ID STAT3_HUMAN Reviewed; 770 AA. AC P40763; A8K7B8; K7ENL3; O14916; Q9BW54; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2004, sequence version 2. DT 29-MAY-2024, entry version 244. DE RecName: Full=Signal transducer and activator of transcription 3 {ECO:0000305}; DE AltName: Full=Acute-phase response factor {ECO:0000303|PubMed:7512451}; GN Name=STAT3 {ECO:0000303|PubMed:9630560, ECO:0000312|HGNC:HGNC:11364}; GN Synonyms=APRF {ECO:0000303|PubMed:7512451}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TYR-561. RC TISSUE=Placenta; RX PubMed=7512451; DOI=10.1016/0092-8674(94)90235-6; RA Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T., RA Yoshida K., Sudo T., Naruto M., Kishimoto T.; RT "Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91- RT related transcription factor involved in the gp130-mediated signaling RT pathway."; RL Cell 77:63-71(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9630560; DOI=10.1016/s0378-1119(98)00185-1; RA Della Pietra L., Bressan A., Pezzotti A., Serlupi-Crescenzi O.; RT "Highly conserved amino-acid sequence between murine STAT3 and a revised RT human STAT3 sequence."; RL Gene 213:119-124(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Feinstein E., Adamsky S., Erlich S., Molitoris B.; RT "Methods for treating chronic kidney disease."; RL Patent number EP2440214, 18-APR-2012. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-143. RG SeattleSNPs variation discovery resource; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DEL-701). RC TISSUE=Kidney, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 564-704. RC TISSUE=Liver; RA Della Pietra L., Bressan A., Pezzotti A.R., Serlupi-Crescenzi O.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [10] RP PHOSPHORYLATION AT SERINE RESIDUES. RX PubMed=7701321; DOI=10.1126/science.7701321; RA Zhang X., Blenis J., Li H.-C., Schindler C., Chen-Kiang S.; RT "Requirement of serine phosphorylation for formation of STAT-promoter RT complexes."; RL Science 267:1990-1994(1995). RN [11] RP INTERACTION WITH PIAS3. RX PubMed=9388184; DOI=10.1126/science.278.5344.1803; RA Chung C.D., Liao J., Liu B., Rao X., Jay P., Berta P., Shuai K.; RT "Specific inhibition of Stat3 signal transduction by PIAS3."; RL Science 278:1803-1805(1997). RN [12] RP PHOSPHORYLATION BY BMX, INTERACTION WITH BMX, AND FUNCTION. RX PubMed=10688651; DOI=10.1128/mcb.20.6.2043-2054.2000; RA Tsai Y.T., Su Y.H., Fang S.S., Huang T.N., Qiu Y., Jou Y.S., Shih H.M., RA Kung H.J., Chen R.H.; RT "Etk, a Btk family tyrosine kinase, mediates cellular transformation by RT linking Src to STAT3 activation."; RL Mol. Cell. Biol. 20:2043-2054(2000). RN [13] RP FUNCTION IN IL6 SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2. RX PubMed=12359225; DOI=10.1016/s0006-291x(02)02291-x; RA Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N., RA Matsuda T.; RT "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates RT interleukin-6-mediated signaling pathway through STAT3 dephosphorylation."; RL Biochem. Biophys. Res. Commun. 297:811-817(2002). RN [14] RP INTERACTION WITH NCOA1. RX PubMed=11773079; DOI=10.1074/jbc.m111486200; RA Giraud S., Bienvenu F., Avril S., Gascan H., Heery D.M., Coqueret O.; RT "Functional interaction of STAT3 transcription factor with the coactivator RT NcoA/SRC1a."; RL J. Biol. Chem. 277:8004-8011(2002). RN [15] RP INTERACTION WITH HCV CORE PROTEIN. RX PubMed=12208879; DOI=10.1084/jem.20012127; RA Yoshida T., Hanada T., Tokuhisa T., Kosai K., Sata M., Kohara M., RA Yoshimura A.; RT "Activation of STAT3 by the hepatitis C virus core protein leads to RT cellular transformation."; RL J. Exp. Med. 196:641-653(2002). RN [16] RP INTERACTION WITH IL23R. RX PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699; RA Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J., RA Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J., RA O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D., RA Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.; RT "A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 RT and a novel cytokine receptor subunit, IL-23R."; RL J. Immunol. 168:5699-5708(2002). RN [17] RP FUNCTION IN EGFR SIGNALING, AND INTERACTION WITH EGFR. RX PubMed=12873986; RA Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.; RT "Identification and characterization of signal transducer and activator of RT transcription 3 recruitment sites within the epidermal growth factor RT receptor."; RL Cancer Res. 63:3923-3930(2003). RN [18] RP PHOSPHORYLATION AT TYR-705 AND SER-727. RX PubMed=12763138; DOI=10.1016/s0301-472x(03)00045-6; RA Wierenga A.T., Vogelzang I., Eggen B.J., Vellenga E.; RT "Erythropoietin-induced serine 727 phosphorylation of STAT3 in erythroid RT cells is mediated by a MEK-, ERK-, and MSK1-dependent pathway."; RL Exp. Hematol. 31:398-405(2003). RN [19] RP FUNCTION, AND INTERACTION WITH IL31RA. RX PubMed=15194700; DOI=10.1074/jbc.m401122200; RA Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.; RT "Characterization of the signaling capacities of the novel gp130-like RT cytokine receptor."; RL J. Biol. Chem. 279:36112-36120(2004). RN [20] RP PHOSPHORYLATION AT SER-727 BY IRAK1. RX PubMed=15465816; DOI=10.1074/jbc.m410369200; RA Huang Y., Li T., Sane D.C., Li L.; RT "IRAK1 serves as a novel regulator essential for lipopolysaccharide-induced RT interleukin-10 gene expression."; RL J. Biol. Chem. 279:51697-51703(2004). RN [21] RP INTERACTION WITH TMF1. RX PubMed=15467733; DOI=10.1038/sj.onc.1208149; RA Perry E., Tsruya R., Levitsky P., Pomp O., Taller M., Weisberg S., RA Parris W., Kulkarni S., Malovani H., Pawson T., Shpungin S., Nir U.; RT "TMF/ARA160 is a BC-box-containing protein that mediates the degradation of RT Stat3."; RL Oncogene 23:8908-8919(2004). RN [22] RP INTERACTION WITH PELP1. RX PubMed=15994929; DOI=10.1158/0008-5472.can-04-4664; RA Manavathi B., Nair S.S., Wang R.-A., Kumar R., Vadlamudi R.K.; RT "Proline-, glutamic acid-, and leucine-rich protein-1 is essential in RT growth factor regulation of signal transducers and activators of RT transcription 3 activation."; RL Cancer Res. 65:5571-5577(2005). RN [23] RP FUNCTION, SUBCELLULAR LOCATION, ACETYLATION AT LYS-49 AND LYS-87, AND RP MUTAGENESIS OF LYS-49 AND LYS-87. RX PubMed=16285960; DOI=10.1053/j.gastro.2005.07.055; RA Ray S., Boldogh I., Brasier A.R.; RT "STAT3 NH2-terminal acetylation is activated by the hepatic acute-phase RT response and required for IL-6 induction of angiotensinogen."; RL Gastroenterology 129:1616-1632(2005). RN [24] RP PHOSPHORYLATION AT SER-727 BY ZIPK/DAPK3, INTERACTION WITH ZIPK/DAPK3, AND RP SUBCELLULAR LOCATION. RX PubMed=16219639; DOI=10.1093/intimm/dxh331; RA Sato N., Kawai T., Sugiyama K., Muromoto R., Imoto S., Sekine Y., RA Ishida M., Akira S., Matsuda T.; RT "Physical and functional interactions between STAT3 and ZIP kinase."; RL Int. Immunol. 17:1543-1552(2005). RN [25] RP INTERACTION WITH SOCS7. RX PubMed=15677474; DOI=10.1074/jbc.m411596200; RA Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L., Gertler A.; RT "Suppressor of cytokine signaling 7 inhibits prolactin, growth hormone, and RT leptin signaling by interacting with STAT5 or STAT3 and attenuating their RT nuclear translocation."; RL J. Biol. Chem. 280:13817-13823(2005). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT TYR-704 (ISOFORM DEL-701), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [27] RP SUBCELLULAR LOCATION, AND NUCLEAR IMPORT MOTIF. RX PubMed=15919823; DOI=10.1073/pnas.0501643102; RA Liu L., McBride K.M., Reich N.C.; RT "STAT3 nuclear import is independent of tyrosine phosphorylation and RT mediated by importin-alpha3."; RL Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005). RN [28] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, ACETYLATION AT LYS-685, AND RP MUTAGENESIS OF LYS-685. RX PubMed=15653507; DOI=10.1126/science.1105166; RA Yuan Z.L., Guan Y.J., Chatterjee D., Chin Y.E.; RT "Stat3 dimerization regulated by reversible acetylation of a single lysine RT residue."; RL Science 307:269-273(2005). RN [29] RP PHOSPHORYLATION AT TYR-705 BY PTK6. RX PubMed=16568091; DOI=10.1038/sj.onc.1209501; RA Liu L., Gao Y., Qiu H., Miller W.T., Poli V., Reich N.C.; RT "Identification of STAT3 as a specific substrate of breast tumor kinase."; RL Oncogene 25:4904-4912(2006). RN [30] RP INTERACTION WITH PRKCE, AND PHOSPHORYLATION AT SER-727. RX PubMed=17875724; DOI=10.1158/0008-5472.can-07-1604; RA Aziz M.H., Manoharan H.T., Church D.R., Dreckschmidt N.E., Zhong W., RA Oberley T.D., Wilding G., Verma A.K.; RT "Protein kinase Cepsilon interacts with signal transducers and activators RT of transcription 3 (Stat3), phosphorylates Stat3Ser727, and regulates its RT constitutive activation in prostate cancer."; RL Cancer Res. 67:8828-8838(2007). RN [31] RP FUNCTION, PHOSPHORYLATION, AND MUTAGENESIS OF 434-GLU-GLU-435 AND TYR-705. RX PubMed=17344214; DOI=10.1074/jbc.m609798200; RA Saxena N.K., Vertino P.M., Anania F.A., Sharma D.; RT "leptin-induced growth stimulation of breast cancer cells involves RT recruitment of histone acetyltransferases and mediator complex to CYCLIN D1 RT promoter via activation of Stat3."; RL J. Biol. Chem. 282:13316-13325(2007). RN [32] RP INTERACTION WITH CDK9. RX PubMed=17956865; DOI=10.1074/jbc.m706458200; RA Hou T., Ray S., Brasier A.R.; RT "The functional role of an interleukin 6-inducible CDK9.STAT3 complex in RT human gamma-fibrinogen gene expression."; RL J. Biol. Chem. 282:37091-37102(2007). RN [33] RP FUNCTION. RX PubMed=18242580; DOI=10.1016/j.bbrc.2007.04.004; RA Jiang H., Yu J., Guo H., Song H., Chen S.; RT "up-regulation of survivin by leptin/STAT3 signaling in MCF-7 cells."; RL Biochem. Biophys. Res. Commun. 368:1-5(2008). RN [34] RP PHOSPHORYLATION AT SER-727 BY DYRK2. RX PubMed=18599021; DOI=10.1016/j.bcp.2008.05.021; RA Yoshida K.; RT "Role for DYRK family kinases on regulation of apoptosis."; RL Biochem. Pharmacol. 76:1389-1394(2008). RN [35] RP IDENTIFICATION IN A COMPLEX WITH LYN AND PAG1. RX PubMed=18070987; DOI=10.1182/blood-2007-05-090985; RA Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., RA van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., RA Hoessli D.C.; RT "Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine RT kinase in human B-NHL rafts."; RL Blood 111:2310-2320(2008). RN [36] RP INTERACTION WITH ARL2BP, PHOSPHORYLATION AT SERINE RESIDUES, AND RP SUBCELLULAR LOCATION. RX PubMed=18234692; DOI=10.1093/intimm/dxm154; RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N., RA Matsuda T.; RT "BART is essential for nuclear retention of STAT3."; RL Int. Immunol. 20:395-403(2008). RN [37] RP FUNCTION, INTERACTION WITH EP300, ACETYLATION AT LYS-49 AND LYS-87, AND RP MUTAGENESIS OF LYS-49 AND LYS-87. RX PubMed=18782771; DOI=10.1074/jbc.m805941200; RA Hou T., Ray S., Lee C., Brasier A.R.; RT "The STAT3 NH2-terminal domain stabilizes enhanceosome assembly by RT interacting with the p300 bromodomain."; RL J. Biol. Chem. 283:30725-30734(2008). RN [38] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [41] RP INTERACTION WITH FER, AND PHOSPHORYLATION BY FER. RX PubMed=19147545; DOI=10.1158/1541-7786.mcr-08-0117; RA Zoubeidi A., Rocha J., Zouanat F.Z., Hamel L., Scarlata E., Aprikian A.G., RA Chevalier S.; RT "The Fer tyrosine kinase cooperates with interleukin-6 to activate signal RT transducer and activator of transcription 3 and promote human prostate RT cancer cell growth."; RL Mol. Cancer Res. 7:142-155(2009). RN [42] RP INTERACTION WITH BIRC5/SURVIVIN. RX PubMed=20826784; DOI=10.1074/jbc.m110.152777; RA Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A., RA Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.; RT "Acetylation directs survivin nuclear localization to repress STAT3 RT oncogenic activity."; RL J. Biol. Chem. 285:36129-36137(2010). RN [43] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [44] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [45] RP PHOSPHORYLATION AT TYR-705 IN RESPONSE TO KIT SIGNALING, AND RP PHOSPHORYLATION AT SER-727. RX PubMed=21135090; DOI=10.1074/jbc.m110.182642; RA Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.; RT "Mechanisms of STAT protein activation by oncogenic KIT mutants in RT neoplastic mast cells."; RL J. Biol. Chem. 286:5956-5966(2011). RN [46] RP FUNCTION, AND PHOSPHORYLATION AT TYR-705. RX PubMed=22306293; DOI=10.1016/j.molcel.2012.01.001; RA Gao X., Wang H., Yang J.J., Liu X., Liu Z.R.; RT "Pyruvate kinase M2 regulates gene transcription by acting as a protein RT kinase."; RL Mol. Cell 45:598-609(2012). RN [47] RP FUNCTION, AND INTERACTION WITH EIF2AK2. RX PubMed=23084476; DOI=10.1016/j.molcel.2012.09.013; RA Shen S., Niso-Santano M., Adjemian S., Takehara T., Malik S.A., Minoux H., RA Souquere S., Marino G., Lachkar S., Senovilla L., Galluzzi L., Kepp O., RA Pierron G., Maiuri M.C., Hikita H., Kroemer R., Kroemer G.; RT "Cytoplasmic STAT3 represses autophagy by inhibiting PKR activity."; RL Mol. Cell 48:667-680(2012). RN [48] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [49] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [50] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705; THR-714 AND SER-727, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-704 (ISOFORM DEL-701), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [52] RP INTERACTION WITH INPP5F, AND MUTAGENESIS OF TYR-705. RX PubMed=25476455; DOI=10.1038/srep07330; RA Kim H.S., Li A., Ahn S., Song H., Zhang W.; RT "Inositol Polyphosphate-5-Phosphatase F (INPP5F) inhibits STAT3 activity RT and suppresses gliomas tumorigenicity."; RL Sci. Rep. 4:7330-7330(2014). RN [53] RP INTERACTION WITH FGFR4. RX PubMed=26675719; DOI=10.1038/nature16449; RA Ulaganathan V.K., Sperl B., Rapp U.R., Ullrich A.; RT "Germline variant FGFR4 p.G388R exposes a membrane-proximal STAT3 binding RT site."; RL Nature 528:570-574(2015). RN [54] RP INTERACTION WITH HHV-5 IMMEDIATE EARLY PROTEIN IE1 (MICROBIAL INFECTION). RX PubMed=27387064; DOI=10.1371/journal.ppat.1005748; RA Harwardt T., Lukas S., Zenger M., Reitberger T., Danzer D., Uebner T., RA Munday D.C., Nevels M., Paulus C.; RT "Human Cytomegalovirus Immediate-Early 1 Protein Rewires Upstream STAT3 to RT Downstream STAT1 Signaling Switching an IL6-Type to an IFNgamma-Like RT Response."; RL PLoS Pathog. 12:e1005748-e1005748(2016). RN [55] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, ALLYSINE AT LYS-601; LYS-615; RP LYS-631 AND LYS-685, AND ACETYLATION AT LYS-601; LYS-615; LYS-631; LYS-685 RP AND LYS-707. RX PubMed=28065600; DOI=10.1016/j.molcel.2016.12.002; RA Ma L., Huang C., Wang X.J., Xin D.E., Wang L.S., Zou Q.C., Zhang Y.S., RA Tan M.D., Wang Y.M., Zhao T.C., Chatterjee D., Altura R.A., Wang C., RA Xu Y.S., Yang J.H., Fan Y.S., Han B.H., Si J., Zhang X., Cheng J., RA Chang Z., Chin Y.E.; RT "Lysyl oxidase 3 is a dual-specificity enzyme involved in STAT3 RT deacetylation and deacetylimination modulation."; RL Mol. Cell 65:296-309(2017). RN [56] {ECO:0007744|PDB:5U5S} RP STRUCTURE BY NMR OF 81-92 IN COMPLEX WITH BRD2, FUNCTION, ACETYLATION AT RP LYS-87, AND INTERACTION WITH BRD2. RX PubMed=28262505; DOI=10.1016/j.molcel.2016.12.022; RA Cheung K.L., Zhang F., Jaganathan A., Sharma R., Zhang Q., Konuma T., RA Shen T., Lee J.Y., Ren C., Chen C.H., Lu G., Olson M.R., Zhang W., RA Kaplan M.H., Littman D.R., Walsh M.J., Xiong H., Zeng L., Zhou M.M.; RT "Distinct roles of Brd2 and Brd4 in potentiating the transcriptional RT program for th17 cell differentiation."; RL Mol. Cell 65:1068-1080(2017). RN [57] RP INTERACTION WITH S.TYPHIMURIUM SARA (MICROBIAL INFECTION), AND RP PHOSPHORYLATION AT TYR-705 (MICROBIAL INFECTION). RX PubMed=29924996; DOI=10.1016/j.celrep.2018.05.072; RA Jaslow S.L., Gibbs K.D., Fricke W.F., Wang L., Pittman K.J., Mammel M.K., RA Thaden J.T., Fowler V.G. Jr., Hammer G.E., Elfenbein J.R., Ko D.C.; RT "Salmonella Activation of STAT3 Signaling by SarA Effector Promotes RT Intracellular Replication and Production of IL-10."; RL Cell Rep. 23:3525-3536(2018). RN [58] RP RETRACTED PAPER. RX PubMed=31462771; DOI=10.1038/s41586-019-1511-x; RA Niu J., Sun Y., Chen B., Zheng B., Jarugumilli G.K., Walker S.R., RA Hata A.N., Mino-Kenudson M., Frank D.A., Wu X.; RT "Fatty acids and cancer-amplified ZDHHC19 promote STAT3 activation through RT S-palmitoylation."; RL Nature 573:139-143(2019). RN [59] RP RETRACTION NOTICE OF PUBMED:31462771. RX PubMed=32555452; DOI=10.1038/s41586-020-2414-6; RA Niu J., Sun Y., Chen B., Zheng B., Jarugumilli G.K., Walker S.R., RA Hata A.N., Mino-Kenudson M., Frank D.A., Wu X.; RL Nature 583:154-154(2020). RN [60] RP FUNCTION, INTERACTION WITH CD274, AND PHOSPHORYLATION AT TYR-705. RX PubMed=32929201; DOI=10.1038/s41556-020-0575-z; RA Hou J., Zhao R., Xia W., Chang C.W., You Y., Hsu J.M., Nie L., Chen Y., RA Wang Y.C., Liu C., Wang W.J., Wu Y., Ke B., Hsu J.L., Huang K., Ye Z., RA Yang Y., Xia X., Li Y., Li C.W., Shao B., Tainer J.A., Hung M.C.; RT "PD-L1-mediated gasdermin C expression switches apoptosis to pyroptosis in RT cancer cells and facilitates tumour necrosis."; RL Nat. Cell Biol. 22:1264-1275(2020). RN [61] RP SUBCELLULAR LOCATION, INTERACTION WITH PHB, PHOSPHORYLATION AT TYR-705 AND RP SER-727, AND TISSUE SPECIFICITY. RX PubMed=31899195; DOI=10.1016/j.imlet.2019.12.008; RA Zhang J., Sun Z., Wu Q., Shen J.; RT "Prohibitin 1 interacts with signal transducer and activator of RT transcription 3 in T-helper 17 cells."; RL Immunol. Lett. 219:8-14(2020). RN [62] RP IDENTIFICATION IN A COMPLEX WITH SLC39A6 AND SLC39A10. RX PubMed=32797246; DOI=10.1007/s00018-020-03616-6; RA Nimmanon T., Ziliotto S., Ogle O., Burt A., Gee J.M.W., Andrews G.K., RA Kille P., Hogstrand C., Maret W., Taylor K.M.; RT "The ZIP6/ZIP10 heteromer is essential for the zinc-mediated trigger of RT mitosis."; RL Cell. Mol. Life Sci. 78:1781-1798(2021). RN [63] RP VARIANTS HIES1 GLN-382; LEU-382; TRP-382; LEU-384; SER-384; GLN-423; RP VAL-463 DEL; ASN-611; VAL-621; ILE-622; LEU-637; MET-637; GLN-644 DEL AND RP CYS-657. RX PubMed=17881745; DOI=10.1056/nejmoa073687; RA Holland S.M., DeLeo F.R., Elloumi H.Z., Hsu A.P., Uzel G., Brodsky N., RA Freeman A.F., Demidowich A., Davis J., Turner M.L., Anderson V.L., RA Darnell D.N., Welch P.A., Kuhns D.B., Frucht D.M., Malech H.L., RA Gallin J.I., Kobayashi S.D., Whitney A.R., Voyich J.M., Musser J.M., RA Woellner C., Schaffer A.A., Puck J.M., Grimbacher B.; RT "STAT3 mutations in the hyper-IgE syndrome."; RL N. Engl. J. Med. 357:1608-1619(2007). RN [64] RP VARIANTS HIES1 GLN-382; TRP-382; ILE-389; TYR-437 AND VAL-463 DEL, AND RP CHARACTERIZATION OF VARIANTS HIES1 GLN-382; TRP-382; ILE-389; TYR-437 AND RP VAL-463 DEL. RX PubMed=17676033; DOI=10.1038/nature06096; RA Minegishi Y., Saito M., Tsuchiya S., Tsuge I., Takada H., Hara T., RA Kawamura N., Ariga T., Pasic S., Stojkovic O., Metin A., Karasuyama H.; RT "Dominant-negative mutations in the DNA-binding domain of STAT3 cause RT hyper-IgE syndrome."; RL Nature 448:1058-1062(2007). RN [65] RP VARIANT HIES1 ILE-389. RX PubMed=23342295; DOI=10.2500/ar.2012.3.0035; RA Crosby K., Swender D., Chernin L., Hafez-Khayyata S., Ochs H., RA Tcheurekdjian H., Hostoffer R.; RT "Signal transducer and activator of transcription 3 mutation with invasive RT eosinophilic disease."; RL Allergy Rhinol. (Providence) 3:E94-E97(2012). RN [66] RP VARIANTS ADMIO1 ARG-392; LYS-646; ASN-658 AND MET-716, AND INVOLVEMENT IN RP ADMIO1. RX PubMed=25038750; DOI=10.1038/ng.3040; RA Flanagan S.E., Haapaniemi E., Russell M.A., Caswell R., Lango Allen H., RA De Franco E., McDonald T.J., Rajala H., Ramelius A., Barton J., RA Heiskanen K., Heiskanen-Kosma T., Kajosaari M., Murphy N.P., Milenkovic T., RA Seppaenen M., Lernmark A., Mustjoki S., Otonkoski T., Kere J., Morgan N.G., RA Ellard S., Hattersley A.T.; RT "Activating germline mutations in STAT3 cause early-onset multi-organ RT autoimmune disease."; RL Nat. Genet. 46:812-814(2014). RN [67] RP VARIANTS HIES1 TRP-382; TYR-395; TYR-425; MET-637 AND CYS-657, RP CHARACTERIZATION OF VARIANTS HIES1 TRP-382; TYR-395; TYR-425; MET-637 AND RP CYS-657, AND PHOSPHORYLATION AT TYR-705 AND SER-727. RX PubMed=26293184; DOI=10.1111/cge.12658; RA Alcantara-Montiel J.C., Staines-Boone T., Lopez-Herrera G., RA Espinosa-Rosales F., Espinosa-Padilla S.E., Hernandez-Rivas R., RA Santos-Argumedo L.; RT "Functional characterization of two new STAT3 mutations associated with RT hyper-IgE syndrome in a Mexican cohort."; RL Clin. Genet. 89:217-221(2016). RN [68] RP VARIANT ADMIO1 SER-330, AND CHARACTERIZATION OF VARIANT ADMIO1 SER-330. RX PubMed=28073828; DOI=10.2337/db16-0867; RA Velayos T., Martinez R., Alonso M., Garcia-Etxebarria K., Aguayo A., RA Camarero C., Urrutia I., Martinez de LaPiscina I., Barrio R., Santin I., RA Castano L.; RT "An activating mutation in STAT3 results in neonatal diabetes through RT reduced insulin synthesis."; RL Diabetes 66:1022-1029(2017). CC -!- FUNCTION: Signal transducer and transcription activator that mediates CC cellular responses to interleukins, KITLG/SCF, LEP and other growth CC factors (PubMed:10688651, PubMed:12359225, PubMed:12873986, CC PubMed:15194700, PubMed:15653507, PubMed:16285960, PubMed:17344214, CC PubMed:18242580, PubMed:18782771, PubMed:22306293, PubMed:23084476, CC PubMed:28262505, PubMed:32929201). Once activated, recruits CC coactivators, such as NCOA1 or MED1, to the promoter region of the CC target gene (PubMed:15653507, PubMed:16285960, PubMed:17344214, CC PubMed:18782771, PubMed:28262505, PubMed:32929201). May mediate CC cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 CC (PubMed:12873986). Upon activation of IL6ST/gp130 signaling by CC interleukin-6 (IL6), binds to the IL6-responsive elements identified in CC the promoters of various acute-phase protein genes (PubMed:12359225). CC Activated by IL31 through IL31RA (PubMed:15194700). Acts as a regulator CC of inflammatory response by regulating differentiation of naive CD4(+) CC T-cells into T-helper Th17 or regulatory T-cells (Treg): acetylation CC promotes its transcription activity and cell differentiation while CC deacetylation and oxidation of lysine residues by LOXL3 inhibits CC differentiation (PubMed:28065600, PubMed:28262505). Involved in cell CC cycle regulation by inducing the expression of key genes for the CC progression from G1 to S phase, such as CCND1 (PubMed:17344214). CC Mediates the effects of LEP on melanocortin production, body energy CC homeostasis and lactation (By similarity). May play an apoptotic role CC by transctivating BIRC5 expression under LEP activation CC (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by CC inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role CC in basal beta cell functions, such as regulation of insulin secretion CC (By similarity). Following JAK/STAT signaling activation and as part of CC a complex with NFATC3 and NFATC4, binds to the alpha-beta E4 promoter CC region of CRYAB and activates transcription in cardiomyocytes (By CC similarity). {ECO:0000250|UniProtKB:P42227, CC ECO:0000269|PubMed:10688651, ECO:0000269|PubMed:12359225, CC ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, CC ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960, CC ECO:0000269|PubMed:17344214, ECO:0000269|PubMed:18242580, CC ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:22306293, CC ECO:0000269|PubMed:23084476, ECO:0000269|PubMed:28065600, CC ECO:0000269|PubMed:28262505, ECO:0000269|PubMed:32929201}. CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family CC member (at least STAT1) (PubMed:15653507, PubMed:28065600). Component CC of a promoter-binding complex composed of STAT3, NFATC3 and NFATC4; CC complex formation is enhanced by calcineurin (By similarity). Interacts CC with IL31RA, NCOA1, PELP1, SIPAR, SOCS7, STATIP1 and TMF1 (By CC similarity) (PubMed:15194700, PubMed:15467733, PubMed:15677474, CC PubMed:15994929, PubMed:17344214). Interacts with IL23R in presence of CC IL23 (PubMed:12023369). Interacts (via SH2 domain) with NLK. Interacts CC with ARL2BP; the interaction is enhanced by LIF and JAK1 expression (By CC similarity). Interacts with KPNA4 and KPNA5; KPNA4 may be the primary CC mediator of nuclear import (By similarity). Interacts with CAV2; the CC interaction is increased on insulin-induced tyrosine phosphorylation of CC CAV2 and leads to STAT3 activation (By similarity). Interacts with CC ARL2BP; interaction is enhanced with ARL2 (PubMed:18234692). Interacts CC with NEK6 (By similarity). Binds to CDK9 when activated and nuclear CC (PubMed:17956865). Interacts with BMX (PubMed:10688651). Interacts with CC ZIPK/DAPK3 (PubMed:16219639). Interacts with PIAS3; the interaction CC occurs on stimulation by IL6, CNTF or OSM and inhibits the DNA binding CC activity of STAT3 (PubMed:9388184). In prostate cancer cells, interacts CC with PRKCE and promotes DNA binding activity of STAT3 CC (PubMed:17875724). Interacts with STMN3, antagonizing its microtubule- CC destabilizing activity (By similarity). Interacts with the 'Lys-129' CC acetylated form of BIRC5/survivin (PubMed:20826784). Interacts with FER CC (PubMed:19147545). Interacts (via SH2 domain) with EIF2AK2/PKR (via the CC kinase catalytic domain) (PubMed:23084476). Interacts with INPP5F; the CC interaction is independent of STAT3 Tyr-705 phosphorylation status CC (PubMed:25476455). Interacts with FGFR4 (PubMed:26675719). Interacts CC with OCAD1 (By similarity). Interacts (unphosphorylated or CC phosphorylated at Ser-727) with PHB1 (PubMed:31899195). Interacts and CC may form heterodimers with NHLH1 (By similarity). Found in a complex CC with SLC39A6, SLC39A10 and with the 'Ser-727' phosphorylated form of CC STAT3 throughout mitosis (PubMed:32797246). Interacts (when CC phosphorylated at Tyr-705) with CD274/PD-L1; promoting nuclear CC translocation of CD274/PD-L1 (PubMed:32929201). Interacts (when CC acetylated) with EP300 (via bromo domain); interaction takes place CC following STAT3 acetylation by EP300 and promotes enhanceosome assembly CC (PubMed:18782771). Interacts (when acetylated) with BRD2 (via bromo CC domain); interaction promotes STAT3 recruitment to chromatin and T- CC helper Th17 cell differentiation (PubMed:28262505). Interacts with CC FAM220A/SIPAR; the interaction occurs in both the nucleus and the CC cytoplasm, is enhanced by IL6 and promotes STAT3 dephosphorylation (By CC similarity). Interacts in both unphosphorylated and phosphorylated CC forms with FAM220A but interacts preferentially in the phosphorylated CC form in the nucleus (By similarity). Interacts with PTPN2; the CC interaction is promoted by FAM220A and leads to STAT3 dephosphorylation CC which negatively regulates STAT3 transcriptional activator activity (By CC similarity). {ECO:0000250|UniProtKB:P42227, CC ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:10688651, CC ECO:0000269|PubMed:11773079, ECO:0000269|PubMed:12023369, CC ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15194700, CC ECO:0000269|PubMed:15467733, ECO:0000269|PubMed:15653507, CC ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:15994929, CC ECO:0000269|PubMed:16219639, ECO:0000269|PubMed:17344214, CC ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:17956865, CC ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18234692, CC ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:19147545, CC ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:23084476, CC ECO:0000269|PubMed:25476455, ECO:0000269|PubMed:26675719, CC ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:28262505, CC ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:32797246, CC ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:9388184}. CC -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein. CC {ECO:0000269|PubMed:12208879}. CC -!- SUBUNIT: (Microbial infection) Interacts with S.typhimurium SarA. CC {ECO:0000269|PubMed:29924996}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC (HHV-5) immediate early protein IE1; this interaction leads to STAT3 CC nuclear accumulation and disruption of IL6-induced STAT3 CC phosphorylation. {ECO:0000269|PubMed:27387064}. CC -!- INTERACTION: CC P40763; O14874: BCKDK; NbExp=2; IntAct=EBI-518675, EBI-1046765; CC P40763; Q96G01: BICD1; NbExp=2; IntAct=EBI-518675, EBI-1104509; CC P40763; P51451: BLK; NbExp=9; IntAct=EBI-518675, EBI-2105445; CC P40763; P51813: BMX; NbExp=8; IntAct=EBI-518675, EBI-696657; CC P40763; P07384: CAPN1; NbExp=2; IntAct=EBI-518675, EBI-1542113; CC P40763; P50750: CDK9; NbExp=2; IntAct=EBI-518675, EBI-1383449; CC P40763; P31146: CORO1A; NbExp=2; IntAct=EBI-518675, EBI-1046676; CC P40763; Q99062: CSF3R; NbExp=4; IntAct=EBI-518675, EBI-7331284; CC P40763; Q9UER7: DAXX; NbExp=4; IntAct=EBI-518675, EBI-77321; CC P40763; O95661: DIRAS3; NbExp=3; IntAct=EBI-518675, EBI-6139214; CC P40763; Q13011: ECH1; NbExp=2; IntAct=EBI-518675, EBI-711968; CC P40763; P30084: ECHS1; NbExp=3; IntAct=EBI-518675, EBI-719602; CC P40763; P00533: EGFR; NbExp=15; IntAct=EBI-518675, EBI-297353; CC P40763; P04626: ERBB2; NbExp=9; IntAct=EBI-518675, EBI-641062; CC P40763; Q15910: EZH2; NbExp=5; IntAct=EBI-518675, EBI-530054; CC P40763; Q8TAE8: GADD45GIP1; NbExp=4; IntAct=EBI-518675, EBI-372506; CC P40763; Q9BVP2: GNL3; NbExp=2; IntAct=EBI-518675, EBI-641642; CC P40763; P12268: IMPDH2; NbExp=3; IntAct=EBI-518675, EBI-353389; CC P40763; P23458: JAK1; NbExp=2; IntAct=EBI-518675, EBI-1383438; CC P40763; Q07666: KHDRBS1; NbExp=2; IntAct=EBI-518675, EBI-1364; CC P40763; P25791: LMO2; NbExp=3; IntAct=EBI-518675, EBI-739696; CC P40763; O43318: MAP3K7; NbExp=4; IntAct=EBI-518675, EBI-358684; CC P40763; O15264: MAPK13; NbExp=2; IntAct=EBI-518675, EBI-2116951; CC P40763; P45984: MAPK9; NbExp=2; IntAct=EBI-518675, EBI-713568; CC P40763; P45984-1: MAPK9; NbExp=3; IntAct=EBI-518675, EBI-713586; CC P40763; Q8TE76: MORC4; NbExp=2; IntAct=EBI-518675, EBI-3940432; CC P40763; Q92665: MRPS31; NbExp=2; IntAct=EBI-518675, EBI-720602; CC P40763; Q16236: NFE2L2; NbExp=5; IntAct=EBI-518675, EBI-2007911; CC P40763; Q14938-3: NFIX; NbExp=3; IntAct=EBI-518675, EBI-20559045; CC P40763; Q14938-4: NFIX; NbExp=3; IntAct=EBI-518675, EBI-20558886; CC P40763; P22736: NR4A1; NbExp=3; IntAct=EBI-518675, EBI-721550; CC P40763; Q9ULD0: OGDHL; NbExp=2; IntAct=EBI-518675, EBI-3940481; CC P40763; P06401: PGR; NbExp=3; IntAct=EBI-518675, EBI-78539; CC P40763; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-518675, EBI-11956563; CC P40763; P32119: PRDX2; NbExp=4; IntAct=EBI-518675, EBI-1266300; CC P40763; P18031: PTPN1; NbExp=2; IntAct=EBI-518675, EBI-968788; CC P40763; Q04206: RELA; NbExp=4; IntAct=EBI-518675, EBI-73886; CC P40763; P07949: RET; NbExp=3; IntAct=EBI-518675, EBI-2480756; CC P40763; O75116: ROCK2; NbExp=3; IntAct=EBI-518675, EBI-366288; CC P40763; P46781: RPS9; NbExp=2; IntAct=EBI-518675, EBI-351206; CC P40763; O00570: SOX1; NbExp=2; IntAct=EBI-518675, EBI-2935583; CC P40763; P08047: SP1; NbExp=4; IntAct=EBI-518675, EBI-298336; CC P40763; P30626: SRI; NbExp=3; IntAct=EBI-518675, EBI-750459; CC P40763; P42224: STAT1; NbExp=8; IntAct=EBI-518675, EBI-1057697; CC P40763; P40763: STAT3; NbExp=8; IntAct=EBI-518675, EBI-518675; CC P40763; Q06520: SULT2A1; NbExp=2; IntAct=EBI-518675, EBI-3921363; CC P40763; P43405: SYK; NbExp=10; IntAct=EBI-518675, EBI-78302; CC P40763; Q810M5: Zdhhc19; Xeno; NbExp=4; IntAct=EBI-518675, EBI-22225085; CC P40763; Q9DUM3; Xeno; NbExp=4; IntAct=EBI-518675, EBI-7971837; CC P40763-2; P05067: APP; NbExp=3; IntAct=EBI-10692009, EBI-77613; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15653507, CC ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:28065600, CC ECO:0000269|PubMed:31899195}. Nucleus {ECO:0000269|PubMed:15653507, CC ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:28065600, CC ECO:0000269|PubMed:31899195}. Note=Shuttles between the nucleus and the CC cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation CC and dimerization, in response to signaling by activated FGFR1, FGFR2, CC FGFR3 or FGFR4 (PubMed:15653507, PubMed:16285960). Constitutive nuclear CC presence is independent of tyrosine phosphorylation. Predominantly CC present in the cytoplasm without stimuli. Upon leukemia inhibitory CC factor (LIF) stimulation, accumulates in the nucleus. The complex CC composed of BART and ARL2 plays an important role in the nuclear CC translocation and retention of STAT3. Identified in a complex with LYN CC and PAG1. Translocates to the nucleus in the presence of EDN1 (By CC similarity). {ECO:0000250|UniProtKB:P52631, CC ECO:0000269|PubMed:15653507, ECO:0000269|PubMed:16285960}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P40763-1; Sequence=Displayed; CC Name=Del-701; CC IsoId=P40763-2; Sequence=VSP_010474; CC Name=3; CC IsoId=P40763-3; Sequence=VSP_055918, VSP_055919; CC -!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal CC muscle, kidney and pancreas. Expressed in naive CD4(+) T cells as well CC as T-helper Th17, Th1 and Th2 cells (PubMed:31899195). CC {ECO:0000269|PubMed:31899195}. CC -!- PTM: Tyrosine phosphorylated upon stimulation with EGF. Tyrosine CC phosphorylated in response to constitutively activated FGFR1, FGFR2, CC FGFR3 and FGFR4 (By similarity). Activated through tyrosine CC phosphorylation by BMX. Tyrosine phosphorylated in response to IL6, CC IL11, LIF, CNTF, KITLG/SCF, CSF1, EGF, PDGF, IFN-alpha, LEP and OSM. CC Activated KIT promotes phosphorylation on tyrosine residues and CC subsequent translocation to the nucleus. Phosphorylated on serine upon CC DNA damage, probably by ATM or ATR. Serine phosphorylation is important CC for the formation of stable DNA-binding STAT3 homodimers and maximal CC transcriptional activity. ARL2BP may participate in keeping the CC phosphorylated state of STAT3 within the nucleus. Upon LPS challenge, CC phosphorylated within the nucleus by IRAK1. Upon erythropoietin CC treatment, phosphorylated on Ser-727 by RPS6KA5. Dephosphorylation on CC tyrosine residues by PTPN2 negatively regulates IL6/interleukin-6 CC signaling (By similarity). Phosphorylation at Tyr-705 by PTK6, isoform CC M2 of PKM (PKM2) or FER leads to an increase of its transcriptional CC activity (PubMed:12763138, PubMed:16568091, PubMed:21135090, CC PubMed:22306293, PubMed:32929201). Phosphorylation at Tyr-705 is CC increased in the presence of calcineurin (By similarity). CC {ECO:0000250|UniProtKB:P42227, ECO:0000269|PubMed:10688651, CC ECO:0000269|PubMed:12359225, ECO:0000269|PubMed:12763138, CC ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:16219639, CC ECO:0000269|PubMed:16568091, ECO:0000269|PubMed:17344214, CC ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:18234692, CC ECO:0000269|PubMed:18599021, ECO:0000269|PubMed:19147545, CC ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:22306293, CC ECO:0000269|PubMed:32929201, ECO:0000269|PubMed:7701321}. CC -!- PTM: Acetylated on lysine residues by EP300/p300, promoting its CC activation (PubMed:15653507, PubMed:16285960, PubMed:18782771). CC Acetylation at Lys-49 and Lys-87 by EP300/p300 promotes its activation CC (PubMed:15653507, PubMed:16285960, PubMed:28262505). Acetylation at CC Lys-87 by EP300/p300 promotes its association with BRD2 and recruitment CC to chromatin (PubMed:28262505). Deacetylated at Lys-49 and Lys-87 by CC HDAC1 (PubMed:16285960). Acetylation at Lys-685 by EP300/p300 promotes CC its homodimerization and activation (PubMed:15653507). Deacetylated at CC Lys-685 by HDAC3 (PubMed:15653507). Acetylated on lysine residues by CC CREBBP (PubMed:28065600). Deacetylation by LOXL3 leads to disrupt STAT3 CC dimerization and inhibit STAT3 transcription activity CC (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 CC preferentially takes place on lysine residues that are acetylated CC (PubMed:28065600). {ECO:0000269|PubMed:15653507, CC ECO:0000269|PubMed:16285960, ECO:0000269|PubMed:18782771, CC ECO:0000269|PubMed:28065600, ECO:0000269|PubMed:28262505}. CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to CC disrupt STAT3 dimerization and inhibit STAT3 transcription activity CC (PubMed:28065600). Oxidation of lysine residues to allysine on STAT3 CC preferentially takes place on lysine residues that are acetylated CC (PubMed:28065600). {ECO:0000269|PubMed:28065600}. CC -!- PTM: (Microbial infection) Phosphorylated on Tyr-705 in the presence of CC S.typhimurium SarA. {ECO:0000269|PubMed:29924996}. CC -!- DISEASE: Hyper-IgE syndrome 1, autosomal dominant, with recurrent CC infections (HIES1) [MIM:147060]: A rare disorder of immunity and CC connective tissue characterized by immunodeficiency, chronic CC eosinophilia, distinctive coarse facial appearance, abnormal dentition, CC hyperextensibility of the joints, and bone fractures. CC {ECO:0000269|PubMed:17676033, ECO:0000269|PubMed:17881745, CC ECO:0000269|PubMed:23342295, ECO:0000269|PubMed:26293184}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Autoimmune disease, multisystem, infantile-onset, 1 (ADMIO1) CC [MIM:615952]: A disorder characterized by early childhood onset of a CC spectrum of autoimmune manifestations affecting multiple organs, CC including insulin-dependent diabetes mellitus and autoimmune CC enteropathy or celiac disease. Other features include short stature, CC non-specific dermatitis, hypothyroidism, autoimmune arthritis, and CC delayed puberty. {ECO:0000269|PubMed:25038750, CC ECO:0000269|PubMed:28073828}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway. CC -!- SIMILARITY: Belongs to the transcription factor STAT family. CC {ECO:0000305}. CC -!- CAUTION: Was shown to be S-palmitoylated by ZDHHC19, leading to STAT3 CC homodimerization. However, this study was later retracted. CC {ECO:0000305|PubMed:31462771, ECO:0000305|PubMed:32555452}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=STAT3 entry; CC URL="https://en.wikipedia.org/wiki/STAT3"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/444/STAT3"; CC -!- WEB RESOURCE: Name=STAT3base; Note=STAT3 mutation db; CC URL="http://structure.bmc.lu.se/idbase/STAT3base/"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/stat3/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L29277; AAA58374.1; -; mRNA. DR EMBL; AJ012463; CAA10032.1; -; mRNA. DR EMBL; JB252046; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK291933; BAF84622.1; -; mRNA. DR EMBL; AY572796; AAS66986.1; -; Genomic_DNA. DR EMBL; AC087691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471152; EAW60822.1; -; Genomic_DNA. DR EMBL; BC000627; AAH00627.1; -; mRNA. DR EMBL; BC014482; AAH14482.1; -; mRNA. DR EMBL; AF029311; AAB84254.1; -; mRNA. DR CCDS; CCDS32656.1; -. [P40763-1] DR CCDS; CCDS32657.1; -. [P40763-2] DR CCDS; CCDS59288.1; -. [P40763-3] DR PIR; A54444; A54444. DR RefSeq; NP_003141.2; NM_003150.3. [P40763-2] DR RefSeq; NP_644805.1; NM_139276.2. [P40763-1] DR RefSeq; NP_998827.1; NM_213662.1. [P40763-3] DR RefSeq; XP_005257673.2; XM_005257616.3. DR RefSeq; XP_005257674.2; XM_005257617.3. DR RefSeq; XP_011523447.1; XM_011525145.2. DR RefSeq; XP_011523448.1; XM_011525146.2. DR RefSeq; XP_016880461.1; XM_017024972.1. DR RefSeq; XP_016880464.1; XM_017024975.1. DR PDB; 5AX3; X-ray; 2.98 A; B=571-582. DR PDB; 5U5S; NMR; -; B=81-92. DR PDB; 6NJS; X-ray; 2.70 A; A=127-688. DR PDB; 6NUQ; X-ray; 3.15 A; A=127-688. DR PDB; 6QHD; X-ray; 2.85 A; A/B=127-715. DR PDB; 6TLC; X-ray; 2.90 A; A/B=127-722. DR PDBsum; 5AX3; -. DR PDBsum; 5U5S; -. DR PDBsum; 6NJS; -. DR PDBsum; 6NUQ; -. DR PDBsum; 6QHD; -. DR PDBsum; 6TLC; -. DR AlphaFoldDB; P40763; -. DR SMR; P40763; -. DR BioGRID; 112651; 427. DR ComplexPortal; CPX-6041; STAT1/STAT3 complex. DR ComplexPortal; CPX-6043; STAT3/STAT5A complex. DR ComplexPortal; CPX-6044; STAT3/STAT5B complex. DR ComplexPortal; CPX-6046; STAT3/STAT4 complex. DR ComplexPortal; CPX-6049; STAT3 homodimer. DR CORUM; P40763; -. DR DIP; DIP-33584N; -. DR ELM; P40763; -. DR IntAct; P40763; 265. DR MINT; P40763; -. DR STRING; 9606.ENSP00000264657; -. DR BindingDB; P40763; -. DR ChEMBL; CHEMBL4026; -. DR DrugBank; DB05959; ENMD-1198. DR DrugBank; DB16630; OPB-111077. DR DrugCentral; P40763; -. DR GuidetoPHARMACOLOGY; 2994; -. DR MoonDB; P40763; Predicted. DR GlyCosmos; P40763; 6 sites, 2 glycans. DR GlyGen; P40763; 6 sites, 2 O-linked glycans (6 sites). DR iPTMnet; P40763; -. DR MetOSite; P40763; -. DR PhosphoSitePlus; P40763; -. DR SwissPalm; P40763; -. DR BioMuta; STAT3; -. DR DMDM; 48429227; -. DR CPTAC; CPTAC-1275; -. DR CPTAC; CPTAC-1276; -. DR CPTAC; CPTAC-1751; -. DR CPTAC; CPTAC-5962; -. DR CPTAC; non-CPTAC-5439; -. DR CPTAC; non-CPTAC-5440; -. DR CPTAC; non-CPTAC-5713; -. DR CPTAC; non-CPTAC-5714; -. DR EPD; P40763; -. DR jPOST; P40763; -. DR MassIVE; P40763; -. DR MaxQB; P40763; -. DR PaxDb; 9606-ENSP00000264657; -. DR PeptideAtlas; P40763; -. DR ProteomicsDB; 55378; -. [P40763-1] DR ProteomicsDB; 55379; -. [P40763-2] DR Pumba; P40763; -. DR ABCD; P40763; 8 sequenced antibodies. DR Antibodypedia; 660; 2986 antibodies from 55 providers. DR CPTC; P40763; 2 antibodies. DR DNASU; 6774; -. DR Ensembl; ENST00000264657.10; ENSP00000264657.4; ENSG00000168610.17. [P40763-1] DR Ensembl; ENST00000404395.3; ENSP00000384943.3; ENSG00000168610.17. [P40763-2] DR Ensembl; ENST00000585517.5; ENSP00000467000.1; ENSG00000168610.17. [P40763-3] DR Ensembl; ENST00000588969.5; ENSP00000467985.1; ENSG00000168610.17. [P40763-1] DR Ensembl; ENST00000677030.1; ENSP00000503662.1; ENSG00000168610.17. [P40763-3] DR Ensembl; ENST00000677723.1; ENSP00000503574.1; ENSG00000168610.17. [P40763-2] DR Ensembl; ENST00000678044.1; ENSP00000503102.1; ENSG00000168610.17. [P40763-1] DR Ensembl; ENST00000678827.1; ENSP00000503634.1; ENSG00000168610.17. [P40763-3] DR Ensembl; ENST00000678906.1; ENSP00000504184.1; ENSG00000168610.17. [P40763-1] DR Ensembl; ENST00000678960.1; ENSP00000503181.1; ENSG00000168610.17. [P40763-1] DR Ensembl; ENST00000679014.1; ENSP00000503237.1; ENSG00000168610.17. [P40763-2] DR Ensembl; ENST00000713583.1; ENSP00000518875.1; ENSG00000168610.17. [P40763-1] DR GeneID; 6774; -. DR KEGG; hsa:6774; -. DR MANE-Select; ENST00000264657.10; ENSP00000264657.4; NM_139276.3; NP_644805.1. DR UCSC; uc002hzl.2; human. [P40763-1] DR AGR; HGNC:11364; -. DR CTD; 6774; -. DR DisGeNET; 6774; -. DR GeneCards; STAT3; -. DR GeneReviews; STAT3; -. DR HGNC; HGNC:11364; STAT3. DR HPA; ENSG00000168610; Low tissue specificity. DR MalaCards; STAT3; -. DR MIM; 102582; gene. DR MIM; 147060; phenotype. DR MIM; 615952; phenotype. DR neXtProt; NX_P40763; -. DR OpenTargets; ENSG00000168610; -. DR Orphanet; 520; Acute promyelocytic leukemia. DR Orphanet; 2314; Autosomal dominant hyper-IgE syndrome due to STAT3 deficiency. DR Orphanet; 512017; Chronic lymphoproliferative disorder of natural killer cells. DR Orphanet; 99885; Isolated permanent neonatal diabetes mellitus. DR Orphanet; 438159; STAT3-related early-onset multisystem autoimmune disease. DR Orphanet; 86872; T-cell large granular lymphocyte leukemia. DR PharmGKB; PA337; -. DR VEuPathDB; HostDB:ENSG00000168610; -. DR eggNOG; KOG3667; Eukaryota. DR GeneTree; ENSGT01050000244905; -. DR HOGENOM; CLU_014189_3_0_1; -. DR InParanoid; P40763; -. DR OrthoDB; 7823at2759; -. DR PhylomeDB; P40763; -. DR TreeFam; TF318648; -. DR PathwayCommons; P40763; -. DR Reactome; R-HSA-1059683; Interleukin-6 signaling. DR Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. DR Reactome; R-HSA-1433557; Signaling by SCF-KIT. DR Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants. DR Reactome; R-HSA-186763; Downstream signal transduction. DR Reactome; R-HSA-198745; Signalling to STAT3. DR Reactome; R-HSA-201556; Signaling by ALK. DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP). DR Reactome; R-HSA-2586552; Signaling by Leptin. DR Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation. DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis. DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells. DR Reactome; R-HSA-6783783; Interleukin-10 signaling. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-8849474; PTK6 Activates STAT3. DR Reactome; R-HSA-8854691; Interleukin-20 family signaling. DR Reactome; R-HSA-8875791; MET activates STAT3. DR Reactome; R-HSA-8983432; Interleukin-15 signaling. DR Reactome; R-HSA-8984722; Interleukin-35 Signalling. DR Reactome; R-HSA-8985947; Interleukin-9 signaling. DR Reactome; R-HSA-9008059; Interleukin-37 signaling. DR Reactome; R-HSA-9020933; Interleukin-23 signaling. DR Reactome; R-HSA-9020956; Interleukin-27 signaling. DR Reactome; R-HSA-9020958; Interleukin-21 signaling. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants. DR Reactome; R-HSA-9673767; Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants. DR Reactome; R-HSA-9673770; Signaling by PDGFRA extracellular domain mutants. DR Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF). DR Reactome; R-HSA-9680350; Signaling by CSF1 (M-CSF) in myeloid cells. DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling. DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling. DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer. DR Reactome; R-HSA-982772; Growth hormone receptor signaling. DR Reactome; R-HSA-9833482; PKR-mediated signaling. DR SignaLink; P40763; -. DR SIGNOR; P40763; -. DR BioGRID-ORCS; 6774; 40 hits in 1196 CRISPR screens. DR ChiTaRS; STAT3; human. DR GeneWiki; STAT3; -. DR GenomeRNAi; 6774; -. DR Pharos; P40763; Tchem. DR PRO; PR:P40763; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P40763; Protein. DR Bgee; ENSG00000168610; Expressed in type B pancreatic cell and 211 other cell types or tissues. DR ExpressionAtlas; P40763; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IMP:BHF-UCL. DR GO; GO:0005667; C:transcription regulator complex; IDA:ARUK-UCL. DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004879; F:nuclear receptor activity; IDA:BHF-UCL. DR GO; GO:0070878; F:primary miRNA binding; IPI:ARUK-UCL. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0140610; F:RNA sequestering activity; IDA:ARUK-UCL. DR GO; GO:0035591; F:signaling adaptor activity; IPI:ARUK-UCL. DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL. DR GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IDA:UniProt. DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl. DR GO; GO:0032870; P:cellular response to hormone stimulus; IDA:BHF-UCL. DR GO; GO:0097398; P:cellular response to interleukin-17; IEA:Ensembl. DR GO; GO:0044320; P:cellular response to leptin stimulus; IDA:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB. DR GO; GO:0006952; P:defense response; IBA:GO_Central. DR GO; GO:0042755; P:eating behavior; ISS:UniProtKB. DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB. DR GO; GO:0001754; P:eye photoreceptor cell differentiation; ISS:UniProtKB. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IDA:BHF-UCL. DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB. DR GO; GO:0038154; P:interleukin-11-mediated signaling pathway; IDA:UniProt. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:UniProt. DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IDA:UniProt. DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; IDA:UniProt. DR GO; GO:0030522; P:intracellular receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProt. DR GO; GO:0106015; P:negative regulation of inflammatory response to wounding; IDA:UniProt. DR GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl. DR GO; GO:2000635; P:negative regulation of primary miRNA processing; IMP:ARUK-UCL. DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProt. DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ARUK-UCL. DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; IGI:ARUK-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IGI:ARUK-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:ARUK-UCL. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IGI:ARUK-UCL. DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; IGI:BHF-UCL. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:ARUK-UCL. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL. DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IEA:Ensembl. DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL. DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB. DR GO; GO:0060019; P:radial glial cell differentiation; ISS:UniProtKB. DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:UniProt. DR GO; GO:0097696; P:receptor signaling pathway via STAT; IMP:BHF-UCL. DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0060259; P:regulation of feeding behavior; ISS:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL. DR GO; GO:0044321; P:response to leptin; IDA:UniProtKB. DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central. DR GO; GO:0060221; P:retinal rod cell differentiation; IEA:Ensembl. DR GO; GO:0019953; P:sexual reproduction; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl. DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; ISS:UniProtKB. DR GO; GO:0072538; P:T-helper 17 type immune response; IDA:UniProtKB. DR GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:ARUK-UCL. DR CDD; cd10374; SH2_STAT3; 1. DR CDD; cd16853; STAT3_CCD; 1. DR CDD; cd16847; STAT3_DBD; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.20.1050.20; STAT transcription factor, all-alpha domain; 1. DR Gene3D; 2.60.40.630; STAT transcription factor, DNA-binding domain; 1. DR Gene3D; 1.10.532.10; STAT transcription factor, N-terminal domain; 1. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR001217; STAT. DR InterPro; IPR035855; STAT3_SH2. DR InterPro; IPR048988; STAT_linker. DR InterPro; IPR036535; STAT_N_sf. DR InterPro; IPR013800; STAT_TF_alpha. DR InterPro; IPR015988; STAT_TF_coiled-coil. DR InterPro; IPR013801; STAT_TF_DNA-bd. DR InterPro; IPR012345; STAT_TF_DNA-bd_N. DR InterPro; IPR013799; STAT_TF_prot_interaction. DR PANTHER; PTHR11801; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1. DR PANTHER; PTHR11801:SF2; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 3; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF01017; STAT_alpha; 1. DR Pfam; PF02864; STAT_bind; 1. DR Pfam; PF02865; STAT_int; 1. DR Pfam; PF21354; STAT_linker; 1. DR SMART; SM00964; STAT_int; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF47655; STAT; 1. DR SUPFAM; SSF48092; Transcription factor STAT-4 N-domain; 1. DR PROSITE; PS50001; SH2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm; KW Diabetes mellitus; Disease variant; DNA-binding; Dwarfism; KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; KW SH2 domain; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..770 FT /note="Signal transducer and activator of transcription 3" FT /id="PRO_0000182417" FT DOMAIN 580..670 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT MOTIF 150..162 FT /note="Essential for nuclear import" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:16285960, FT ECO:0000269|PubMed:18782771" FT MOD_RES 87 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:16285960, FT ECO:0000269|PubMed:18782771, ECO:0000269|PubMed:28262505" FT MOD_RES 601 FT /note="Allysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 601 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 615 FT /note="Allysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 615 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 631 FT /note="Allysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 631 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 685 FT /note="Allysine; alternate" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 685 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:15653507, FT ECO:0000269|PubMed:28065600" FT MOD_RES 705 FT /note="Phosphotyrosine; by FER and PTK6" FT /evidence="ECO:0000269|PubMed:12763138, FT ECO:0000269|PubMed:16568091, ECO:0000269|PubMed:21135090, FT ECO:0000269|PubMed:22306293, ECO:0000269|PubMed:26293184, FT ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:32929201, FT ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:24275569" FT MOD_RES 707 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:28065600" FT MOD_RES 714 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 727 FT /note="Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5, FT ZIPK/DAPK3 and PKC/PRKCE" FT /evidence="ECO:0000269|PubMed:12763138, FT ECO:0000269|PubMed:15465816, ECO:0000269|PubMed:16219639, FT ECO:0000269|PubMed:17875724, ECO:0000269|PubMed:18599021, FT ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:26293184, FT ECO:0000269|PubMed:31899195, ECO:0000269|PubMed:32797246, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 701 FT /note="Missing (in isoform Del-701)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_010474" FT VAR_SEQ 716..722 FT /note="TTCSNTI -> FIDAVWK (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_055918" FT VAR_SEQ 723..770 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_055919" FT VARIANT 32 FT /note="Q -> K (in dbSNP:rs1803125)" FT /id="VAR_018683" FT VARIANT 143 FT /note="M -> I (in dbSNP:rs17878478)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_018679" FT VARIANT 330 FT /note="P -> S (in ADMIO1; increases transcriptional FT activity; increases binding to ISL1 promoter region; FT decreases glucose stimulated insulin secretion)" FT /evidence="ECO:0000269|PubMed:28073828" FT /id="VAR_078445" FT VARIANT 382 FT /note="R -> L (in HIES1; dbSNP:rs113994136)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037365" FT VARIANT 382 FT /note="R -> Q (in HIES1; loss of function; FT dbSNP:rs113994136)" FT /evidence="ECO:0000269|PubMed:17676033, FT ECO:0000269|PubMed:17881745" FT /id="VAR_037366" FT VARIANT 382 FT /note="R -> W (in HIES1; loss of function; reduced DNA- FT binding ability; dbSNP:rs113994135)" FT /evidence="ECO:0000269|PubMed:17676033, FT ECO:0000269|PubMed:17881745, ECO:0000269|PubMed:26293184" FT /id="VAR_037367" FT VARIANT 384 FT /note="F -> L (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037368" FT VARIANT 384 FT /note="F -> S (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037369" FT VARIANT 389 FT /note="T -> I (in HIES1; loss of function; FT dbSNP:rs397514766)" FT /evidence="ECO:0000269|PubMed:17676033, FT ECO:0000269|PubMed:23342295" FT /id="VAR_037370" FT VARIANT 392 FT /note="K -> R (in ADMIO1; dbSNP:rs587777648)" FT /evidence="ECO:0000269|PubMed:25038750" FT /id="VAR_071885" FT VARIANT 395 FT /note="N -> Y (in HIES1; uncertain significance; reduced FT DNA-binding ability)" FT /evidence="ECO:0000269|PubMed:26293184" FT /id="VAR_075414" FT VARIANT 423 FT /note="R -> Q (in HIES1; dbSNP:rs113994137)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037371" FT VARIANT 425 FT /note="N -> Y (in HIES1; uncertain significance; reduced FT DNA-binding ability)" FT /evidence="ECO:0000269|PubMed:26293184" FT /id="VAR_075415" FT VARIANT 437 FT /note="H -> Y (in HIES1; loss of function)" FT /evidence="ECO:0000269|PubMed:17676033" FT /id="VAR_037372" FT VARIANT 463 FT /note="Missing (in HIES1; loss of function)" FT /evidence="ECO:0000269|PubMed:17676033, FT ECO:0000269|PubMed:17881745" FT /id="VAR_037373" FT VARIANT 561 FT /note="F -> Y (in dbSNP:rs1064116)" FT /evidence="ECO:0000269|PubMed:7512451" FT /id="VAR_037374" FT VARIANT 611 FT /note="S -> N (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037375" FT VARIANT 621 FT /note="F -> V (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037376" FT VARIANT 622 FT /note="T -> I (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037377" FT VARIANT 637 FT /note="V -> L (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037378" FT VARIANT 637 FT /note="V -> M (in HIES1; reduced DNA-binding ability; FT dbSNP:rs113994139)" FT /evidence="ECO:0000269|PubMed:17881745, FT ECO:0000269|PubMed:26293184" FT /id="VAR_037379" FT VARIANT 644 FT /note="Missing (in HIES1)" FT /evidence="ECO:0000269|PubMed:17881745" FT /id="VAR_037380" FT VARIANT 646 FT /note="N -> K (in ADMIO1; dbSNP:rs587777649)" FT /evidence="ECO:0000269|PubMed:25038750" FT /id="VAR_071886" FT VARIANT 657 FT /note="Y -> C (in HIES1; reduced DNA-binding ability; FT dbSNP:rs193922721)" FT /evidence="ECO:0000269|PubMed:17881745, FT ECO:0000269|PubMed:26293184" FT /id="VAR_037381" FT VARIANT 658 FT /note="K -> N (in ADMIO1; dbSNP:rs587777650)" FT /evidence="ECO:0000269|PubMed:25038750" FT /id="VAR_071887" FT VARIANT 716 FT /note="T -> M (in ADMIO1; dbSNP:rs869312892)" FT /evidence="ECO:0000269|PubMed:25038750" FT /id="VAR_071888" FT MUTAGEN 49 FT /note="K->Q: Mimics acetylation; increased interaction with FT EP300; when associated with Q-87." FT /evidence="ECO:0000269|PubMed:18782771" FT MUTAGEN 49 FT /note="K->R: Decreased transcription activator activity and FT interaction with EP300; when associated with R-87." FT /evidence="ECO:0000269|PubMed:16285960, FT ECO:0000269|PubMed:18782771" FT MUTAGEN 87 FT /note="K->Q: Mimics acetylation; increased interaction with FT EP300; when associated with Q-49." FT /evidence="ECO:0000269|PubMed:18782771" FT MUTAGEN 87 FT /note="K->R: Decreased transcription activator activity and FT interaction with EP300; when associated with R-49." FT /evidence="ECO:0000269|PubMed:16285960, FT ECO:0000269|PubMed:18782771" FT MUTAGEN 434..435 FT /note="EE->AA: Inhibits leptin-mediated transactivation of FT CCND1 promoter. No effect on interaction with INPP5F." FT /evidence="ECO:0000269|PubMed:17344214, FT ECO:0000269|PubMed:25476455" FT MUTAGEN 685 FT /note="K->R: Decreased acetylation by EP300/p300, leading FT to impaired homodimerization and activation." FT /evidence="ECO:0000269|PubMed:15653507" FT MUTAGEN 705 FT /note="Y->F: Inhibits leptin-mediated transactivation of FT CCND1 promoter. Abolished phosphorylation by isoform M2 of FT PKM (PKM2)." FT /evidence="ECO:0000269|PubMed:17344214, FT ECO:0000269|PubMed:22306293" FT CONFLICT 133 FT /note="T -> A (in Ref. 4; BAF84622)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="Q -> H (in Ref. 1; AAA58374)" FT /evidence="ECO:0000305" FT CONFLICT 460 FT /note="P -> S (in Ref. 1; AAA58374)" FT /evidence="ECO:0000305" FT CONFLICT 548 FT /note="K -> N (in Ref. 1; AAA58374)" FT /evidence="ECO:0000305" FT CONFLICT 652 FT /note="E -> V (in Ref. 4; BAF84622)" FT /evidence="ECO:0000305" FT CONFLICT 667 FT /note="V -> L (in Ref. 1; AAA58374)" FT /evidence="ECO:0000305" FT CONFLICT 730 FT /note="T -> A (in Ref. 1; AAA58374)" FT /evidence="ECO:0000305" FT HELIX 139..177 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 194..237 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 239..251 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 261..290 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 297..320 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 345..353 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:6NJS" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 363..368 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:6QHD" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:6NJS" FT TURN 398..401 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 404..415 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 439..447 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 450..457 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 467..469 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 470..483 FT /evidence="ECO:0007829|PDB:6NJS" FT TURN 490..494 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 501..513 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 514..517 FT /evidence="ECO:0007829|PDB:6TLC" FT HELIX 522..533 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 546..549 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 557..559 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 561..574 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 577..582 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 591..600 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 605..610 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 619..626 FT /evidence="ECO:0007829|PDB:6NJS" FT STRAND 632..636 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 642..645 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 650..656 FT /evidence="ECO:0007829|PDB:6NJS" FT TURN 674..676 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 679..683 FT /evidence="ECO:0007829|PDB:6NJS" FT HELIX 684..686 FT /evidence="ECO:0007829|PDB:6NJS" FT MOD_RES P40763-2:704 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455, FT ECO:0007744|PubMed:24275569" SQ 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 //