STAT3_MOUSE
ID STAT3_MOUSE Reviewed; 770 AA.
AC P42227; A2A5D1; B7ZC17;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Signal transducer and activator of transcription 3 {ECO:0000312|MGI:MGI:103038};
DE AltName: Full=Acute-phase response factor;
GN Name=Stat3 {ECO:0000312|MGI:MGI:103038};
GN Synonyms=Aprf {ECO:0000312|MGI:MGI:103038};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A), AND PROTEIN SEQUENCE OF
RP 154-158; 181-185 AND 632-640.
RC STRAIN=BALB/cJ; TISSUE=Liver;
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 DEL-701).
RC TISSUE=Brain;
RX PubMed=7523373; DOI=10.1016/s0021-9258(19)51096-1;
RA Raz R., Durbin J.E., Levy D.E.;
RT "Acute phase response factor and additional members of the interferon-
RT stimulated gene factor 3 family integrate diverse signals from cytokines,
RT interferons, and growth factors.";
RL J. Biol. Chem. 269:24391-24395(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
RC TISSUE=Thymus;
RX PubMed=8140422; DOI=10.1126/science.8140422;
RA Zhong Z., Wen Z., Darnell J.E. Jr.;
RT "Stat3: a STAT family member activated by tyrosine phosphorylation in
RT response to epidermal growth factor and interleukin-6.";
RL Science 264:95-98(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3B).
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Liver;
RX PubMed=7568080; DOI=10.1073/pnas.92.20.9097;
RA Schaefer T.S., Sanders L.K., Nathans D.;
RT "Cooperative transcriptional activity of Jun and Stat3 beta, a short form
RT of Stat3.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9097-9101(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM STAT3A).
RC STRAIN=129/SvJ;
RX PubMed=11161808; DOI=10.1006/geno.2000.6433;
RA Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
RA Oka T., Dewar K., Hennighausen L.;
RT "Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
RT zebrafish to mouse.";
RL Genomics 71:150-155(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
RC STRAIN=C57BL/6J, and NOD/LtJ;
RA Davoodi-Semiromi A., She J.-X.;
RT "A mutant Stat5b with weaker DNA binding defines a key defective pathway in
RT non-obese diabetic (NOD) mice.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM STAT3A).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 PHOSPHORYLATION AT SER-727, AND MUTAGENESIS.
RX PubMed=7543024; DOI=10.1016/0092-8674(95)90311-9;
RA Wen Z., Zhong Z., Darnell J.E. Jr.;
RT "Maximal activation of transcription by Stat1 and Stat3 requires both
RT tyrosine and serine phosphorylation.";
RL Cell 82:241-250(1995).
RN [10]
RP INTERACTION WITH PIAS3.
RC TISSUE=Thymus;
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 [11]
RP PHOSPHORYLATION BY FER, AND INTERACTION WITH FER.
RX PubMed=10878010; DOI=10.1074/jbc.m003402200;
RA Priel-Halachmi S., Ben-Dor I., Shpungin S., Tennenbaum T., Molavani H.,
RA Bachrach M., Salzberg S., Nir U.;
RT "FER kinase activation of Stat3 is determined by the N-terminal sequence.";
RL J. Biol. Chem. 275:28902-28910(2000).
RN [12]
RP INTERACTION WITH STATIP1.
RX PubMed=10954736; DOI=10.1073/pnas.170192197;
RA Collum R.G., Brutsaert S., Lee G., Schindler C.;
RT "A Stat3-interacting protein (StIP1) regulates cytokine signal
RT transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10120-10125(2000).
RN [13]
RP PHOSPHORYLATION AT TYR-705 AND SER-727.
RX PubMed=11553624; DOI=10.1074/jbc.m106044200;
RA Zhang Y., Liu G., Dong Z.;
RT "MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse
RT epidermal JB6 cells.";
RL J. Biol. Chem. 276:42534-42542(2001).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-705.
RX PubMed=11294897; DOI=10.1091/mbc.12.4.931;
RA Hart K.C., Robertson S.C., Donoghue D.J.;
RT "Identification of tyrosine residues in constitutively activated fibroblast
RT growth factor receptor 3 involved in mitogenesis, Stat activation, and
RT phosphatidylinositol 3-kinase activation.";
RL Mol. Biol. Cell 12:931-942(2001).
RN [15]
RP FUNCTION.
RX PubMed=12594516; DOI=10.1038/nature01388;
RA Bates S.H., Stearns W.H., Dundon T.A., Schubert M., Tso A.W., Wang Y.,
RA Banks A.S., Lavery H.J., Haq A.K., Maratos-Flier E., Neel B.G.,
RA Schwartz M.W., Myers M.G. Jr.;
RT "STAT3 signalling is required for leptin regulation of energy balance but
RT not reproduction.";
RL Nature 421:856-859(2003).
RN [16]
RP INTERACTION WITH NLK, PHOSPHORYLATION AT SER-727, AND MUTAGENESIS OF
RP SER-727.
RX PubMed=15004007; DOI=10.1101/gad.1166904;
RA Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N.,
RA Matsumoto K., Shibuya H.;
RT "Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm
RT induction.";
RL Genes Dev. 18:381-386(2004).
RN [17]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-77; LEU-78; PHE-174; ARG-609 AND
RP TYR-705, INTERACTION WITH KPNA4 AND KPNA5, 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 [18]
RP INTERACTION WITH SIPAR.
RC STRAIN=Swiss Webster / NIH;
RA Ning H., Rong Y., Zhang Y., Chang Z.;
RT "SIPAR interacts with STAT3 to regulate its signal pathway.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 32:173-179(2005).
RN [19]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=16825198; DOI=10.1074/jbc.m601991200;
RA Gonzalez R.R., Cherfils S., Escobar M., Yoo J.H., Carino C., Styer A.K.,
RA Sullivan B.T., Sakamoto H., Olawaiye A., Serikawa T., Lynch M.P.,
RA Rueda B.R.;
RT "Leptin signaling promotes the growth of mammary tumors and increases the
RT expression of vascular endothelial growth factor (VEGF) and its receptor
RT type two (VEGF-R2).";
RL J. Biol. Chem. 281:26320-26328(2006).
RN [20]
RP INTERACTION WITH STMN3.
RX PubMed=16401721; DOI=10.1083/jcb.200503021;
RA Ng D.C., Lin B.H., Lim C.P., Huang G., Zhang T., Poli V., Cao X.;
RT "Stat3 regulates microtubules by antagonizing the depolymerization activity
RT of stathmin.";
RL J. Cell Biol. 172:245-257(2006).
RN [21]
RP INTERACTION WITH ARL2BP.
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [23]
RP INTERACTION WITH NHLH1.
RX PubMed=18356286; DOI=10.1210/me.2008-0010;
RA Fox D.L., Good D.J.;
RT "Nescient helix-loop-helix 2 interacts with signal transducer and activator
RT of transcription 3 to regulate transcription of prohormone convertase
RT 1/3.";
RL Mol. Endocrinol. 22:1438-1448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-714 AND SER-727, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [25]
RP PHOSPHORYLATION AT SER-727, AND INTERACTION WITH NEK6.
RX PubMed=20595392; DOI=10.1074/jbc.m110.137190;
RA Jeon Y.J., Lee K.Y., Cho Y.Y., Pugliese A., Kim H.G., Jeong C.H.,
RA Bode A.M., Dong Z.;
RT "Role of NEK6 in tumor promoter-induced transformation in JB6 C141 mouse
RT skin epidermal cells.";
RL J. Biol. Chem. 285:28126-28133(2010).
RN [26]
RP PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
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 [27]
RP FUNCTION.
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 [28]
RP INTERACTION WITH OCAD1, AND SUBUNIT.
RX PubMed=23972987; DOI=10.1016/j.celrep.2013.07.029;
RA Sinha A., Khadilkar R.J., Vinay K.S., Roychowdhury Sinha A., Inamdar M.S.;
RT "Conserved regulation of the Jak/STAT pathway by the endosomal protein
RT asrij maintains stem cell potency.";
RL Cell Rep. 4:649-658(2013).
RN [29]
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=23401489; DOI=10.1084/jem.20120260;
RA Choi S.M., McAleer J.P., Zheng M., Pociask D.A., Kaplan M.H., Qin S.,
RA Reinhart T.A., Kolls J.K.;
RT "Innate Stat3-mediated induction of the antimicrobial protein Reg3gamma is
RT required for host defense against MRSA pneumonia.";
RL J. Exp. Med. 210:551-561(2013).
RN [30]
RP PHOSPHORYLATION AT TYR-705 (MICROBIAL INFECTION).
RC STRAIN=C57BL/6J;
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 [31]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 136-716.
RX PubMed=9671298; DOI=10.1038/28101;
RA Becker S., Groner B., Mueller C.W.;
RT "Three-dimensional structure of the Stat3beta homodimer bound to DNA.";
RL Nature 394:145-151(1998).
RN [32]
RP DISRUPTION PHENOTYPE.
RX PubMed=9108058; DOI=10.1073/pnas.94.8.3801;
RA Takeda K., Noguchi K., Shi W., Tanaka T., Matsumoto M., Yoshida N.,
RA Kishimoto T., Akira S.;
RT "Targeted disruption of the mouse Stat3 gene leads to early embryonic
RT lethality.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3801-3804(1997).
RN [33]
RP FUNCTION.
RX PubMed=20215569; DOI=10.1210/en.2009-1199;
RA Kostromina E., Gustavsson N., Wang X., Lim C.Y., Radda G.K., Li C., Han W.;
RT "Glucose intolerance and impaired insulin secretion in pancreas-specific
RT signal transducer and activator of transcription-3 knockout mice are
RT associated with microvascular alterations in the pancreas.";
RL Endocrinology 151:2050-2059(2010).
CC -!- FUNCTION: Signal transducer and transcription activator that mediates
CC cellular responses to interleukins, KITLG/SCF, LEP and other growth
CC factors (By similarity). Once activated, recruits coactivators, such as
CC NCOA1 or MED1, to the promoter region of the target gene (By
CC similarity). May mediate cellular responses to activated FGFR1, FGFR2,
CC FGFR3 and FGFR4 (By similarity). Upon activation of IL6ST/gp130
CC signaling by interleukin-6 (IL6), binds to the IL6-responsive elements
CC identified in the promoters of various acute-phase protein genes (By
CC similarity). Activated by IL31 through IL31RA (By similarity). Acts as
CC a regulator of inflammatory response by regulating differentiation of
CC naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg):
CC deacetylation and oxidation of lysine residues by LOXL3, leads to
CC disrupt STAT3 dimerization and inhibit its transcription activity (By
CC similarity). Involved in cell cycle regulation by inducing the
CC expression of key genes for the progression from G1 to S phase, such as
CC CCND1 (By similarity). Mediates the effects of LEP on melanocortin
CC production, body energy homeostasis and lactation (PubMed:12594516).
CC May play an apoptotic role by transctivating BIRC5 expression under LEP
CC activation (PubMed:16825198). Cytoplasmic STAT3 represses
CC macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity).
CC Plays a crucial role in basal beta cell functions, such as regulation
CC of insulin secretion (PubMed:20215569). Plays an important role in host
CC defense in methicillin-resistant S.aureus lung infection by regulating
CC the expression of the antimicrobial lectin REG3G (PubMed:23401489).
CC {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:11294897,
CC ECO:0000269|PubMed:12594516, ECO:0000269|PubMed:16825198,
CC ECO:0000269|PubMed:20215569, ECO:0000269|PubMed:23084476,
CC ECO:0000269|PubMed:23401489}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1, SIPAR,
CC SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence of IL23.
CC Interacts (via SH2 domain) with NLK. Interacts with ARL2BP; the
CC interaction is enhanced by LIF and JAK1 expression (By similarity).
CC Interacts with KPNA4 and KPNA5; KPNA4 may be the primary mediator of
CC nuclear import (By similarity). Interacts with CAV2; the interaction is
CC increased on insulin-induced tyrosine phosphorylation of CAV2 and leads
CC to STAT3 activation (By similarity). Interacts with ARL2BP; interaction
CC is enhanced with ARL2. Interacts with NEK6 (By similarity). Binds to
CC CDK9 when activated and nuclear. Interacts with BMX. Interacts with
CC ZIPK/DAPK3. Interacts with PIAS3; the interaction occurs on stimulation
CC by IL6, CNTF or OSM and inhibits the DNA binding activity of STAT3. In
CC prostate cancer cells, interacts with PRKCE and promotes DNA binding
CC activity of STAT3. Interacts with STMN3, antagonizing its microtubule-
CC destabilizing activity. Interacts with the 'Lys-129' acetylated form of
CC BIRC5/survivin. Interacts with FER. Interacts (via SH2 domain) with
CC EIF2AK2/PKR (via the kinase catalytic domain) (By similarity).
CC Interacts with FGFR4 (By similarity). Interacts with INPP5F; the
CC interaction is independent of STAT3 Tyr-705 phosphorylation status (By
CC similarity). Interacts with OCAD1 (PubMed:23972987). Interacts
CC (unphosphorylated or phosphorylated at Ser-727) with PHB1 (By
CC similarity). Interacts and may form heterodimers with NHLH1
CC (PubMed:18356286). {ECO:0000250|UniProtKB:P40763,
CC ECO:0000250|UniProtKB:P52631, ECO:0000269|PubMed:10878010,
CC ECO:0000269|PubMed:10954736, ECO:0000269|PubMed:11553624,
CC ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:15919823,
CC ECO:0000269|PubMed:16401721, ECO:0000269|PubMed:18234692,
CC ECO:0000269|PubMed:18356286, ECO:0000269|PubMed:20595392,
CC ECO:0000269|PubMed:23972987, ECO:0000269|PubMed:9388184,
CC ECO:0000269|Ref.18}.
CC -!- INTERACTION:
CC P42227; Q80VH0: Bank1; NbExp=4; IntAct=EBI-602878, EBI-646949;
CC P42227; Q64261: Cdk6; NbExp=3; IntAct=EBI-602878, EBI-847380;
CC P42227; P23927: Cryab; NbExp=3; IntAct=EBI-602878, EBI-299046;
CC P42227; O54784: Dapk3; NbExp=8; IntAct=EBI-602878, EBI-77359;
CC P42227; P70424: Erbb2; NbExp=4; IntAct=EBI-602878, EBI-2945468;
CC P42227; O35387: Hax1; NbExp=11; IntAct=EBI-602878, EBI-642449;
CC P42227; Q00175: Pgr; NbExp=4; IntAct=EBI-602878, EBI-346821;
CC P42227; P42227: Stat3; NbExp=3; IntAct=EBI-602878, EBI-602878;
CC P42227; P48025: Syk; NbExp=5; IntAct=EBI-602878, EBI-300116;
CC P42227; P30084: ECHS1; Xeno; NbExp=3; IntAct=EBI-602878, EBI-719602;
CC P42227; Q8TAE8: GADD45GIP1; Xeno; NbExp=3; IntAct=EBI-602878, EBI-372506;
CC P42227; P40189: IL6ST; Xeno; NbExp=4; IntAct=EBI-602878, EBI-1030834;
CC P42227; Q9NRF2: SH2B1; Xeno; NbExp=5; IntAct=EBI-602878, EBI-310491;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40763}. Nucleus
CC {ECO:0000250|UniProtKB:P40763}. Note=Predominantly present in the
CC cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF)
CC stimulation, accumulates in the nucleus. The complex composed of BART
CC and ARL2 plays an important role in the nuclear translocation and
CC retention of STAT3 (By similarity). Shuttles between the nucleus and
CC the cytoplasm. Translocated into the nucleus upon tyrosine
CC phosphorylation and dimerization, in response to signaling by activated
CC FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is
CC independent of tyrosine phosphorylation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Stat3A;
CC IsoId=P42227-1; Sequence=Displayed;
CC Name=Stat3B;
CC IsoId=P42227-2; Sequence=VSP_006287;
CC Name=Del-701;
CC IsoId=P42227-3; Sequence=VSP_010475;
CC -!- TISSUE SPECIFICITY: STAT3A is seen in the liver, spleen, and kidney.
CC STAT3B is also detected in the liver, although in a much less abundant
CC manner. Expressed in the lung and an increase in expression levels seen
CC during methicillin-resistant S.aureus infection.
CC {ECO:0000269|PubMed:23401489}.
CC -!- PTM: Activated through tyrosine phosphorylation by BMX. Tyrosine
CC phosphorylated in response to IL6, IL11, CNTF, LIF, KITLG/SCF, CSF1,
CC EGF, PDGF, IFN-alpha, LEP and OSM. Activated KIT promotes
CC phosphorylation on tyrosine residues and subsequent translocation to
CC the nucleus. Tyrosine phosphorylated in response to constitutively
CC activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine
CC phosphorylated upon stimulation with EGF. Upon LPS challenge,
CC phosphorylated within the nucleus by IRAK1 (By similarity). Upon UV-A
CC treatment, phosphorylated on Ser-727 by RPS6KA5 (By similarity).
CC Dephosphorylation on tyrosine residues by PTPN2 negatively regulates
CC IL6/interleukin-6 signaling (By similarity). Phosphorylation at Tyr-705
CC by PTK6, isoform M2 of PKM (PKM2) or FER leads to an increase of its
CC transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:P40763, ECO:0000269|PubMed:10878010,
CC ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11553624,
CC ECO:0000269|PubMed:15004007, ECO:0000269|PubMed:16825198,
CC ECO:0000269|PubMed:20595392, ECO:0000269|PubMed:21135090,
CC ECO:0000269|PubMed:23401489, ECO:0000269|PubMed:7543024}.
CC -!- PTM: Acetylated on lysine residues by CREBBP. Deacetylation by LOXL3
CC leads to disrupt STAT3 dimerization and inhibit STAT3 transcription
CC activity. Oxidation of lysine residues to allysine on STAT3
CC preferentially takes place on lysine residues that are acetylated.
CC {ECO:0000250|UniProtKB:P40763}.
CC -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, leading to
CC disrupt STAT3 dimerization and inhibit STAT3 transcription activity.
CC Oxidation of lysine residues to allysine on STAT3 preferentially takes
CC place on lysine residues that are acetylated.
CC {ECO:0000250|UniProtKB:P40763}.
CC -!- PTM: (Microbial infection) Phosphorylated on Tyr-705 in the presence of
CC S.typhimurium SarA. {ECO:0000269|PubMed:29924996}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality, day 6.5-7.5.
CC Conditional, tissue specific mutants are variably viable and show
CC diverse defects including obesity, diabetes, thermal dysregulation and
CC infertility. {ECO:0000269|PubMed:20215569, ECO:0000269|PubMed:9108058}.
CC -!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; L29278; AAA37254.1; -; mRNA.
DR EMBL; U08378; AAA56668.1; -; mRNA.
DR EMBL; U06922; AAA19452.1; -; mRNA.
DR EMBL; U30709; AAC52612.1; -; mRNA.
DR EMBL; AF246978; AAL59017.1; -; Genomic_DNA.
DR EMBL; AY299489; AAQ75418.1; -; mRNA.
DR EMBL; AY299490; AAQ75419.1; -; mRNA.
DR EMBL; AL591466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003806; AAH03806.1; -; mRNA.
DR CCDS; CCDS25440.1; -. [P42227-1]
DR CCDS; CCDS25441.1; -. [P42227-2]
DR CCDS; CCDS48934.1; -. [P42227-3]
DR PIR; I49508; I49508.
DR RefSeq; NP_998824.1; NM_213659.3. [P42227-1]
DR RefSeq; NP_998825.1; NM_213660.3. [P42227-3]
DR PDB; 1BG1; X-ray; 2.25 A; A=127-715.
DR PDB; 3CWG; X-ray; 3.05 A; A/B=127-688.
DR PDB; 4E68; X-ray; 2.58 A; A=127-715.
DR PDB; 4ZIA; X-ray; 2.70 A; A/B/C/D/E=3-127.
DR PDBsum; 1BG1; -.
DR PDBsum; 3CWG; -.
DR PDBsum; 4E68; -.
DR PDBsum; 4ZIA; -.
DR AlphaFoldDB; P42227; -.
DR SMR; P42227; -.
DR BioGRID; 203523; 32.
DR CORUM; P42227; -.
DR DIP; DIP-442N; -.
DR IntAct; P42227; 31.
DR MINT; P42227; -.
DR STRING; 10090.ENSMUSP00000120152; -.
DR BindingDB; P42227; -.
DR ChEMBL; CHEMBL5402; -.
DR MoonDB; P42227; Predicted.
DR MoonProt; P42227; -.
DR iPTMnet; P42227; -.
DR PhosphoSitePlus; P42227; -.
DR SwissPalm; P42227; -.
DR EPD; P42227; -.
DR jPOST; P42227; -.
DR MaxQB; P42227; -.
DR PaxDb; P42227; -.
DR PeptideAtlas; P42227; -.
DR PRIDE; P42227; -.
DR ProteomicsDB; 258659; -. [P42227-1]
DR ProteomicsDB; 258660; -. [P42227-2]
DR ProteomicsDB; 258661; -. [P42227-3]
DR ABCD; P42227; 1 sequenced antibody.
DR Antibodypedia; 660; 2538 antibodies from 56 providers.
DR DNASU; 20848; -.
DR Ensembl; ENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040. [P42227-3]
DR Ensembl; ENSMUST00000103114; ENSMUSP00000099403; ENSMUSG00000004040. [P42227-2]
DR Ensembl; ENSMUST00000127638; ENSMUSP00000120152; ENSMUSG00000004040. [P42227-1]
DR GeneID; 20848; -.
DR KEGG; mmu:20848; -.
DR UCSC; uc007lmp.1; mouse. [P42227-1]
DR UCSC; uc007lmq.1; mouse. [P42227-3]
DR CTD; 6774; -.
DR MGI; MGI:103038; Stat3.
DR VEuPathDB; HostDB:ENSMUSG00000004040; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244905; -.
DR HOGENOM; CLU_014189_3_0_1; -.
DR InParanoid; P42227; -.
DR OMA; RCLWEEN; -.
DR PhylomeDB; P42227; -.
DR TreeFam; TF318648; -.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR Reactome; R-MMU-6783783; Interleukin-10 signaling.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-8849474; PTK6 Activates STAT3.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8875791; MET activates STAT3.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9008059; Interleukin-37 signaling.
DR Reactome; R-MMU-9020933; Interleukin-23 signaling.
DR Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-9701898; STAT3 nuclear events downstream of ALK signaling.
DR BioGRID-ORCS; 20848; 4 hits in 82 CRISPR screens.
DR ChiTaRS; Stat3; mouse.
DR EvolutionaryTrace; P42227; -.
DR PRO; PR:P42227; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P42227; protein.
DR Bgee; ENSMUSG00000004040; Expressed in right lung lobe and 290 other tissues.
DR ExpressionAtlas; P42227; baseline and differential.
DR Genevisible; P42227; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0031730; F:CCR5 chemokine receptor binding; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0070878; F:primary miRNA binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IPI:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0048708; P:astrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
DR GO; GO:0097398; P:cellular response to interleukin-17; IDA:MGI.
DR GO; GO:0044320; P:cellular response to leptin stimulus; ISS:UniProtKB.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0042755; P:eating behavior; IMP:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IDA:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030522; P:intracellular receptor signaling pathway; ISO:MGI.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IMP:MGI.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:2001223; P:negative regulation of neuron migration; IGI:MGI.
DR GO; GO:2000635; P:negative regulation of primary miRNA processing; ISO:MGI.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IMP:MGI.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1900017; P:positive regulation of cytokine production involved in inflammatory response; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR GO; GO:1902728; P:positive regulation of growth factor dependent skeletal muscle satellite cell proliferation; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:MGI.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0099527; P:postsynapse to nucleus signaling pathway; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0060019; P:radial glial cell differentiation; IMP:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
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:0060259; P:regulation of feeding behavior; IMP:UniProtKB.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0019953; P:sexual reproduction; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0072540; P:T-helper 17 cell lineage commitment; IMP:UniProtKB.
DR GO; GO:0072538; P:T-helper 17 type immune response; ISS:UniProtKB.
DR GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR CDD; cd10374; SH2_STAT3; 1.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50277; -.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR035855; STAT3_SH2.
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; PTHR11801; 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 SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF47655; SSF47655; 1.
DR SUPFAM; SSF48092; SSF48092; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Acute phase; Alternative splicing;
KW Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT CHAIN 2..770
FT /note="Signal transducer and activator of transcription 3"
FT /id="PRO_0000182418"
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:0000250|UniProtKB:P40763"
FT MOD_RES 601
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 601
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 615
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 615
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 631
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 631
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 685
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 685
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 705
FT /note="Phosphotyrosine; by FER and PTK6"
FT /evidence="ECO:0000269|PubMed:11294897,
FT ECO:0000269|PubMed:11553624, ECO:0007744|PubMed:18034455"
FT MOD_RES 707
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40763"
FT MOD_RES 714
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 727
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 727
FT /note="Phosphoserine; by DYRK2, NLK, NEK6, IRAK1, RPS6KA5,
FT ZIPK/DAPK3 and PKC/PRKCE"
FT /evidence="ECO:0000305|PubMed:11553624,
FT ECO:0000305|PubMed:15004007, ECO:0000305|PubMed:20595392,
FT ECO:0000305|PubMed:7543024, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 701
FT /note="Missing (in isoform Del-701)"
FT /evidence="ECO:0000303|PubMed:7523373"
FT /id="VSP_010475"
FT VAR_SEQ 716..770
FT /note="TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLTFDMDLTSECAT
FT SPM -> FIDAVWK (in isoform Stat3B)"
FT /evidence="ECO:0000303|PubMed:7568080"
FT /id="VSP_006287"
FT MUTAGEN 77
FT /note="V->A: No effect on nuclear import; when associated
FT with A-78 and W-174."
FT /evidence="ECO:0000269|PubMed:15919823"
FT MUTAGEN 78
FT /note="L->A: No effect on nuclear import; when associated
FT with A-77 and W-174."
FT /evidence="ECO:0000269|PubMed:15919823"
FT MUTAGEN 174
FT /note="F->W: No effect on nuclear import; when associated
FT with A-77 and A-78."
FT /evidence="ECO:0000269|PubMed:15919823"
FT MUTAGEN 609
FT /note="R->A: Nuclear localization to the same extent as
FT wild-type; when associated with F-705."
FT /evidence="ECO:0000269|PubMed:15919823"
FT MUTAGEN 705
FT /note="Y->F: Nuclear localization to the same extent as
FT wild-type; when associated with A-609."
FT /evidence="ECO:0000269|PubMed:15919823"
FT MUTAGEN 727
FT /note="S->A: Decreased transcriptional activation."
FT /evidence="ECO:0000269|PubMed:15004007"
FT CONFLICT 16
FT /note="E -> K (in Ref. 2; AAA19452)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="S -> T (in Ref. 2; AAA19452 and 4; AAC52612)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="M -> I (in Ref. 1; AAA37254)"
FT /evidence="ECO:0000305"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:4ZIA"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:4ZIA"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 50..73
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 77..94
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 98..120
FT /evidence="ECO:0007829|PDB:4ZIA"
FT HELIX 139..180
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 199..237
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 261..290
FT /evidence="ECO:0007829|PDB:1BG1"
FT TURN 297..301
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 302..320
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 345..353
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1BG1"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4E68"
FT STRAND 404..415
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 450..457
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 470..483
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 501..515
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 522..533
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:4E68"
FT HELIX 561..574
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:3CWG"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:1BG1"
FT TURN 596..600
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:1BG1"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:1BG1"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:1BG1"
FT TURN 679..683
FT /evidence="ECO:0007829|PDB:1BG1"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:1BG1"
SQ SEQUENCE 770 AA; 88054 MW; 6C00626711C8012D 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 QFESLTFDMD LTSECATSPM
