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P10914 (IRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon regulatory factor 1

Short name=IRF-1
Gene names
Name:IRF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses. These include the regulation of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage. Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters. Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, DDX58/RIG-I, TNFSF10/TRAIL, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA. Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4. Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53. Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells. Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development. Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24

Enzyme regulation

Activated by MYD88 By similarity.

Subunit structure

Monomer. Homodimer. Interacts with MYD88 and PIAS3 By similarity. Interacts with EP300. Ref.12

Subcellular location

Nucleus. Cytoplasm. Note: MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1.

Induction

By viruses and interferon (IFN).

Post-translational modification

Phosphorylated by CK2 and this positively regulates its activity. Ref.7

Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation. Inactivates the tumor suppressor activity. Elevated levels in tumor cells. Major site is Lys-275. Sumoylation is enhanced by PIAS3 By similarity. Desumoylated by SENP1 in tumor cells and appears to compete with ubiquitination on C-terminal sites. Ref.16

Ubiquitinated. Appears to compete with sumoylation on C-terminal sites. Ref.16

Involvement in disease

Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.25 Ref.26

Miscellaneous

Deletion or rearrangement of IRF1 are found in preleukemic myelodysplastic syndrome (MDS) and acute myelogenous leukemia (AML).

Sequence similarities

Belongs to the IRF family.

Contains 1 IRF tryptophan pentad repeat DNA-binding domain.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DiseaseDisease mutation
Tumor suppressor
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCD8-positive, alpha-beta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from direct assay Ref.21. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell cycle arrest

Inferred from direct assay Ref.23. Source: UniProtKB

cellular response to interferon-beta

Inferred from direct assay PubMed 18035482. Source: BHF-UCL

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from direct assay Ref.22. Source: UniProtKB

interferon-gamma-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Traceable author statement Ref.10. Source: UniProtKB

negative regulation of regulatory T cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.15Ref.23. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from mutant phenotype Ref.22. Source: UniProtKB

positive regulation of interleukin-12 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.23. Source: UniProtKB

positive regulation of type I interferon production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of CD8-positive, alpha-beta T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of MyD88-dependent toll-like receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of adaptive immune response

Traceable author statement Ref.9. Source: UniProtKB

regulation of cell cycle

Traceable author statement Ref.10. Source: UniProtKB

regulation of innate immune response

Traceable author statement Ref.9. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement PubMed 2475256. Source: ProtInc

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nuclear chromatin

Inferred from direct assay PubMed 18035482. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Traceable author statement Ref.9. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.9. Source: UniProtKB

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

Inferred from direct assay PubMed 18035482. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E7P031293EBI-1055781,EBI-866453From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 325325Interferon regulatory factor 1
PRO_0000154545

Regions

DNA binding5 – 113109IRF tryptophan pentad repeat

Amino acid modifications

Modified residue781N6-acetyllysine Ref.24
Cross-link275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16
Cross-link299Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16

Natural variations

Natural variant81M → L in GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity. Ref.25
VAR_065134
Natural variant111W → R in GASC; the mutation abolishes DNA binding and transactivating activities. Ref.26
VAR_065135

Experimental info

Mutagenesis781K → R: Loss of acetylation. Partial loss of DNA-binding and transcriptional activity. Ref.24
Mutagenesis2751K → R: Some loss of sumoylation. Partial inhibition of acetylation and activity. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-299. Ref.16
Mutagenesis2991K → R: Large loss of sumoylation. Abolishes sumoylation, diminished ubiquitination, higher resistance to degradation, and increased apoptotic activity; when associated with R-275. Ref.16
Sequence conflict51R → W no nucleotide entry Ref.1
Sequence conflict51R → W no nucleotide entry Ref.2
Sequence conflict34 – 352FQ → LE no nucleotide entry Ref.1
Sequence conflict34 – 352FQ → LE no nucleotide entry Ref.2
Sequence conflict2201T → I no nucleotide entry Ref.1
Sequence conflict2201T → I no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P10914 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: 2E06245A212D1541

FASTA32536,502
        10         20         30         40         50         60 
MPITRMRMRP WLEMQINSNQ IPGLIWINKE EMIFQIPWKH AAKHGWDINK DACLFRSWAI 

        70         80         90        100        110        120 
HTGRYKAGEK EPDPKTWKAN FRCAMNSLPD IEEVKDQSRN KGSSAVRVYR MLPPLTKNQR 

       130        140        150        160        170        180 
KERKSKSSRD AKSKAKRKSC GDSSPDTFSD GLSSSTLPDD HSSYTVPGYM QDLEVEQALT 

       190        200        210        220        230        240 
PALSPCAVSS TLPDWHIPVE VVPDSTSDLY NFQVSPMPST SEATTDEDEE GKLPEDIMKL 

       250        260        270        280        290        300 
LEQSEWQPTN VDGKGYLLNE PGVQPTSVYG DFSCKEEPEI DSPGGDIGLS LQRVFTDLKN 

       310        320 
MDATWLDSLL TPVRLPSIQA IPCAP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a cDNA coding for human IRF-1."
Maruyama M., Fujita T., Taniguchi T.
Nucleic Acids Res. 17:3292-3292(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Regulated expression of a gene encoding a nuclear factor, IRF-1, that specifically binds to IFN-beta gene regulatory elements."
Miyamoto M., Fujita T., Kimura Y., Maruyama M., Harada H., Sudo Y., Miyata T., Taniguchi T.
Cell 54:903-913(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Human interferon regulatory factor 1: intron-exon organization."
Cha Y., Sims S.H., Romine M.F., Kaufmann M., Deisseroth A.B.
DNA Cell Biol. 11:605-611(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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].
Tissue: Pancreas.
[6]"Deletion of IRF-1, mapping to chromosome 5q31.1, in human leukemia and preleukemic myelodysplasia."
Willman C.L., Sever C.E., Pallavicini M.G., Harada H., Tanaka N., Slovak M.L., Yamamoto H., Harada K., Meeker T.C., List A.F., Taniguchi T.
Science 259:968-971(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LEUKEMIAS.
[7]"A role for casein kinase II phosphorylation in the regulation of IRF-1 transcriptional activity."
Lin R., Hiscott J.
Mol. Cell. Biochem. 191:169-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"IRF family of transcription factors as regulators of host defense."
Taniguchi T., Ogasawara K., Takaoka A., Tanaka N.
Annu. Rev. Immunol. 19:623-655(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[9]"Activities of IRF-1."
Kroeger A., Koester M., Schroeder K., Hauser H., Mueller P.P.
J. Interferon Cytokine Res. 22:5-14(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[10]"IRF-1 as a negative regulator of cell proliferation."
Romeo G., Fiorucci G., Chiantore M.V., Percario Z.A., Vannucchi S., Affabris E.
J. Interferon Cytokine Res. 22:39-47(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[11]"Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-regulate gene expression and production of interleukin-7 in human intestinal epithelial cells."
Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R., Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H., Watanabe M.
Mol. Cell. Biol. 24:6298-6310(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53."
Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R., Ball K.L.
Mol. Cell. Biol. 24:10083-10098(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EP300.
[13]"IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors."
Honda K., Taniguchi T.
Nat. Rev. Immunol. 6:644-658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[14]"Central role of interferon regulatory factor-1 (IRF-1) in controlling retinoic acid inducible gene-I (RIG-I) expression."
Su Z.Z., Sarkar D., Emdad L., Barral P.M., Fisher P.B.
J. Cell. Physiol. 213:502-510(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"RNA interference of interferon regulatory factor-1 gene expression in THP-1 cell line leads to Toll-like receptor-4 overexpression/activation as well as up-modulation of annexin-II."
Maratheftis C.I., Giannouli S., Spachidou M.P., Panayotou G., Voulgarelis M.
Neoplasia 9:1012-1020(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Elevated level of SUMOylated IRF-1 in tumor cells interferes with IRF-1-mediated apoptosis."
Park J., Kim K., Lee E.-J., Seo Y.-J., Lim S.-N., Park K., Rho S.B., Lee S.-H., Lee J.-H.
Proc. Natl. Acad. Sci. U.S.A. 104:17028-17033(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-275 AND LYS-299, UBIQUITINATION AT LYS-275 AND LYS-299, FUNCTION, MUTAGENESIS OF LYS-275 AND LYS-299.
[17]"IRF-1 promotes apoptosis in p53-damaged basal-type human mammary epithelial cells: a model for early basal-type mammary carcinogenesis."
Bowie M.L., Ibarra C., Seewalt V.L.
Adv. Exp. Med. Biol. 617:367-374(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"IFN regulatory factor-1 negatively regulates CD4+ CD25+ regulatory T cell differentiation by repressing Foxp3 expression."
Fragale A., Gabriele L., Stellacci E., Borghi P., Perrotti E., Ilari R., Lanciotti A., Remoli A.L., Venditti M., Belardelli F., Battistini A.
J. Immunol. 181:1673-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"Type I interferons and interferon regulatory factors regulate TNF-related apoptosis-inducing ligand (TRAIL) in HIV-1-infected macrophages."
Huang Y., Walstrom A., Zhang L., Zhao Y., Cui M., Ye L., Zheng J.C.
PLoS ONE 4:E5397-E5397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"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.
[21]"IRF-1 transcriptionally upregulates PUMA, which mediates the mitochondrial apoptotic pathway in IRF-1-induced apoptosis in cancer cells."
Gao J., Senthil M., Ren B., Yan J., Xing Q., Yu J., Zhang L., Yim J.H.
Cell Death Differ. 17:699-709(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Human papillomavirus type 16 E5 protein induces expression of beta interferon through interferon regulatory factor 1 in human keratinocytes."
Muto V., Stellacci E., Lamberti A.G., Perrotti E., Carrabba A., Matera G., Sgarbanti M., Battistini A., Liberto M.C., Foca A.
J. Virol. 85:5070-5080(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Interferon regulatory factor 1 (IRF-1) induces p21(WAF1/CIP1) dependent cell cycle arrest and p21(WAF1/CIP1) independent modulation of survivin in cancer cells."
Armstrong M.J., Stang M.T., Liu Y., Gao J., Ren B., Zuckerbraun B.S., Mahidhara R.S., Xing Q., Pizzoferrato E., Yim J.H.
Cancer Lett. 319:56-65(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Interferon regulatory factor 1 transactivates the expression of human DNA polymerase eta in response to the carcinogen N-methyl-N'-nitro-N-nitrosoguanidine."
Qi H., Zhu H., Lou M., Fan Y., Liu H., Shen J., Li Z., Lv X., Shan J., Zhu L., Chin Y.E., Shao J.
J. Biol. Chem. 287:12622-12633(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACETYLATION AT LYS-78, MUTAGENESIS OF LYS-78.
[25]"Functionally inactivating point mutation in the tumor-suppressor IRF-1 gene identified in human gastric cancer."
Nozawa H., Oda E., Ueda S., Tamura G., Maesawa C., Muto T., Taniguchi T., Tanaka N.
Int. J. Cancer 77:522-527(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GASC LEU-8, CHARACTERIZATION OF VARIANT GASC LEU-8.
[26]"Interferon regulatory factor 1 tryptophan 11 to arginine point mutation abolishes DNA binding."
Eason D.D., Shepherd A.T., Blanck G.
Biochim. Biophys. Acta 1446:140-144(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GASC ARG-11.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14454 mRNA. Translation: CAA32624.1.
L05072 Genomic DNA. Translation: AAA36043.1.
BT019756 mRNA. Translation: AAV38561.1.
BC009483 mRNA. Translation: AAH09483.1.
CCDSCCDS4155.1.
PIRB31595.
I52998.
RefSeqNP_002189.1. NM_002198.2.
UniGeneHs.436061.

3D structure databases

ProteinModelPortalP10914.
SMRP10914. Positions 7-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109867. 31 interactions.
DIPDIP-40988N.
IntActP10914. 4 interactions.
MINTMINT-123145.
STRING9606.ENSP00000245414.

PTM databases

PhosphoSiteP10914.

Polymorphism databases

DMDM20178295.

Proteomic databases

PaxDbP10914.
PRIDEP10914.

Protocols and materials databases

DNASU3659.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245414; ENSP00000245414; ENSG00000125347.
ENST00000405885; ENSP00000384406; ENSG00000125347.
GeneID3659.
KEGGhsa:3659.
UCSCuc003kxa.2. human.

Organism-specific databases

CTD3659.
GeneCardsGC05M131817.
H-InvDBHIX0200727.
HGNCHGNC:6116. IRF1.
HPACAB011662.
MIM147575. gene.
613659. phenotype.
neXtProtNX_P10914.
PharmGKBPA29915.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42582.
HOGENOMHOG000037937.
HOVERGENHBG003455.
InParanoidP10914.
KOK09444.
OMACKEEPEV.
OrthoDBEOG72ZCFD.
PhylomeDBP10914.
TreeFamTF328512.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP10914.

Gene expression databases

ArrayExpressP10914.
BgeeP10914.
CleanExHS_IRF1.
GenevestigatorP10914.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR017431. Interferon_reg_fac-1/2.
IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00605. IRF. 1 hit.
[Graphical view]
PIRSFPIRSF038196. IFN_RF1/2. 1 hit.
PRINTSPR00267. INTFRNREGFCT.
SMARTSM00348. IRF. 1 hit.
[Graphical view]
PROSITEPS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiIRF1.
GenomeRNAi3659.
NextBio14311.
PROP10914.
SOURCESearch...

Entry information

Entry nameIRF1_HUMAN
AccessionPrimary (citable) accession number: P10914
Secondary accession number(s): Q96GG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 138 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

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 5

Human chromosome 5: entries, gene names and cross-references to MIM