STAT3
entrez
6774
canonical
uniprot
P40763
canonical
ensembl
ENSG00000168610
resolver
ensp
ENSP00000264657
resolver
ensp
ENSP00000373923
resolver
ensp
ENSP00000384943
resolver
ensp
ENSP00000467000
resolver
ensp
ENSP00000467985
resolver
ensp
ENSP00000503237
resolver
ensp
ENSP00000503308
resolver
ensp
ENSP00000503332
resolver
ensp
ENSP00000503333
resolver
ensp
ENSP00000503559
resolver
ensp
ENSP00000503574
resolver
ensp
ENSP00000503634
resolver
ensp
ENSP00000503662
resolver
ensp
ENSP00000503799
resolver
ensp
ENSP00000503872
resolver
ensp
ENSP00000504062
resolver
ensp
ENSP00000504081
resolver
ensp
ENSP00000504182
resolver
ensp
ENSP00000504324
resolver
ensp
ENSP00000504350
resolver
ensp
ENSP00000520412
resolver
ensp
ENSP00000528616
resolver
ensp
ENSP00000592828
resolver
ensp
ENSP00000613847
resolver
ensp
ENSP00000613852
resolver
ensp
ENSP00000613857
resolver
ensp
ENSP00000613861
resolver
ensp
ENSP00000722035
resolver
enst
ENST00000677442
resolver
enst
ENST00000677479
resolver
enst
ENST00000677603
resolver
enst
ENST00000678043
resolver
enst
ENST00000678048
resolver
enst
ENST00000678535
resolver
enst
ENST00000678572
resolver
enst
ENST00000678674
resolver
enst
ENST00000678905
resolver
enst
ENST00000679166
resolver
enst
ENST00000679185
resolver
enst
ENST00000922769
resolver
enst
ENST00000943793
resolver
enst
ENST00000943802
resolver
genesymbol
STAT3
resolver
genesymbol_syn
APRF
resolver
hgnc
HGNC:11364
resolver
uniprot
A0A7I2V395
resolver
uniprot
A0A7I2V444
resolver
uniprot
A0A7I2V4C8
resolver
uniprot
A0A7I2V4R2
resolver
uniprot
A0A7I2V4R3
resolver
uniprot
A0A7I2V552
resolver
uniprot
A0A7I2YQD2
resolver
uniprot
A0A7I2YQR5
resolver
uniprot
A8K7B8
resolver
uniprot
K7ENL3
resolver
uniprot
O14916
resolver
uniprot
Q9BW54
resolver
uniprot_entry
A0A7I2V395_HUMAN
resolver
uniprot_entry
A0A7I2V444_HUMAN
resolver
uniprot_entry
A0A7I2V4C8_HUMAN
resolver
uniprot_entry
A0A7I2V4R2_HUMAN
resolver
uniprot_entry
A0A7I2V4R3_HUMAN
resolver
uniprot_entry
A0A7I2V552_HUMAN
resolver
uniprot_entry
A0A7I2YQD2_HUMAN
resolver
uniprot_entry
A0A7I2YQR5_HUMAN
resolver
uniprot_entry
STAT3_HUMAN
resolver
uniprot_sec
A8K7B8
resolver
uniprot_sec
K7ENL3
resolver
uniprot_sec
O14916
resolver
uniprot_sec
Q9BW54
resolver
amino_acid_sequence
MAQWNQLQQLDTRYLEQLHQLYSDSFPMELRQFLAPWIESQDWAYAASKESHATLVFHNLLGEIDQQYSRFLQESNVLYQHNLRRIKQFLQSRYLEKPMEIARIVARCLWEESRLLQTAATAAQQGGQANHPTAAVVTEKQQMLEQHLQDVRKRVQDLEQKMKVVENLQDDFDFNYKTLKSQGDMQDLNGNNQSVTRQKMQQLEQMLTALDQMRRSIVSELAGLLSAMEYVQKTLTDEELADWKRRQQIACIGGPPNICLDRLENWITSLAESQLQTRQQIKKLEELQQKVSYKGDPIVQHRPMLEERIVELFRNLMKSAFVVERQPCMPMHPDRPLVIKTGVQFTTKVRLLVKFPELNYQLKIKVCIDKDSGDVAALRGSRKFNILGTNTKVMNMEESNNGSLSAEFKHLTLREQRCGNGGRANCDASLIVTEELHLITFETEVYHQGLKIDLETHSLPVVVISNICQMPNAWASILWYNMLTNNPKNVNFFTKPPIGTWDQVAEVLSWQFSSTTKRGLSIEQLTTLAEKLLGPGVNYSGCQITWAKFCKENMAGKGFSFWVWLDNIIDLVKKYILALWNEGYIMGFISKERERAILSTKPPGTFLLRFSESSKEGGVTFTWVEKDISGKTQIQSVEPYTKQQLNNMSFAEIIMGYKIMDATNILVSPLVYLYPDIPKEEAFGKYCRPESQEHPEADPGSAAPYLKTKFICVTPTTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMELTSECATSPM
uniprot
proteins
disease_involvement
DISEASE: Hyper-IgE syndrome 1, autosomal dominant, with recurrent infections (HIES1) [MIM:147060]: A rare disorder of immunity and connective tissue characterized by immunodeficiency, chronic eosinophilia, distinctive coarse facial appearance, abnormal dentition, hyperextensibility of the joints, and bone fractures. {ECO:0000269|PubMed:17676033, ECO:0000269|PubMed:17881745, ECO:0000269|PubMed:23342295, ECO:0000269|PubMed:26293184}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Autoimmune disease, multisystem, infantile-onset, 1 (ADMIO1) [MIM:615952]: A disorder characterized by early childhood onset of a spectrum of autoimmune manifestations affecting multiple organs, including insulin-dependent diabetes mellitus and autoimmune enteropathy or celiac disease. Other features include short stature, non-specific dermatitis, hypothyroidism, autoimmune arthritis, and delayed puberty. {ECO:0000269|PubMed:25038750, ECO:0000269|PubMed:25359994, ECO:0000269|PubMed:28073828, ECO:0000269|PubMed:28253502, ECO:0000269|PubMed:28579554, ECO:0000269|PubMed:29162862, ECO:0000269|PubMed:36228738, ECO:0000269|PubMed:38404237}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:10688651, PubMed:11294841, PubMed:12359225, PubMed:12873986, PubMed:15194700, PubMed:15653507, PubMed:16285960, PubMed:17344214, PubMed:18242580, PubMed:18782771, PubMed:22306293, PubMed:23084476, PubMed:28262505, PubMed:32929201, PubMed:38404237). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:15653507, PubMed:16285960, PubMed:17344214, PubMed:18782771, PubMed:28262505, PubMed:32929201). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). 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 (PubMed:12359225). Activated by IL31 through IL31RA (PubMed:15194700). 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 (PubMed:28065600, PubMed:28262505). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transactivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity). 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 (By similarity). 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) (PubMed:9188471). {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11294841, ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580, ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:38404237, ECO:0000269|PubMed:9188471}.
uniprot
proteins
mass_dalton
88068
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="K->Q: Mimics acetylation; increased interaction with EP300; when associated with Q-87."; /evidence="ECO:0000269|PubMed:18782771"; MUTAGEN 49; /note="K->R: Decreased transcription activator activity and interaction with EP300; when associated with R-87."; /evidence="ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:18782771"; MUTAGEN 87; /note="K->Q: Mimics acetylation; increased interaction with EP300; when associated with Q-49."; /evidence="ECO:0000269|PubMed:18782771"; MUTAGEN 87; /note="K->R: Decreased transcription activator activity and interaction with EP300; when associated with R-49."; /evidence="ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:18782771"; MUTAGEN 434..435; /note="EE->AA: Inhibits leptin-mediated transactivation of CCND1 promoter. No effect on interaction with INPP5F."; /evidence="ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:25476455"; MUTAGEN 685; /note="K->R: Decreased acetylation by EP300/p300, leading to impaired homodimerization and activation."; /evidence="ECO:0000269|PubMed:15653507"; MUTAGEN 705; /note="Y->F: Inhibits leptin-mediated transactivation of CCND1 promoter. Abolished phosphorylation by isoform M2 of PKM (PKM2)."; /evidence="ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:22306293
uniprot
proteins
post_translational_modification
PTM: Tyrosine phosphorylated upon stimulation with EGF. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Activated through tyrosine phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. 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. Upon LPS challenge, phosphorylated within the nucleus by IRAK1. Upon erythropoietin treatment, phosphorylated on Ser-727 by RPS6KA5. 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 (PubMed:12763138, PubMed:16568091, PubMed:21135090, PubMed:22306293, PubMed:32929201). Phosphorylation at Tyr-705 is increased in the presence of calcineurin (By similarity). Phosphorylation at Tyr-640 by TYK2 negatively regulates transcriptional activity (PubMed:29162862). {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12763138, ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:16568091, ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19147545, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:29162862, ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:7701321}.; PTM: Acetylated on lysine residues by EP300/p300, promoting its activation (PubMed:15653507, PubMed:16285960, PubMed:18782771). Acetylation at Lys-49 and Lys-87 by EP300/p300 promotes its activation (PubMed:15653507, PubMed:16285960, PubMed:28262505). Acetylation at Lys-87 by EP300/p300 promotes its association with BRD2 and recruitment to chromatin (PubMed:28262505). Deacetylated at Lys-49 and Lys-87 by HDAC1 (PubMed:16285960). Acetylation at Lys-685 by EP300/p300 promotes its homodimerization and activation (PubMed:15653507). Deacetylated at Lys-685 by HDAC3 (PubMed:15653507). Acetylated on lysine residues by CREBBP (PubMed:28065600). Deacetylation by LOXL3 leads to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). {ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:28262505}.; PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to disrupt STAT3 dimerization and inhibit STAT3 transcription activity (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 preferentially takes place on lysine residues that are acetylated (PubMed:28065600). {ECO:0000269|PubMed:28065600}.; 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:0000269|PubMed:41219491}.; PTM: (Microbial infection) Phosphorylated on Tyr-705 in the presence of S.typhimurium SarA. {ECO:0000269|PubMed:29924996}.; PTM: Methylated at Lys-140. Demethylation at Lys-140 by Jmjd1c facilitates its dephosphorylation by Ptpn6. {ECO:0000250|UniProtKB:P42227}.
uniprot
proteins
protein_family
Transcription factor STAT family
uniprot
proteins
pubmed
10688651
uniprot
proteins
pubmed
11294841
uniprot
proteins
pubmed
11773079
uniprot
proteins
pubmed
12023369
uniprot
proteins
pubmed
12208879
uniprot
proteins
pubmed
12359225
uniprot
proteins
pubmed
12763138
uniprot
proteins
pubmed
12873986
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15194700
uniprot
proteins
pubmed
15465816
uniprot
proteins
pubmed
15467733
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15653507
uniprot
proteins
pubmed
15677474
uniprot
proteins
pubmed
15919823
uniprot
proteins
pubmed
15994929
uniprot
proteins
pubmed
16219639
uniprot
proteins
pubmed
16285960
uniprot
proteins
pubmed
16568091
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
17344214
uniprot
proteins
pubmed
17676033
uniprot
proteins
pubmed
17875724
uniprot
proteins
pubmed
17881745
uniprot
proteins
pubmed
17956865
uniprot
proteins
pubmed
18070987
uniprot
proteins
pubmed
18234692
uniprot
proteins
pubmed
18242580
uniprot
proteins
pubmed
18599021
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18782771
uniprot
proteins
pubmed
19147545
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20826784
uniprot
proteins
pubmed
21135090
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22306293
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23084476
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23342295
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25038750
uniprot
proteins
pubmed
25359994
uniprot
proteins
pubmed
25476455
uniprot
proteins
pubmed
26293184
uniprot
proteins
pubmed
26675719
uniprot
proteins
pubmed
26918609
uniprot
proteins
pubmed
27387064
uniprot
proteins
pubmed
28065600
uniprot
proteins
pubmed
28073828
uniprot
proteins
pubmed
28253502
uniprot
proteins
pubmed
28262505
uniprot
proteins
pubmed
28579554
uniprot
proteins
pubmed
29162862
uniprot
proteins
pubmed
29743632
uniprot
proteins
pubmed
29924996
uniprot
proteins
pubmed
31462771
uniprot
proteins
pubmed
31899195
uniprot
proteins
pubmed
32555452
uniprot
proteins
pubmed
32797246
uniprot
proteins
pubmed
32929201
uniprot
proteins
pubmed
36228738
uniprot
proteins
pubmed
38404237
uniprot
proteins
pubmed
38582550
uniprot
proteins
pubmed
41219491
uniprot
proteins
pubmed
7512451
uniprot
proteins
pubmed
7701321
uniprot
proteins
pubmed
9188471
uniprot
proteins
pubmed
9388184
uniprot
proteins
pubmed
9630560
uniprot
proteins
sequence_length
770
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:41219491}. Nucleus {ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:29162862, ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:41219491}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:29162862). Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4 (PubMed:15653507, PubMed:16285960). Constitutive nuclear presence is independent of tyrosine phosphorylation. 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. Identified in a complex with LYN and PAG1. Translocates to the nucleus in the presence of EDN1 (By similarity). {ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:29162862}.
uniprot
proteins