
PhylomeDBiQ92985.
TreeFamiTF328512.

Enzyme and pathway databases

ReactomeiR-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-877300. Interferon gamma signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ92985.
SIGNORiQ92985.

Miscellaneous databases

ChiTaRSiIRF7. human.
GeneWikiiIRF7.
GenomeRNAii3665.
PROiQ92985.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185507.
CleanExiHS_IRF7.
ExpressionAtlasiQ92985. baseline and differential.
GenevisibleiQ92985. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.200.10. 1 hit.
InterProiIPR019817. 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]
PfamiPF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]
PRINTSiPR00267. INTFRNREGFCT.
SMARTiSM00348. IRF. 1 hit.
SM01243. IRF-3. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF49879. SSF49879. 1 hit.
PROSITEiPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIRF7_HUMAN
AccessioniPrimary (citable) accession number: Q92985
Secondary accession number(s): B9EGL3
, O00331, O00332, O00333, O75924, Q9UE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: September 7, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.