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Signal transducer and activator of transcription 5A

 STA5A_HUMAN             Reviewed;         794 AA.
P42229; Q1KLZ6;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
12-SEP-2018, entry version 189.
RecName: Full=Signal transducer and activator of transcription 5A;
Name=STAT5A; Synonyms=STAT5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7719937; DOI=10.1016/1074-7613(95)90140-X;
Hou J., Schindler U., Henzel W.J., Wong S.C., McKnight S.L.;
"Identification and purification of human Stat proteins activated in
response to interleukin-2.";
Immunity 2:321-329(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lin J.X., Mietz J., Modi W.S., John S., Leonard W.J.;
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
Tan D., Deng C., Luben R.A., Walker A.M.;
"Cloning and characterization of a variant of human stat5a, missing a
portion of the n-terminal region, with dominant negative effects on
the growth of breast cancer cells and [beta]-casein gene expression.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CAUTION.
PubMed=11773439; DOI=10.1210/mend.16.1.0761;
Aoki N., Matsuda T.;
"A nuclear protein tyrosine phosphatase TC-PTP is a potential negative
regulator of the PRL-mediated signaling pathway: dephosphorylation and
deactivation of signal transducer and activator of transcription 5a
and 5b by TC-PTP in nucleus.";
Mol. Endocrinol. 16:58-69(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-90; SER-128; SER-193;
TYR-682 AND SER-780, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
RETRACTION, AND CAUTION.
PubMed=24319783; DOI=10.1210/me.2013-1264;
Aoki N., Matsuda T.;
"Retraction.";
Mol. Endocrinol. 27:1982-1982(2013).
[13]
INTERACTION WITH NCOA1.
PubMed=12954634; DOI=10.1074/jbc.M303644200;
Litterst C.M., Kliem S., Marilley D., Pfitzner E.;
"NCoA-1/SRC-1 is an essential coactivator of STAT5 that binds to the
FDL motif in the alpha-helical region of the STAT5 transactivation
domain.";
J. Biol. Chem. 278:45340-45351(2003).
[14]
PHOSPHORYLATION AT TYR-694 BY JAK2.
PubMed=12529425; DOI=10.1091/mbc.E02-08-0454;
Benitah S.A., Valeron P.F., Rui H., Lacal J.C.;
"STAT5a activation mediates the epithelial to mesenchymal transition
induced by oncogenic RhoA.";
Mol. Biol. Cell 14:40-53(2003).
[15]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=14504097; DOI=10.1182/blood-2003-02-0418;
Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R.,
Tsuchida M., Sugita K., Ida K., Hayashi Y.;
"FLT3 mutations in the activation loop of tyrosine kinase domain are
frequently found in infant ALL with MLL rearrangements and pediatric
ALL with hyperdiploidy.";
Blood 103:1085-1088(2004).
[16]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[17]
FUNCTION, INTERACTION WITH ERBB4, AND SUBCELLULAR LOCATION.
PubMed=15534001; DOI=10.1083/jcb.200403155;
Williams C.C., Allison J.G., Vidal G.A., Burow M.E., Beckman B.S.,
Marrero L., Jones F.E.;
"The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by
functioning as a STAT5A nuclear chaperone.";
J. Cell Biol. 167:469-478(2004).
[18]
INTERACTION WITH SOCS7.
PubMed=15677474; DOI=10.1074/jbc.M411596200;
Martens N., Uzan G., Wery M., Hooghe R., Hooghe-Peters E.L.,
Gertler A.;
"Suppressor of cytokine signaling 7 inhibits prolactin, growth
hormone, and leptin signaling by interacting with STAT5 or STAT3 and
attenuating their nuclear translocation.";
J. Biol. Chem. 280:13817-13823(2005).
[19]
PHOSPHORYLATION AT TYR-694 IN RESPONSE TO KIT SIGNALING.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
-!- FUNCTION: Carries out a dual function: signal transduction and
activation of transcription. Mediates cellular responses to the
cytokine KITLG/SCF and other growth factors. Mediates cellular
responses to ERBB4. May mediate cellular responses to activated
FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and
activates PRL-induced transcription. Regulates the expression of
milk proteins during lactation. {ECO:0000269|PubMed:15534001}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member. Binds NR3C1 (By similarity). Interacts with NCOA1 and
SOCS7. Interacts with ERBB4. {ECO:0000250,
ECO:0000269|PubMed:12954634, ECO:0000269|PubMed:15534001,
ECO:0000269|PubMed:15677474}.
-!- INTERACTION:
Q99490-2:AGAP2; NbExp=3; IntAct=EBI-749537, EBI-7737644;
P00533:EGFR; NbExp=3; IntAct=EBI-749537, EBI-297353;
P18031:PTPN1; NbExp=2; IntAct=EBI-749537, EBI-968788;
Q99081:TCF12; NbExp=3; IntAct=EBI-749537, EBI-722877;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15534001}.
Nucleus {ECO:0000269|PubMed:15534001}. Note=Translocated into the
nucleus in response to phosphorylation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P42229-1; Sequence=Displayed;
Name=2;
IsoId=P42229-2; Sequence=VSP_053332;
-!- PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3,
IL7, IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (By similarity).
Activated KIT promotes phosphorylation on tyrosine residues and
subsequent translocation to the nucleus (PubMed:21135090).
Tyrosine phosphorylated in response to constitutively activated
FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Tyrosine
phosphorylation is required for DNA-binding activity and
dimerization. Serine phosphorylation is also required for maximal
transcriptional activity (By similarity). Tyrosine phosphorylated
in response to signaling via activated FLT3; wild-type FLT3
results in much weaker phosphorylation than constitutively
activated mutant FLT3 (PubMed:14504097). Alternatively, can be
phosphorylated by JAK2 at Tyr-694 (PubMed:12529425).
{ECO:0000250|UniProtKB:P40763, ECO:0000250|UniProtKB:P42230,
ECO:0000250|UniProtKB:Q62771, ECO:0000269|PubMed:12529425,
ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:21135090}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P42230}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
-!- CAUTION: It was reported that dephosphorylation on tyrosine
residues by PTPN2 would negatively regulate prolactin signaling
pathway (PubMed:11773439). However, the corresponding article has
been retracted (PubMed:24319783). {ECO:0000269|PubMed:11773439,
ECO:0000303|PubMed:24319783}.
-!- WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry;
URL="https://en.wikipedia.org/wiki/STAT5";
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EMBL; L41142; AAA73962.1; -; mRNA.
EMBL; U43185; AAB06589.1; -; mRNA.
EMBL; DQ471288; ABF17939.1; -; mRNA.
EMBL; AK301457; BAH13486.1; -; mRNA.
EMBL; AC087691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027036; AAH27036.1; -; mRNA.
CCDS; CCDS11424.1; -. [P42229-1]
CCDS; CCDS74067.1; -. [P42229-2]
PIR; G02317; G02317.
RefSeq; NP_001275647.1; NM_001288718.1. [P42229-1]
RefSeq; NP_001275648.1; NM_001288719.1. [P42229-2]
RefSeq; NP_001275649.1; NM_001288720.1.
RefSeq; NP_003143.2; NM_003152.3. [P42229-1]
UniGene; Hs.437058; -.
ProteinModelPortal; P42229; -.
SMR; P42229; -.
BioGrid; 112653; 83.
CORUM; P42229; -.
DIP; DIP-396N; -.
IntAct; P42229; 52.
MINT; P42229; -.
STRING; 9606.ENSP00000341208; -.
BindingDB; P42229; -.
ChEMBL; CHEMBL5403; -.
iPTMnet; P42229; -.
PhosphoSitePlus; P42229; -.
BioMuta; STAT5A; -.
DMDM; 1174462; -.
EPD; P42229; -.
MaxQB; P42229; -.
PaxDb; P42229; -.
PeptideAtlas; P42229; -.
PRIDE; P42229; -.
ProteomicsDB; 55495; -.
DNASU; 6776; -.
Ensembl; ENST00000345506; ENSP00000341208; ENSG00000126561. [P42229-1]
Ensembl; ENST00000546010; ENSP00000443107; ENSG00000126561. [P42229-2]
Ensembl; ENST00000590949; ENSP00000468749; ENSG00000126561. [P42229-1]
GeneID; 6776; -.
KEGG; hsa:6776; -.
UCSC; uc002hzj.3; human. [P42229-1]
CTD; 6776; -.
DisGeNET; 6776; -.
EuPathDB; HostDB:ENSG00000126561.16; -.
GeneCards; STAT5A; -.
HGNC; HGNC:11366; STAT5A.
HPA; CAB003860; -.
HPA; HPA027873; -.
HPA; HPA042128; -.
HPA; HPA049883; -.
HPA; HPA051156; -.
MIM; 601511; gene.
neXtProt; NX_P42229; -.
OpenTargets; ENSG00000126561; -.
PharmGKB; PA338; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOGENOM; HOG000230988; -.
HOVERGEN; HBG107486; -.
InParanoid; P42229; -.
KO; K11223; -.
OMA; ITIAWVN; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P42229; -.
TreeFam; TF318648; -.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
Reactome; R-HSA-8854691; Interleukin-20 family signaling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-8985947; Interleukin-9 signaling.
Reactome; R-HSA-9020558; Interleukin-2 signaling.
Reactome; R-HSA-9020958; Interleukin-21 signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P42229; -.
SIGNOR; P42229; -.
ChiTaRS; STAT5A; human.
GeneWiki; STAT5A; -.
GenomeRNAi; 6776; -.
PRO; PR:P42229; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000126561; Expressed in 148 organ(s), highest expression level in subcutaneous adipose tissue.
CleanEx; HS_STAT5A; -.
ExpressionAtlas; P42229; baseline and differential.
Genevisible; P42229; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:BHF-UCL.
GO; GO:0000255; P:allantoin metabolic process; ISS:BHF-UCL.
GO; GO:0006101; P:citrate metabolic process; ISS:BHF-UCL.
GO; GO:0006600; P:creatine metabolic process; ISS:BHF-UCL.
GO; GO:0046449; P:creatinine metabolic process; ISS:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006631; P:fatty acid metabolic process; ISS:BHF-UCL.
GO; GO:0035723; P:interleukin-15-mediated signaling pathway; TAS:Reactome.
GO; GO:0038110; P:interleukin-2-mediated signaling pathway; TAS:Reactome.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0038113; P:interleukin-9-mediated signaling pathway; TAS:Reactome.
GO; GO:0006549; P:isoleucine metabolic process; ISS:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0007595; P:lactation; IEA:UniProtKB-KW.
GO; GO:0006107; P:oxaloacetate metabolic process; ISS:BHF-UCL.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:BHF-UCL.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0006105; P:succinate metabolic process; ISS:BHF-UCL.
GO; GO:0019530; P:taurine metabolic process; ISS:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006573; P:valine metabolic process; ISS:BHF-UCL.
Gene3D; 1.10.532.10; -; 1.
Gene3D; 2.60.40.630; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001217; STAT.
InterPro; IPR035858; STAT5a/5b.
InterPro; IPR036535; STAT_N_sf.
InterPro; IPR013800; STAT_TF_alpha.
InterPro; IPR015988; STAT_TF_coiled-coil.
InterPro; IPR013801; STAT_TF_DNA-bd.
InterPro; IPR012345; STAT_TF_DNA-bd_N.
InterPro; IPR013799; STAT_TF_prot_interaction.
PANTHER; PTHR11801; PTHR11801; 1.
PANTHER; PTHR11801:SF47; PTHR11801:SF47; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF01017; STAT_alpha; 1.
Pfam; PF02864; STAT_bind; 1.
Pfam; PF02865; STAT_int; 1.
SMART; SM00252; SH2; 1.
SMART; SM00964; STAT_int; 1.
SUPFAM; SSF47655; SSF47655; 1.
SUPFAM; SSF48092; SSF48092; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; Cytoplasm;
DNA-binding; Lactation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; SH2 domain; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 794 Signal transducer and activator of
transcription 5A.
/FTId=PRO_0000182423.
DOMAIN 589 686 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 682 682 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 694 694 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:12529425,
ECO:0000269|PubMed:21135090}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 96 125 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_053332.
VARIANT 389 389 R -> H (in dbSNP:rs2230134).
/FTId=VAR_052073.
CONFLICT 88 88 G -> R (in Ref. 2; AAB06589).
{ECO:0000305}.
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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