GenomeNet

Database: UniProt
Entry: STA5A_HUMAN
LinkDB: STA5A_HUMAN
Original site: 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   31-JUL-2019, entry version 197.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   the 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA   Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA   Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA   Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA   Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA   Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA   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
RT   the 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
RT   project: 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
RT   and 5b 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
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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;
RP   TYR-682 AND SER-780, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   SCALE 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, 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
RT   FDL motif in the alpha-helical region of the STAT5 transactivation
RT   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
RT   ALL 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.,
RA   Gertler A.;
RT   "Suppressor of cytokine signaling 7 inhibits prolactin, growth
RT   hormone, and leptin signaling by interacting with STAT5 or STAT3 and
RT   attenuating their 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
CC       FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and
CC       activates PRL-induced transcription. Regulates the expression of
CC       milk proteins during 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
CC       SOCS7. Interacts with ERBB4. {ECO:0000250,
CC       ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:15534001,
CC       ECO:0000269|PubMed:15677474}.
CC   -!- INTERACTION:
CC       Q99490-2:AGAP2; NbExp=3; IntAct=EBI-749537, EBI-7737644;
CC       P00533:EGFR; NbExp=3; IntAct=EBI-749537, EBI-297353;
CC       P18031:PTPN1; NbExp=2; IntAct=EBI-749537, EBI-968788;
CC       Q99081:TCF12; NbExp=3; IntAct=EBI-749537, EBI-722877;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15534001}.
CC       Nucleus {ECO:0000269|PubMed:15534001}. Note=Translocated into the
CC       nucleus in 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,
CC       IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (By similarity).
CC       Activated KIT promotes phosphorylation on tyrosine residues and
CC       subsequent translocation to the nucleus (PubMed:21135090).
CC       Tyrosine phosphorylated in response to constitutively activated
CC       FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Tyrosine
CC       phosphorylation is required for DNA-binding activity and
CC       dimerization. Serine phosphorylation is also required for maximal
CC       transcriptional activity (By similarity). Tyrosine phosphorylated
CC       in response to signaling via activated FLT3; wild-type FLT3
CC       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
CC       residues by PTPN2 would negatively regulate prolactin signaling
CC       pathway (PubMed:11773439). However, the corresponding article has
CC       been 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";
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   SMR; P42229; -.
DR   BioGrid; 112653; 83.
DR   CORUM; P42229; -.
DR   DIP; DIP-396N; -.
DR   IntAct; P42229; 51.
DR   MINT; P42229; -.
DR   STRING; 9606.ENSP00000341208; -.
DR   BindingDB; P42229; -.
DR   ChEMBL; CHEMBL5403; -.
DR   iPTMnet; P42229; -.
DR   PhosphoSitePlus; P42229; -.
DR   BioMuta; STAT5A; -.
DR   DMDM; 1174462; -.
DR   CPTAC; CPTAC-1270; -.
DR   CPTAC; CPTAC-1271; -.
DR   EPD; P42229; -.
DR   jPOST; P42229; -.
DR   MaxQB; P42229; -.
DR   PaxDb; P42229; -.
DR   PeptideAtlas; P42229; -.
DR   PRIDE; P42229; -.
DR   ProteomicsDB; 55495; -. [P42229-1]
DR   ProteomicsDB; 61218; -.
DR   DNASU; 6776; -.
DR   Ensembl; ENST00000345506; ENSP00000341208; ENSG00000126561. [P42229-1]
DR   Ensembl; ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
DR   Ensembl; ENST00000590949; ENSP00000468749; ENSG00000126561. [P42229-1]
DR   GeneID; 6776; -.
DR   KEGG; hsa:6776; -.
DR   UCSC; uc002hzj.3; human. [P42229-1]
DR   CTD; 6776; -.
DR   DisGeNET; 6776; -.
DR   GeneCards; STAT5A; -.
DR   HGNC; HGNC:11366; STAT5A.
DR   HPA; CAB003860; -.
DR   HPA; HPA027873; -.
DR   HPA; HPA042128; -.
DR   HPA; HPA049883; -.
DR   HPA; HPA051156; -.
DR   MIM; 601511; gene.
DR   neXtProt; NX_P42229; -.
DR   OpenTargets; ENSG00000126561; -.
DR   PharmGKB; PA338; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   eggNOG; ENOG410XPN8; LUCA.
DR   GeneTree; ENSGT00950000182688; -.
DR   HOGENOM; HOG000230988; -.
DR   InParanoid; P42229; -.
DR   KO; K11223; -.
DR   OMA; TMDERGH; -.
DR   OrthoDB; 327469at2759; -.
DR   PhylomeDB; P42229; -.
DR   TreeFam; TF318648; -.
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-982772; Growth hormone receptor signaling.
DR   SignaLink; P42229; -.
DR   SIGNOR; P42229; -.
DR   ChiTaRS; STAT5A; human.
DR   GeneWiki; STAT5A; -.
DR   GenomeRNAi; 6776; -.
DR   PRO; PR:P42229; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000126561; Expressed in 148 organ(s), highest expression level in subcutaneous adipose tissue.
DR   ExpressionAtlas; P42229; baseline and differential.
DR   Genevisible; P42229; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
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 proximal promoter 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:0035723; P:interleukin-15-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038110; P:interleukin-2-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0038113; P:interleukin-9-mediated signaling pathway; TAS:Reactome.
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; IBA:GO_Central.
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; TAS:ProtInc.
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; Complete proteome; Cytoplasm;
KW   DNA-binding; Lactation; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    794       Signal transducer and activator of
FT                                transcription 5A.
FT                                /FTId=PRO_0000182423.
FT   DOMAIN      589    686       SH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00191}.
FT   MOD_RES      90     90       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     128    128       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     193    193       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     682    682       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     694    694       Phosphotyrosine; by JAK2.
FT                                {ECO:0000269|PubMed:12529425,
FT                                ECO:0000269|PubMed:21135090}.
FT   MOD_RES     780    780       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ      96    125       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_053332.
FT   VARIANT     389    389       R -> H (in dbSNP:rs2230134).
FT                                /FTId=VAR_052073.
FT   CONFLICT     88     88       G -> R (in Ref. 2; AAB06589).
FT                                {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
//
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