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UniProtKB - P42224 (STAT1_HUMAN)

Entry version 240 (12 Aug 2020)
Sequence version 2 (01 Nov 1997)
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Protein

Signal transducer and activator of transcription 1-alpha/beta

Gene

STAT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

Caution

Has been shown to be mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14 which prevents phosphorylation at Tyr-701 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question (PubMed:29858569). It has been suggested that the lack of phosphorylation may be due to sumoylation of Lys-703 (PubMed:29858569).1 Publication1 Publication

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P42224

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1059683, Interleukin-6 signaling [P42224-1]
R-HSA-1169408, ISG15 antiviral mechanism
R-HSA-1433557, Signaling by SCF-KIT [P42224-1]
R-HSA-1839117, Signaling by cytosolic FGFR1 fusion mutants
R-HSA-186763, Downstream signal transduction
R-HSA-6785807, Interleukin-4 and Interleukin-13 signaling
R-HSA-877300, Interferon gamma signaling [P42224-1]
R-HSA-877312, Regulation of IFNG signaling [P42224-1]
R-HSA-8854691, Interleukin-20 family signaling
R-HSA-8939902, Regulation of RUNX2 expression and activity
R-HSA-8984722, Interleukin-35 Signalling
R-HSA-8985947, Interleukin-9 signaling
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-9673767, Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants
R-HSA-9673770, Signaling by PDGFRA extracellular domain mutants
R-HSA-982772, Growth hormone receptor signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P42224

SIGNOR Signaling Network Open Resource

More...SIGNORi		P42224

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Signal transducer and activator of transcription 1-alpha/beta
Alternative name(s):
Transcription factor ISGF-3 components p91/p84
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:STAT1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000115415.18

Human Gene Nomenclature Database

More...HGNCi		HGNC:11362, STAT1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600555, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P42224

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_065815201K → 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_018265600L → 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_075500701Y → C in IMD31B; disrupts transactivation activity in response to IFNG. 1 Publication1
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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065816320E → Q in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852680EnsemblClinVar.1
Natural variantiVAR_065817463Q → H in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852679EnsemblClinVar.1
Natural variantiVAR_068713637K → 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_068714673K → 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_018266706L → 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_065934165D → 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_065935165D → H in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906767EnsemblClinVar.1
Natural variantiVAR_065936170Y → N in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906766EnsemblClinVar.1
Natural variantiVAR_065937174C → R in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906763EnsemblClinVar.1
Natural variantiVAR_075494179N → K in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777628EnsemblClinVar.1
Natural variantiVAR_065938202M → I in IMD31C. 1 Publication1
Natural variantiVAR_065939202M → V in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906762EnsemblClinVar.1
Natural variantiVAR_065940267A → V in IMD31C. 2 PublicationsCorresponds to variant dbSNP:rs387906759EnsemblClinVar.1
Natural variantiVAR_065941271Q → P in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906768EnsemblClinVar.1
Natural variantiVAR_065942274R → 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_065943274R → 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_075495278K → 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_075496285Q → R in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777629EnsemblClinVar.1
Natural variantiVAR_065944286K → I in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906761EnsemblClinVar.1
Natural variantiVAR_065945288T → A in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906765EnsemblClinVar.1
Natural variantiVAR_075497298K → N in IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation. 1 Publication1
Natural variantiVAR_075498384G → 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_075499385T → 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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi110K → R: Sumoylated. 1 Publication1
Mutagenesisi114K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication1
Mutagenesisi175K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication1
Mutagenesisi296K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication1
Mutagenesisi366K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication1
Mutagenesisi525K → A: Strongly reduced IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. Does not affect ability to homodimerize. 1 Publication1
Mutagenesisi636 – 637KK → AA: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication2
Mutagenesisi656 – 658AEN → 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 Publication3
Mutagenesisi657E → Q: Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-705. 1 Publication1
Mutagenesisi665K → A: No effect on IFN-alpha-induced STAT1 phosphorylation and nuclear translocation. 1 Publication1
Mutagenesisi701Y → E: Not phosphorylated at S-708 upon IFNB induction. 2 Publications1
Mutagenesisi701Y → F: No effect on basal sumoylation. Enhances sumoylation in the presence of MAPK stimulation. Phosphorylated at S-708 upon IFNB induction. 2 Publications1
Mutagenesisi703K → R: Abolishes sumoylation by SUMO1. Increased IFN-gamma-mediated transactivation. 2 Publications1
Mutagenesisi705E → Q: Loss of ADP-ribosylation and increased Tyr-701 phosphorylation; when associated with Q-657. 1 Publication1
Mutagenesisi708S → A: Phosphorylated at Y-701 upon IFNB induction. 1 Publication1
Mutagenesisi708S → D: Not phosphorylated at Y-701 upon IFNB induction. 1 Publication1
Mutagenesisi727S → 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 Publications1
Mutagenesisi727S → D: No change in enhancement of MAPK-induced sumoylation. Basal interaction with PIAS1. Interaction with PIAS1 increased on MAPK stimulation. 3 Publications1
Mutagenesisi727S → E: No change in enhancement of MAPK-induced sumoylation. 3 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		6772

MalaCards human disease database

More...MalaCardsi		STAT1
MIMi613796, phenotype
614162, phenotype
614892, phenotype

Open Targets

More...OpenTargetsi		ENSG00000115415

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		391487, Autoimmune enteropathy and endocrinopathy-susceptibility to chronic infections syndrome
319595, Mendelian susceptibility to mycobacterial diseases due to partial STAT1 deficiency
391311, Susceptibility to viral and mycobacterial infections

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36183

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P42224, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL6101

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		STAT1

Domain mapping of disease mutations (DMDM)

More...DMDMi		2507413

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001824102 – 750Signal transducer and activator of transcription 1-alpha/betaAdd BLAST749

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei114N6-methyllysine1 Publication1
Modified residuei175N6-methyllysine1 Publication1
Modified residuei296N6-methyllysine1 Publication1
Modified residuei366N6-methyllysine1 Publication1
Modified residuei525N6-methyllysine1 Publication1
Modified residuei637N6-methyllysine1 Publication1
Modified residuei657ADP-ribosyl glutamic acid; by PARP141 Publication1
Modified residuei665N6-methyllysine1 Publication1
Modified residuei701Phosphotyrosine; by JAK1, JAK2 or TYK28 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei705ADP-ribosyl glutamic acid; by PARP141 Publication1
Modified residuei708Phosphoserine; by IKKE1 Publication1
Modified residuei727Phosphoserine; by MAPK14Combined sources6 Publications1
Modified residuei745Phosphoserine; by IKKEBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of phosphorylation has been called into question and the lack of phosphorylation may be due to sumoylation of Lys-703 (PubMed:29858569).1 Publication1 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

The CPTAC Assay portal

More...CPTACi		CPTAC-1272
CPTAC-1746

Encyclopedia of Proteome Dynamics

More...EPDi		P42224

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P42224

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P42224

MaxQB - The MaxQuant DataBase

More...MaxQBi		P42224

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P42224

PeptideAtlas

More...PeptideAtlasi		P42224

PRoteomics IDEntifications database

More...PRIDEi		P42224

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55491 [P42224-1]
55492 [P42224-2]

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P42224

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P42224

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P42224

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P42224

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P42224

<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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000115415, Expressed in epithelium of bronchus and 244 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42224, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P42224, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000115415, Low tissue specificity

<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>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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; the interaction results in release of STAT1 from its target gene (PubMed:9724754, PubMed:17897103).

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 similarity9 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

(Microbial infection) Interacts with ebolavirus protein VP24.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
P42224
With#Exp.IntAct
DDB1 [Q16531]2EBI-1057697,EBI-350322
DDX58 [O95786]4EBI-1057697,EBI-995350
E2F1 [Q01094]2EBI-1057697,EBI-448924
EGFR [P00533]7EBI-1057697,EBI-297353
EIF1AD [Q8N9N8]4EBI-1057697,EBI-750700
ERBB2 [P04626]3EBI-1057697,EBI-641062
FOS [P01100]6EBI-1057697,EBI-852851
IFNAR1 [P17181]2EBI-1057697,EBI-1547250
IFNAR2 [P48551]2EBI-1057697,EBI-958408
IFNGR1 [P15260]4EBI-1057697,EBI-1030755
KPNA1 [P52294]4EBI-1057697,EBI-358383
MAVS [Q7Z434]3EBI-1057697,EBI-995373
OTUD4 [Q01804]3EBI-1057697,EBI-1054396
RXRA [P19793]2EBI-1057697,EBI-78598
itself4EBI-1057697,EBI-1057697
STAT2 [P52630]15EBI-1057697,EBI-1546963
STAT3 [P40763]5EBI-1057697,EBI-518675
H1L [P07239] from Vaccinia virus (strain Western Reserve).2EBI-1057697,EBI-7789600
UL47 [Q4VW77] from Bovine alphaherpesvirus 1.2EBI-1057697,EBI-11499224
Isoform early E1A 32 kDa protein [P03255-1] from Human adenovirus C serotype 5.2EBI-1057697,EBI-6692439
Isoform early E1A 26 kDa protein [P03255-2] from Human adenovirus C serotype 5.2EBI-1057697,EBI-6859460
P26664 from Hepatitis C virus genotype 1a (isolate 1).5EBI-1057697,EBI-6941357
Core protein p21 (PRO_0000037566) from Hepatitis C virus genotype 1a (isolate H).2EBI-1057697,EBI-6377335
Non-structural protein 5A (PRO_0000037576) from Hepatitis C virus genotype 1a (isolate H).4EBI-1057697,EBI-8753518
STAT1 - isoform Alpha [P42224-1]
With#Exp.IntAct
KDM3A [Q9Y4C1]8EBI-15711971,EBI-2515339
itself3EBI-15711971,EBI-15711971
P06498 from Human adenovirus C serotype 5.2EBI-15711971,EBI-16085959
STAT1 - isoform Beta [P42224-2]
With#Exp.IntAct
itself4EBI-15712015,EBI-15712015

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		112649, 192 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P42224

Database of interacting proteins

More...DIPi		DIP-46140N

Protein interaction database and analysis system

More...IntActi		P42224, 161 interactors

Molecular INTeraction database

More...MINTi		P42224

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000354394

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P42224

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P42224, protein

<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

1750
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P42224

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P42224

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini573 – 670SH2PROSITE-ProRule annotationAdd BLAST98

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili136 – 3171 PublicationAdd BLAST182

<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

Belongs to the transcription factor STAT family.Curated

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3667, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00990000203599

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_014189_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P42224

KEGG Orthology (KO)

More...KOi		K11220

Identification of Orthologs from Complete Genome Data

More...OMAi		DTMMNAV

Database of Orthologous Groups

More...OrthoDBi		327469at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P42224

TreeFam database of animal gene trees

More...TreeFami		TF318648

Family and domain databases

Conserved Domains Database

More...CDDi		cd10372, SH2_STAT1, 1 hit

Database of protein disorder

More...DisProti		DP00962

Gene3D Structural and Functional Annotation of Protein Families

More...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

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00046

Integrated resource of protein families, domains and functional sites

More...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

The PANTHER Classification System

More...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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00964, STAT_int, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47655, SSF47655, 1 hit
SSF48092, SSF48092, 1 hit
SSF49417, SSF49417, 1 hit
SSF55550, SSF55550, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50001, SH2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 15 potential isoforms that are computationally mapped.Show allAlign All

Isoform Alpha (identifier: P42224-1) [UniParc]FASTAAdd to basket
Also known as: p91

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i054A813522364BA6
GO
Isoform Beta (identifier: P42224-2) [UniParc]FASTAAdd to basket
Also known as: p84

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

Show »
Length:712
Mass (Da):83,043
Checksum:i31408601223700BB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 15 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KPM9J3KPM9_HUMAN
Signal transducer and activator of ...
STAT1
714Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KB53A0A669KB53_HUMAN
Signal transducer and activator of ...
STAT1
791Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KB56A0A669KB56_HUMAN
Signal transducer and activator of ...
STAT1
748Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KB68A0A669KB68_HUMAN
Signal transducer and activator of ...
STAT1
748Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KBA4A0A669KBA4_HUMAN
Signal transducer and activator of ...
STAT1
779Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KBI6A0A669KBI6_HUMAN
Signal transducer and activator of ...
STAT1
716Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A669KB52A0A669KB52_HUMAN
Signal transducer and activator of ...
STAT1
636Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EPD2E7EPD2_HUMAN
Signal transducer and activator of ...
STAT1
377Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D2KFR9D2KFR9_HUMAN
Signal transducer and activator of ...
STAT1
193Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ENM1E7ENM1_HUMAN
Signal transducer and activator of ...
STAT1
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti46A → T in ADA59516 (Ref. 2) Curated1
Sequence conflicti307S → G in BAF85293 (PubMed:14702039).Curated1
Sequence conflicti718Q → R in CAH18430 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03452130I → T. Corresponds to variant dbSNP:rs34255470Ensembl.1
Natural variantiVAR_065934165D → 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_065935165D → H in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906767EnsemblClinVar.1
Natural variantiVAR_065936170Y → N in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906766EnsemblClinVar.1
Natural variantiVAR_065937174C → R in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906763EnsemblClinVar.1
Natural variantiVAR_075494179N → K in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777628EnsemblClinVar.1
Natural variantiVAR_065815201K → 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_065938202M → I in IMD31C. 1 Publication1
Natural variantiVAR_065939202M → V in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906762EnsemblClinVar.1
Natural variantiVAR_065940267A → V in IMD31C. 2 PublicationsCorresponds to variant dbSNP:rs387906759EnsemblClinVar.1
Natural variantiVAR_065941271Q → P in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906768EnsemblClinVar.1
Natural variantiVAR_065942274R → 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_065943274R → 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_075495278K → 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_075496285Q → R in IMD31C; gain of function; increases transactivation activity in response to IFNG. 1 PublicationCorresponds to variant dbSNP:rs587777629EnsemblClinVar.1
Natural variantiVAR_065944286K → I in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906761EnsemblClinVar.1
Natural variantiVAR_065945288T → A in IMD31C. 1 PublicationCorresponds to variant dbSNP:rs387906765EnsemblClinVar.1
Natural variantiVAR_075497298K → N in IMD31C; gain of function; increases basal STAT1 phosphorylation levels which are 10-20 fold higher than controls after IFNG stimulation. 1 Publication1
Natural variantiVAR_065816320E → Q in IMD31A; affects the DNA-binding activity of the protein. 1 PublicationCorresponds to variant dbSNP:rs137852680EnsemblClinVar.1
Natural variantiVAR_075498384G → 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:rs796065052