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UniProtKB - Q14653 (IRF3_HUMAN)

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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)DescriptionActionsGraphical viewLength
DNA bindingi5 – 111IRF tryptophan pentad repeatPROSITE-ProRule annotationAdd BLAST107

GO - Molecular functioni

  • DNA binding Source: BHF-UCL
  • identical protein binding Source: IntAct
  • protein domain specific binding Source: CAFA
  • protein homodimerization activity Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
  • transcription cofactor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionActivator, DNA-binding
Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity, Transcription, Transcription regulation

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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: HPA
  • 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)DescriptionActionsGraphical viewLength
Natural variantiVAR_075805285R → 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 PublicationCorresponds to variant dbSNP:rs750526659Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi77 – 78KR → NG: Abolishes nuclear localization. 1 Publication2
Mutagenesisi86 – 87RK → LQ: No effect on subcellular localization. 1 Publication2
Mutagenesisi139 – 140IL → MM: Abolishes nuclear export. 1 Publication2
Mutagenesisi193K → R: Highly diminished ISGylation; when associated with R-360 and R-366. 1 Publication1
Mutagenesisi360K → R: Highly diminished ISGylation; when associated with R-193 and R-366. 1 Publication1
Mutagenesisi366K → R: Highly diminished ISGylation; when associated with R-193 and R-360. 1 Publication1
Mutagenesisi385 – 386SS → AA: Complete loss of viral infection induced phosphorylation. 1 Publication2
Mutagenesisi385S → A, D or E: Complete loss of viral infection induced phosphorylation. 1 Publication1
Mutagenesisi386S → A, D or E: Complete loss of viral infection induced phosphorylation. 2 Publications1
Mutagenesisi386S → A: Abolishes dimerization after phosphorylation. 2 Publications1
Mutagenesisi396 – 405SNSHPLSLTS → ANAHPLALAA: Complete loss of viral infection induced phosphorylation. 1 Publication10
Mutagenesisi396 – 405SNSHPLSLTS → DNDHPLDLDD: Acts as a constitutively activated IRF3. 1 Publication10
Mutagenesisi396 – 398SNS → ANA: Complete loss of viral infection induced phosphorylation. 3
Mutagenesisi402 – 405SLTS → ALAA: Complete loss of viral infection induced phosphorylation. 4

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3661.
MalaCardsiIRF3.
MIMi616532. phenotype.
OpenTargetsiENSG00000126456.
PharmGKBiPA29917.

Polymorphism and mutation databases

BioMutaiIRF3.
DMDMi2497442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001545531 – 427Interferon regulatory factor 3Add BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3Phosphothreonine1 Publication1
Modified residuei14Phosphoserine1 Publication1
Modified residuei75Phosphothreonine1 Publication1
Modified residuei97Phosphoserine1 Publication1
Modified residuei123PhosphoserineBy similarity1
Modified residuei180Phosphothreonine1 Publication1
Modified residuei188Phosphoserine1 Publication1
Cross-linki193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Modified residuei237Phosphothreonine1 Publication1
Modified residuei244Phosphothreonine1 Publication1
Modified residuei253Phosphothreonine1 Publication1
Disulfide bondi267 ↔ 2892 Publications
Cross-linki360Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Cross-linki366Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)1 Publication
Modified residuei386Phosphoserine; by TBK11 Publication1
Modified residuei396Phosphoserine; by IKKE1 Publication1
Modified residuei398Phosphoserine1 Publication1
Modified residuei404Phosphothreonine1 Publication1
Modified residuei427Phosphoserine1 Publication1

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.
PhosphoSitePlusiQ14653.

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). Interacts with RIOK3; RIOK3 probybly mediates the interaction of TBK1 with IRF3.11 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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein domain specific binding Source: CAFA
  • protein homodimerization activity Source: BHF-UCL
Complete GO annotation...

Protein-protein interaction databases

BioGridi109869. 80 interactors.
DIPiDIP-41448N.
IntActiQ14653. 47 interactors.
MINTiMINT-253351.
STRINGi9606.ENSP00000310127.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 18Combined sources11
Beta strandi25 – 27Combined sources3
Beta strandi28 – 31Combined sources4
Beta strandi33 – 37Combined sources5
Beta strandi41 – 45Combined sources5
Helixi49 – 51Combined sources3
Helixi53 – 60Combined sources8
Beta strandi66 – 69Combined sources4
Helixi73 – 85Combined sources13
Beta strandi90 – 96Combined sources7
Beta strandi100 – 102Combined sources3
Beta strandi104 – 109Combined sources6
Helixi191 – 196Combined sources6
Beta strandi204 – 210Combined sources7
Beta strandi213 – 220Combined sources8
Beta strandi226 – 229Combined sources4
Beta strandi238 – 244Combined sources7
Helixi248 – 250Combined sources3
Beta strandi252 – 254Combined sources3
Helixi255 – 266Combined sources12
Turni267 – 270Combined sources4
Beta strandi272 – 277Combined sources6
Beta strandi280 – 285Combined sources6
Beta strandi287 – 289Combined sources3
Beta strandi291 – 297Combined sources7
Beta strandi304 – 306Combined sources3
Beta strandi308 – 310Combined sources3
Beta strandi313 – 315Combined sources3
Beta strandi317 – 321Combined sources5
Helixi322 – 333Combined sources12
Beta strandi343 – 350Combined sources8
Beta strandi354 – 356Combined sources3
Helixi358 – 360Combined sources3
Beta strandi361 – 369Combined sources9
Helixi370 – 383Combined sources14
Beta strandi384 – 391Combined sources8
Beta strandi395 – 397Combined sources3
Beta strandi401 – 404Combined sources4
Helixi405 – 417Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14653.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 360Involved in HERC5 bindingAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi139 – 149Nuclear export signalAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi151 – 191Pro-richAdd BLAST41

Sequence similaritiesi

Belongs to the IRF family.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.
InterProiView protein in InterPro
IPR019817. 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.
PANTHERiPTHR11949. PTHR11949. 1 hit.
PfamiView protein in Pfam
PF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
PRINTSiPR00267. INTFRNREGFCT.
SMARTiView protein in SMART
SM00348. IRF. 1 hit.
SM01243. IRF-3. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF49879. SSF49879. 1 hit.
PROSITEiView protein in PROSITE
PS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.

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)DescriptionActionsGraphical viewLength
Sequence conflicti196L → F in BAG37040 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01190196R → Q. Corresponds to variant dbSNP:rs968457Ensembl.1
Natural variantiVAR_049643107Y → F. Corresponds to variant dbSNP:rs34745118Ensembl.1
Natural variantiVAR_075805285R → 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 PublicationCorresponds to variant dbSNP:rs750526659Ensembl.1
Natural variantiVAR_011902377E → K. Corresponds to variant dbSNP:rs1049486Ensembl.1
Natural variantiVAR_011903427S → T2 PublicationsCorresponds to variant dbSNP:rs7251Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0469111 – 146Missing in isoform 3. 1 PublicationAdd BLAST146
Alternative sequenceiVSP_04769056 – 104AWAEA…PHDPH → ELGTFPSQTPLRTPMVEAVL LIPRKTFWMSYWVTWCWPHS QIRDPQAWL in isoform 5. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_047691105 – 427Missing in isoform 5. 1 PublicationAdd BLAST323
Alternative sequenceiVSP_043319201 – 327Missing in isoform 2 and isoform 3. 1 PublicationAdd BLAST127
Alternative sequenceiVSP_046912328 – 427DLITF…GPGES → GSWAPRSDYLHGRKRTLTTL CPLVLCGGVMAPGPAVDQEA RDGQGCAHVPQGLGRNGPGR GCLLPGEYCGPAHFQQPPTL PHLRPVQGLPAGLGGGHGFP GPWGELSPRSSWCASNPPVP HHLNQ in isoform 4. 1 PublicationAdd BLAST100

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]
XP_016882255.1. XM_017026766.1. [Q14653-1]
XP_016882256.1. XM_017026767.1. [Q14653-1]
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

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.

Entry informationi

Entry nameiIRF3_HUMAN
AccessioniPrimary (citable) accession number: Q14653
Secondary accession number(s): A8K7L2
, B2RAZ3, Q5FBY1, Q5FBY2, Q5FBY4, Q7Z5G6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 5, 2017
This is version 170 of the entry and version 1 of the sequence. See 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