STA5B_MOUSE
ID STA5B_MOUSE Reviewed; 786 AA.
AC P42232; A2A5D5; Q541Q5; Q60804; Q8K3Q1; Q9JKM1; Q9R0X8;
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 5B;
GN Name=Stat5b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X A/J; TISSUE=Liver;
RX PubMed=7720707; DOI=10.1002/j.1460-2075.1995.tb07100.x;
RA Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.;
RT "Interleukin-3, granulocyte-macrophage colony stimulating factor and
RT interleukin-5 transduce signals through two STAT5 homologs.";
RL EMBO J. 14:1166-1175(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=7568026; DOI=10.1073/pnas.92.19.8831;
RA Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.;
RT "Cloning and expression of Stat5 and an additional homologue (Stat5b)
RT involved in prolactin signal transduction in mouse mammary tissue.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=11161808; DOI=10.1006/geno.2000.6433;
RA Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
RA Oka T., Dewar K., Hennighausen L.;
RT "Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
RT zebrafish to mouse.";
RL Genomics 71:150-155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT MET-327.
RC STRAIN=BALB/cJ, C3H/HeJ, C57BL/6J, CBA/J, and NOD;
RX PubMed=14701862; DOI=10.1074/jbc.m312110200;
RA Davoodi-Semiromi A., Laloraya M., Kumar G.P., Purohit S., Jha R.K.,
RA She J.-X.;
RT "A mutant Stat5b with weaker DNA binding affinity defines a key defective
RT pathway in non-obese diabetic (NOD) mice.";
RL J. Biol. Chem. 279:11553-11561(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Dendritic cell, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-389.
RX PubMed=10835485; DOI=10.1007/s002390010058;
RA Seyfert H.-M., Pitra C., Meyer L., Brunner R.M., Wheeler T.T., Molenaar A.,
RA McCracken J.Y., Herrmann J., Thiesen H.-J., Schwerin M.;
RT "Molecular characterization of STAT5A- and STAT5B-encoding genes reveals
RT extended intragenic sequence homogeneity in cattle and mouse and different
RT degrees of divergent evolution of various domains.";
RL J. Mol. Evol. 50:550-561(2000).
RN [9]
RP INTERACTION WITH INSR, AND MUTAGENESIS OF THR-684.
RX PubMed=9428692; DOI=10.1111/j.1432-1033.1997.0411a.x;
RA Sawka-Verhelle D., Filloux C., Tartare-Deckert S., Mothe I.,
RA Van Obberghen E.;
RT "Identification of Stat 5B as a substrate of the insulin receptor.";
RL Eur. J. Biochem. 250:411-417(1997).
RN [10]
RP INTERACTION WITH NR3C1.
RX PubMed=9528750; DOI=10.1128/mcb.18.4.1783;
RA Cella N., Groner B., Hynes N.E.;
RT "Characterization of Stat5a and Stat5b homodimers and heterodimers and
RT their association with the glucocortiocoid receptor in mammary cells.";
RL Mol. Cell. Biol. 18:1783-1792(1998).
RN [11]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=11090077;
RA Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
RA Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J.,
RA Kanakura Y., Berdel W.E., Serve H.;
RT "Flt3 mutations from patients with acute myeloid leukemia induce
RT transformation of 32D cells mediated by the Ras and STAT5 pathways.";
RL Blood 96:3907-3914(2000).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-699, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP RETRACTION NOTICE OF PUBMED:21183079, 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 [15]
RP INTERACTION WITH CPEB3, AND SUBCELLULAR LOCATION.
RX PubMed=20639532; DOI=10.1093/nar/gkq634;
RA Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
RT "A novel role of CPEB3 in regulating EGFR gene transcription via
RT association with Stat5b in neurons.";
RL Nucleic Acids Res. 38:7446-7457(2010).
RN [16]
RP PHOSPHORYLATION 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).
RN [17]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=21262971; DOI=10.1074/jbc.m110.205021;
RA Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
RA Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
RA Muller J.P.;
RT "Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3
RT signaling.";
RL J. Biol. Chem. 286:10918-10929(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. Binds to the GAS element
CC and activates PRL-induced transcription. Positively regulates
CC hematopoietic/erythroid differentiation. {ECO:0000269|PubMed:7568026}.
CC -!- SUBUNIT: Upon activation, forms a homodimer or a heterodimer with a
CC related family member. Binds NR3C1 (PubMed:9528750). Interacts with
CC NCOA1 (By similarity). Interacts with SOCS7 (By similarity). Interacts
CC (via SH2 domain) with INSR (PubMed:9428692). Interacts with CPEB3; this
CC inhibits STAT5B-mediated transcriptional activation (PubMed:20639532).
CC {ECO:0000250|UniProtKB:P51692, ECO:0000269|PubMed:20639532,
CC ECO:0000269|PubMed:9428692, ECO:0000269|PubMed:9528750}.
CC -!- INTERACTION:
CC P42232; Q96EY1: DNAJA3; Xeno; NbExp=3; IntAct=EBI-617454, EBI-356767;
CC P42232; Q96EY1-1: DNAJA3; Xeno; NbExp=2; IntAct=EBI-617454, EBI-4322330;
CC P42232; Q96EY1-2: DNAJA3; Xeno; NbExp=2; IntAct=EBI-617454, EBI-3952284;
CC P42232; P19941: GHR; Xeno; NbExp=6; IntAct=EBI-617454, EBI-7526279;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20639532}. Nucleus
CC {ECO:0000269|PubMed:20639532}. Note=Translocated into the nucleus in
CC response to phosphorylation.
CC -!- TISSUE SPECIFICITY: In the virgin, found in most tissues. Particularly
CC abundant in muscle tissue of virgin and lactating females, and of
CC males. {ECO:0000269|PubMed:7568026}.
CC -!- DEVELOPMENTAL STAGE: Detected both in virgin mouse and after mammary
CC gland involution. The level of STAT5A increases constantly during
CC pregnancy, but decreases during lactation.
CC {ECO:0000269|PubMed:7568026}.
CC -!- PTM: Tyrosine phosphorylated in response to signaling via activated
CC KIT, resulting in translocation to the nucleus. Tyrosine phosphorylated
CC in response to signaling via activated FLT3; wild-type FLT3 results in
CC much weaker phosphorylation than constitutively activated mutant FLT3.
CC Alternatively, can be phosphorylated by JAK2 (By similarity).
CC Phosphorylation at Tyr-699 by PTK6 or HCK leads to an increase of its
CC transcriptional activity (By similarity).
CC {ECO:0000250|UniProtKB:P51692, ECO:0000269|PubMed:11773439,
CC ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21262971}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; Z48539; CAA88420.1; -; mRNA.
DR EMBL; U21110; AAC52282.1; -; mRNA.
DR EMBL; AF234171; AAF62911.2; -; Genomic_DNA.
DR EMBL; AY040231; AAK74074.1; -; mRNA.
DR EMBL; AY042906; AAL05590.1; -; mRNA.
DR EMBL; AY044901; AAK97791.1; -; mRNA.
DR EMBL; AY044902; AAK97792.1; -; mRNA.
DR EMBL; AY044903; AAK97793.1; -; mRNA.
DR EMBL; AK150098; BAE29305.1; -; mRNA.
DR EMBL; AK154014; BAE32317.1; -; mRNA.
DR EMBL; AK154664; BAE32752.1; -; mRNA.
DR EMBL; AL591466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024319; AAH24319.1; -; mRNA.
DR EMBL; AJ237939; CAB51862.1; -; Genomic_DNA.
DR CCDS; CCDS25438.1; -.
DR PIR; I49274; I49274.
DR RefSeq; NP_001107035.1; NM_001113563.1.
DR RefSeq; NP_035619.3; NM_011489.3.
DR RefSeq; XP_017169892.1; XM_017314403.1.
DR AlphaFoldDB; P42232; -.
DR SMR; P42232; -.
DR BioGRID; 203526; 6.
DR DIP; DIP-898N; -.
DR IntAct; P42232; 5.
DR MINT; P42232; -.
DR STRING; 10090.ENSMUSP00000102981; -.
DR BindingDB; P42232; -.
DR ChEMBL; CHEMBL4523225; -.
DR GlyConnect; 2715; 1 N-Linked glycan (1 site).
DR GlyGen; P42232; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; P42232; -.
DR PhosphoSitePlus; P42232; -.
DR SwissPalm; P42232; -.
DR EPD; P42232; -.
DR jPOST; P42232; -.
DR MaxQB; P42232; -.
DR PaxDb; P42232; -.
DR PeptideAtlas; P42232; -.
DR PRIDE; P42232; -.
DR ProteomicsDB; 258652; -.
DR Antibodypedia; 3804; 947 antibodies from 43 providers.
DR DNASU; 20851; -.
DR Ensembl; ENSMUST00000004143; ENSMUSP00000004143; ENSMUSG00000020919.
DR Ensembl; ENSMUST00000107358; ENSMUSP00000102981; ENSMUSG00000020919.
DR GeneID; 20851; -.
DR KEGG; mmu:20851; -.
DR UCSC; uc007lmi.2; mouse.
DR CTD; 6777; -.
DR MGI; MGI:103035; Stat5b.
DR VEuPathDB; HostDB:ENSMUSG00000020919; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR HOGENOM; CLU_014189_2_2_1; -.
DR InParanoid; P42232; -.
DR OMA; HYNMYTQ; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; P42232; -.
DR TreeFam; TF318648; -.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR BioGRID-ORCS; 20851; 7 hits in 83 CRISPR screens.
DR ChiTaRS; Stat5b; mouse.
DR PRO; PR:P42232; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P42232; protein.
DR Bgee; ENSMUSG00000020919; Expressed in gastrocnemius medialis and 241 other tissues.
DR Genevisible; P42232; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:0006953; P:acute-phase response; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:MGI.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IGI:MGI.
DR GO; GO:0007565; P:female pregnancy; IMP:MGI.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IGI:MGI.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IDA:BHF-UCL.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IGI:MGI.
DR GO; GO:0001889; P:liver development; ISO:MGI.
DR GO; GO:0001553; P:luteinization; IGI:MGI.
DR GO; GO:0030098; P:lymphocyte differentiation; IGI:MGI.
DR GO; GO:0097531; P:mast cell migration; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:MGI.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0001787; P:natural killer cell proliferation; IMP:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IGI:MGI.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IGI:MGI.
DR GO; GO:0048541; P:Peyer's patch development; IGI:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:MGI.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IGI:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IGI:MGI.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IGI:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IMP:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0042448; P:progesterone metabolic process; IGI:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:BHF-UCL.
DR GO; GO:0019218; P:regulation of steroid metabolic process; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; ISO:MGI.
DR GO; GO:0070672; P:response to interleukin-15; IMP:MGI.
DR GO; GO:0070669; P:response to interleukin-2; IMP:MGI.
DR GO; GO:0070670; P:response to interleukin-4; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0007548; P:sex differentiation; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IGI:MGI.
DR GO; GO:0019530; P:taurine metabolic process; IGI:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR CDD; cd10420; SH2_STAT5b; 1.
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; IPR035886; STAT5b_SH2.
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; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT CHAIN 1..786
FT /note="Signal transducer and activator of transcription 5B"
FT /id="PRO_0000182430"
FT DOMAIN 589..686
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P51692"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51692"
FT MOD_RES 682
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT MOD_RES 699
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VARIANT 327
FT /note="L -> M (in strain: NOD; reduces DNA-binding
FT affinity)"
FT /evidence="ECO:0000269|PubMed:14701862"
FT MUTAGEN 684
FT /note="T->A: Fails to interact with INSR."
FT /evidence="ECO:0000269|PubMed:9428692"
FT CONFLICT 210
FT /note="S -> P (in Ref. 8; CAB51862)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="E -> G (in Ref. 2; AAC52282 and 4; AAL05590/
FT AAK97791/AAK97792/AAK97793)"
FT /evidence="ECO:0000305"
SQ 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
