Stat3
entrez
20848
canonical
uniprot
P42227
canonical
ensembl
ENSMUSG00000004040
resolver
ensp
ENSMUSP00000090342
resolver
ensp
ENSMUSP00000099403
resolver
ensp
ENSMUSP00000120152
resolver
ensp
ENSMUSP00000310620
resolver
genesymbol
Stat3
resolver
genesymbol_syn
Aprf
resolver
uniprot
A2A5D1
resolver
uniprot
B7ZC17
resolver
uniprot
Q3ULI4
resolver
uniprot
Q6GU23
resolver
uniprot_entry
Q3ULI4_MOUSE
resolver
uniprot_entry
Q6GU23_MOUSE
resolver
uniprot_entry
STAT3_MOUSE
resolver
uniprot_sec
A2A5D1
resolver
uniprot_sec
B7ZC17
resolver
amino_acid_sequence
MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECATSPM
uniprot
proteins
function
FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:23917203, PubMed:26026268). 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): acetylation promotes its transcription activity and cell differentiation while deacetylation and oxidation of lysine residues by LOXL3 inhibits differentiation (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 transactivating 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). Following JAK/STAT signaling activation and as part of a complex with NFATC3 and NFATC4, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (PubMed:19538478). 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). Involved in the oncostatin-M-mediated signaling pathway through both type I OSM receptor complex (heterodimers composed of LIFR and IL6ST) and type II OSM receptor complex (heterodimers composed of OSMR and IL6ST) (By similarity). {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:20215569, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:23917203, ECO:0000269|PubMed:26026268}.
uniprot
proteins
mass_dalton
88054
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="V->A: No effect on nuclear import; when associated with A-78 and W-174."; /evidence="ECO:0000269|PubMed:15919823"; MUTAGEN 78; /note="L->A: No effect on nuclear import; when associated with A-77 and W-174."; /evidence="ECO:0000269|PubMed:15919823"; MUTAGEN 140; /note="K->R: Forms stronger interaction with Ptpn6 phosphatase."; /evidence="ECO:0000269|PubMed:35995859"; MUTAGEN 174; /note="F->W: No effect on nuclear import; when associated with A-77 and A-78."; /evidence="ECO:0000269|PubMed:15919823"; MUTAGEN 609; /note="R->A: No effect on nuclear localization; when associated with F-705."; /evidence="ECO:0000269|PubMed:15919823"; MUTAGEN 705; /note="Y->F: Loss of interaction with Fam220a. No effect on nuclear localization; when associated with A-609."; /evidence="ECO:0000269|PubMed:15919823, ECO:0000269|PubMed:23917203, ECO:0000269|PubMed:26026268"; MUTAGEN 727; /note="S->A: Decreased transcriptional activation."; /evidence="ECO:0000269|PubMed:15004007
uniprot
proteins
post_translational_modification
PTM: 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, isoform M2 of PKM (PKM2) or FER leads to an increase of its transcriptional activity (By similarity). Phosphorylation at Tyr-705 is increased in the presence of calcineurin (PubMed:19538478). Phosphorylation at Tyr-640 by TYK2 negatively regulates transcriptional activity (By similarity). {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:10878010, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11553624, ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:16825198, ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:7543024}.; PTM: Acetylated on lysine residues by EP300/p300, promoting its activation (By similarity). Acetylation at Lys-49 and Lys-87 by EP300/p300 promotes its activation (By similarity). Acetylation at Lys-87 by EP300/p300 promotes its association with BRD2 and recruitment to chromatin (By similarity). Deacetylated at Lys-49 and Lys-87 by HDAC1 (By similarity). Acetylation at Lys-685 by EP300/p300 promotes its homodimerization and activation (By similarity). Deacetylated at Lys-685 by HDAC3 (By similarity). Acetylated on lysine residues by CREBBP (By similarity). Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (By similarity). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (By similarity). {ECO:0000250|UniProtKB:P40763}.; PTM: 'Lys-63'-linked polyubiquitination at Lys-615, Lys-626, Lys-631 and Lys-642 by RNF220 regulates STAT3 stability, phosphorylation, nuclear translocation, and transcriptional activity. {ECO:0000250|UniProtKB:P40763}.; PTM: 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. {ECO:0000250|UniProtKB:P40763}.; PTM: Methylated at Lys-140. Demethylation at Lys-140 by Jmjd1c facilitates its dephosphorylation by Ptpn6. {ECO:0000269|PubMed:35995859}.; PTM: (Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA. {ECO:0000269|PubMed:29924996}.
uniprot
proteins
protein_family
Transcription factor STAT family
uniprot
proteins
pubmed
10878010
uniprot
proteins
pubmed
10954736
uniprot
proteins
pubmed
11161808
uniprot
proteins
pubmed
11294897
uniprot
proteins
pubmed
11553624
uniprot
proteins
pubmed
12594516
uniprot
proteins
pubmed
15004007
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15919823
uniprot
proteins
pubmed
16401721
uniprot
proteins
pubmed
16825198
uniprot
proteins
pubmed
18034455
uniprot
proteins
pubmed
18234692
uniprot
proteins
pubmed
18356286
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19538478
uniprot
proteins
pubmed
20215569
uniprot
proteins
pubmed
20595392
uniprot
proteins
pubmed
21135090
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23084476
uniprot
proteins
pubmed
23401489
uniprot
proteins
pubmed
23917203
uniprot
proteins
pubmed
23972987
uniprot
proteins
pubmed
26026268
uniprot
proteins
pubmed
29924996
uniprot
proteins
pubmed
35995859
uniprot
proteins
pubmed
7512451
uniprot
proteins
pubmed
7523373
uniprot
proteins
pubmed
7543024
uniprot
proteins
pubmed
7568080
uniprot
proteins
pubmed
8140422
uniprot
proteins
pubmed
9108058
uniprot
proteins
pubmed
9388184
uniprot
proteins
pubmed
9671298
uniprot
proteins
sequence_length
770
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23917203}. Nucleus {ECO:0000269|PubMed:19538478, ECO:0000269|PubMed:23917203, ECO:0000269|PubMed:26026268}. Note=Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3 (By similarity). Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Translocates to the nucleus in the presence of EDN1 (By similarity). {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P52631}.
uniprot
proteins