STA5A_HUMAN
ID STA5A_HUMAN Reviewed; 794 AA.
AC P42229; Q1KLZ6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Signal transducer and activator of transcription 5A;
GN Name=STAT5A; Synonyms=STAT5;
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).
RX PubMed=7719937; DOI=10.1016/1074-7613(95)90140-x;
RA Hou J., Schindler U., Henzel W.J., Wong S.C., McKnight S.L.;
RT "Identification and purification of human Stat proteins activated in
RT response to interleukin-2.";
RL Immunity 2:321-329(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Lin J.X., Mietz J., Modi W.S., John S., Leonard W.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA Tan D., Deng C., Luben R.A., Walker A.M.;
RT "Cloning and characterization of a variant of human stat5a, missing a
RT portion of the n-terminal region, with dominant negative effects on the
RT growth of breast cancer cells and [beta]-casein gene expression.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Synovium;
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 [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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [7]
RP CAUTION.
RX PubMed=11773439; DOI=10.1210/mend.16.1.0761;
RA Aoki N., Matsuda T.;
RT "A nuclear protein tyrosine phosphatase TC-PTP is a potential negative
RT regulator of the PRL-mediated signaling pathway: dephosphorylation and
RT deactivation of signal transducer and activator of transcription 5a and 5b
RT by TC-PTP in nucleus.";
RL Mol. Endocrinol. 16:58-69(2002).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-90; SER-128; SER-193; TYR-682
RP AND SER-780, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [12]
RP RETRACTION NOTICE OF PUBMED:23186163, AND CAUTION.
RX PubMed=24319783; DOI=10.1210/me.2013-1264;
RA Aoki N., Matsuda T.;
RT "Retraction.";
RL Mol. Endocrinol. 27:1982-1982(2013).
RN [13]
RP INTERACTION WITH NCOA1.
RX PubMed=12954634; DOI=10.1074/jbc.m303644200;
RA Litterst C.M., Kliem S., Marilley D., Pfitzner E.;
RT "NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the FDL
RT motif in the alpha-helical region of the STAT5 transactivation domain.";
RL J. Biol. Chem. 278:45340-45351(2003).
RN [14]
RP PHOSPHORYLATION AT TYR-694 BY JAK2.
RX PubMed=12529425; DOI=10.1091/mbc.e02-08-0454;
RA Benitah S.A., Valeron P.F., Rui H., Lacal J.C.;
RT "STAT5a activation mediates the epithelial to mesenchymal transition
RT induced by oncogenic RhoA.";
RL Mol. Biol. Cell 14:40-53(2003).
RN [15]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=14504097; DOI=10.1182/blood-2003-02-0418;
RA Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R.,
RA Tsuchida M., Sugita K., Ida K., Hayashi Y.;
RT "FLT3 mutations in the activation loop of tyrosine kinase domain are
RT frequently found in infant ALL with MLL rearrangements and pediatric ALL
RT with hyperdiploidy.";
RL Blood 103:1085-1088(2004).
RN [16]
RP REVIEW ON ROLE IN KIT SIGNALING.
RX PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
RA Ronnstrand L.;
RT "Signal transduction via the stem cell factor receptor/c-Kit.";
RL Cell. Mol. Life Sci. 61:2535-2548(2004).
RN [17]
RP FUNCTION, INTERACTION WITH ERBB4, AND SUBCELLULAR LOCATION.
RX PubMed=15534001; DOI=10.1083/jcb.200403155;
RA Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S.,
RA Marrero L., Jones F.E.;
RT "The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by
RT functioning as a STAT5A nuclear chaperone.";
RL J. Cell Biol. 167:469-478(2004).
RN [18]
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 [19]
RP PHOSPHORYLATION AT TYR-694 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).
CC -!- FUNCTION: Carries out a dual function: signal transduction and
CC activation of transcription. Mediates cellular responses to the
CC cytokine KITLG/SCF and other growth factors. Mediates cellular
CC responses to ERBB4. May mediate cellular responses to activated FGFR1,
CC FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-
CC induced transcription. Regulates the expression of milk proteins during
CC lactation. {ECO:0000269|PubMed:15534001}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member. Binds NR3C1 (By similarity). Interacts with NCOA1 and SOCS7.
CC Interacts with ERBB4. {ECO:0000250, ECO:0000269|PubMed:12954634,
CC ECO:0000269|PubMed:15534001, ECO:0000269|PubMed:15677474}.
CC -!- INTERACTION:
CC P42229; Q99490-2: AGAP2; NbExp=3; IntAct=EBI-749537, EBI-7737644;
CC P42229; P00533: EGFR; NbExp=4; IntAct=EBI-749537, EBI-297353;
CC P42229; P18031: PTPN1; NbExp=2; IntAct=EBI-749537, EBI-968788;
CC P42229; Q99081: TCF12; NbExp=3; IntAct=EBI-749537, EBI-722877;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15534001}. Nucleus
CC {ECO:0000269|PubMed:15534001}. Note=Translocated into the nucleus in
CC response to phosphorylation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P42229-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42229-2; Sequence=VSP_053332;
CC -!- PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7,
CC IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (By similarity). Activated KIT
CC promotes phosphorylation on tyrosine residues and subsequent
CC translocation to the nucleus (PubMed:21135090). Tyrosine phosphorylated
CC in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4
CC (By similarity). Tyrosine phosphorylation is required for DNA-binding
CC activity and dimerization. Serine phosphorylation is also required for
CC maximal transcriptional activity (By similarity). Tyrosine
CC phosphorylated in response to signaling via activated FLT3; wild-type
CC FLT3 results in much weaker phosphorylation than constitutively
CC activated mutant FLT3 (PubMed:14504097). Alternatively, can be
CC phosphorylated by JAK2 at Tyr-694 (PubMed:12529425).
CC {ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P42230,
CC ECO:0000250|UniProtKB:Q62771, ECO:0000269|PubMed:12529425,
CC ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:21135090}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P42230}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
CC -!- CAUTION: It was reported that dephosphorylation on tyrosine residues by
CC PTPN2 would negatively regulate prolactin signaling pathway
CC (PubMed:11773439). However, the corresponding article has been
CC retracted (PubMed:24319783). {ECO:0000269|PubMed:11773439,
CC ECO:0000303|PubMed:24319783}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry;
CC URL="https://en.wikipedia.org/wiki/STAT5";
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DR EMBL; L41142; AAA73962.1; -; mRNA.
DR EMBL; U43185; AAB06589.1; -; mRNA.
DR EMBL; DQ471288; ABF17939.1; -; mRNA.
DR EMBL; AK301457; BAH13486.1; -; mRNA.
DR EMBL; AC087691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027036; AAH27036.1; -; mRNA.
DR CCDS; CCDS11424.1; -. [P42229-1]
DR CCDS; CCDS74067.1; -. [P42229-2]
DR PIR; G02317; G02317.
DR RefSeq; NP_001275647.1; NM_001288718.1. [P42229-1]
DR RefSeq; NP_001275648.1; NM_001288719.1. [P42229-2]
DR RefSeq; NP_001275649.1; NM_001288720.1.
DR RefSeq; NP_003143.2; NM_003152.3. [P42229-1]
DR AlphaFoldDB; P42229; -.
DR SMR; P42229; -.
DR BioGRID; 112653; 96.
DR ComplexPortal; CPX-6043; STAT3/STAT5A complex.
DR ComplexPortal; CPX-6045; STAT5A/STAT5B complex.
DR CORUM; P42229; -.
DR DIP; DIP-396N; -.
DR IntAct; P42229; 80.
DR MINT; P42229; -.
DR STRING; 9606.ENSP00000341208; -.
DR BindingDB; P42229; -.
DR ChEMBL; CHEMBL5403; -.
DR GlyGen; P42229; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42229; -.
DR PhosphoSitePlus; P42229; -.
DR BioMuta; STAT5A; -.
DR DMDM; 1174462; -.
DR CPTAC; CPTAC-1270; -.
DR CPTAC; CPTAC-1271; -.
DR CPTAC; CPTAC-1728; -.
DR EPD; P42229; -.
DR jPOST; P42229; -.
DR MassIVE; P42229; -.
DR MaxQB; P42229; -.
DR PaxDb; P42229; -.
DR PeptideAtlas; P42229; -.
DR PRIDE; P42229; -.
DR ProteomicsDB; 55495; -. [P42229-1]
DR ProteomicsDB; 61218; -.
DR Antibodypedia; 3553; 1839 antibodies from 54 providers.
DR DNASU; 6776; -.
DR Ensembl; ENST00000345506.8; ENSP00000341208.4; ENSG00000126561.18. [P42229-1]
DR Ensembl; ENST00000546010.6; ENSP00000443107.1; ENSG00000126561.18. [P42229-2]
DR Ensembl; ENST00000590949.6; ENSP00000468749.1; ENSG00000126561.18. [P42229-1]
DR Ensembl; ENST00000676585.1; ENSP00000504449.1; ENSG00000126561.18. [P42229-1]
DR Ensembl; ENST00000677301.1; ENSP00000503262.1; ENSG00000126561.18. [P42229-1]
DR GeneID; 6776; -.
DR KEGG; hsa:6776; -.
DR MANE-Select; ENST00000590949.6; ENSP00000468749.1; NM_001288718.2; NP_001275647.1.
DR UCSC; uc002hzj.3; human. [P42229-1]
DR CTD; 6776; -.
DR DisGeNET; 6776; -.
DR GeneCards; STAT5A; -.
DR HGNC; HGNC:11366; STAT5A.
DR HPA; ENSG00000126561; Tissue enhanced (adipose).
DR MIM; 601511; gene.
DR neXtProt; NX_P42229; -.
DR OpenTargets; ENSG00000126561; -.
DR PharmGKB; PA338; -.
DR VEuPathDB; HostDB:ENSG00000126561; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR HOGENOM; CLU_014189_2_2_1; -.
DR InParanoid; P42229; -.
DR OMA; GCPMELV; -.
DR PhylomeDB; P42229; -.
DR TreeFam; TF318648; -.
DR PathwayCommons; P42229; -.
DR Reactome; R-HSA-1170546; Prolactin receptor signaling.
DR Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
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-2586552; Signaling by Leptin.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR Reactome; R-HSA-8983432; Interleukin-15 signaling.
DR Reactome; R-HSA-8985947; Interleukin-9 signaling.
DR Reactome; R-HSA-9020558; Interleukin-2 signaling.
DR Reactome; R-HSA-9020958; Interleukin-21 signaling.
DR Reactome; R-HSA-9027283; Erythropoietin activates STAT5.
DR Reactome; R-HSA-9645135; STAT5 Activation.
DR Reactome; R-HSA-9670439; Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants.
DR Reactome; R-HSA-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-HSA-9702518; STAT5 activation downstream of FLT3 ITD mutants.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-9725371; Nuclear events stimulated by ALK signaling in cancer.
DR Reactome; R-HSA-982772; Growth hormone receptor signaling.
DR SignaLink; P42229; -.
DR SIGNOR; P42229; -.
DR BioGRID-ORCS; 6776; 246 hits in 1108 CRISPR screens.
DR ChiTaRS; STAT5A; human.
DR GeneWiki; STAT5A; -.
DR GenomeRNAi; 6776; -.
DR Pharos; P42229; Tchem.
DR PRO; PR:P42229; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P42229; protein.
DR Bgee; ENSG00000126561; Expressed in granulocyte and 117 other tissues.
DR ExpressionAtlas; P42229; baseline and differential.
DR Genevisible; P42229; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
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:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; IDA:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR GO; GO:0019530; P:taurine metabolic process; ISS:BHF-UCL.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 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; IPR035858; STAT5a/5b.
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 PANTHER; PTHR11801:SF47; PTHR11801:SF47; 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; SM00252; SH2; 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 Activator; Alternative splicing; Cytoplasm; DNA-binding; Lactation;
KW Nucleus; Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..794
FT /note="Signal transducer and activator of transcription 5A"
FT /id="PRO_0000182423"
FT DOMAIN 589..686
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 773..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 682
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 694
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000269|PubMed:12529425,
FT ECO:0000269|PubMed:21135090"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 96..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_053332"
FT VARIANT 389
FT /note="R -> H (in dbSNP:rs2230134)"
FT /id="VAR_052073"
FT CONFLICT 88
FT /note="G -> R (in Ref. 2; AAB06589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 90647 MW; C64237295F88CFBE CRC64;
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRAQATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQKTYDR CPLELVRCIR HILYNEQRLV
REANNCSSPA GILVDAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLA QLSPQERLSR ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN
SSSHLEDYSG LSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPERNL WNLKPFTTRD FSIRSLADRL
GDLSYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK QVVPEFVNAS ADAGGSSATY
MDQAPSPAVC PQAPYNMYPQ NPDHVLDQDG EFDLDETMDV ARHVEELLRR PMDSLDSRLS
PPAGLFTSAR GSLS
