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Protein

Interferon regulatory factor 3

Gene

IRF3

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 which 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. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.

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 bindingi5 – 111107IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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-1169408. ISG15 antiviral mechanism.
R-HSA-1606341. IRF3 mediated activation of type 1 IFN.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
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-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiQ14653.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon regulatory factor 3
Short name:
IRF-3
Gene namesi
Name:IRF3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:6118. IRF3.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm.

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Herpes simplex encephalitis 7 (HSE7)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.
See also OMIM:616532
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti285 – 2851R → Q in HSE7; loss of viral infection-induced phosphorylation at S-386; loss of viral infection-induced homodimerization; loss of viral infection-induced transcription factor activity; unable to activate interferon transcription in response to viral infection. 1 Publication
Corresponds to variant rs750526659 [ dbSNP | Ensembl ].
VAR_075805

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 782KR → NG: Abolishes nuclear localization. 1 Publication
Mutagenesisi86 – 872RK → LQ: No effect on subcellular localization. 1 Publication
Mutagenesisi139 – 1402IL → MM: Abolishes nuclear export. 1 Publication
Mutagenesisi193 – 1931K → R: Highly diminished ISGylation; when associated with R-360 and R-366. 1 Publication
Mutagenesisi360 – 3601K → R: Highly diminished ISGylation; when associated with R-193 and R-366. 1 Publication
Mutagenesisi366 – 3661K → R: Highly diminished ISGylation; when associated with R-193 and R-360. 1 Publication
Mutagenesisi385 – 3862SS → AA: Complete loss of viral infection induced phosphorylation. 1 Publication
Mutagenesisi385 – 3851S → A, D or E: Complete loss of viral infection induced phosphorylation. 1 Publication
Mutagenesisi386 – 3861S → A, D or E: Complete loss of viral infection induced phosphorylation. 2 Publications
Mutagenesisi386 – 3861S → A: Abolishes dimerization after phosphorylation. 2 Publications
Mutagenesisi396 – 40510SNSHPLSLTS → ANAHPLALAA: Complete loss of viral infection induced phosphorylation. 1 Publication
Mutagenesisi396 – 40510SNSHPLSLTS → DNDHPLDLDD: Acts as a constitutively activated IRF3. 1 Publication
Mutagenesisi396 – 3983SNS → ANA: Complete loss of viral infection induced phosphorylation.
Mutagenesisi402 – 4054SLTS → ALAA: Complete loss of viral infection induced phosphorylation.

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi616532. phenotype.
PharmGKBiPA29917.

Polymorphism and mutation databases

BioMutaiIRF3.
DMDMi2497442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Interferon regulatory factor 3PRO_0000154553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Phosphothreonine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei75 – 751Phosphothreonine1 Publication
Modified residuei97 – 971Phosphoserine1 Publication
Modified residuei123 – 1231PhosphoserineBy similarity
Modified residuei180 – 1801Phosphothreonine1 Publication
Modified residuei188 – 1881Phosphoserine1 Publication
Cross-linki193 – 193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei244 – 2441Phosphothreonine1 Publication
Modified residuei253 – 2531Phosphothreonine1 Publication
Disulfide bondi267 ↔ 2892 Publications
Cross-linki360 – 360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Cross-linki366 – 366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)
Modified residuei386 – 3861Phosphoserine; by TBK11 Publication
Modified residuei396 – 3961Phosphoserine; by IKKE1 Publication
Modified residuei398 – 3981Phosphoserine1 Publication
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei427 – 4271Phosphoserine1 Publication

Post-translational modificationi

Constitutively phosphorylated on many Ser/Thr residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Phosphorylated at Ser-396 by IKBKE upon ssRNA viral infection. Ser-385 and Ser-386 may be specifically phosphorylated in response to induction. Phosphorylation at Ser-386 by TBK1 results in oligomerization. An alternate model propose that the five serine/threonine residues between 396 and 405 are phosphorylated in response to a viral infection.2 Publications
(Microbial infection) Phosphorylation and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3.1 Publication
Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation.2 Publications
ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation.3 Publications

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14653.
MaxQBiQ14653.
PaxDbiQ14653.
PeptideAtlasiQ14653.
PRIDEiQ14653.

PTM databases

iPTMnetiQ14653.
PhosphoSiteiQ14653.

Expressioni

Tissue specificityi

Expressed constitutively in a variety of tissues.

Gene expression databases

BgeeiENSG00000126456.
CleanExiHS_IRF3.
ExpressionAtlasiQ14653. baseline and differential.
GenevisibleiQ14653. HS.

Organism-specific databases

HPAiCAB013018.
HPA004895.

Interactioni

Subunit structurei

Monomer. Homodimer; phosphorylation-induced. Heterodimer with IRF7. Interacts with CREBBP. May interact with MAVS. Interacts with IKBKE and TBK1. Interacts with TICAM1 and TICAM2. Interacts with RBCK1. Interacts with HERC5. Interacts with DDX3X (phosphorylated at 'Ser-102'); the interaction allows the phosphorylation and activation of IRF3 by IKBKE. Interacts with TRIM21 and ULK1, in the presence of TRIM21; this interaction leads to IRF3 degradation by autophagy (PubMed:26347139).10 Publications
(Microbial infection) Interacts with rotavirus A NSP1 (via C-terminus); this interaction leads to the proteasome-dependent degradation of IRF3 (PubMed:12186937).1 Publication
(Microbial infection) Interacts with herpes virus 8/HHV-8 protein VIRF1 (PubMed:11314014).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself11EBI-2650369,EBI-2650369
CREBBPQ927934EBI-2650369,EBI-81215
GRIP1Q9Y3R02EBI-2650369,EBI-5349621
IKBKEQ141642EBI-2650369,EBI-307369
MAFBQ9Y5Q34EBI-2650369,EBI-3649340
RB1P064002EBI-2650369,EBI-491274
RBL1P287492EBI-2650369,EBI-971402
SGTAO437653EBI-2650369,EBI-347996
TBK1Q9UHD28EBI-2650369,EBI-356402

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi109869. 78 interactions.
DIPiDIP-41448N.
IntActiQ14653. 45 interactions.
MINTiMINT-253351.
STRINGi9606.ENSP00000310127.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 1811Combined sources
Beta strandi25 – 273Combined sources
Beta strandi28 – 314Combined sources
Beta strandi33 – 375Combined sources
Beta strandi41 – 455Combined sources
Helixi49 – 513Combined sources
Helixi53 – 608Combined sources
Beta strandi66 – 694Combined sources
Helixi73 – 8513Combined sources
Beta strandi90 – 967Combined sources
Beta strandi100 – 1023Combined sources
Beta strandi104 – 1096Combined sources
Helixi191 – 1955Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi213 – 2219Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi239 – 2446Combined sources
Helixi248 – 2503Combined sources
Helixi255 – 26713Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi287 – 2893Combined sources
Beta strandi291 – 2966Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi317 – 3215Combined sources
Helixi322 – 33312Combined sources
Beta strandi343 – 3486Combined sources
Beta strandi354 – 3563Combined sources
Helixi357 – 3604Combined sources
Beta strandi363 – 3697Combined sources
Helixi370 – 38314Combined sources
Beta strandi389 – 3913Combined sources
Beta strandi401 – 4033Combined sources
Helixi405 – 41612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2FX-ray2.30A/B175-427[»]
1QWTX-ray2.10A/B173-427[»]
1T2KX-ray3.00A/B1-112[»]
1ZOQX-ray2.37A/B196-386[»]
2O61X-ray2.80A9-111[»]
2O6GX-ray3.10E/F/G/H1-123[»]
2PI0X-ray2.31A/B/C/D1-113[»]
3A77X-ray1.80A/B/C/D189-427[»]
3QU6X-ray2.30A/B/C1-113[»]
5JEJX-ray2.00A/B189-427[»]
5JEKX-ray2.40A/B189-427[»]
5JELX-ray1.60A189-427[»]
5JEMX-ray2.50A/B/E/G189-398[»]
5JEOX-ray1.72A189-427[»]
5JERX-ray2.91A/C/E/G189-427[»]
ProteinModelPortaliQ14653.
SMRiQ14653. Positions 1-112, 189-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14653.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 360161Involved in HERC5 bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi139 – 14911Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 19141Pro-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IXD8. Eukaryota.
ENOG410YA4B. LUCA.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000033705.
HOVERGENiHBG105601.
InParanoidiQ14653.
KOiK05411.
OMAiCHTYWAV.
OrthoDBiEOG091G067P.
PhylomeDBiQ14653.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14653-1) [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
MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED
60 70 80 90 100
FGIFQAWAEA TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP
110 120 130 140 150
HDPHKIYEFV NSGVGDFSQP DTSPDTNGGG STSDTQEDIL DELLGNMVLA
160 170 180 190 200
PLPDPGPPSL AVAPEPCPQP LRSPSLDNPT PFPNLGPSEN PLKRLLVPGE
210 220 230 240 250
EWEFEVTAFY RGRQVFQQTI SCPEGLRLVG SEVGDRTLPG WPVTLPDPGM
260 270 280 290 300
SLTDRGVMSY VRHVLSCLGG GLALWRAGQW LWAQRLGHCH TYWAVSEELL
310 320 330 340 350
PNSGHGPDGE VPKDKEGGVF DLGPFIVDLI TFTEGSGRSP RYALWFCVGE
360 370 380 390 400
SWPQDQPWTK RLVMVKVVPT CLRALVEMAR VGGASSLENT VDLHISNSHP
410 420
LSLTSDQYKA YLQDLVEGMD FQGPGES
Length:427
Mass (Da):47,219
Last modified:November 1, 1997 - v1
Checksum:iF536676FA78B0110
GO
Isoform 2 (identifier: Q14653-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     201-327: Missing.

Show »
Length:300
Mass (Da):33,170
Checksum:i1195BFBBA65C2DCE
GO
Isoform 3 (identifier: Q14653-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.
     201-327: Missing.

Show »
Length:154
Mass (Da):16,730
Checksum:i7A327E1716F74231
GO
Isoform 4 (identifier: Q14653-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     328-427: DLITFTEGSG...GMDFQGPGES → GSWAPRSDYL...NPPVPHHLNQ

Note: No experimental confirmation available.
Show »
Length:452
Mass (Da):49,134
Checksum:i96B059A029751B64
GO
Isoform 5 (identifier: Q14653-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-104: AWAEATGAYV...DRSKDPHDPH → ELGTFPSQTP...SQIRDPQAWL
     105-427: Missing.

Show »
Length:104
Mass (Da):12,330
Checksum:i7DA489EFD316732D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961L → F in BAG37040 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961R → Q.
Corresponds to variant rs968457 [ dbSNP | Ensembl ].
VAR_011901
Natural varianti107 – 1071Y → F.
Corresponds to variant rs34745118 [ dbSNP | Ensembl ].
VAR_049643
Natural varianti285 – 2851R → Q in HSE7; loss of viral infection-induced phosphorylation at S-386; loss of viral infection-induced homodimerization; loss of viral infection-induced transcription factor activity; unable to activate interferon transcription in response to viral infection. 1 Publication
Corresponds to variant rs750526659 [ dbSNP | Ensembl ].
VAR_075805
Natural varianti377 – 3771E → K.
Corresponds to variant rs1049486 [ dbSNP | Ensembl ].
VAR_011902
Natural varianti427 – 4271S → T.2 Publications
Corresponds to variant rs7251 [ dbSNP | Ensembl ].
VAR_011903

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform 3. 1 PublicationVSP_046911Add
BLAST
Alternative sequencei56 – 10449AWAEA…PHDPH → ELGTFPSQTPLRTPMVEAVL LIPRKTFWMSYWVTWCWPHS QIRDPQAWL in isoform 5. 1 PublicationVSP_047690Add
BLAST
Alternative sequencei105 – 427323Missing in isoform 5. 1 PublicationVSP_047691Add
BLAST
Alternative sequencei201 – 327127Missing in isoform 2 and isoform 3. 1 PublicationVSP_043319Add
BLAST
Alternative sequencei328 – 427100DLITF…GPGES → GSWAPRSDYLHGRKRTLTTL CPLVLCGGVMAPGPAVDQEA RDGQGCAHVPQGLGRNGPGR GCLLPGEYCGPAHFQQPPTL PHLRPVQGLPAGLGGGHGFP GPWGELSPRSSWCASNPPVP HHLNQ in isoform 4. 1 PublicationVSP_046912Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z56281 mRNA. Translation: CAA91227.1.
AB102884 mRNA. Translation: BAD89413.1.
AB102886 mRNA. Translation: BAD89415.1.
AB102887 mRNA. Translation: BAD89416.1.
AK292027 mRNA. Translation: BAF84716.1.
AK314421 mRNA. Translation: BAG37040.1.
AC011495 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52510.1.
BC000660 mRNA. Translation: AAH00660.1.
BC071721 mRNA. Translation: AAH71721.1.
U86636 Genomic DNA. Translation: AAC68818.1.
CCDSiCCDS12775.1. [Q14653-1]
CCDS56099.1. [Q14653-2]
CCDS59407.1. [Q14653-3]
CCDS59409.1. [Q14653-4]
RefSeqiNP_001184051.1. NM_001197122.1. [Q14653-4]
NP_001184052.1. NM_001197123.1.
NP_001184053.1. NM_001197124.1. [Q14653-2]
NP_001184054.1. NM_001197125.1.
NP_001184055.1. NM_001197126.1.
NP_001184056.1. NM_001197127.1. [Q14653-3]
NP_001184057.1. NM_001197128.1. [Q14653-3]
NP_001562.1. NM_001571.5. [Q14653-1]
XP_006723260.1. XM_006723197.1. [Q14653-4]
XP_006723261.1. XM_006723198.1. [Q14653-4]
UniGeneiHs.289052.
Hs.731922.
Hs.75254.

Genome annotation databases

EnsembliENST00000309877; ENSP00000310127; ENSG00000126456. [Q14653-1]
ENST00000377139; ENSP00000366344; ENSG00000126456. [Q14653-1]
ENST00000442265; ENSP00000400378; ENSG00000126456. [Q14653-5]
ENST00000596765; ENSP00000470512; ENSG00000126456. [Q14653-3]
ENST00000597198; ENSP00000469113; ENSG00000126456. [Q14653-1]
ENST00000599223; ENSP00000471358; ENSG00000126456. [Q14653-2]
ENST00000600022; ENSP00000472700; ENSG00000126456. [Q14653-3]
ENST00000601291; ENSP00000471896; ENSG00000126456. [Q14653-4]
GeneIDi3661.
KEGGihsa:3661.
UCSCiuc002pot.3. human. [Q14653-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z56281 mRNA. Translation: CAA91227.1.
AB102884 mRNA. Translation: BAD89413.1.
AB102886 mRNA. Translation: BAD89415.1.
AB102887 mRNA. Translation: BAD89416.1.
AK292027 mRNA. Translation: BAF84716.1.
AK314421 mRNA. Translation: BAG37040.1.
AC011495 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52510.1.
BC000660 mRNA. Translation: AAH00660.1.
BC071721 mRNA. Translation: AAH71721.1.
U86636 Genomic DNA. Translation: AAC68818.1.
CCDSiCCDS12775.1. [Q14653-1]
CCDS56099.1. [Q14653-2]
CCDS59407.1. [Q14653-3]
CCDS59409.1. [Q14653-4]
RefSeqiNP_001184051.1. NM_001197122.1. [Q14653-4]
NP_001184052.1. NM_001197123.1.
NP_001184053.1. NM_001197124.1. [Q14653-2]
NP_001184054.1. NM_001197125.1.
NP_001184055.1. NM_001197126.1.
NP_001184056.1. NM_001197127.1. [Q14653-3]
NP_001184057.1. NM_001197128.1. [Q14653-3]
NP_001562.1. NM_001571.5. [Q14653-1]
XP_006723260.1. XM_006723197.1. [Q14653-4]
XP_006723261.1. XM_006723198.1. [Q14653-4]
UniGeneiHs.289052.
Hs.731922.
Hs.75254.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J2FX-ray2.30A/B175-427[»]
1QWTX-ray2.10A/B173-427[»]
1T2KX-ray3.00A/B1-112[»]
1ZOQX-ray2.37A/B196-386[»]
2O61X-ray2.80A9-111[»]
2O6GX-ray3.10E/F/G/H1-123[»]
2PI0X-ray2.31A/B/C/D1-113[»]
3A77X-ray1.80A/B/C/D189-427[»]
3QU6X-ray2.30A/B/C1-113[»]
5JEJX-ray2.00A/B189-427[»]
5JEKX-ray2.40A/B189-427[»]
5JELX-ray1.60A189-427[»]
5JEMX-ray2.50A/B/E/G189-398[»]
5JEOX-ray1.72A189-427[»]
5JERX-ray2.91A/C/E/G189-427[»]
ProteinModelPortaliQ14653.
SMRiQ14653. Positions 1-112, 189-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109869. 78 interactions.
DIPiDIP-41448N.
IntActiQ14653. 45 interactions.
MINTiMINT-253351.
STRINGi9606.ENSP00000310127.

PTM databases

iPTMnetiQ14653.
PhosphoSiteiQ14653.

Polymorphism and mutation databases

BioMutaiIRF3.
DMDMi2497442.

Proteomic databases

EPDiQ14653.
MaxQBiQ14653.
PaxDbiQ14653.
PeptideAtlasiQ14653.
PRIDEiQ14653.

Protocols and materials databases

DNASUi3661.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309877; ENSP00000310127; ENSG00000126456. [Q14653-1]
ENST00000377139; ENSP00000366344; ENSG00000126456. [Q14653-1]
ENST00000442265; ENSP00000400378; ENSG00000126456. [Q14653-5]
ENST00000596765; ENSP00000470512; ENSG00000126456. [Q14653-3]
ENST00000597198; ENSP00000469113; ENSG00000126456. [Q14653-1]
ENST00000599223; ENSP00000471358; ENSG00000126456. [Q14653-2]
ENST00000600022; ENSP00000472700; ENSG00000126456. [Q14653-3]
ENST00000601291; ENSP00000471896; ENSG00000126456. [Q14653-4]
GeneIDi3661.
KEGGihsa:3661.
UCSCiuc002pot.3. human. [Q14653-1]

Organism-specific databases

CTDi3661.
GeneCardsiIRF3.
HGNCiHGNC:6118. IRF3.
HPAiCAB013018.
HPA004895.
MIMi603734. gene.
616532. phenotype.
neXtProtiNX_Q14653.
PharmGKBiPA29917.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXD8. Eukaryota.
ENOG410YA4B. LUCA.
GeneTreeiENSGT00760000119093.
HOGENOMiHOG000033705.
HOVERGENiHBG105601.
InParanoidiQ14653.
KOiK05411.
OMAiCHTYWAV.
OrthoDBiEOG091G067P.
PhylomeDBiQ14653.
TreeFamiTF328512.

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-1606341. IRF3 mediated activation of type 1 IFN.
R-HSA-3134973. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
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-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiQ14653.

Miscellaneous databases

ChiTaRSiIRF3. human.
EvolutionaryTraceiQ14653.
GeneWikiiIRF3.
GenomeRNAii3661.
PROiQ14653.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126456.
CleanExiHS_IRF3.
ExpressionAtlasiQ14653. baseline and differential.
GenevisibleiQ14653. 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 nameiIRF3_HUMAN
AccessioniPrimary (citable) accession number: Q14653
Secondary accession number(s): A8K7L2
, B2RAZ3, Q5FBY1, Q5FBY2, Q5FBY4, Q7Z5G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 160 of the entry and version 1 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 19
    Human chromosome 19: 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.