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Signal transducer and activator of transcription 5B

 STA5B_HUMAN             Reviewed;         787 AA.
P51692; Q8WWS8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
20-JUN-2018, entry version 187.
RecName: Full=Signal transducer and activator of transcription 5B;
Name=STAT5B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8732682; DOI=10.1210/mend.10.5.8732682;
Silva C.M., Lu H., Day R.N.;
"Characterization and cloning of STAT5 from IM-9 cells and its
activation by growth hormone.";
Mol. Endocrinol. 10:508-518(1996).
[2]
SEQUENCE REVISION TO 628; 717 AND 720.
Silva C.M., Lu H.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8631883; DOI=10.1074/jbc.271.18.10690;
Lin J.-X., Mietz J., Modi W.S., John S., Leonard W.J.;
"Cloning of human Stat5B. Reconstitution of interleukin-2-induced
Stat5A and Stat5B DNA binding activity in COS-7 cells.";
J. Biol. Chem. 271:10738-10744(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12039059; DOI=10.1016/S0378-1119(02)00421-3;
Ambrosio R., Fimiani G., Monfregola J., Sanzari E., De Felice N.,
Salerno M.C., Pignata C., D'Urso M., Ursini M.V.;
"The structure of human STAT5A and B genes reveals two regions of
nearly identical sequence and an alternative tissue specific STAT5B
promoter.";
Gene 285:311-318(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
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).
[6]
PHOSPHORYLATION BY INSR, INTERACTION WITH INSR, AND MUTAGENESIS OF
THR-684.
PubMed=9428692; DOI=10.1111/j.1432-1033.1997.0411a.x;
Sawka-Verhelle D., Filloux C., Tartare-Deckert S., Mothe I.,
Van Obberghen E.;
"Identification of Stat 5B as a substrate of the insulin receptor.";
Eur. J. Biochem. 250:411-417(1997).
[7]
INTERACTION WITH NMI.
PubMed=9989503; DOI=10.1016/S0092-8674(00)80965-4;
Zhu M.-H., John S., Berg M., Leonard W.J.;
"Functional association of Nmi with Stat5 and Stat1 in IL-2- and
IFNgamma-mediated signaling.";
Cell 96:121-130(1999).
[8]
PHOSPHORYLATION AT TYR-699, AND MUTAGENESIS OF TYR-699.
PubMed=12411494; DOI=10.1093/emboj/cdf562;
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A.,
Wilson M., Smithgall T.E., Skorski T.;
"The Src family kinase Hck couples BCR/ABL to STAT5 activation in
myeloid leukemia cells.";
EMBO J. 21:5766-5774(2002).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-90; SER-128 AND SER-193,
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).
[17]
RETRACTION, AND CAUTION.
PubMed=24319783; DOI=10.1210/me.2013-1264;
Aoki N., Matsuda T.;
"Retraction.";
Mol. Endocrinol. 27:1982-1982(2013).
[18]
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).
[19]
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).
[20]
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).
[21]
PHOSPHORYLATION BY JAK2.
PubMed=15121872; DOI=10.1128/MCB.24.10.4557-4570.2004;
Kurzer J.H., Argetsinger L.S., Zhou Y.J., Kouadio J.L., O'Shea J.J.,
Carter-Su C.;
"Tyrosine 813 is a site of JAK2 autophosphorylation critical for
activation of JAK2 by SH2-B beta.";
Mol. Cell. Biol. 24:4557-4570(2004).
[22]
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).
[23]
INVOLVEMENT IN GHII.
PubMed=15827093; DOI=10.1210/jc.2005-0515;
Hwa V., Little B., Adiyaman P., Kofoed E.M., Pratt K.L., Ocal G.,
Berberoglu M., Rosenfeld R.G.;
"Severe growth hormone insensitivity resulting from total absence of
signal transducer and activator of transcription 5b.";
J. Clin. Endocrinol. Metab. 90:4260-4266(2005).
[24]
PHOSPHORYLATION AT TYR-699 BY PTK6.
PubMed=17997837; DOI=10.1186/bcr1794;
Weaver A.M., Silva C.M.;
"Signal transducer and activator of transcription 5b: a new target of
breast tumor kinase/protein tyrosine kinase 6.";
Breast Cancer Res. 9:R79-R79(2007).
[25]
FUNCTION.
PubMed=20702587; DOI=10.1091/mbc.E10-01-0040;
Vignudelli T., Selmi T., Martello A., Parenti S., Grande A.,
Gemelli C., Zanocco-Marani T., Ferrari S.;
"ZFP36L1 negatively regulates erythroid differentiation of CD34+
hematopoietic stem cells by interfering with the Stat5b pathway.";
Mol. Biol. Cell 21:3340-3351(2010).
[26]
INTERACTION WITH CPEB3.
PubMed=20639532; DOI=10.1093/nar/gkq634;
Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
"A novel role of CPEB3 in regulating EGFR gene transcription via
association with Stat5b in neurons.";
Nucleic Acids Res. 38:7446-7457(2010).
[27]
PHOSPHORYLATION 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).
[28]
VARIANT GHII PRO-630.
PubMed=13679528; DOI=10.1056/NEJMoa022926;
Kofoed E.M., Hwa V., Little B., Woods K.A., Buckway C.K., Tsubaki J.,
Pratt K.L., Bezrodnik L., Jasper H., Tepper A., Heinrich J.J.,
Rosenfeld R.G.;
"Growth hormone insensitivity associated with a STAT5b mutation.";
N. Engl. J. Med. 349:1139-1147(2003).
[29]
VARIANT GHII SER-646, AND CHARACTERIZATION OF VARIANT GHII SER-646.
PubMed=22419735; DOI=10.1210/jc.2011-2554;
Scaglia P.A., Martinez A.S., Feigerlova E., Bezrodnik L.,
Gaillard M.I., Di Giovanni D., Ballerini M.G., Jasper H.G.,
Heinrich J.J., Fang P., Domene H.M., Rosenfeld R.G., Hwa V.;
"A Novel Missense Mutation in the SH2 Domain of the STAT5B Gene
Results in a transcriptionally inactive STAT5b associated with severe
IGF-I deficiency, immune dysfunction, and lack of pulmonary disease.";
J. Clin. Endocrinol. Metab. 97:E830-839(2012).
-!- FUNCTION: Carries out a dual function: signal transduction and
activation of transcription. Mediates cellular responses to the
cytokine KITLG/SCF and other growth factors. Binds to the GAS
element and activates PRL-induced transcription. Positively
regulates hematopoietic/erythroid differentiation.
{ECO:0000269|PubMed:20702587, ECO:0000269|PubMed:8732682}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member. Binds NR3C1 (By similarity). Interacts with NCOA1
(PubMed:12954634). Interacts with NMI (PubMed:9989503). Interacts
with SOCS7 (PubMed:15677474). Interacts (via SH2 domain) with INSR
(PubMed:9428692). Interacts with CPEB3; this inhibits STAT5B-
mediated transcriptional activation (PubMed:20639532).
{ECO:0000250|UniProtKB:P42232, ECO:0000269|PubMed:12954634,
ECO:0000269|PubMed:15677474, ECO:0000269|PubMed:20639532,
ECO:0000269|PubMed:9428692, ECO:0000269|PubMed:9989503}.
-!- INTERACTION:
Q96EY1:DNAJA3; NbExp=2; IntAct=EBI-1186119, EBI-356767;
Q13287:NMI; NbExp=7; IntAct=EBI-1186119, EBI-372942;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42232}.
Nucleus {ECO:0000250|UniProtKB:P42232}. Note=Translocated into the
nucleus in response to phosphorylation. {ECO:0000250}.
-!- PTM: Tyrosine phosphorylated in response to signaling via
activated KIT, resulting in translocation to the nucleus. Tyrosine
phosphorylated in response to signaling via activated FLT3; wild-
type FLT3 results in much weaker phosphorylation than
constitutively activated mutant FLT3. Alternatively, can be
phosphorylated by JAK2. Phosphorylation at Tyr-699 by PTK6 or HCK
leads to an increase of its transcriptional activity.
{ECO:0000269|PubMed:12411494, ECO:0000269|PubMed:14504097,
ECO:0000269|PubMed:15121872, ECO:0000269|PubMed:17997837,
ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:9428692}.
-!- DISEASE: Growth hormone insensitivity with immunodeficiency (GHII)
[MIM:245590]: A disease characterized by short stature, growth
hormone deficiency in the presence of normal to elevated
circulating concentrations of growth hormone, resistance to
hexogeneous growth hormone therapy, and recurrent infections.
{ECO:0000269|PubMed:13679528, ECO:0000269|PubMed:15827093,
ECO:0000269|PubMed:22419735}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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=STAT5Bbase; Note=STAT5B mutation db;
URL="http://structure.bmc.lu.se/idbase/STAT5Bbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=STAT5 entry;
URL="https://en.wikipedia.org/wiki/STAT5";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STAT5BID217ch17q21.html";
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EMBL; U48730; AAC50485.2; -; mRNA.
EMBL; U47686; AAC50491.1; -; mRNA.
EMBL; AJ412888; CAD19638.1; -; Genomic_DNA.
EMBL; AJ412889; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412890; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412891; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412892; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412893; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412894; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412895; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412896; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412897; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412898; CAD19638.1; JOINED; Genomic_DNA.
EMBL; AJ412899; CAD19638.1; JOINED; Genomic_DNA.
EMBL; BC065227; AAH65227.1; -; mRNA.
CCDS; CCDS11423.1; -.
RefSeq; NP_036580.2; NM_012448.3.
UniGene; Hs.595276; -.
ProteinModelPortal; P51692; -.
SMR; P51692; -.
BioGrid; 112654; 58.
CORUM; P51692; -.
IntAct; P51692; 26.
MINT; P51692; -.
STRING; 9606.ENSP00000293328; -.
BindingDB; P51692; -.
ChEMBL; CHEMBL5817; -.
DrugBank; DB01254; Dasatinib.
iPTMnet; P51692; -.
PhosphoSitePlus; P51692; -.
BioMuta; STAT5B; -.
DMDM; 41019536; -.
EPD; P51692; -.
MaxQB; P51692; -.
PaxDb; P51692; -.
PeptideAtlas; P51692; -.
PRIDE; P51692; -.
ProteomicsDB; 56378; -.
DNASU; 6777; -.
Ensembl; ENST00000293328; ENSP00000293328; ENSG00000173757.
GeneID; 6777; -.
KEGG; hsa:6777; -.
UCSC; uc002hzh.4; human.
CTD; 6777; -.
DisGeNET; 6777; -.
EuPathDB; HostDB:ENSG00000173757.9; -.
GeneCards; STAT5B; -.
HGNC; HGNC:11367; STAT5B.
HPA; CAB004298; -.
HPA; HPA042128; -.
HPA; HPA049883; -.
HPA; HPA051156; -.
MalaCards; STAT5B; -.
MIM; 245590; phenotype.
MIM; 604260; gene.
neXtProt; NX_P51692; -.
OpenTargets; ENSG00000173757; -.
Orphanet; 520; Acute promyelocytic leukemia.
Orphanet; 220465; Laron syndrome with immunodeficiency.
PharmGKB; PA36186; -.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOVERGEN; HBG107486; -.
InParanoid; P51692; -.
KO; K11224; -.
OMA; YHQTTGT; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P51692; -.
TreeFam; TF318648; -.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
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, 5 and GM-CSF signaling.
Reactome; R-HSA-8854691; Interleukin-20 family signaling.
Reactome; R-HSA-8983432; Interleukin-15 signaling.
Reactome; R-HSA-9020558; Interleukin-2 signaling.
Reactome; R-HSA-9020958; Interleukin-21 signaling.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
SignaLink; P51692; -.
SIGNOR; P51692; -.
ChiTaRS; STAT5B; human.
GeneWiki; STAT5B; -.
GenomeRNAi; 6777; -.
PMAP-CutDB; P51692; -.
PRO; PR:P51692; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000173757; -.
CleanEx; HS_STAT5B; -.
ExpressionAtlas; P51692; baseline and differential.
Genevisible; P51692; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; TAS:ProtInc.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:BHF-UCL.
GO; GO:0000255; P:allantoin metabolic process; ISS:BHF-UCL.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IDA: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:0046543; P:development of secondary female sexual characteristics; IEA:Ensembl.
GO; GO:0046544; P:development of secondary male sexual characteristics; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; ISS:BHF-UCL.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
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: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; IDA:BHF-UCL.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0001553; P:luteinization; IEA:Ensembl.
GO; GO:0097531; P:mast cell migration; IEA:Ensembl.
GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IEA:Ensembl.
GO; GO:0006107; P:oxaloacetate metabolic process; ISS:BHF-UCL.
GO; GO:0048541; P:Peyer's patch development; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:UniProtKB.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IEA:Ensembl.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IEA:Ensembl.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; IEA:Ensembl.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IEA:Ensembl.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:BHF-UCL.
GO; GO:0019218; P:regulation of steroid metabolic process; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
GO; GO:0070670; P:response to interleukin-4; IEA:Ensembl.
GO; GO:0006105; P:succinate metabolic process; ISS:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0019530; P:taurine metabolic process; ISS:BHF-UCL.
GO; GO:0006573; P:valine metabolic process; ISS:BHF-UCL.
CDD; cd10420; SH2_STAT5b; 1.
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; IPR035886; STAT5b_SH2.
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:SF39; PTHR11801:SF39; 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; Complete proteome; Cytoplasm; Disease mutation;
DNA-binding; Dwarfism; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; SH2 domain; Transcription;
Transcription regulation.
CHAIN 1 787 Signal transducer and activator of
transcription 5B.
/FTId=PRO_0000182429.
DOMAIN 589 686 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 232 321 Required for interaction with NMI.
{ECO:0000269|PubMed:9989503}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 682 682 Phosphotyrosine.
{ECO:0000250|UniProtKB:P42229}.
MOD_RES 699 699 Phosphotyrosine; by HCK, JAK and PTK6.
{ECO:0000269|PubMed:12411494,
ECO:0000269|PubMed:17997837}.
VARIANT 130 130 A -> V (in dbSNP:rs2277619).
/FTId=VAR_052074.
VARIANT 630 630 A -> P (in GHII; affects activation by
growth hormone or interferon-gamma;
dbSNP:rs121908501).
{ECO:0000269|PubMed:13679528}.
/FTId=VAR_018728.
VARIANT 646 646 F -> S (in GHII; transcriptionally
inactive). {ECO:0000269|PubMed:22419735}.
/FTId=VAR_067368.
MUTAGEN 684 684 T->A: Abolishes interaction with INSR.
{ECO:0000269|PubMed:9428692}.
MUTAGEN 699 699 Y->F: Abolishes phosphorylation by HCK.
{ECO:0000269|PubMed:12411494}.
CONFLICT 230 230 A -> P (in Ref. 2; AAC50491).
{ECO:0000305}.
SEQUENCE 787 AA; 89866 MW; AA2F1CAB20955ACA CRC64;
MAVWIQAQQL QGEALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSVDLDN PQENIKATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNGSSPA GSLADAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFGPLA QLSPQERLSR ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRSDRR GAESVTEEKF TILFESQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNN
SSSHLEDYSG LSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL
GDLNYLIYVF PDRPKDEVYS KYYTPVPCES ATAKAVDGYV KPQIKQVVPE FVNASADAGG
GSATYMDQAP SPAVCPQAHY NMYPQNPDSV LDTDGDFDLE DTMDVARRVE ELLGRPMDSQ
WIPHAQS


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