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Signal transducer and activator of transcription 5B

 STA5B_MOUSE             Reviewed;         786 AA.
P42232; A2A5D5; Q541Q5; Q60804; Q8K3Q1; Q9JKM1; Q9R0X8;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 182.
RecName: Full=Signal transducer and activator of transcription 5B;
Name=Stat5b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X A/J; TISSUE=Liver;
PubMed=7720707;
Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.;
"Interleukin-3, granulocyte-macrophage colony stimulating factor and
interleukin-5 transduce signals through two STAT5 homologs.";
EMBO J. 14:1166-1175(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J;
PubMed=7568026; DOI=10.1073/pnas.92.19.8831;
Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.;
"Cloning and expression of Stat5 and an additional homologue (Stat5b)
involved in prolactin signal transduction in mouse mammary tissue.";
Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=11161808; DOI=10.1006/geno.2000.6433;
Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
Oka T., Dewar K., Hennighausen L.;
"Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
zebrafish to mouse.";
Genomics 71:150-155(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-327.
STRAIN=BALB/cJ, C3H/HeJ, C57BL/6J, CBA/J, and NOD;
PubMed=14701862; DOI=10.1074/jbc.M312110200;
Davoodi-Semiromi A., Laloraya M., Kumar G.P., Purohit S., Jha R.K.,
She J.-X.;
"A mutant Stat5b with weaker DNA binding affinity defines a key
defective pathway in non-obese diabetic (NOD) mice.";
J. Biol. Chem. 279:11553-11561(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Dendritic cell, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
PubMed=10835485; DOI=10.1007/s002390010058;
Seyfert H.-M., Pitra C., Meyer L., Brunner R.M., Wheeler T.T.,
Molenaar A., McCracken J.Y., Herrmann J., Thiesen H.-J., Schwerin M.;
"Molecular characterization of STAT5A- and STAT5B-encoding genes
reveals extended intragenic sequence homogeneity in cattle and mouse
and different degrees of divergent evolution of various domains.";
J. Mol. Evol. 50:550-561(2000).
[9]
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).
[10]
INTERACTION WITH NR3C1.
PubMed=9528750; DOI=10.1128/MCB.18.4.1783;
Cella N., Groner B., Hynes N.E.;
"Characterization of Stat5a and Stat5b homodimers and heterodimers and
their association with the glucocortiocoid receptor in mammary
cells.";
Mol. Cell. Biol. 18:1783-1792(1998).
[11]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=11090077;
Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T.,
Kienast J., Kanakura Y., Berdel W.E., Serve H.;
"Flt3 mutations from patients with acute myeloid leukemia induce
transformation of 32D cells mediated by the Ras and STAT5 pathways.";
Blood 96:3907-3914(2000).
[12]
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).
[13]
RETRACTION, AND CAUTION.
PubMed=24319783; DOI=10.1210/me.2013-1264;
Aoki N., Matsuda T.;
"Retraction.";
Mol. Endocrinol. 27:1982-1982(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
INTERACTION WITH CPEB3, AND SUBCELLULAR LOCATION.
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).
[16]
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).
[17]
PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(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. Binds to the GAS
element and activates PRL-induced transcription. Positively
regulates hematopoietic/erythroid differentiation.
{ECO:0000269|PubMed:7568026}.
-!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
member. Binds NR3C1 (PubMed:9528750). Interacts with NCOA1 (By
similarity). Interacts with SOCS7 (By similarity). Interacts (via
SH2 domain) with INSR (PubMed:9428692). Interacts with CPEB3; this
inhibits STAT5B-mediated transcriptional activation
(PubMed:20639532). {ECO:0000250|UniProtKB:P51692,
ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:9428692,
ECO:0000269|PubMed:9528750}.
-!- INTERACTION:
Q96EY1:DNAJA3 (xeno); NbExp=3; IntAct=EBI-617454, EBI-356767;
Q96EY1-1:DNAJA3 (xeno); NbExp=2; IntAct=EBI-617454, EBI-4322330;
Q96EY1-2:DNAJA3 (xeno); NbExp=2; IntAct=EBI-617454, EBI-3952284;
P19941:GHR (xeno); NbExp=6; IntAct=EBI-617454, EBI-7526279;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639532}.
Nucleus {ECO:0000269|PubMed:20639532}. Note=Translocated into the
nucleus in response to phosphorylation.
-!- TISSUE SPECIFICITY: In the virgin, found in most tissues.
Particularly abundant in muscle tissue of virgin and lactating
females, and of males. {ECO:0000269|PubMed:7568026}.
-!- DEVELOPMENTAL STAGE: Detected both in virgin mouse and after
mammary gland involution. The level of STAT5A increases constantly
during pregnancy, but decreases during lactation.
{ECO:0000269|PubMed:7568026}.
-!- 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 (By similarity). Phosphorylation at Tyr-699
by PTK6 or HCK leads to an increase of its transcriptional
activity (By similarity). {ECO:0000250|UniProtKB:P51692,
ECO:0000269|PubMed:11773439, ECO:0000269|PubMed:21135090,
ECO:0000269|PubMed:21262971}.
-!- SIMILARITY: Belongs to the transcription factor STAT family.
{ECO:0000305}.
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EMBL; Z48539; CAA88420.1; -; mRNA.
EMBL; U21110; AAC52282.1; -; mRNA.
EMBL; AF234171; AAF62911.2; -; Genomic_DNA.
EMBL; AY040231; AAK74074.1; -; mRNA.
EMBL; AY042906; AAL05590.1; -; mRNA.
EMBL; AY044901; AAK97791.1; -; mRNA.
EMBL; AY044902; AAK97792.1; -; mRNA.
EMBL; AY044903; AAK97793.1; -; mRNA.
EMBL; AK150098; BAE29305.1; -; mRNA.
EMBL; AK154014; BAE32317.1; -; mRNA.
EMBL; AK154664; BAE32752.1; -; mRNA.
EMBL; AL591466; CAM19465.1; -; Genomic_DNA.
EMBL; BC024319; AAH24319.1; -; mRNA.
EMBL; AJ237939; CAB51862.1; -; Genomic_DNA.
CCDS; CCDS25438.1; -.
PIR; I49274; I49274.
RefSeq; NP_001107035.1; NM_001113563.1.
RefSeq; NP_035619.3; NM_011489.3.
RefSeq; XP_017169892.1; XM_017314403.1.
UniGene; Mm.34064; -.
ProteinModelPortal; P42232; -.
SMR; P42232; -.
BioGrid; 203526; 6.
DIP; DIP-898N; -.
IntAct; P42232; 4.
STRING; 10090.ENSMUSP00000004143; -.
iPTMnet; P42232; -.
PhosphoSitePlus; P42232; -.
EPD; P42232; -.
MaxQB; P42232; -.
PaxDb; P42232; -.
PeptideAtlas; P42232; -.
PRIDE; P42232; -.
Ensembl; ENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919.
Ensembl; ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
GeneID; 20851; -.
KEGG; mmu:20851; -.
UCSC; uc007lmi.2; mouse.
CTD; 6777; -.
MGI; MGI:103035; Stat5b.
eggNOG; KOG3667; Eukaryota.
eggNOG; ENOG410XPN8; LUCA.
GeneTree; ENSGT00760000119236; -.
HOVERGEN; HBG107486; -.
InParanoid; P42232; -.
KO; K11224; -.
OMA; VWNLMPY; -.
OrthoDB; EOG091G03O3; -.
PhylomeDB; P42232; -.
TreeFam; TF318648; -.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-2586551; Signaling by Leptin.
Reactome; R-MMU-2586552; Signaling by Leptin.
Reactome; R-MMU-451927; Interleukin-2 family signaling.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-8983432; Interleukin-15 signaling.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
ChiTaRS; Stat5b; mouse.
PRO; PR:P42232; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020919; -.
Genevisible; P42232; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0035259; F:glucocorticoid receptor binding; ISO:MGI.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0004871; F:signal transducer activity; IGI:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006103; P:2-oxoglutarate metabolic process; IMP:BHF-UCL.
GO; GO:0000255; P:allantoin metabolic process; IMP: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; IDA:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
GO; GO:0006101; P:citrate metabolic process; IMP:BHF-UCL.
GO; GO:0006600; P:creatine metabolic process; IMP:BHF-UCL.
GO; GO:0046449; P:creatinine metabolic process; IMP:BHF-UCL.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:MGI.
GO; GO:0046544; P:development of secondary male sexual characteristics; IMP:MGI.
GO; GO:0006631; P:fatty acid metabolic process; IMP:BHF-UCL.
GO; GO:0007565; P:female pregnancy; IMP:MGI.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0006549; P:isoleucine metabolic process; IMP:BHF-UCL.
GO; GO:0007259; P:JAK-STAT cascade; IDA:MGI.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
GO; GO:0007595; P:lactation; IMP:MGI.
GO; GO:0019915; P:lipid storage; IGI:MGI.
GO; GO:0001553; P:luteinization; IGI:MGI.
GO; GO:0097531; P:mast cell migration; IMP:MGI.
GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IGI:MGI.
GO; GO:0006107; P:oxaloacetate metabolic process; IMP:BHF-UCL.
GO; GO:0048541; P:Peyer's patch development; IGI:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IGI:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; IGI:MGI.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IGI:MGI.
GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IGI:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0042448; P:progesterone metabolic process; IGI:MGI.
GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IDA:BHF-UCL.
GO; GO:0019218; P:regulation of steroid metabolic process; IGI:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0032355; P:response to estradiol; ISO:MGI.
GO; GO:0070672; P:response to interleukin-15; IMP:MGI.
GO; GO:0070669; P:response to interleukin-2; IMP:MGI.
GO; GO:0070670; P:response to interleukin-4; IMP:MGI.
GO; GO:0007548; P:sex differentiation; IMP:MGI.
GO; GO:0006105; P:succinate metabolic process; IMP:BHF-UCL.
GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI.
GO; GO:0043029; P:T cell homeostasis; IGI:MGI.
GO; GO:0019530; P:taurine metabolic process; IMP:BHF-UCL.
GO; GO:0006573; P:valine metabolic process; IMP: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; DNA-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
Transcription; Transcription regulation.
CHAIN 1 786 Signal transducer and activator of
transcription 5B.
/FTId=PRO_0000182430.
DOMAIN 589 686 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000250|UniProtKB:P51692}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:P51692}.
MOD_RES 699 699 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
VARIANT 327 327 L -> M (in strain: NOD; reduces DNA-
binding affinity).
{ECO:0000269|PubMed:14701862}.
MUTAGEN 684 684 T->A: Fails to interact with INSR.
{ECO:0000269|PubMed:9428692}.
CONFLICT 210 210 S -> P (in Ref. 8; CAB51862).
{ECO:0000305}.
CONFLICT 433 433 E -> G (in Ref. 2; AAC52282 and 4;
AAL05590/AAK97791/AAK97792/AAK97793).
{ECO:0000305}.
SEQUENCE 786 AA; 90002 MW; A8FE76405E41B2EF CRC64;
MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQSTYDR CPMELVRCIR HILYNEQRLV
REANNGSSPA GSLADAMSQK HLQINQTFEE LRLITQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLG QLNPQERMSR ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRSDRR GAESVTEEKF TILFDSQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI
SSNHLEDYNS MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL
GDLNYLIYVF PDRPKDEVYS KYYTPVPCEP ATAKAADGYV KPQIKQVVPE FANASTDAGS
GATYMDQAPS PVVCPQAHYN MYPPNPDSVL DTDGDFDLED TMDVARRVEE LLGRPMDSQW
IPHAQS


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