Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P42227 (STAT3_MOUSE)

Entry version 226 (07 Oct 2020)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Signal transducer and activator of transcription 3

Gene

Stat3

Organism
Mus musculus (Mouse)
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 interleukins, KITLG/SCF, LEP and other growth factors (By similarity). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (By similarity). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes (By similarity). Activated by IL31 through IL31RA (By similarity). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4+ T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (PubMed:12594516). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:16825198). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (PubMed:20215569). Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (PubMed:23401489). Interacts with ZDHHC19, leading to palmitoylation which promotes homodimerization and activation (By similarity).By similarity6 Publications

Miscellaneous

Involved in the gp130-mediated signaling pathway.

<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 processAcute phase, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-1059683, Interleukin-6 signaling
R-MMU-1266695, Interleukin-7 signaling
R-MMU-1433557, Signaling by SCF-KIT
R-MMU-186763, Downstream signal transduction
R-MMU-6783783, Interleukin-10 signaling
R-MMU-6785807, Interleukin-4 and Interleukin-13 signaling
R-MMU-8849474, PTK6 Activates STAT3
R-MMU-8854691, Interleukin-20 family signaling
R-MMU-8875791, MET activates STAT3
R-MMU-8983432, Interleukin-15 signaling
R-MMU-8984722, Interleukin-35 Signalling
R-MMU-8985947, Interleukin-9 signaling
R-MMU-9008059, Interleukin-37 signaling
R-MMU-9020933, Interleukin-23 signaling
R-MMU-9020956, Interleukin-27 signaling
R-MMU-9020958, Interleukin-21 signaling

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		P42227, Predicted

MoonProt database of moonlighting proteins

More...MoonProti		P42227

<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 3Imported
Alternative name(s):
Acute-phase response factor
<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:Stat3Imported
Synonyms:AprfImported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:103038, Stat3

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Early embryonic lethality, day 6.5-7.5. Conditional, tissue specific mutants are variably viable and show diverse defects including obesity, diabetes, thermal dysregulation and infertility.2 Publications

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>Mutagenesisi77V → A: No effect on nuclear import; when associated with A-78 and W-174. 1 Publication1
Mutagenesisi78L → A: No effect on nuclear import; when associated with A-77 and W-174. 1 Publication1
Mutagenesisi174F → W: No effect on nuclear import; when associated with A-77 and A-78. 1 Publication1
Mutagenesisi609R → A: Nuclear localization to the same extent as wild-type; when associated with F-705. 1 Publication1
Mutagenesisi705Y → F: Nuclear localization to the same extent as wild-type; when associated with A-609. 1 Publication1
Mutagenesisi727S → A: Decreased transcriptional activation. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5402

<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 methionineiRemovedBy similarity
<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_00001824182 – 770Signal transducer and activator of transcription 3Add BLAST769

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-acetylalanineBy similarity1
Modified residuei601Allysine; alternateBy similarity1
Modified residuei601N6-acetyllysine; alternateBy similarity1
Modified residuei615Allysine; alternateBy similarity1
Modified residuei615N6-acetyllysine; alternateBy similarity1
Modified residuei631Allysine; alternateBy similarity1
Modified residuei631N6-acetyllysine; alternateBy similarity1
Modified residuei685Allysine; alternateBy similarity1
Modified residuei685N6-acetyllysine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi687S-palmitoyl cysteineBy similarity1
Modified residuei705Phosphotyrosine; by FER and PTK6Combined sources2 Publications1
Modified residuei707N6-acetyllysineBy similarity1
Lipidationi712S-palmitoyl cysteineBy similarity1
Modified residuei714PhosphothreonineCombined sources1
Modified residuei727PhosphoserineCombined sources1
Modified residuei727Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCECombined sources4 Publications1

<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

Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated on serine upon DNA damage, probably by ATM or ATR. Serine phosphorylation is important for the formation of stable DNA-binding STAT3 homodimers and maximal transcriptional activity. ARL2BP may participate in keeping the phosphorylated state of STAT3 within the nucleus. Tyrosine phosphorylated upon stimulation with EGF. Upon LPS challenge, phosphorylated within the nucleus by IRAK1 (By similarity). Upon UV-A treatment, phosphorylated on Ser-727 by RPS6KA5 (By similarity). Dephosphorylation on tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 signaling (By similarity). Phosphorylation at Tyr-705 by PTK6 or FER leads to an increase of its transcriptional activity (By similarity).By similarity9 Publications
Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.By similarity
Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity. Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated.By similarity
(Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA.1 Publication
S-palmitoylated by ZDHHC19 in SH2 putative lipid-binding pockets, leading to homodimerization.By similarity
S-stearoylated, probably by ZDHHC19.By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P42227

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P42227

MaxQB - The MaxQuant DataBase

More...MaxQBi		P42227

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

More...PaxDbi		P42227

PeptideAtlas

More...PeptideAtlasi		P42227

PRoteomics IDEntifications database

More...PRIDEi		P42227

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P42227

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

More...PhosphoSitePlusi		P42227

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P42227

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

STAT3A is seen in the liver, spleen, and kidney. STAT3B is also detected in the liver, although in a much less abundant manner. Expressed in the lung and an increase in expression levels seen during methicillin-resistant S.aureus infection.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000004040, Expressed in subcutaneous adipose tissue and 345 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42227, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P42227, MM

<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

Forms a homodimer or a heterodimer with a related family member (at least STAT1).

Interacts with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1.

Interacts with IL23R in presence of IL23.

Interacts (via SH2 domain) with NLK.

Interacts with ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By similarity).

Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of nuclear import (By similarity).

Interacts with CAV2; the interaction is increased on insulin-induced tyrosine phosphorylation of CAV2 and leads to STAT3 activation (By similarity).

Interacts with ARL2BP; interaction is enhanced with ARL2.

Interacts with NEK6 (By similarity). Binds to CDK9 when activated and nuclear.

Interacts with BMX.

Interacts with ZIPK/DAPK3.

Interacts with PIAS3; the interaction occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In prostate cancer cells, interacts with STAT3 and promotes DNA binding activity of STAT3.

Interacts with STMN3, antagonizing its microtubule-destabilizing activity.

Interacts with the 'Lys-129' acetylated form of BIRC5/survivin.

Interacts with FER.

Interacts (via SH2 domain) with EIF2AK2/PKR (via the kinase catalytic domain) (By similarity).

Interacts with FGFR4 (By similarity).

Interacts with STAT3; the interaction is independent of STAT3 Tyr-705 phosphorylation status (By similarity).

Interacts with OCAD1 (PubMed:23972987).

Interacts (unphosphorylated or phosphorylated at Ser-727) with PHB (By similarity).

By similarity11 Publications

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		203523, 31 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P42227

Database of interacting proteins

More...DIPi		DIP-442N

Protein interaction database and analysis system

More...IntActi		P42227, 31 interactors

Molecular INTeraction database

More...MINTi		P42227

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000120152

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P42227

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P42227, 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

1770
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		P42227

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		P42227

<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>Domaini580 – 670SH2PROSITE-ProRule annotationAdd BLAST91

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi150 – 162Essential for nuclear importAdd BLAST13

<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

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		P42227

KEGG Orthology (KO)

More...KOi		K04692

Identification of Orthologs from Complete Genome Data

More...OMAi		GKYCRSE

Database for complete collections of gene phylogenies

More...PhylomeDBi		P42227

TreeFam database of animal gene trees

More...TreeFami		TF318648

Family and domain databases

Conserved Domains Database

More...CDDi		cd10374, SH2_STAT3, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.532.10, 1 hit
2.60.40.630, 1 hit
3.30.505.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50277

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
IPR035855, STAT3_SH2
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
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 (3+)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 3 <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 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Stat3A (identifier: P42227-1) [UniParc]FASTAAdd to basket

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
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE 
        60         70         80         90        100
SHATLVFHNL LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME 
       110        120        130        140        150
IARIVARCLW EESRLLQTAA TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD 
       160        170        180        190        200
VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK SQGDMQDLNG NNQSVTRQKM 
       210        220        230        240        250
QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL ADWKRRQQIA 
       260        270        280        290        300
CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ 
       310        320        330        340        350
HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR 
       360        370        380        390        400
LLVKFPELNY QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN 
       410        420        430        440        450
NGSLSAEFKH LTLREQRCGN GGRANCDASL IVTEELHLIT FETEVYHQGL 
       460        470        480        490        500
KIDLETHSLP VVVISNICQM PNAWASILWY NMLTNNPKNV NFFTKPPIGT 
       510        520        530        540        550
WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS GCQITWAKFC 
       560        570        580        590        600
KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST 
       610        620        630        640        650
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF 
       660        670        680        690        700
AEIIMGYKIM DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG 
       710        720        730        740        750
SAAPYLKTKF ICVTPTTCSN TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG 
       760        770
QFESLTFDMD LTSECATSPM
Length:770
Mass (Da):88,054
Last modified:October 1, 1996 - 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:i6C00626711C8012D
GO
Isoform Stat3B (identifier: P42227-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     716-770: TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM → FIDAVWK

Show »
Length:722
Mass (Da):83,126
Checksum:i09226A697966D947
GO
Isoform Del-701 (identifier: P42227-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     701-701: Missing.

Show »
Length:769
Mass (Da):87,967
Checksum:iA374A26FB9D28077
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7ZC18B7ZC18_MOUSE
Signal transducer and activator of ...
Stat3
744Annotation 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>

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 conflicti16E → K in AAA19452 (PubMed:7523373).Curated1
Sequence conflicti25S → T in AAA19452 (PubMed:7523373).Curated1
Sequence conflicti25S → T in AAC52612 (PubMed:7568080).Curated1
Sequence conflicti394M → I in AAA37254 (PubMed:7512451).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010475701Missing in isoform Del-701. 1 Publication1
Alternative sequenceiVSP_006287716 – 770TTCSN…ATSPM → FIDAVWK in isoform Stat3B. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L29278 mRNA Translation: AAA37254.1
U08378 mRNA Translation: AAA56668.1
U06922 mRNA Translation: AAA19452.1
U30709 mRNA Translation: AAC52612.1
AF246978 Genomic DNA Translation: AAL59017.1
AY299489 mRNA Translation: AAQ75418.1
AY299490 mRNA Translation: AAQ75419.1
AL591466 Genomic DNA No translation available.
BC003806 mRNA Translation: AAH03806.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS25440.1 [P42227-1]
CCDS25441.1 [P42227-2]
CCDS48934.1 [P42227-3]

Protein sequence database of the Protein Information Resource

More...PIRi		I49508

NCBI Reference Sequences

More...RefSeqi		NP_998824.1, NM_213659.3 [P42227-1]
NP_998825.1, NM_213660.3 [P42227-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040 [P42227-3]
ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040 [P42227-2]
ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040 [P42227-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		20848

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:20848

UCSC genome browser

More...UCSCi		uc007lmp.1, mouse [P42227-1]
uc007lmq.1, mouse [P42227-3]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29278 mRNA Translation: AAA37254.1
U08378 mRNA Translation: AAA56668.1
U06922 mRNA Translation: AAA19452.1
U30709 mRNA Translation: AAC52612.1
AF246978 Genomic DNA Translation: AAL59017.1
AY299489 mRNA Translation: AAQ75418.1
AY299490 mRNA Translation: AAQ75419.1
AL591466 Genomic DNA No translation available.
BC003806 mRNA Translation: AAH03806.1
CCDSiCCDS25440.1 [P42227-1]
CCDS25441.1 [P42227-2]
CCDS48934.1 [P42227-3]
PIRiI49508
RefSeqiNP_998824.1, NM_213659.3 [P42227-1]
NP_998825.1, NM_213660.3 [P42227-3]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BG1X-ray2.25A127-715[»]
3CWGX-ray3.05A/B127-688[»]
4E68X-ray2.58A127-715[»]
4ZIAX-ray2.70A/B/C/D/E3-127[»]
SMRiP42227
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi203523, 31 interactors
CORUMiP42227
DIPiDIP-442N
IntActiP42227, 31 interactors
MINTiP42227
STRINGi10090.ENSMUSP00000120152

Chemistry databases

BindingDBiP42227
ChEMBLiCHEMBL5402

Protein family/group databases

MoonDBiP42227, Predicted
MoonProtiP42227

PTM databases

iPTMnetiP42227
PhosphoSitePlusiP42227
SwissPalmiP42227

Proteomic databases

EPDiP42227
jPOSTiP42227
MaxQBiP42227
PaxDbiP42227
PeptideAtlasiP42227
PRIDEiP42227

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		660, 2384 antibodies

Genome annotation databases

EnsembliENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040 [P42227-3]
ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040 [P42227-2]
ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040 [P42227-1]
GeneIDi20848
KEGGimmu:20848
UCSCiuc007lmp.1, mouse [P42227-1]
uc007lmq.1, mouse [P42227-3]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6774
MGIiMGI:103038, Stat3

Phylogenomic databases

eggNOGiKOG3667, Eukaryota
GeneTreeiENSGT00990000203599
HOGENOMiCLU_014189_3_0_1
InParanoidiP42227
KOiK04692
OMAiGKYCRSE
PhylomeDBiP42227
TreeFamiTF318648

Enzyme and pathway databases

ReactomeiR-MMU-1059683, Interleukin-6 signaling
R-MMU-1266695, Interleukin-7 signaling
R-MMU-1433557, Signaling by SCF-KIT
R-MMU-186763, Downstream signal transduction
R-MMU-6783783, Interleukin-10 signaling
R-MMU-6785807, Interleukin-4 and Interleukin-13 signaling
R-MMU-8849474, PTK6 Activates STAT3
R-MMU-8854691, Interleukin-20 family signaling
R-MMU-8875791, MET activates STAT3
R-MMU-8983432, Interleukin-15 signaling
R-MMU-8984722, Interleukin-35 Signalling
R-MMU-8985947, Interleukin-9 signaling
R-MMU-9008059, Interleukin-37 signaling
R-MMU-9020933, Interleukin-23 signaling
R-MMU-9020956, Interleukin-27 signaling
R-MMU-9020958, Interleukin-21 signaling

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		20848, 4 hits in 23 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Stat3, mouse
EvolutionaryTraceiP42227

Protein Ontology

More...PROi		PR:P42227
RNActiP42227, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000004040, Expressed in subcutaneous adipose tissue and 345 other tissues
ExpressionAtlasiP42227, baseline and differential
GenevisibleiP42227, MM

Family and domain databases

CDDicd10374, SH2_STAT3, 1 hit
Gene3Di1.10.532.10, 1 hit
2.60.40.630, 1 hit
3.30.505.10, 1 hit
IDEALiIID50277
InterProiView protein in InterPro
IPR008967, p53-like_TF_DNA-bd
IPR000980, SH2
IPR036860, SH2_dom_sf
IPR001217, STAT
IPR035855, STAT3_SH2
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
PANTHERiPTHR11801, PTHR11801, 1 hit
PfamiView protein in Pfam
PF00017, SH2, 1 hit
PF01017, STAT_alpha, 1 hit
PF02864, STAT_bind, 1 hit
PF02865, STAT_int, 1 hit
SMARTiView protein in SMART
SM00964, STAT_int, 1 hit
SUPFAMiSSF47655, SSF47655, 1 hit
SSF48092, SSF48092, 1 hit
SSF49417, SSF49417, 1 hit
SSF55550, SSF55550, 1 hit
PROSITEiView protein in PROSITE
PS50001, SH2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSTAT3_MOUSE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P42227
Secondary accession number(s): A2A5D1, B7ZC17
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 1, 1996
Last modified: October 7, 2020
This is version 226 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again