P10914 (IRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon regulatory factor 1
Short name=IRF-1

Gene names

Name:

IRF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Antiviral defense Immunity Innate immunity Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Disease	Disease mutation Tumor suppressor
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CD8-positive, alpha-beta T cell differentiation Inferred from electronic annotation. Source: Compara 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 defense response to virus Inferred from direct assay Ref.22. Source: UniProtKB induction of apoptosis Inferred from direct assay Ref.21. 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-dependent 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: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.23. 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 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-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear chromatin Inferred from direct assay PubMed 18035482. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 18035482. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 325	325	Interferon regulatory factor 1		PRO_0000154545
Regions
	DNA binding	5 – 113	109	IRF tryptophan pentad repeat
Amino acid modifications
	Modified residue	78	1	N6-acetyllysine Ref.24
	Cross-link	275		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16
	Cross-link	299		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16
Natural variations
	Natural variant	8	1	M → L in GASC; somatic mutation; produces a protein with markedly reduced transcriptional activity but unaltered DNA-binding activity. Ref.25		VAR_065134
	Natural variant	11	1	W → R in GASC; the mutation abolishes DNA binding and transactivating activities. Ref.26		VAR_065135
Experimental info
	Mutagenesis	78	1	K → R: Loss of acetylation. Partial loss of DNA-binding and transcriptional activity. Ref.24
	Mutagenesis	275	1	K → 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
	Mutagenesis	299	1	K → 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 conflict	5	1	R → W no nucleotide entry Ref.1
	Sequence conflict	5	1	R → W no nucleotide entry Ref.2
	Sequence conflict	34 – 35	2	FQ → LE no nucleotide entry Ref.1
	Sequence conflict	34 – 35	2	FQ → LE no nucleotide entry Ref.2
	Sequence conflict	220	1	T → I no nucleotide entry Ref.1
	Sequence conflict	220	1	T → I no nucleotide entry Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10914 [UniParc]. Last modified April 16, 2002. Version 2. Checksum: 2E06245A212D1541	FASTA	325	36,502
	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

References

	« Hide 'large scale' referencesShow '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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.
IPI	IPI00023600.
PIR	B31595. I52998.
RefSeq	NP_002189.1. NM_002198.2.
UniGene	Hs.436061.
3D structure databases
ProteinModelPortal	P10914.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40988N.
IntAct	P10914. 2 interactions.
MINT	MINT-123145.
STRING	9606.ENSP00000245414.
PTM databases
PhosphoSite	P10914.
Polymorphism databases
DMDM	20178295.
Proteomic databases
PaxDb	P10914.
PRIDE	P10914.
Protocols and materials databases
DNASU	3659.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000245414; ENSP00000245414; ENSG00000125347. ENST00000405885; ENSP00000384406; ENSG00000125347.
GeneID	3659.
KEGG	hsa:3659.
UCSC	uc003kxa.2. human.
Organism-specific databases
CTD	3659.
GeneCards	GC05M131817.
H-InvDB	HIX0200727.
HGNC	HGNC:6116. IRF1.
HPA	CAB011662.
MIM	147575. gene. 613659. phenotype.
neXtProt	NX_P10914.
PharmGKB	PA29915.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42582.
HOGENOM	HOG000037937.
HOVERGEN	HBG003455.
InParanoid	P10914.
KO	K09444.
OMA	CKEEPEV.
OrthoDB	EOG4JWVDV.
PhylomeDB	P10914.
Enzyme and pathway databases
Pathway_Interaction_DB	ifngpathway. IFN-gamma pathway. il12_stat4pathway. IL12 signaling mediated by STAT4. il6_7pathway. IL6-mediated signaling events. telomerasepathway. Regulation of Telomerase.
Reactome	REACT_604. Hemostasis. REACT_6900. Immune System.
SignaLink	P10914.
Gene expression databases
ArrayExpress	P10914.
Bgee	P10914.
CleanEx	HS_IRF1.
Genevestigator	P10914.
GermOnline	ENSG00000125347. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 1 hit.
InterPro	IPR017431. Interferon_reg_fac-1/2. IPR019817. Interferon_reg_fac_CS. IPR001346. Interferon_reg_fact_DNA-bd_dom. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00605. IRF. 1 hit. [Graphical view]
PIRSF	PIRSF038196. IFN_RF1/2. 1 hit.
PRINTS	PR00267. INTFRNREGFCT.
SMART	SM00348. IRF. 1 hit. [Graphical view]
PROSITE	PS00601. IRF_1. 1 hit. PS51507. IRF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	3659.
NextBio	14311.
SOURCE	Search...

Entry information

Entry name

IRF1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.