Protein

Signal transducer and activator of transcription 1-alpha/beta

Gene

STAT1

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus (PubMed:28753426). ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated (PubMed:26479788). It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.7 Publications

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

blood circulation Source: UniProtKB
cellular response to insulin stimulus Source: Ensembl
cellular response to interferon-beta
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 18035482
cellular response to interferon-gamma
Source: UniProtKB
Inferred from direct assayⁱ
- 23386060
cellular response to organic cyclic compound Source: Ensembl
cytokine-mediated signaling pathway Source: Reactome
defense response to virus
Source: UniProtKB
Inferred from direct assayⁱ
- 28753426
interferon-gamma-mediated signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 21268089
interleukin-21-mediated signaling pathway Source: Reactome
interleukin-27-mediated signaling pathway Source: Reactome
interleukin-35-mediated signaling pathway Source: Reactome
interleukin-6-mediated signaling pathway Source: Reactome
JAK-STAT cascade
Source: UniProtKB
Inferred from direct assayⁱ
- 22002246
macrophage derived foam cell differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 26504087
metanephric mesenchymal cell differentiation Source: UniProtKB
metanephric mesenchymal cell proliferation involved in metanephros development Source: UniProtKB
negative regulation by virus of viral protein levels in host cell
Source: AgBase
Inferred from mutant phenotypeⁱ
- 15825084
negative regulation of angiogenesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16585190
negative regulation of endothelial cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16585190
negative regulation of I-kappaB kinase/NF-kappaB signaling
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10848577
negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis Source: UniProtKB
negative regulation of metanephric nephron tubule epithelial cell differentiation Source: UniProtKB
negative regulation of transcription by RNA polymerase II Source: UniProtKB
positive regulation of defense response to virus by host
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 26479788
positive regulation of erythrocyte differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 28283061
positive regulation of interferon-alpha production
Source: UniProtKB
Inferred from direct assayⁱ
- 28753426
positive regulation of mesenchymal cell proliferation Source: UniProtKB
positive regulation of nitric-oxide synthase biosynthetic process Source: Ensembl
positive regulation of smooth muscle cell proliferation Source: UniProtKB
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 10973496
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 10820245
positive regulation of transcription of Notch receptor target Source: Reactome
regulation of apoptotic process
Source: UniProtKB
Traceable author statementⁱ
- 12108949
regulation of interferon-gamma-mediated signaling pathway Source: Reactome
renal tubule development
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20861313
response to cAMP Source: UniProtKB
response to cytokine Source: UniProtKB
response to hydrogen peroxide Source: Ensembl
response to interferon-beta
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 24882218
response to mechanical stimulus Source: Ensembl
response to nutrient Source: Ensembl
response to peptide hormone Source: UniProtKB
transcription, DNA-templated Source: UniProtKB-KW
tumor necrosis factor-mediated signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 10848577
type I interferon signaling pathway
Source: UniProtKB
Inferred from direct assayⁱ
- 23386060
viral process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	Antiviral defense, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1059683 Interleukin-6 signaling R-HSA-1169408 ISG15 antiviral mechanism R-HSA-1433557 Signaling by SCF-KIT R-HSA-1839117 Signaling by cytosolic FGFR1 fusion mutants R-HSA-186763 Downstream signal transduction R-HSA-6785807 Interleukin-4 and 13 signaling R-HSA-877300 Interferon gamma signaling R-HSA-877312 Regulation of IFNG signaling R-HSA-8854691 Interleukin-20 family signaling R-HSA-8939902 Regulation of RUNX2 expression and activity R-HSA-8984722 Interleukin-35 Signalling R-HSA-9013508 NOTCH3 Intracellular Domain Regulates Transcription R-HSA-9020956 Interleukin-27 signaling R-HSA-9020958 Interleukin-21 signaling R-HSA-909733 Interferon alpha/beta signaling R-HSA-912694 Regulation of IFNA signaling R-HSA-982772 Growth hormone receptor signaling
SignaLinkⁱ	P42224
SIGNORⁱ	P42224

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Signal transducer and activator of transcription 1-alpha/beta Alternative name(s): Transcription factor ISGF-3 components p91/p84
Gene namesⁱ	Name:STAT1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000115415.18
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11362 STAT1
MIMⁱ	600555 gene
neXtProtⁱ	NX_P42224

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Immunodeficiency 31B (IMD31B)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by susceptibility to severe mycobacterial and viral infections. Affected individuals can develop disseminated infections and die of viral illness.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_065815	201	K → N in IMD31B; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%. 1 PublicationCorresponds to variant dbSNP:rs587776870EnsemblClinVar.	1
Natural variantⁱVAR_018265	600	L → P in IMD31B; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 PublicationCorresponds to variant dbSNP:rs137852678EnsemblClinVar.	1
Natural variantⁱVAR_075500	701	Y → C in IMD31B; disrupts transactivation activity in response to IFNG. 1 Publication	1

Immunodeficiency 31A (IMD31A)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Mendelian susceptibility to mycobacterial disease, a rare condition caused by impairment of interferon-gamma mediated immunity. It is characterized by predisposition to illness caused by moderately virulent mycobacterial species, such as Bacillus Calmette-Guerin (BCG) vaccine, environmental non-tuberculous mycobacteria, and by the more virulent Mycobacterium tuberculosis. Other microorganisms rarely cause severe clinical disease in individuals with susceptibility to mycobacterial infections, with the exception of Salmonella which infects less than 50% of these individuals. Clinical outcome severity depends on the degree of impairment of interferon-gamma mediated immunity. Some patients die of overwhelming mycobacterial disease with lepromatous-like lesions in early childhood, whereas others develop, later in life, disseminated but curable infections with tuberculoid granulomas. IMD31A has low penetrance, and affected individuals have relatively mild disease and good prognosis. IMD31A confers a predisposition to mycobacterial infections only, with no increased susceptibility to viral infections.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_065816	320	E → Q in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852680EnsemblClinVar.	1
Natural variantⁱVAR_065817	463	Q → H in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852679EnsemblClinVar.	1
Natural variantⁱVAR_068713	637	K → E in IMD31A; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 PublicationCorresponds to variant dbSNP:rs587777705EnsemblClinVar.	1
Natural variantⁱVAR_068714	673	K → R in IMD31A; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 PublicationCorresponds to variant dbSNP:rs587777704EnsemblClinVar.	1
Natural variantⁱVAR_018266	706	L → S in IMD31A; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein. 2 PublicationsCorresponds to variant dbSNP:rs137852677EnsemblClinVar.	1

Immunodeficiency 31C (IMD31C)5 Publications

The disease is caused by mutations affecting the gene represented in this entry. STAT1 mutations in patients with autosomal dominant candidiasis lead to defective responses of type 1 and type 17 helper T-cells, characterized by reduced production of interferon-alpha, interleukin-17, and interleukin-22. These cytokines are crucial for the antifungal defense of skin and mucosa (PubMed:21714643).1 Publication

Disease descriptionA primary immunodeficiency disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_065934	165	D → G in IMD31C; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs387906764EnsemblClinVar.	1
Natural variantⁱVAR_065935	165	D → H in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906767EnsemblClinVar.	1
Natural variantⁱVAR_065936	170	Y → N in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906766EnsemblClinVar.	1
Natural variantⁱVAR_065937	174	C → R in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906763EnsemblClinVar.	1
Natural variantⁱVAR_075494	179	N → K in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777628EnsemblClinVar.	1
Natural variantⁱVAR_065938	202	M → I in IMD31C. 1 Publication	1
Natural variantⁱVAR_065939	202	M → V in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906762EnsemblClinVar.	1
Natural variantⁱVAR_065940	267	A → V in IMD31C. 2 PublicationsCorresponds to variant dbSNP:rs387906759EnsemblClinVar.	1
Natural variantⁱVAR_065941	271	Q → P in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906768EnsemblClinVar.	1
Natural variantⁱVAR_065942	274	R → Q in IMD31C; gain of function; increases STAT1 phosphorylation due to impaired nuclear dephosphorylation; increases transactivation activity in response to IFNG. 2 PublicationsCorresponds to variant dbSNP:rs387906760EnsemblClinVar.	1
Natural variantⁱVAR_065943	274	R → W in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation. 3 PublicationsCorresponds to variant dbSNP:rs387906758EnsemblClinVar.	1
Natural variantⁱVAR_075495	278	K → E in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. 1 PublicationCorresponds to variant dbSNP:rs863223398EnsemblClinVar.	1
Natural variantⁱVAR_075496	285	Q → R in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777629EnsemblClinVar.	1
Natural variantⁱVAR_065944	286	K → I in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906761EnsemblClinVar.	1
Natural variantⁱVAR_065945	288	T → A in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906765EnsemblClinVar.	1
Natural variantⁱVAR_075497	298	K → N in IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation. 1 Publication	1
Natural variantⁱVAR_075498	384	G → D in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. 1 PublicationCorresponds to variant dbSNP:rs796065052EnsemblClinVar.	1
Natural variantⁱVAR_075499	385	T → M in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs587777630EnsemblClinVar.	1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	110	K → R: Sumoylated. 1 Publication	1
Mutagenesisⁱ	114	K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	1
Mutagenesisⁱ	175	K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	1
Mutagenesisⁱ	296	K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	1
Mutagenesisⁱ	366	K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	1
Mutagenesisⁱ	525	K → A: Strongly reduced IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. Does not affect ability to homodimerize. 1 Publication	1
Mutagenesisⁱ	636 – 637	KK → AA: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	2
Mutagenesisⁱ	656 – 658	AEN → CEC: Enhances STAT1 nuclear translocation and interferon (IFN)-stimulated gene (ISG) expression in response to IFN-beta stimulation. Reduces viral load in infected cultured cells. 1 Publication	3
Mutagenesisⁱ	657	E → Q: Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-705. 1 Publication	1
Mutagenesisⁱ	665	K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication	1
Mutagenesisⁱ	701	Y → E: Not phosphorylated at S-708 upon IFNB induction. 2 Publications	1
Mutagenesisⁱ	701	Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. 2 Publications	1
Mutagenesisⁱ	703	K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. 2 Publications	1
Mutagenesisⁱ	705	E → Q: Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-657. 1 Publication	1
Mutagenesisⁱ	708	S → A: Phosphorylated at Y-701 upon IFNB induction. 1 Publication	1
Mutagenesisⁱ	708	S → D: Not phosphorylated at Y-701 upon IFNB induction. 1 Publication	1
Mutagenesisⁱ	727	S → A: Decreased transcriptional activation. No effect on basal sumoylation. No enhancement of sumoylation on MAPK stimulation. No PRKCD-induced apoptosis. Upon IFNB induction, phosphorylated at Y-701 but not at S-708. 3 Publications	1
Mutagenesisⁱ	727	S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. 3 Publications	1
Mutagenesisⁱ	727	S → E: No change in enhancement of MAPK-induced sumoylation. 3 Publications	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6772
MalaCards human disease database More...MalaCardsⁱ	STAT1
MIMⁱ	613796 phenotype 614162 phenotype 614892 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000115415
Orphanetⁱ	391487 Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome 1334 Chronic mucocutaneous candidosis 319595 Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency 391311 Susceptibility to viral and mycobacterial infections
PharmGKBⁱ	PA36183

Chemistry databases

ChEMBLⁱ	CHEMBL6101

ChEMBLⁱ

CHEMBL6101

Polymorphism and mutation databases

BioMutaⁱ	STAT1
DMDMⁱ	2507413

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		RemovedCombined sources
ChainⁱPRO_0000182410	2 – 750	Signal transducer and activator of transcription 1-alpha/betaAdd BLAST		749

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserineCombined sources	1
Modified residueⁱ	114	N6-methyllysine1 Publication	1
Modified residueⁱ	175	N6-methyllysine1 Publication	1
Modified residueⁱ	296	N6-methyllysine1 Publication	1
Modified residueⁱ	366	N6-methyllysine1 Publication	1
Modified residueⁱ	525	N6-methyllysine1 Publication	1
Modified residueⁱ	637	N6-methyllysine1 Publication	1
Modified residueⁱ	657	ADP-ribosyl glutamic acid; by PARP141 Publication	1
Modified residueⁱ	665	N6-methyllysine1 Publication	1
Modified residueⁱ	701	Phosphotyrosine; by JAK1, JAK2 or TYK28 Publications	1
Cross-linkⁱ	703	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linkⁱ	703	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residueⁱ	705	ADP-ribosyl glutamic acid; by PARP141 Publication	1
Modified residueⁱ	708	Phosphoserine; by IKKE1 Publication	1
Modified residueⁱ	727	Phosphoserine; by MAPK14Combined sources6 Publications	1
Modified residueⁱ	745	Phosphoserine; by IKKEBy similarity	1

Post-translational modificationⁱ

Phosphorylated on tyrosine and serine residues in response to a variety of cytokines/growth hormones including IFN-alpha, IFN-gamma, PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Upon EGF stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1, JAK2 or TYK2 promotes dimerization and subsequent translocation to the nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes sumoylation though increasing interaction with PIAS. Phosphorylation on Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents. Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most likely this is catalyzed by a SRC family kinase. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates interferon-mediated signaling. Upon viral infection or IFN induction, phosphorylation on Ser-708 occurs much later than phosphorylation on Tyr-701 and is required for the binding of ISGF3 on the ISREs of a subset of IFN-stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-708 are mutually exclusive, phosphorylation at Ser-708 requires previous dephosphorylation of Tyr-701.10 Publications

Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by IFN-gamma-induced phosphorylation on Ser-727, and by interaction with PIAS proteins. Enhances the transactivation activity.5 Publications

ISGylated.1 Publication

Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-ribosylation prevents phosphorylation at Tyr-701.1 Publication

Monomethylated at Lys-525 by SETD2; monomethylation is necessary for phosphorylation at Tyr-701, translocation into the nucleus and activation of the antiviral defense.1 Publication

Keywords - PTMⁱ

Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P42224
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P42224
PaxDbⁱ	P42224
PeptideAtlas More...PeptideAtlasⁱ	P42224
PRIDEⁱ	P42224
ProteomicsDBⁱ	55491 55492 [P42224-2]

PTM databases

CarbonylDBⁱ	P42224
iPTMnetⁱ	P42224
PhosphoSitePlusⁱ	P42224
SwissPalmⁱ	P42224

Miscellaneous databases

PMAP-CutDBⁱ	P42224

PMAP-CutDBⁱ

P42224

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000115415
CleanExⁱ	HS_STAT1
ExpressionAtlasⁱ	P42224 baseline and differential
Genevisibleⁱ	P42224 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB004049 HPA000931 HPA000982

HPAⁱ

CAB004049
HPA000931
HPA000982

Interactionⁱ

Subunit structureⁱ

Isoform alpha homodimerizes upon IFN-gamma induced phosphorylation (PubMed:8605877, PubMed:28753426). Heterodimer with STAT2 upon IFN-alpha/beta induced phosphorylation (PubMed:8605877). The heterodimer STAT1:STAT2 forms the interferon-stimulated gene factor 3 complex (ISGF3) with IRF9 (By similarity). Interacts (phosphorylated at Ser-727) with PIAS1 (dimethylated on arginine); the interaction results in release of STAT1 from its target gene (PubMed:9724754, PubMed:17897103, PubMed:19136629). Interacts with IFNAR1; the interaction requires the phosphorylation of IFNAR1 at 'Tyr-466' (PubMed:9121453). Interacts with IFNAR2 (PubMed:9121453). Found in a complex with NMI and CREBBP/CBP (PubMed:9989503). Interacts with NMI which is required for CREBBP/CBP recruitment to the complex (PubMed:9989503). Interacts with PTK2/FAK1 (PubMed:11278462). Interacts with SRC (By similarity). Interacts with ERBB4 (phosphorylated) (PubMed:18721752). Interacts with PARP9 and DTX3L independently of IFN-beta or IFN-gamma-mediated STAT1 'Tyr-701' phosphorylation (PubMed:26479788). Interacts with histone acetyltransferase EP300/p300 in response to INF-gamma stimulation (PubMed:26479788). Interacts with OTOP1 (By similarity).By similarity10 Publications

(Microbial infection) Interacts with Sendai virus C', C, Y1 and Y2 proteins, preventing activation of ISRE and GAS promoter.

(Microbial infection) Interacts with Nipah virus P, V and W proteins preventing activation of ISRE and GAS promoter.

(Microbial infection) Interacts with Rabies virus phosphoprotein preventing activation of ISRE and GAS promoter.2 Publications

(Microbial infection) Interacts with HCV core protein; the interaction results in STAT1 degradation.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-1057697,EBI-1057697
	P03255-1	2	EBI-1057697,EBI-6692439	From a different organism.
	P03255-2	2	EBI-1057697,EBI-6859460	From a different organism.
	P06498	2	EBI-15711971,EBI-16085959	From Human adenovirus C serotype 5.
	P26664	5	EBI-1057697,EBI-6941357	From Hepatitis C virus genotype 1a (isolate 1).
	P27958	2	EBI-1057697,EBI-6377335	From Hepatitis C virus genotype 1a (isolate H).
DDB1	Q16531	2	EBI-1057697,EBI-350322
DDX58	O95786	4	EBI-1057697,EBI-995350
E2F1	Q01094	2	EBI-1057697,EBI-448924
EGFR	P00533	6	EBI-1057697,EBI-297353
EIF1AD	Q8N9N8	4	EBI-1057697,EBI-750700
ERBB2	P04626	3	EBI-1057697,EBI-641062
FOS	P01100	6	EBI-1057697,EBI-852851
H1L	P07239	3	EBI-1057697,EBI-7789600	From Vaccinia virus (strain Western Reserve).
IFNAR1	P17181	2	EBI-1057697,EBI-1547250
IFNAR2	P48551	2	EBI-1057697,EBI-958408
IFNGR1	P15260	4	EBI-1057697,EBI-1030755
KDM3A	Q9Y4C1	8	EBI-15711971,EBI-2515339
MAVS	Q7Z434	3	EBI-1057697,EBI-995373
OTUD4	Q01804	3	EBI-1057697,EBI-1054396
RXRA	P19793	2	EBI-1057697,EBI-78598
STAT2	P52630	15	EBI-1057697,EBI-1546963
STAT3	P40763	4	EBI-1057697,EBI-518675
UL47	Q4VW77	2	EBI-1057697,EBI-11499224	From Bovine alphaherpesvirus 1.

Show more details

GO - Molecular functionⁱ

cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
CCR5 chemokine receptor binding Source: Ensembl
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 22002246
- 26479788
histone acetyltransferase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 26479788
histone binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 26479788
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
nuclear hormone receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 26504087
protein homodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 28753426
- 9630226
protein phosphatase 2A binding Source: Ensembl
repressing transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 23386060
tumor necrosis factor receptor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 10848577
ubiquitin-like protein ligase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 26479788

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	112649, 163 interactors
CORUMⁱ	P42224
Database of interacting proteins More...DIPⁱ	DIP-46140N
IntActⁱ	P42224, 102 interactors
Molecular INTeraction database More...MINTⁱ	P42224
STRINGⁱ	9606.ENSP00000354394

Chemistry databases

BindingDBⁱ	P42224

BindingDBⁱ

P42224

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 7	Combined sources	5
Helixⁱ	12 – 21	Combined sources	10
Beta strandⁱ	23 – 26	Combined sources	4
Helixⁱ	28 – 33	Combined sources	6
Helixⁱ	35 – 40	Combined sources	6
Helixⁱ	43 – 46	Combined sources	4
Helixⁱ	50 – 73	Combined sources	24
Helixⁱ	77 – 94	Combined sources	18
Helixⁱ	99 – 120	Combined sources	22
Helixⁱ	121 – 125	Combined sources	5
Helixⁱ	137 – 179	Combined sources	43
Helixⁱ	189 – 192	Combined sources	4
Helixⁱ	193 – 195	Combined sources	3
Helixⁱ	198 – 247	Combined sources	50
Helixⁱ	257 – 286	Combined sources	30
Helixⁱ	293 – 316	Combined sources	24
Beta strandⁱ	317 – 321	Combined sources	5
Beta strandⁱ	334 – 336	Combined sources	3
Beta strandⁱ	339 – 347	Combined sources	9
Helixⁱ	352 – 354	Combined sources	3
Turnⁱ	355 – 357	Combined sources	3
Beta strandⁱ	359 – 365	Combined sources	7
Helixⁱ	370 – 373	Combined sources	4
Beta strandⁱ	374 – 376	Combined sources	3
Beta strandⁱ	380 – 382	Combined sources	3
Beta strandⁱ	386 – 389	Combined sources	4
Beta strandⁱ	391 – 395	Combined sources	5
Turnⁱ	396 – 398	Combined sources	3
Beta strandⁱ	399 – 408	Combined sources	10
Beta strandⁱ	421 – 425	Combined sources	5
Beta strandⁱ	433 – 441	Combined sources	9
Beta strandⁱ	444 – 451	Combined sources	8
Beta strandⁱ	455 – 460	Combined sources	6
Helixⁱ	461 – 463	Combined sources	3
Helixⁱ	464 – 477	Combined sources	14
Helixⁱ	486 – 488	Combined sources	3
Helixⁱ	495 – 509	Combined sources	15
Helixⁱ	516 – 526	Combined sources	11
Helixⁱ	539 – 543	Combined sources	5
Beta strandⁱ	550 – 552	Combined sources	3
Helixⁱ	554 – 568	Combined sources	15
Helixⁱ	570 – 574	Combined sources	5
Helixⁱ	584 – 590	Combined sources	7
Turnⁱ	591 – 593	Combined sources	3
Beta strandⁱ	601 – 603	Combined sources	3
Beta strandⁱ	612 – 616	Combined sources	5
Beta strandⁱ	621 – 624	Combined sources	4
Beta strandⁱ	627 – 631	Combined sources	5
Helixⁱ	636 – 640	Combined sources	5
Helixⁱ	644 – 649	Combined sources	6
Beta strandⁱ	657 – 659	Combined sources	3
Helixⁱ	673 – 677	Combined sources	5
Turnⁱ	678 – 680	Combined sources	3
Helixⁱ	728 – 738	Combined sources	11
Turnⁱ	739 – 742	Combined sources	4
Helixⁱ	743 – 745	Combined sources	3
Turnⁱ	746 – 748	Combined sources	3

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00962
ProteinModelPortalⁱ	P42224
SMRⁱ	P42224
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P42224

EvolutionaryTraceⁱ

P42224

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	573 – 670	SH2PROSITE-ProRule annotationAdd BLAST		98

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	136 – 317	1 PublicationAdd BLAST		182

Sequence similaritiesⁱ

Belongs to the transcription factor STAT family.Curated

Keywords - Domainⁱ

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGⁱ	KOG3667 Eukaryota ENOG410XPN8 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000119236
HOVERGENⁱ	HBG055669
InParanoidⁱ	P42224
KEGG Orthology (KO) More...KOⁱ	K11220
OMAⁱ	WYNMLTT
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03O3
PhylomeDBⁱ	P42224
TreeFamⁱ	TF318648

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd10372 SH2_STAT1, 1 hit
Gene3Dⁱ	1.10.532.10, 1 hit 1.10.8.1200, 1 hit 2.60.40.630, 1 hit 3.30.505.10, 1 hit
InterProⁱ	View protein in InterPro IPR008967 p53-like_TF_DNA-bd IPR000980 SH2 IPR036860 SH2_dom_sf IPR001217 STAT IPR038295 STAT1_C_sf IPR035859 STAT1_SH2 IPR022752 STAT1_TAZ2-bd_C IPR036535 STAT_N_sf IPR013800 STAT_TF_alpha IPR015988 STAT_TF_coiled-coil IPR013801 STAT_TF_DNA-bd IPR012345 STAT_TF_DNA-bd_N IPR013799 STAT_TF_prot_interaction
PANTHERⁱ	PTHR11801 PTHR11801, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00017 SH2, 1 hit PF12162 STAT1_TAZ2bind, 1 hit PF01017 STAT_alpha, 1 hit PF02864 STAT_bind, 1 hit PF02865 STAT_int, 1 hit
SMARTⁱ	View protein in SMART SM00964 STAT_int, 1 hit
SUPFAMⁱ	SSF47655 SSF47655, 1 hit SSF48092 SSF48092, 1 hit SSF49417 SSF49417, 1 hit SSF55550 SSF55550, 1 hit
PROSITEⁱ	View protein in PROSITE PS50001 SH2, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform Alpha (identifier: P42224-1) [UniParc]FASTA Add to basket

Also known as: p91

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
MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV 
        60         70         80         90        100
SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ 
       110        120        130        140        150
MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK 
       160        170        180        190        200
DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK 
       210        220        230        240        250
KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG 
       260        270        280        290        300
PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV 
       310        320        330        340        350
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK 
       360        370        380        390        400
LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL 
       410        420        430        440        450
AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET 
       460        470        480        490        500
TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE 
       510        520        530        540        550
VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK 
       560        570        580        590        600
NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL 
       610        620        630        640        650
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN 
       660        670        680        690        700
YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG 
       710        720        730        740        750
YIKTELISVS EVHPSRLQTT DNLLPMSPEE FDEVSRIVGS VEFDSMMNTV

Length:750

Mass (Da):87,335

Last modified:November 1, 1997 - v2

Checksum:ⁱ054A813522364BA6

Isoform Beta (identifier: P42224-2) [UniParc]FASTA Add to basket

Also known as: p84

The sequence of this isoform differs from the canonical sequence as follows:
713-750: Missing.

« Hide

        10         20         30         40         50
MSQWYELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAANDV 
        60         70         80         90        100
SFATIRFHDL LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPIQ 
       110        120        130        140        150
MSMIIYSCLK EERKILENAQ RFNQAQSGNI QSTVMLDKQK ELDSKVRNVK 
       160        170        180        190        200
DKVMCIEHEI KSLEDLQDEY DFKCKTLQNR EHETNGVAKS DQKQEQLLLK 
       210        220        230        240        250
KMYLMLDNKR KEVVHKIIEL LNVTELTQNA LINDELVEWK RRQQSACIGG 
       260        270        280        290        300
PPNACLDQLQ NWFTIVAESL QQVRQQLKKL EELEQKYTYE HDPITKNKQV 
       310        320        330        340        350
LWDRTFSLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKLRLLVK 
       360        370        380        390        400
LQELNYNLKV KVLFDKDVNE RNTVKGFRKF NILGTHTKVM NMEESTNGSL 
       410        420        430        440        450
AAEFRHLQLK EQKNAGTRTN EGPLIVTEEL HSLSFETQLC QPGLVIDLET 
       460        470        480        490        500
TSLPVVVISN VSQLPSGWAS ILWYNMLVAE PRNLSFFLTP PCARWAQLSE 
       510        520        530        540        550
VLSWQFSSVT KRGLNVDQLN MLGEKLLGPN ASPDGLIPWT RFCKENINDK 
       560        570        580        590        600
NFPFWLWIES ILELIKKHLL PLWNDGCIMG FISKERERAL LKDQQPGTFL 
       610        620        630        640        650
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN 
       660        670        680        690        700
YKVMAAENIP ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDGPKGTG 
       710 
YIKTELISVS EV

Show »

Length:712

Mass (Da):83,043

Checksum:ⁱ31408601223700BB

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	46	A → T in ADA59516 (Ref. 2) Curated	1
Sequence conflictⁱ	307	S → G in BAF85293 (PubMed:14702039).Curated	1
Sequence conflictⁱ	718	Q → R in CAH18430 (PubMed:17974005).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_034521	30	I → T. Corresponds to variant dbSNP:rs34255470Ensembl.	1
Natural variantⁱVAR_065934	165	D → G in IMD31C; gain of function mutation associated with increased STAT1 phosphorylation due to impaired nuclear dephosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs387906764EnsemblClinVar.	1
Natural variantⁱVAR_065935	165	D → H in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906767EnsemblClinVar.	1
Natural variantⁱVAR_065936	170	Y → N in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906766EnsemblClinVar.	1
Natural variantⁱVAR_065937	174	C → R in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906763EnsemblClinVar.	1
Natural variantⁱVAR_075494	179	N → K in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777628EnsemblClinVar.	1
Natural variantⁱVAR_065815	201	K → N in IMD31B; not deleterious in terms of most STAT1 functions; causes abnormal splicing out of exon 8 from most mRNAs thereby decreasing protein levels by approximately 70%. 1 PublicationCorresponds to variant dbSNP:rs587776870EnsemblClinVar.	1
Natural variantⁱVAR_065938	202	M → I in IMD31C. 1 Publication	1
Natural variantⁱVAR_065939	202	M → V in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906762EnsemblClinVar.	1
Natural variantⁱVAR_065940	267	A → V in IMD31C. 2 PublicationsCorresponds to variant dbSNP:rs387906759EnsemblClinVar.	1
Natural variantⁱVAR_065941	271	Q → P in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906768EnsemblClinVar.	1
Natural variantⁱVAR_065942	274	R → Q in IMD31C; gain of function; increases STAT1 phosphorylation due to impaired nuclear dephosphorylation; increases transactivation activity in response to IFNG. 2 PublicationsCorresponds to variant dbSNP:rs387906760EnsemblClinVar.	1
Natural variantⁱVAR_065943	274	R → W in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation. 3 PublicationsCorresponds to variant dbSNP:rs387906758EnsemblClinVar.	1
Natural variantⁱVAR_075495	278	K → E in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. 1 PublicationCorresponds to variant dbSNP:rs863223398EnsemblClinVar.	1
Natural variantⁱVAR_075496	285	Q → R in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777629EnsemblClinVar.	1
Natural variantⁱVAR_065944	286	K → I in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906761EnsemblClinVar.	1
Natural variantⁱVAR_065945	288	T → A in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906765EnsemblClinVar.	1
Natural variantⁱVAR_075497	298	K → N in IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation. 1 Publication	1
Natural variantⁱVAR_065816	320	E → Q in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852680EnsemblClinVar.	1
Natural variantⁱVAR_075498	384	G → D in IMD31C; gain of function; increases phosphorylation in response to IFNG and IFNA due to a loss of dephosphorylation. 1 PublicationCorresponds to variant dbSNP:rs796065052EnsemblClinVar.	1
Natural variantⁱVAR_075499	385	T → M in IMD31C; gain of function; increases phosphorylation in response to IFNG, IFNA and IL27 due to a loss of dephosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs587777630EnsemblClinVar.	1
Natural variantⁱVAR_065817	463	Q → H in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852679EnsemblClinVar.	1
Natural variantⁱVAR_036001	491	P → A in a breast cancer sample; somatic mutation. 1 Publication	1
Natural variantⁱVAR_018265	600	L → P in IMD31B; found in an infant who died of a viral-like illness associated with complete STAT1 deficiency. 1 PublicationCorresponds to variant dbSNP:rs137852678EnsemblClinVar.	1
Natural variantⁱVAR_068713	637	K → E in IMD31A; affects both phosphorylation and DNA-binding activity; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 PublicationCorresponds to variant dbSNP:rs587777705EnsemblClinVar.	1
Natural variantⁱVAR_068714	673	K → R in IMD31A; impairs tyrosine phosphorylation; results in impaired STAT1-mediated cellular response to IFN-gamma and interleukin-27. 1 PublicationCorresponds to variant dbSNP:rs587777704EnsemblClinVar.	1
Natural variantⁱVAR_075500	701	Y → C in IMD31B; disrupts transactivation activity in response to IFNG. 1 Publication	1
Natural variantⁱVAR_018266	706	L → S in IMD31A; loss of GAF and ISGF3 activation; impairs the nuclear accumulation of GAF but not of ISGF3 in heterozygous cells stimulated by IFNs; affects phosphorylation of the protein. 2 PublicationsCorresponds to variant dbSNP:rs137852677EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_006282	713 – 750	Missing in isoform Beta. 2 PublicationsAdd BLAST		38

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M97935 mRNA Translation: AAB64012.1 M97936 mRNA No translation available. GU211347 mRNA Translation: ADA59516.1 AY865620 Genomic DNA Translation: AAW56072.1 AK292604 mRNA Translation: BAF85293.1 AK315002 mRNA Translation: BAG37497.1 CR749636 mRNA Translation: CAH18430.1 BT007241 mRNA Translation: AAP35905.1 AC067945 Genomic DNA Translation: AAY24183.1 CH471058 Genomic DNA Translation: EAX10850.1 CH471058 Genomic DNA Translation: EAX10851.1 CH471058 Genomic DNA Translation: EAX10852.1 CH471058 Genomic DNA Translation: EAX10855.1 BC002704 mRNA Translation: AAH02704.1 U18662 Genomic DNA No translation available. U18663 Genomic DNA No translation available. U18664 Genomic DNA No translation available. U18665 Genomic DNA No translation available. U18666 Genomic DNA No translation available. U18667 Genomic DNA No translation available. U18668 Genomic DNA No translation available. U18669 Genomic DNA No translation available. U18670 Genomic DNA No translation available.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2309.1 [P42224-1] CCDS42793.1 [P42224-2]
PIRⁱ	A46159
NCBI Reference Sequences More...RefSeqⁱ	NP_009330.1, NM_007315.3 [P42224-1] NP_644671.1, NM_139266.2 [P42224-2] XP_006712781.1, XM_006712718.1 [P42224-1]
UniGeneⁱ	Hs.642990 Hs.743244

Genome annotation databases

Ensemblⁱ	ENST00000361099; ENSP00000354394; ENSG00000115415 [P42224-1] ENST00000392322; ENSP00000376136; ENSG00000115415 [P42224-2] ENST00000409465; ENSP00000386244; ENSG00000115415 [P42224-1]
GeneIDⁱ	6772
KEGGⁱ	hsa:6772
UCSC genome browser More...UCSCⁱ	uc002usj.3 human [P42224-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P42224 (STAT1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Signal transducer and activator of transcription 1-alpha/beta

STAT1

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Other locations

Cytosol

Nucleus

Other locations

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

Miscellaneous databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Coiled coil

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Web resourcesⁱ