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Signal transducer and activator of transcription 3 (Acute-phase response factor)

 STAT3_HUMAN             Reviewed;         770 AA.
P40763; A8K7B8; K7ENL3; O14916; Q9BW54;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 2.
30-AUG-2017, entry version 195.
RecName: Full=Signal transducer and activator of transcription 3 {ECO:0000312|HGNC:HGNC:11364};
AltName: Full=Acute-phase response factor;
Name=STAT3 {ECO:0000312|HGNC:HGNC:11364};
Synonyms=APRF {ECO:0000312|HGNC:HGNC:11364};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-561.
TISSUE=Placenta;
PubMed=7512451; DOI=10.1016/0092-8674(94)90235-6;
Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T.,
Yoshida K., Sudo T., Naruto M., Kishimoto T.;
"Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-
related transcription factor involved in the gp130-mediated signaling
pathway.";
Cell 77:63-71(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9630560; DOI=10.1016/S0378-1119(98)00185-1;
Della Pietra L., Bressan A., Pezzotti A., Serlupi-Crescenzi O.;
"Highly conserved amino-acid sequence between murine STAT3 and a
revised human STAT3 sequence.";
Gene 213:119-124(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Feinstein E., Adamsky S., Erlich S., Molitoris B.;
"Methods for treating chronic kidney disease.";
Patent number EP2440214, 18-APR-2012.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-143.
SeattleSNPs variation discovery resource;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DEL-701).
TISSUE=Kidney, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 564-704.
TISSUE=Liver;
Della Pietra L., Bressan A., Pezzotti A.R., Serlupi-Crescenzi O.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[10]
PHOSPHORYLATION AT SERINE RESIDUES.
PubMed=7701321; DOI=10.1126/science.7701321;
Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.;
"Requirement of serine phosphorylation for formation of STAT-promoter
complexes.";
Science 267:1990-1994(1995).
[11]
INTERACTION WITH PIAS3.
PubMed=9388184; DOI=10.1126/science.278.5344.1803;
Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.;
"Specific inhibition of Stat3 signal transduction by PIAS3.";
Science 278:1803-1805(1997).
[12]
PHOSPHORYLATION BY BMX, INTERACTION WITH BMX, AND FUNCTION.
PubMed=10688651; DOI=10.1128/MCB.20.6.2043-2054.2000;
Tsai Y.T., Su Y.H., Fang S.S., Huang T.N., Qiu Y., Jou Y.S.,
Shih H.M., Kung H.J., Chen R.H.;
"Etk, a Btk family tyrosine kinase, mediates cellular transformation
by linking Src to STAT3 activation.";
Mol. Cell. Biol. 20:2043-2054(2000).
[13]
FUNCTION IN IL6 SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY
PTPN2.
PubMed=12359225; DOI=10.1016/S0006-291X(02)02291-X;
Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N.,
Matsuda T.;
"The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates
interleukin-6-mediated signaling pathway through STAT3
dephosphorylation.";
Biochem. Biophys. Res. Commun. 297:811-817(2002).
[14]
INTERACTION WITH NCOA1.
PubMed=11773079; DOI=10.1074/jbc.M111486200;
Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.;
"Functional interaction of STAT3 transcription factor with the
coactivator NcoA/SRC1a.";
J. Biol. Chem. 277:8004-8011(2002).
[15]
INTERACTION WITH HCV CORE PROTEIN.
PubMed=12208879; DOI=10.1084/jem.20012127;
Yoshida T., Hanada T., Tokuhisa T., Kosai K., Sata M., Kohara M.,
Yoshimura A.;
"Activation of STAT3 by the hepatitis C virus core protein leads to
cellular transformation.";
J. Exp. Med. 196:641-653(2002).
[16]
INTERACTION WITH IL23R.
PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699;
Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J.,
Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J.,
O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D.,
Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.;
"A receptor for the heterodimeric cytokine IL-23 is composed of IL-
12Rbeta1 and a novel cytokine receptor subunit, IL-23R.";
J. Immunol. 168:5699-5708(2002).
[17]
FUNCTION IN EGFR SIGNALING, AND INTERACTION WITH EGFR.
PubMed=12873986;
Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.;
"Identification and characterization of signal transducer and
activator of transcription 3 recruitment sites within the epidermal
growth factor receptor.";
Cancer Res. 63:3923-3930(2003).
[18]
PHOSPHORYLATION AT TYR-705 AND SER-727.
PubMed=12763138; DOI=10.1016/S0301-472X(03)00045-6;
Wierenga A.T., Vogelzang I., Eggen B.J., Vellenga E.;
"Erythropoietin-induced serine 727 phosphorylation of STAT3 in
erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent
pathway.";
Exp. Hematol. 31:398-405(2003).
[19]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[20]
FUNCTION, AND INTERACTION WITH IL31RA.
PubMed=15194700; DOI=10.1074/jbc.M401122200;
Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C.,
Hermanns H.M.;
"Characterization of the signaling capacities of the novel gp130-like
cytokine receptor.";
J. Biol. Chem. 279:36112-36120(2004).
[21]
PHOSPHORYLATION AT SER-727 BY IRAK1.
PubMed=15465816; DOI=10.1074/jbc.M410369200;
Huang Y., Li T., Sane D.C., Li L.;
"IRAK1 serves as a novel regulator essential for lipopolysaccharide-
induced interleukin-10 gene expression.";
J. Biol. Chem. 279:51697-51703(2004).
[22]
INTERACTION WITH TMF1.
PubMed=15467733; DOI=10.1038/sj.onc.1208149;
Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S.,
Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.;
"TMF/ARA160 is a BC-box-containing protein that mediates the
degradation of Stat3.";
Oncogene 23:8908-8919(2004).
[23]
INTERACTION WITH PELP1.
PubMed=15994929; DOI=10.1158/0008-5472.CAN-04-4664;
Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.;
"Proline-, glutamic acid-, and leucine-rich protein-1 is essential in
growth factor regulation of signal transducers and activators of
transcription 3 activation.";
Cancer Res. 65:5571-5577(2005).
[24]
PHOSPHORYLATION AT SER-727 BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3,
AND SUBCELLULAR LOCATION.
PubMed=16219639; DOI=10.1093/intimm/dxh331;
Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y.,
Ishida M., Akira S., Matsuda T.;
"Physical and functional interactions between STAT3 and ZIP kinase.";
Int. Immunol. 17:1543-1552(2005).
[25]
INTERACTION WITH SOCS7.
PubMed=15677474; DOI=10.1074/jbc.M411596200;
Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L.,
Gertler A.;
"Suppressor of cytokine signaling 7 inhibits prolactin, growth
hormone, and leptin signaling by interacting with STAT5 or STAT3 and
attenuating their nuclear translocation.";
J. Biol. Chem. 280:13817-13823(2005).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT TYR-704 (ISOFORM DEL-701), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[27]
PHOSPHORYLATION AT TYR-705 BY PTK6.
PubMed=16568091; DOI=10.1038/sj.onc.1209501;
Liu L., Gao Y., Qiu H., Miller W.T., Poli V., Reich N.C.;
"Identification of STAT3 as a specific substrate of breast tumor
kinase.";
Oncogene 25:4904-4912(2006).
[28]
INTERACTION WITH PRKCE, AND PHOSPHORYLATION AT SER-727.
PubMed=17875724; DOI=10.1158/0008-5472.CAN-07-1604;
Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W.,
Oberley T.D., Wilding G., Verma A.K.;
"Protein kinase Cepsilon interacts with signal transducers and
activators of transcription 3 (Stat3), phosphorylates Stat3Ser727, and
regulates its constitutive activation in prostate cancer.";
Cancer Res. 67:8828-8838(2007).
[29]
SUBCELLULAR LOCATION, AND NUCLEAR IMPORT MOTIF.
PubMed=15919823; DOI=10.1073/pnas.0501643102;
Liu L., McBride K.M., Reich N.C.;
"STAT3 nuclear import is independent of tyrosine phosphorylation and
mediated by importin-alpha3.";
Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005).
[30]
FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF 434-GLU-GLU-435 AND
TYR-705.
PubMed=17344214; DOI=10.1074/jbc.M609798200;
Saxena N.K., Vertino P.M., Anania F.A., Sharma D.;
"leptin-induced growth stimulation of breast cancer cells involves
recruitment of histone acetyltransferases and mediator complex to
CYCLIN D1 promoter via activation of Stat3.";
J. Biol. Chem. 282:13316-13325(2007).
[31]
INTERACTION WITH CDK9.
PubMed=17956865; DOI=10.1074/jbc.M706458200;
Hou T., Ray S., Brasier A.R.;
"The functional role of an interleukin 6-inducible CDK9.STAT3 complex
in human gamma-fibrinogen gene expression.";
J. Biol. Chem. 282:37091-37102(2007).
[32]
FUNCTION.
PubMed=18242580; DOI=10.1016/j.bbrc.2007.04.004;
Jiang H., Yu J., Guo H., Song H., Chen S.;
"up-regulation of survivin by leptin/STAT3 signaling in MCF-7 cells.";
Biochem. Biophys. Res. Commun. 368:1-5(2008).
[33]
PHOSPHORYLATION AT SER-727 BY DYRK2.
PubMed=18599021; DOI=10.1016/j.bcp.2008.05.021;
Yoshida K.;
"Role for DYRK family kinases on regulation of apoptosis.";
Biochem. Pharmacol. 76:1389-1394(2008).
[34]
IDENTIFICATION IN A COMPLEX WITH LYN AND PAG1.
PubMed=18070987; DOI=10.1182/blood-2007-05-090985;
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,
van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U.,
Borisch B., Hoessli D.C.;
"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn
tyrosine kinase in human B-NHL rafts.";
Blood 111:2310-2320(2008).
[35]
INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, AND
SUBCELLULAR LOCATION.
PubMed=18234692; DOI=10.1093/intimm/dxm154;
Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
Matsuda T.;
"BART is essential for nuclear retention of STAT3.";
Int. Immunol. 20:395-403(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[39]
INTERACTION WITH FER, AND PHOSPHORYLATION BY FER.
PubMed=19147545; DOI=10.1158/1541-7786.MCR-08-0117;
Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E.,
Aprikian A.G., Chevalier S.;
"The Fer tyrosine kinase cooperates with interleukin-6 to activate
signal transducer and activator of transcription 3 and promote human
prostate cancer cell growth.";
Mol. Cancer Res. 7:142-155(2009).
[40]
INTERACTION WITH BIRC5/SURVIVIN.
PubMed=20826784; DOI=10.1074/jbc.M110.152777;
Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A.,
Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.;
"Acetylation directs survivin nuclear localization to repress STAT3
oncogenic activity.";
J. Biol. Chem. 285:36129-36137(2010).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[43]
PHOSPHORYLATION AT TYR-705 IN RESPONSE TO KIT SIGNALING, AND
PHOSPHORYLATION AT SER-727.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[44]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=23084476; DOI=10.1016/j.molcel.2012.09.013;
Shen S., Niso-Santano M., Adjemian S., Takehara T., Malik S.A.,
Minoux H., Souquere S., Marino G., Lachkar S., Senovilla L.,
Galluzzi L., Kepp O., Pierron G., Maiuri M.C., Hikita H., Kroemer R.,
Kroemer G.;
"Cytoplasmic STAT3 represses autophagy by inhibiting PKR activity.";
Mol. Cell 48:667-680(2012).
[45]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[46]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705; THR-714 AND
SER-727, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-704 (ISOFORM
DEL-701), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[49]
INTERACTION WITH INPP5F, AND MUTAGENESIS OF TYR-705.
PubMed=25476455; DOI=10.1038/srep07330;
Kim H.S., Li A., Ahn S., Song H., Zhang W.;
"Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3
activity and suppresses gliomas tumorigenicity.";
Sci. Rep. 4:7330-7330(2014).
[50]
INTERACTION WITH FGFR4.
PubMed=26675719; DOI=10.1038/nature16449;
Ulaganathan V.K., Sperl B., Rapp U.R., Ullrich A.;
"Germline variant FGFR4 p.G388R exposes a membrane-proximal STAT3
binding site.";
Nature 528:570-574(2015).
[51]
SUBCELLULAR LOCATION, SUBUNIT, ALLYSINE AT LYS-601; LYS-615; LYS-631
AND LYS-685, AND ACETYLATION AT LYS-601; LYS-615; LYS-631; LYS-685 AND
LYS-707.
PubMed=28065600; DOI=10.1016/j.molcel.2016.12.002;
Ma L., Huang C., Wang X.J., Xin D.E., Wang L.S., Zou Q.C., Zhang Y.S.,
Tan M.D., Wang Y.M., Zhao T.C., Chatterjee D., Altura R.A., Wang C.,
Xu Y.S., Yang J.H., Fan Y.S., Han B.H., Si J., Zhang X., Cheng J.,
Chang Z., Chin Y.E.;
"Lysyl oxidase 3 is a dual-specificity enzyme involved in STAT3
deacetylation and deacetylimination modulation.";
Mol. Cell 65:296-309(2017).
[52]
VARIANTS AD-HIES GLN-382; LEU-382; TRP-382; LEU-384; SER-384; GLN-423;
VAL-463 DEL; ASN-611; VAL-621; ILE-622; LEU-637; MET-637; GLN-644 DEL
AND CYS-657.
PubMed=17881745; DOI=10.1056/NEJMoa073687;
Holland S.M., DeLeo F.R., Elloumi H.Z., Hsu A.P., Uzel G., Brodsky N.,
Freeman A.F., Demidowich A., Davis J., Turner M.L., Anderson V.L.,
Darnell D.N., Welch P.A., Kuhns D.B., Frucht D.M., Malech H.L.,
Gallin J.I., Kobayashi S.D., Whitney A.R., Voyich J.M., Musser J.M.,
Woellner C., Schaffer A.A., Puck J.M., Grimbacher B.;
"STAT3 mutations in the hyper-IgE syndrome.";
N. Engl. J. Med. 357:1608-1619(2007).
[53]
VARIANTS AD-HIES GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL,
AND CHARACTERIZATION OF VARIANTS AD-HIES GLN-382; TRP-382; ILE-389;
TYR-437 AND VAL-463 DEL.
PubMed=17676033; DOI=10.1038/nature06096;
Minegishi Y., Saito M., Tsuchiya S., Tsuge I., Takada H., Hara T.,
Kawamura N., Ariga T., Pasic S., Stojkovic O., Metin A.,
Karasuyama H.;
"Dominant-negative mutations in the DNA-binding domain of STAT3 cause
hyper-IgE syndrome.";
Nature 448:1058-1062(2007).
[54]
VARIANT AD-HIES ILE-389.
PubMed=23342295; DOI=10.2500/ar.2012.3.0035;
Crosby K., Swender D., Chernin L., Hafez-Khayyata S., Ochs H.,
Tcheurekdjian H., Hostoffer R.;
"Signal transducer and activator of transcription 3 mutation with
invasive eosinophilic disease.";
Allergy Rhinol. (Providence) 3:E94-E97(2012).
[55]
VARIANTS ADMIO1 ARG-392; LYS-646; ASN-658 AND MET-716, AND INVOLVEMENT
IN ADMIO1.
PubMed=25038750; DOI=10.1038/ng.3040;
Flanagan S.E., Haapaniemi E., Russell M.A., Caswell R.,
Lango Allen H., De Franco E., McDonald T.J., Rajala H., Ramelius A.,
Barton J., Heiskanen K., Heiskanen-Kosma T., Kajosaari M.,
Murphy N.P., Milenkovic T., Seppaenen M., Lernmark A., Mustjoki S.,
Otonkoski T., Kere J., Morgan N.G., Ellard S., Hattersley A.T.;
"Activating germline mutations in STAT3 cause early-onset multi-organ
autoimmune disease.";
Nat. Genet. 46:812-814(2014).
[56]
VARIANTS AD-HIES TRP-382; TYR-395; TYR-425; MET-637 AND CYS-657,
CHARACTERIZATION OF VARIANTS AD-HIES TRP-382; TYR-395; TYR-425;
MET-637 AND CYS-657, AND PHOSPHORYLATION AT TYR-705 AND SER-727.
PubMed=26293184; DOI=10.1111/cge.12658;
Alcantara-Montiel J.C., Staines-Boone T., Lopez-Herrera G.,
Espinosa-Rosales F., Espinosa-Padilla S.E., Hernandez-Rivas R.,
Santos-Argumedo L.;
"Functional characterization of two new STAT3 mutations associated
with hyper-IgE syndrome in a Mexican cohort.";
Clin. Genet. 89:217-221(2016).
[57]
VARIANT ADMIO1 SER-330, AND CHARACTERIZATION OF VARIANT ADMIO1
SER-330.
PubMed=28073828; DOI=10.2337/db16-0867;
Velayos T., Martinez R., Alonso M., Garcia-Etxebarria K., Aguayo A.,
Camarero C., Urrutia I., Martinez de LaPiscina I., Barrio R.,
Santin I., Castano L.;
"An activating mutation in STAT3 results in neonatal diabetes through
reduced insulin synthesis.";
Diabetes 66:1022-1029(2017).
-!- FUNCTION: Signal transducer and transcription activator that
mediates cellular responses to interleukins, KITLG/SCF, LEP and
other growth factors (PubMed:10688651, PubMed:12359225,
PubMed:12873986, PubMed:15194700, PubMed:17344214,
PubMed:18242580, PubMed:23084476). Once activated, recruits
coactivators, such as NCOA1 or MED1, to the promoter region of the
target gene (PubMed:17344214). May mediate cellular responses to
activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). Binds
to the interleukin-6 (IL-6)-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): deacetylation and oxidation of lysine residues by LOXL3,
leads to disrupt STAT3 dimerization and inhibit its transcription
activity (PubMed:28065600). 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
transctivating 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). {ECO:0000250|UniProtKB:P42227,
ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225,
ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580,
ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:28065600}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member (at least STAT1) (PubMed:28065600). 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). Interacts with STAT3; the interaction is
independent of STAT3 TYR-705 phosphorylation status
(PubMed:25476455). Interacts with FGFR4 (PubMed:26675719).
{ECO:0000250|UniProtKB:P42227, ECO:0000250|UniProtKB:P52631,
ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:11773079,
ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:12873986,
ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15467733,
ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:15994929,
ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17875724,
ECO:0000269|PubMed:17956865, ECO:0000269|PubMed:18070987,
ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:19147545,
ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:23084476,
ECO:0000269|PubMed:25476455, ECO:0000269|PubMed:26675719,
ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:9388184}.
-!- SUBUNIT: (Microbial infection) Interacts with HCV core protein.
{ECO:0000269|PubMed:12208879}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-518675, EBI-518675;
Q9DUM3:- (xeno); NbExp=4; IntAct=EBI-518675, EBI-7971837;
O14874:BCKDK; NbExp=2; IntAct=EBI-518675, EBI-1046765;
Q96G01:BICD1; NbExp=2; IntAct=EBI-518675, EBI-1104509;
P51451:BLK; NbExp=5; IntAct=EBI-518675, EBI-2105445;
P51813:BMX; NbExp=6; IntAct=EBI-518675, EBI-696657;
P07384:CAPN1; NbExp=2; IntAct=EBI-518675, EBI-1542113;
P31146:CORO1A; NbExp=2; IntAct=EBI-518675, EBI-1046676;
Q99062:CSF3R; NbExp=4; IntAct=EBI-518675, EBI-7331284;
Q9UER7:DAXX; NbExp=4; IntAct=EBI-518675, EBI-77321;
O95661:DIRAS3; NbExp=3; IntAct=EBI-518675, EBI-6139214;
Q13011:ECH1; NbExp=2; IntAct=EBI-518675, EBI-711968;
P30084:ECHS1; NbExp=3; IntAct=EBI-518675, EBI-719602;
P00533:EGFR; NbExp=14; IntAct=EBI-518675, EBI-297353;
P04626:ERBB2; NbExp=9; IntAct=EBI-518675, EBI-641062;
Q15910:EZH2; NbExp=5; IntAct=EBI-518675, EBI-530054;
Q8TAE8:GADD45GIP1; NbExp=4; IntAct=EBI-518675, EBI-372506;
Q9BVP2:GNL3; NbExp=2; IntAct=EBI-518675, EBI-641642;
Q07666:KHDRBS1; NbExp=2; IntAct=EBI-518675, EBI-1364;
P25791:LMO2; NbExp=3; IntAct=EBI-518675, EBI-739696;
O43318:MAP3K7; NbExp=4; IntAct=EBI-518675, EBI-358684;
P45984:MAPK9; NbExp=2; IntAct=EBI-518675, EBI-713568;
P45984-1:MAPK9; NbExp=3; IntAct=EBI-518675, EBI-713586;
Q8TE76:MORC4; NbExp=2; IntAct=EBI-518675, EBI-3940432;
Q92665:MRPS31; NbExp=2; IntAct=EBI-518675, EBI-720602;
P22736:NR4A1; NbExp=3; IntAct=EBI-518675, EBI-721550;
Q9ULD0:OGDHL; NbExp=2; IntAct=EBI-518675, EBI-3940481;
P06401:PGR; NbExp=3; IntAct=EBI-518675, EBI-78539;
P18031:PTPN1; NbExp=2; IntAct=EBI-518675, EBI-968788;
Q04206:RELA; NbExp=4; IntAct=EBI-518675, EBI-73886;
P07949:RET; NbExp=3; IntAct=EBI-518675, EBI-2480756;
P46781:RPS9; NbExp=2; IntAct=EBI-518675, EBI-351206;
O00570:SOX1; NbExp=2; IntAct=EBI-518675, EBI-2935583;
P08047:SP1; NbExp=4; IntAct=EBI-518675, EBI-298336;
P30626:SRI; NbExp=2; IntAct=EBI-518675, EBI-750459;
P42224:STAT1; NbExp=3; IntAct=EBI-518675, EBI-1057697;
Q06520:SULT2A1; NbExp=2; IntAct=EBI-518675, EBI-3921363;
P43405:SYK; NbExp=6; IntAct=EBI-518675, EBI-78302;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus
{ECO:0000269|PubMed:28065600}. Note=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. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P40763-1; Sequence=Displayed;
Name=Del-701;
IsoId=P40763-2; Sequence=VSP_010474;
Note=Contains a phosphotyrosine at position 704.
{ECO:0000244|PubMed:15592455, ECO:0000244|PubMed:24275569};
Name=3;
IsoId=P40763-3; Sequence=VSP_055918, VSP_055919;
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal
muscle, kidney and pancreas.
-!- 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. Phosphorylation at Tyr-705
by PTK6 or FER leads to an increase of its transcriptional
activity. Dephosphorylation on tyrosine residues by PTPN2
negatively regulates IL6/interleukin-6 signaling.
{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:7701321}.
-!- PTM: Acetylated on lysine residues by CREBBP. 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:28065600}.
-!- 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}.
-!- DISEASE: Hyperimmunoglobulin E recurrent infection syndrome,
autosomal dominant (AD-HIES) [MIM:147060]: A rare disorder of
immunity and connective tissue characterized by immunodeficiency,
chronic eczema, recurrent Staphylococcal infections, increased
serum IgE, 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
mutations 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:28073828}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=STAT3 entry;
URL="https://en.wikipedia.org/wiki/STAT3";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STAT3ID444.html";
-!- WEB RESOURCE: Name=STAT3base; Note=STAT3 mutation db;
URL="http://structure.bmc.lu.se/idbase/STAT3base/";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/stat3/";
-----------------------------------------------------------------------
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EMBL; L29277; AAA58374.1; -; mRNA.
EMBL; AJ012463; CAA10032.1; -; mRNA.
EMBL; JB252046; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK291933; BAF84622.1; -; mRNA.
EMBL; AY572796; AAS66986.1; -; Genomic_DNA.
EMBL; AC087691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60822.1; -; Genomic_DNA.
EMBL; BC000627; AAH00627.1; -; mRNA.
EMBL; BC014482; AAH14482.1; -; mRNA.
EMBL; AF029311; AAB84254.1; -; mRNA.
CCDS; CCDS32656.1; -. [P40763-1]
CCDS; CCDS32657.1; -. [P40763-2]
CCDS; CCDS59288.1; -. [P40763-3]
PIR; A54444; A54444.
RefSeq; NP_003141.2; NM_003150.3. [P40763-2]
RefSeq; NP_644805.1; NM_139276.2. [P40763-1]
RefSeq; NP_998827.1; NM_213662.1. [P40763-3]
RefSeq; XP_005257673.2; XM_005257616.3. [P40763-2]
RefSeq; XP_005257674.2; XM_005257617.3. [P40763-1]
RefSeq; XP_011523447.1; XM_011525145.2. [P40763-1]
RefSeq; XP_011523448.1; XM_011525146.2. [P40763-3]
RefSeq; XP_016880461.1; XM_017024972.1. [P40763-3]
RefSeq; XP_016880464.1; XM_017024975.1. [P40763-2]
UniGene; Hs.463059; -.
PDB; 5AX3; X-ray; 2.98 A; B=571-582.
PDB; 5U5S; NMR; -; B=81-92.
PDBsum; 5AX3; -.
PDBsum; 5U5S; -.
ProteinModelPortal; P40763; -.
SMR; P40763; -.
BioGrid; 112651; 245.
DIP; DIP-33584N; -.
ELM; P40763; -.
IntAct; P40763; 160.
MINT; MINT-146801; -.
STRING; 9606.ENSP00000264657; -.
BindingDB; P40763; -.
ChEMBL; CHEMBL4026; -.
iPTMnet; P40763; -.
PhosphoSitePlus; P40763; -.
BioMuta; STAT3; -.
DMDM; 48429227; -.
EPD; P40763; -.
MaxQB; P40763; -.
PaxDb; P40763; -.
PeptideAtlas; P40763; -.
PRIDE; P40763; -.
DNASU; 6774; -.
Ensembl; ENST00000264657; ENSP00000264657; ENSG00000168610. [P40763-1]
Ensembl; ENST00000404395; ENSP00000384943; ENSG00000168610. [P40763-2]
Ensembl; ENST00000585517; ENSP00000467000; ENSG00000168610. [P40763-3]
Ensembl; ENST00000588969; ENSP00000467985; ENSG00000168610. [P40763-1]
GeneID; 6774; -.
KEGG; hsa:6774; -.
UCSC; uc002hzl.2; human. [P40763-1]
CTD; 6774; -.
DisGeNET; 6774; -.
GeneCards; STAT3; -.
GeneReviews; STAT3; -.
HGNC; HGNC:11364; STAT3.
HPA; CAB003859; -.
HPA; CAB068241; -.
HPA; CAB068242; -.
HPA; HPA001671; -.
HPA; HPA058603; -.
MalaCards; STAT3; -.
MIM; 102582; gene.
MIM; 147060; phenotype.
MIM; 615952; phenotype.
neXtProt; NX_P40763; -.
OpenTargets; ENSG00000168610; -.
Orphanet; 2314; Autosomal dominant hyper-IgE syndrome.
PharmGKB; PA337; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000220792; -.
HOVERGEN; HBG055669; -.
InParanoid; P40763; -.
KO; K04692; -.
OMA; NSMSFAE; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P40763; -.
TreeFam; TF318648; -.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-198745; Signalling to STAT3.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8849474; PTK6 Activates STAT3.
Reactome; R-HSA-8875791; MET activates STAT3.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P40763; -.
SIGNOR; P40763; -.
ChiTaRS; STAT3; human.
GeneWiki; STAT3; -.
GenomeRNAi; 6774; -.
PMAP-CutDB; P40763; -.
PRO; PR:P40763; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000168610; -.
CleanEx; HS_STAT3; -.
ExpressionAtlas; P40763; baseline and differential.
Genevisible; P40763; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IMP:BHF-UCL.
GO; GO:0031730; F:CCR5 chemokine receptor binding; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0004879; F:RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IMP:BHF-UCL.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0032870; P:cellular response to hormone stimulus; IDA:BHF-UCL.
GO; GO:0044320; P:cellular response to leptin stimulus; IDA:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0042755; P:eating behavior; ISS:UniProtKB.
GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; TAS:UniProtKB.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0035278; P:miRNA mediated inhibition of translation; IDA:BHF-UCL.
GO; GO:0006928; P:movement of cell or subcellular component; TAS:ProtInc.
GO; GO:0042789; P:mRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CACAO.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; IEA:Ensembl.
GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; IGI:BHF-UCL.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0044321; P:response to leptin; IDA:UniProtKB.
GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB.
GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR001217; STAT.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_sub.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; Diabetes mellitus; Disease mutation;
DNA-binding; Dwarfism; Host-virus interaction; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 770 Signal transducer and activator of
transcription 3.
/FTId=PRO_0000182417.
DOMAIN 580 670 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOTIF 150 162 Essential for nuclear import.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 601 601 Allysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 601 601 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 615 615 Allysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 615 615 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 631 631 Allysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 631 631 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 685 685 Allysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 685 685 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:28065600}.
MOD_RES 705 705 Phosphotyrosine; by FER and PTK6.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12763138,
ECO:0000269|PubMed:16568091,
ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:26293184}.
MOD_RES 707 707 N6-acetyllysine.
{ECO:0000269|PubMed:28065600}.
MOD_RES 714 714 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 727 727 Phosphoserine; by DYRK2, NLK, NEK6,
IRAK1, RPS6KA5, ZIPK/DAPK3 and PKC/PRKCE.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:12763138,
ECO:0000269|PubMed:15465816,
ECO:0000269|PubMed:16219639,
ECO:0000269|PubMed:17875724,
ECO:0000269|PubMed:18599021,
ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:26293184}.
VAR_SEQ 701 701 Missing (in isoform Del-701).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010474.
VAR_SEQ 716 722 TTCSNTI -> FIDAVWK (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_055918.
VAR_SEQ 723 770 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_055919.
VARIANT 32 32 Q -> K (in dbSNP:rs1803125).
/FTId=VAR_018683.
VARIANT 143 143 M -> I (in dbSNP:rs17878478).
{ECO:0000269|Ref.5}.
/FTId=VAR_018679.
VARIANT 330 330 P -> S (in ADMIO1; increases
transcriptional activity; increases
binding to ISL1 promoter region;
decreases glucose stimulated insulin
secretion).
{ECO:0000269|PubMed:28073828}.
/FTId=VAR_078445.
VARIANT 382 382 R -> L (in AD-HIES; dbSNP:rs113994136).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037365.
VARIANT 382 382 R -> Q (in AD-HIES; loss of function;
dbSNP:rs113994136).
{ECO:0000269|PubMed:17676033,
ECO:0000269|PubMed:17881745}.
/FTId=VAR_037366.
VARIANT 382 382 R -> W (in AD-HIES; loss of function;
reduced DNA-binding ability;
dbSNP:rs113994135).
{ECO:0000269|PubMed:17676033,
ECO:0000269|PubMed:17881745,
ECO:0000269|PubMed:26293184}.
/FTId=VAR_037367.
VARIANT 384 384 F -> L (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037368.
VARIANT 384 384 F -> S (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037369.
VARIANT 389 389 T -> I (in AD-HIES; loss of function;
dbSNP:rs397514766).
{ECO:0000269|PubMed:17676033,
ECO:0000269|PubMed:23342295}.
/FTId=VAR_037370.
VARIANT 392 392 K -> R (in ADMIO1; dbSNP:rs587777648).
{ECO:0000269|PubMed:25038750}.
/FTId=VAR_071885.
VARIANT 395 395 N -> Y (in AD-HIES; unknown pathological
significance; reduced DNA-binding
ability). {ECO:0000269|PubMed:26293184}.
/FTId=VAR_075414.
VARIANT 423 423 R -> Q (in AD-HIES; dbSNP:rs113994137).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037371.
VARIANT 425 425 N -> Y (in AD-HIES; unknown pathological
significance; reduced DNA-binding
ability). {ECO:0000269|PubMed:26293184}.
/FTId=VAR_075415.
VARIANT 437 437 H -> Y (in AD-HIES; loss of function).
{ECO:0000269|PubMed:17676033}.
/FTId=VAR_037372.
VARIANT 463 463 Missing (in AD-HIES; loss of function).
{ECO:0000269|PubMed:17676033,
ECO:0000269|PubMed:17881745}.
/FTId=VAR_037373.
VARIANT 561 561 F -> Y (in dbSNP:rs1064116).
{ECO:0000269|PubMed:7512451}.
/FTId=VAR_037374.
VARIANT 611 611 S -> N (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037375.
VARIANT 621 621 F -> V (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037376.
VARIANT 622 622 T -> I (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037377.
VARIANT 637 637 V -> L (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037378.
VARIANT 637 637 V -> M (in AD-HIES; reduced DNA-binding
ability; dbSNP:rs113994139).
{ECO:0000269|PubMed:17881745,
ECO:0000269|PubMed:26293184}.
/FTId=VAR_037379.
VARIANT 644 644 Missing (in AD-HIES).
{ECO:0000269|PubMed:17881745}.
/FTId=VAR_037380.
VARIANT 646 646 N -> K (in ADMIO1; dbSNP:rs587777649).
{ECO:0000269|PubMed:25038750}.
/FTId=VAR_071886.
VARIANT 657 657 Y -> C (in AD-HIES; reduced DNA-binding
ability; dbSNP:rs193922721).
{ECO:0000269|PubMed:17881745,
ECO:0000269|PubMed:26293184}.
/FTId=VAR_037381.
VARIANT 658 658 K -> N (in ADMIO1; dbSNP:rs587777650).
{ECO:0000269|PubMed:25038750}.
/FTId=VAR_071887.
VARIANT 716 716 T -> M (in ADMIO1; dbSNP:rs869312892).
{ECO:0000269|PubMed:25038750}.
/FTId=VAR_071888.
MUTAGEN 434 435 EE->AA: Inhibits leptin-mediated
transactivation of CCND1 promoter. No
effect on interaction with INPP5F.
{ECO:0000269|PubMed:17344214,
ECO:0000269|PubMed:25476455}.
MUTAGEN 705 705 Y->F: Inhibits leptin-mediated
transactivation of CCND1 promoter.
{ECO:0000269|PubMed:17344214}.
CONFLICT 133 133 T -> A (in Ref. 4; BAF84622).
{ECO:0000305}.
CONFLICT 288 288 Q -> H (in Ref. 1; AAA58374).
{ECO:0000305}.
CONFLICT 460 460 P -> S (in Ref. 1; AAA58374).
{ECO:0000305}.
CONFLICT 548 548 K -> N (in Ref. 1; AAA58374).
{ECO:0000305}.
CONFLICT 652 652 E -> V (in Ref. 4; BAF84622).
{ECO:0000305}.
CONFLICT 667 667 V -> L (in Ref. 1; AAA58374).
{ECO:0000305}.
CONFLICT 730 730 T -> A (in Ref. 1; AAA58374).
{ECO:0000305}.
SEQUENCE 770 AA; 88068 MW; 6C00632211C8012D CRC64;
MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL
LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA
TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK
SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL
ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY
QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN
GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY
NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS
GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM
DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN
TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDME LTSECATSPM


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