STAT1_MOUSE
ID STAT1_MOUSE Reviewed; 749 AA.
AC P42225;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Signal transducer and activator of transcription 1;
GN Name=Stat1;
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].
RC TISSUE=Thymus;
RX PubMed=7545930; DOI=10.1073/pnas.91.11.4806;
RA Zhong Z., Wen Z., Darnell J.E. Jr.;
RT "Stat3 and Stat4: members of the family of signal transducers and
RT activators of transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4806-4810(1994).
RN [2]
RP PHOSPHORYLATION, FUNCTION, AND INTERACTION WITH SRC.
RX PubMed=9344858; DOI=10.1006/bbrc.1997.7493;
RA Cirri P., Chiarugi P., Marra F., Raugei G., Camici G., Manao G.,
RA Ramponi G.;
RT "c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3 cells.";
RL Biochem. Biophys. Res. Commun. 239:493-497(1997).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
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 [4]
RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
RX PubMed=12138178; DOI=10.1128/mcb.22.16.5662-5668.2002;
RA ten Hoeve J., de Jesus Ibarra-Sanchez M., Fu Y., Zhu W., Tremblay M.,
RA David M., Shuai K.;
RT "Identification of a nuclear Stat1 protein tyrosine phosphatase.";
RL Mol. Cell. Biol. 22:5662-5668(2002).
RN [5]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [6]
RP IDENTIFICATION IN THE ISGF3 COMPLEX, PHOSPHORYLATION AT SER-708 AND
RP SER-744, AND MUTAGENESIS OF SER-708 AND 744-SER--SER-747.
RX PubMed=17332413; DOI=10.1126/science.1136567;
RA Tenoever B.R., Ng S.L., Chua M.A., McWhirter S.M., Garcia-Sastre A.,
RA Maniatis T.;
RT "Multiple functions of the IKK-related kinase IKKepsilon in interferon-
RT mediated antiviral immunity.";
RL Science 315:1274-1278(2007).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-701 IN RESPONSE TO CONSTITUTIVELY
RP ACTIVATED FGFR3.
RX PubMed=19088846; DOI=10.1371/journal.pone.0003961;
RA Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A.,
RA Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.;
RT "Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal
RT dysplasia undermines dominant role of STAT1 in FGFR3 signaling in
RT cartilage.";
RL PLoS ONE 3:E3961-E3961(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [9]
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 [10]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-701; SER-708 AND SER-727.
RX PubMed=22065572; DOI=10.1074/jbc.m111.285205;
RA Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.;
RT "Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2
RT proteins define novel innate immune effector pathway against West Nile
RT virus infection.";
RL J. Biol. Chem. 286:44412-44423(2011).
RN [11]
RP INTERACTION WITH OTOP1.
RX PubMed=24379350; DOI=10.2337/db13-1139;
RA Wang G.X., Cho K.W., Uhm M., Hu C.R., Li S., Cozacov Z., Xu A.E.,
RA Cheng J.X., Saltiel A.R., Lumeng C.N., Lin J.D.;
RT "Otopetrin 1 protects mice from obesity-associated metabolic dysfunction
RT through attenuating adipose tissue inflammation.";
RL Diabetes 63:1340-1352(2014).
CC -!- FUNCTION: Signal transducer and transcription activator that mediates
CC cellular responses to interferons (IFNs), cytokine KITLG/SCF and other
CC cytokines and other growth factors. Following type I IFN (IFN-alpha and
CC IFN-beta) binding to cell surface receptors, signaling via protein
CC kinases leads to activation of Jak kinases (TYK2 and JAK1) and to
CC tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs
CC dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3
CC transcription factor, that enters the nucleus. ISGF3 binds to the IFN
CC stimulated response element (ISRE) to activate the transcription of
CC IFN-stimulated genes (ISG), which drive the cell in an antiviral state.
CC In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-
CC phosphorylated. It then forms a homodimer termed IFN-gamma-activated
CC factor (GAF), migrates into the nucleus and binds to the IFN gamma
CC activated sequence (GAS) to drive the expression of the target genes,
CC inducing a cellular antiviral state. Becomes activated in response to
CC KITLG/SCF and KIT signaling. May mediate cellular responses to
CC activated FGFR1, FGFR2, FGFR3 and FGFR4. {ECO:0000269|PubMed:11294897,
CC ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:22065572,
CC ECO:0000269|PubMed:9344858}.
CC -!- SUBUNIT: Homodimerizes upon IFN-gamma induced phosphorylation (By
CC similarity). Heterodimer with STAT2 upon IFN-alpha/beta induced
CC phosphorylation (By similarity). The heterodimer STAT1:STAT2 forms the
CC interferon-stimulated gene factor 3 complex (ISGF3) with IRF9
CC (PubMed:17332413). Interacts (phosphorylated at Ser-727) with PIAS1;
CC the interaction results in release of STAT1 from its target gene (By
CC similarity). Interacts with IFNAR1 (By similarity). Interacts with
CC IFNAR2 (By similarity). Found in a complex with NMI and CREBBP/CBP (By
CC similarity). Interacts with NMI which is required for CREBBP/CBP
CC recruitment to the complex (By similarity). Interacts with PTK2/FAK1
CC (By similarity). Interacts with SRC (PubMed:9344858). Interacts with
CC ERBB4 (phosphorylated) (By similarity). Interacts with PARP9 and DTX3L
CC independently of IFN-beta or IFN-gamma-mediated STAT1 'Tyr-701'
CC phosphorylation (By similarity). Interacts with histone
CC acetyltransferase EP300/p300 in response to INF-gamma stimulation (By
CC similarity). Interacts with OTOP1 (PubMed:24379350). Interacts with
CC IFNGR1 (By similarity). {ECO:0000250|UniProtKB:P42224,
CC ECO:0000269|PubMed:17332413, ECO:0000269|PubMed:24379350,
CC ECO:0000269|PubMed:9344858}.
CC -!- INTERACTION:
CC P42225; P29351: Ptpn6; NbExp=2; IntAct=EBI-647118, EBI-2620699;
CC P42225; P42228: Stat4; NbExp=2; IntAct=EBI-647118, EBI-6253572;
CC P42225; Q61069: Usf1; NbExp=2; IntAct=EBI-647118, EBI-2325635;
CC P42225; Q64705: Usf2; NbExp=3; IntAct=EBI-647118, EBI-647583;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11294897}. Nucleus
CC {ECO:0000269|PubMed:11294897}. Note=Translocated into the nucleus upon
CC tyrosine phosphorylation and dimerization, in response to IFN-gamma and
CC signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Monomethylation at
CC Lys-525 is required for phosphorylation at Tyr-701 and translocation
CC into the nucleus. Translocates into the nucleus in response to
CC interferon-beta stimulation. {ECO:0000250|UniProtKB:P42224}.
CC -!- INDUCTION: By IFN and EGF.
CC -!- PTM: Phosphorylated on tyrosine and serine residues in response to a
CC variety of cytokines/growth hormones including IFN-alpha, IFN-gamma,
CC PDGF and EGF. Activated KIT promotes phosphorylation on tyrosine
CC residues and subsequent translocation to the nucleus. Upon EGF
CC stimulation, phosphorylation on Tyr-701 (lacking in beta form) by JAK1,
CC JAK2 or TYK2 promotes dimerization and subsequent translocation to the
CC nucleus. Growth hormone (GH) activates STAT1 signaling only via JAK2.
CC Tyrosine phosphorylated in response to constitutively activated FGFR1,
CC FGFR2, FGFR3 and FGFR4. Phosphorylation on Ser-727 by several kinases
CC including MAPK14, ERK1/2 and CAMKII on IFN-gamma stimulation, regulates
CC STAT1 transcriptional activity. Phosphorylation on Ser-727 promotes
CC sumoylation though increasing interaction with PIAS. Phosphorylation on
CC Ser-727 by PRKCD induces apoptosis in response to DNA-damaging agents.
CC Phosphorylated on tyrosine residues when PTK2/FAK1 is activated; most
CC likely this is catalyzed by a SRC family kinase. Dephosphorylation on
CC tyrosine residues by PTPN2 negatively regulates interferon-mediated
CC signaling. Upon viral infection or IFN induction, phosphorylation on
CC Ser-708 occurs much later than phosphorylation on Tyr-701 and is
CC required for the binding of ISGF3 on the ISREs of a subset of IFN-
CC stimulated genes IKBKE-dependent. Phosphorylation at Tyr-701 and Ser-
CC 708 are mutually exclusive, phosphorylation at Ser-708 requires
CC previous dephosphorylation of Tyr-701. {ECO:0000269|PubMed:11294897,
CC ECO:0000269|PubMed:12138178, ECO:0000269|PubMed:17332413,
CC ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:21135090,
CC ECO:0000269|PubMed:22065572, ECO:0000269|PubMed:9344858}.
CC -!- PTM: Sumoylated with SUMO1, SUMO2 and SUMO3. Sumoylation is enhanced by
CC IFN-gamma-induced phosphorylation on Ser-727, and by interaction with
CC PIAS proteins. Enhances the transactivation activity.
CC {ECO:0000250|UniProtKB:P42224}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- PTM: Mono-ADP-ribosylated at Glu-657 and Glu-705 by PARP14; ADP-
CC riboslyation prevents phosphorylation at Tyr-701. However, the role of
CC ADP-ribosylation in the prevention of phosphorylation has been called
CC into question and the lack of phosphorylation may be due to sumoylation
CC of Lys-703. {ECO:0000250|UniProtKB:P42224}.
CC -!- PTM: Monomethylated at Lys-525 by SETD2; monomethylation is necessary
CC for phosphorylation at Tyr-701, translocation into the nucleus and
CC activation of the antiviral defense. {ECO:0000250|UniProtKB:P42224}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
CC -!- CAUTION: Has been shown to be mono-ADP-ribosylated at Glu-657 and Glu-
CC 705 by PARP14 which prevents phosphorylation at Tyr-701 (By
CC similarity). However, the role of ADP-ribosylation in the prevention of
CC phosphorylation has been called into question (By similarity). It has
CC been suggested that the lack of phosphorylation may be due to
CC sumoylation of Lys-703 (By similarity). {ECO:0000250|UniProtKB:P42224}.
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DR EMBL; U06924; AAA19454.1; -; mRNA.
DR CCDS; CCDS56628.1; -.
DR AlphaFoldDB; P42225; -.
DR SMR; P42225; -.
DR DIP; DIP-38739N; -.
DR IntAct; P42225; 22.
DR MINT; P42225; -.
DR STRING; 10090.ENSMUSP00000066743; -.
DR BindingDB; P42225; -.
DR ChEMBL; CHEMBL1667670; -.
DR iPTMnet; P42225; -.
DR PhosphoSitePlus; P42225; -.
DR SwissPalm; P42225; -.
DR EPD; P42225; -.
DR MaxQB; P42225; -.
DR PaxDb; P42225; -.
DR PeptideAtlas; P42225; -.
DR PRIDE; P42225; -.
DR ProteomicsDB; 257088; -.
DR MGI; MGI:103063; Stat1.
DR eggNOG; KOG3667; Eukaryota.
DR InParanoid; P42225; -.
DR PhylomeDB; P42225; -.
DR Reactome; R-MMU-1059683; Interleukin-6 signaling.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-877300; Interferon gamma signaling.
DR Reactome; R-MMU-877312; Regulation of IFNG signaling.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8984722; Interleukin-35 Signalling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9020956; Interleukin-27 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR SABIO-RK; P42225; -.
DR ChiTaRS; Stat1; mouse.
DR PRO; PR:P42225; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P42225; protein.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0070721; C:ISGF3 complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0008015; P:blood circulation; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:ARUK-UCL.
DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:MGI.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
DR GO; GO:0072136; P:metanephric mesenchymal cell proliferation involved in metanephros development; ISS:UniProtKB.
DR GO; GO:0046725; P:negative regulation by virus of viral protein levels in host cell; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0034240; P:negative regulation of macrophage fusion; IMP:MGI.
DR GO; GO:0003340; P:negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB.
DR GO; GO:0072308; P:negative regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061326; P:renal tubule development; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:MGI.
DR GO; GO:0051591; P:response to cAMP; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; ISS:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR GO; GO:0035456; P:response to interferon-beta; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR GO; GO:0034340; P:response to type I interferon; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:MGI.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0060337; P:type I interferon signaling pathway; IMP:UniProtKB.
DR CDD; cd10372; SH2_STAT1; 1.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR Gene3D; 6.10.250.3310; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR038295; STAT1_C_sf.
DR InterPro; IPR035859; STAT1_SH2.
DR InterPro; IPR022752; STAT1_TAZ2-bd_C.
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; PF12162; STAT1_TAZ2bind; 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 Acetylation; Activator; ADP-ribosylation; Coiled coil; Cytoplasm;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT CHAIN 2..749
FT /note="Signal transducer and activator of transcription 1"
FT /id="PRO_0000182411"
FT DOMAIN 573..670
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT COILED 136..317
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 114
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 175
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 296
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 366
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 525
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 637
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 657
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 665
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 701
FT /note="Phosphotyrosine; by JAK1, JAK2 or TYK2"
FT /evidence="ECO:0000269|PubMed:19088846,
FT ECO:0000269|PubMed:22065572"
FT MOD_RES 705
FT /note="ADP-ribosyl glutamic acid"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 708
FT /note="Phosphoserine; by IKKE"
FT /evidence="ECO:0000269|PubMed:17332413,
FT ECO:0000269|PubMed:22065572"
FT MOD_RES 727
FT /note="Phosphoserine; by MAPK14"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MOD_RES 744
FT /note="Phosphoserine; by IKKE"
FT /evidence="ECO:0000305|PubMed:17332413"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT CROSSLNK 703
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P42224"
FT MUTAGEN 708
FT /note="Missing: Strongly decreases ISGF3 binding to the
FT ISRE of IKBKE-dependent genes but noo effect on ISGF3
FT binding to the ISRE of IKBKE-independent genes."
FT /evidence="ECO:0000269|PubMed:17332413"
FT MUTAGEN 744..747
FT /note="SMMS->MM: No effect on ISGF3 binding to ISREs."
FT /evidence="ECO:0000269|PubMed:17332413"
SQ SEQUENCE 749 AA; 87197 MW; 249D919952BE65F1 CRC64;
MSQWFELQQL DSKFLEQVHQ LYDDSFPMEI RQYLAQWLEK QDWEHAAYDV SFATIRFHDL
LSQLDDQYSR FSLENNFLLQ HNIRKSKRNL QDNFQEDPVQ MSMIIYNCLK EERKILENAQ
RFNQAQEGNI QNTVMLDKQK ELDSKVRNVK DQVMCIEQEI KTLEELQDEY DFKCKTSQNR
EGEANGVAKS DQKQEQLLLH KMFLMLDNKR KEIIHKIREL LNSIELTQNT LINDELVEWK
RRQQSACIGG PPNACLDQLQ TWFTIVAETL QQIRQQLKKL EELEQKFTYE PDPITKNKQV
LSDRTFLLFQ QLIQSSFVVE RQPCMPTHPQ RPLVLKTGVQ FTVKSRLLVK LQESNLLTKV
KCHFDKDVNE KNTVKGFRKF NILGTHTKVM NMEESTNGSL AAELRHLQLK EQKNAGNRTN
EGPLIVTEEL HSLSFETQLC QPGLVIDLET TSLPVVVISN VSQLPSGWAS ILWYNMLVTE
PRNLSFFLNP PCAWWSQLSE VLSWQFSSVT KRGLNADQLS MLGEKLLGPN AGPDGLIPWT
RFCKENINDK NFSFWPWIDT ILELIKNDLL CLWNDGCIMG FISKERERAL LKDQQPGTFL
LRFSESSREG AITFTWVERS QNGGEPDFHA VEPYTKKELS AVTFPDIIRN YKVMAAENIP
ENPLKYLYPN IDKDHAFGKY YSRPKEAPEP MELDDPKRTG YIKTELISVS EVHPSRLQTT
DNLLPMSPEE FDEMSRIVGP EFDSMMSTV
