IRF7
entrez
3665
canonical
uniprot
Q92985
canonical
ensembl
ENSG00000185507
resolver
ensembl
ENSG00000276561
resolver
ensp
ENSP00000329411
resolver
ensp
ENSP00000331803
resolver
ensp
ENSP00000380700
resolver
ensp
ENSP00000434009
resolver
ensp
ENSP00000479277
resolver
ensp
ENSP00000529039
resolver
ensp
ENSP00000641645
resolver
enst
ENST00000397570
resolver
enst
ENST00000617397
resolver
genesymbol
IRF7
resolver
hgnc
HGNC:6122
resolver
uniprot
A0A0A0MS82
resolver
uniprot
B4E1B1
resolver
uniprot
B9EGL3
resolver
uniprot
M9RSF4
resolver
uniprot
O00331
resolver
uniprot
O00332
resolver
uniprot
O00333
resolver
uniprot
O75924
resolver
uniprot
Q9UE79
resolver
uniprot_entry
A0A0A0MS82_HUMAN
resolver
uniprot_entry
B4E1B1_HUMAN
resolver
uniprot_entry
IRF7_HUMAN
resolver
uniprot_entry
M9RSF4_HUMAN
resolver
uniprot_sec
B9EGL3
resolver
uniprot_sec
O00331
resolver
uniprot_sec
O00332
resolver
uniprot_sec
O00333
resolver
uniprot_sec
O75924
resolver
uniprot_sec
Q9UE79
resolver
activity_regulation
ACTIVITY 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.
uniprot
proteins
amino_acid_sequence
MALAPERAAPRVLFGEWLLGEISSGCYEGLQWLDEARTCFRVPWKHFARKDLSEADARIFKAWAVARGRWPPSSRGGGPPPEAETAERAGWKTNFRCALRSTRRFVMLRDNSGDPADPHKVYALSRELCWREGPGTDQTEAEAPAAVPPPQGGPPGPFLAHTHAGLQAPGPLPAPAGDKGDLLLQAVQQSCLADHLLTASWGADPVPTKAPGEGQEGLPLTGACAGGPGLPAGELYGWAVETTPSPGPQPAALTTGEAAAPESPHQAEPYLSPSPSACTAVQEPSPGALDVTIMYKGRTVLQKVVGHPSCTFLYGPPDPAVRATDPQQVAFPSPAELPDQKQLRYTEELLRHVAPGLHLELRGPQLWARRMGKCKVYWEVGGPPGSASPSTPACLLPRNCDTPIFDFRVFFQELVEFRARQRRGSPRYTIYLGFGQDLSAGRPKEKSLVLVKLEPWLCRVHLEGTQREGVSSLDSSSLSLCLSSANSLYDDIECFLMELEQPA
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 39, susceptibility to viral infections (IMD39) [MIM:616345]: An autosomal recessive primary immunodeficiency causing severe, life-threatening acute respiratory distress upon infection with certain viruses, mainly H1N1 influenza A, SARS-CoV-2 and RSV. {ECO:0000269|PubMed:25814066}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
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 (PubMed:28342865, PubMed:28768858). 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 (PubMed:17574024, PubMed:32972995). 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. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (By similarity). 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 (By similarity) (PubMed:11073981, PubMed:12374802, PubMed:15361868, PubMed:17404045). {ECO:0000250|UniProtKB:P70434, ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802, ECO:0000269|PubMed:15361868, ECO:0000269|PubMed:17404045, ECO:0000269|PubMed:17574024, ECO:0000269|PubMed:28342865, ECO:0000269|PubMed:28768858, ECO:0000269|PubMed:32972995}.
uniprot
proteins
mass_dalton
54278
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="G->T: Loss of acetylation, increased DNA-binding and activity; when associated with R-93."; /evidence="ECO:0000269|PubMed:12374802"; MUTAGEN 92; /note="K->R: Loss of acetylation, DNA-binding and activity."; /evidence="ECO:0000269|PubMed:12374802"; MUTAGEN 93; /note="T->R: Loss of acetylation, increased DNA-binding and activity; when associated with T-90."; /evidence="ECO:0000269|PubMed:12374802"; MUTAGEN 151; /note="Q->A: No effect on cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 167; /note="Q->A: Complete loss of inactivation of IFN-I production; when associated with R-189."; /evidence="ECO:0000269|PubMed:26608321"; MUTAGEN 167; /note="Q->A: No effect on cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 185; /note="Q->A: No effect on cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 188; /note="Q->A: No effect on cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 189; /note="Q->A: Complete loss of cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 189; /note="Q->R: Complete loss of inactivation of IFN-I production; when associated with A-167."; /evidence="ECO:0000269|PubMed:26608321"; MUTAGEN 215; /note="Q->A: No effect on cleavage by enterovirus 71."; /evidence="ECO:0000269|PubMed:23175366"; MUTAGEN 375; /note="K->R: Loss of NEURL3-mediated ubiquitination."; /evidence="ECO:0000269|PubMed:35792897"; MUTAGEN 477..479; /note="SLS->ALA: Complete loss of TBK1 and IKKE phosphorylation."; /evidence="ECO:0000269|PubMed:15367631
uniprot
proteins
post_translational_modification
PTM: Acetylation inhibits its DNA-binding ability and activity. {ECO:0000269|PubMed:12374802}.; PTM: 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. {ECO:0000269|PubMed:11073981, ECO:0000269|PubMed:12374802, ECO:0000269|PubMed:15367631, ECO:0000269|PubMed:15767370}.; PTM: TRAF6-mediated ubiquitination is required for IRF7 activation (By similarity). TRIM35 mediates IRF7 'Lys-48'-linked polyubiquitination and subsequent proteasomal degradation (PubMed:25907537). Ubiquitinated by UBE3C, leading to its degradation (PubMed:21167755). {ECO:0000250|UniProtKB:P70434, ECO:0000269|PubMed:21167755, ECO:0000269|PubMed:25907537}.; PTM: Sumoylated by TRIM28, which inhibits its transactivation activity. {ECO:0000269|PubMed:21940674}.; PTM: (Microbial infection) Cleaved and inactivated by the protease 3C of enterovirus 71 allowing the virus to disrupt the host type I interferon production. {ECO:0000269|PubMed:23175366}.; PTM: (Microbial infection) Cleaved and inactivated by the protease 3C of human enterovirus 68D (EV68) allowing the virus to disrupt the host type I interferon production. {ECO:0000269|PubMed:26608321}.; PTM: 'Lys-48'-linked polyubiquitination and subsequent proteasomal degradation is NMI-dependent in response to Sendai virus infection. {ECO:0000250|UniProtKB:P70434}.; PTM: 'Lys-63'-linked ubiquitination by NEURL3 promotes IRF7 activation. {ECO:0000269|PubMed:35792897}.
uniprot
proteins
protein_family
IRF family
uniprot
proteins
pubmed
11073981
uniprot
proteins
pubmed
11124948
uniprot
proteins
pubmed
11314014
uniprot
proteins
pubmed
11846980
uniprot
proteins
pubmed
11943871
uniprot
proteins
pubmed
12374802
uniprot
proteins
pubmed
14517278
uniprot
proteins
pubmed
14739303
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15361868
uniprot
proteins
pubmed
15367631
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15492225
uniprot
proteins
pubmed
15767370
uniprot
proteins
pubmed
16846591
uniprot
proteins
pubmed
16979567
uniprot
proteins
pubmed
17301153
uniprot
proteins
pubmed
17404045
uniprot
proteins
pubmed
17574024
uniprot
proteins
pubmed
18987133
uniprot
proteins
pubmed
19017798
uniprot
proteins
pubmed
19557165
uniprot
proteins
pubmed
20049431
uniprot
proteins
pubmed
21167755
uniprot
proteins
pubmed
21490621
uniprot
proteins
pubmed
21940674
uniprot
proteins
pubmed
23175366
uniprot
proteins
pubmed
25814066
uniprot
proteins
pubmed
25907537
uniprot
proteins
pubmed
26608321
uniprot
proteins
pubmed
28342865
uniprot
proteins
pubmed
28768858
uniprot
proteins
pubmed
28768861
uniprot
proteins
pubmed
29427864
uniprot
proteins
pubmed
30598516
uniprot
proteins
pubmed
32972995
uniprot
proteins
pubmed
35792897
uniprot
proteins
pubmed
9315633
uniprot
proteins
pubmed
9786932
uniprot
proteins
sequence_length
503
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=The phosphorylated and active form accumulates selectively in the nucleus.
uniprot
proteins