ID   STA5B_RAT               Reviewed;         786 AA.
AC   P52632;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   24-JAN-2024, entry version 172.
DE   RecName: Full=Signal transducer and activator of transcription 5B;
GN   Name=Stat5b;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8530402; DOI=10.1074/jbc.270.50.29998;
RA   Ripperger J.A., Fritz S., Richter K., Hocke G.M., Lottspeich F., Fey G.H.;
RT   "Transcription factors Stat3 and Stat5b are present in rat liver nuclei
RT   late in an acute phase response and bind interleukin-6 response elements.";
RL   J. Biol. Chem. 270:29998-30006(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Noble; TISSUE=Lymph node;
RA   Luo G., Yu-Lee L.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128 AND TYR-699, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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.
CC       {ECO:0000250|UniProtKB:P51692}.
CC   -!- SUBUNIT: Upon activation, forms a homodimer or a heterodimer with a
CC       related family member. Binds NR3C1. Interacts with NCOA1. Interacts
CC       with NMI. Interacts with SOCS7. Interacts (via SH2 domain) with INSR.
CC       Interacts with CPEB3; this inhibits STAT5B-mediated transcriptional
CC       activation. {ECO:0000250|UniProtKB:P42232,
CC       ECO:0000250|UniProtKB:P51692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42232}. Nucleus
CC       {ECO:0000250|UniProtKB:P42232}. Note=Translocated into the nucleus in
CC       response to phosphorylation. {ECO:0000250}.
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. Phosphorylation at Tyr-
CC       699 by PTK6 or HCK leads to an increase of its transcriptional
CC       activity. {ECO:0000250|UniProtKB:P51692}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
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DR   EMBL; X91988; CAA63043.1; ALT_TERM; mRNA.
DR   EMBL; X91988; CAA63042.1; -; mRNA.
DR   EMBL; X97541; CAA66141.1; -; mRNA.
DR   RefSeq; NP_071775.1; NM_022380.1.
DR   AlphaFoldDB; P52632; -.
DR   SMR; P52632; -.
DR   DIP; DIP-60986N; -.
DR   IntAct; P52632; 3.
DR   STRING; 10116.ENSRNOP00000026354; -.
DR   iPTMnet; P52632; -.
DR   PhosphoSitePlus; P52632; -.
DR   jPOST; P52632; -.
DR   PaxDb; 10116-ENSRNOP00000026354; -.
DR   GeneID; 25126; -.
DR   KEGG; rno:25126; -.
DR   UCSC; RGD:3774; rat.
DR   AGR; RGD:3774; -.
DR   CTD; 6777; -.
DR   RGD; 3774; Stat5b.
DR   eggNOG; KOG3667; Eukaryota.
DR   InParanoid; P52632; -.
DR   OrthoDB; 7823at2759; -.
DR   PhylomeDB; P52632; -.
DR   TreeFam; TF318648; -.
DR   Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR   Reactome; R-RNO-186763; Downstream signal transduction.
DR   Reactome; R-RNO-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR   Reactome; R-RNO-8854691; Interleukin-20 family signaling.
DR   Reactome; R-RNO-8983432; Interleukin-15 signaling.
DR   Reactome; R-RNO-8985947; Interleukin-9 signaling.
DR   Reactome; R-RNO-9020958; Interleukin-21 signaling.
DR   Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR   PRO; PR:P52632; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:RGD.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:RGD.
DR   GO; GO:0046983; F:protein dimerization activity; ISS: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; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:0050798; P:activated T cell proliferation; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; IDA:RGD.
DR   GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; ISO:RGD.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0046543; P:development of secondary female sexual characteristics; ISO:RGD.
DR   GO; GO:0046544; P:development of secondary male sexual characteristics; ISO:RGD.
DR   GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0007565; P:female pregnancy; ISO:RGD.
DR   GO; GO:0042492; P:gamma-delta T cell differentiation; ISO:RGD.
DR   GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; ISO:RGD.
DR   GO; GO:0007595; P:lactation; ISO:RGD.
DR   GO; GO:0019915; P:lipid storage; ISO:RGD.
DR   GO; GO:0001889; P:liver development; IDA:RGD.
DR   GO; GO:0001553; P:luteinization; IDA:RGD.
DR   GO; GO:0030098; P:lymphocyte differentiation; ISO:RGD.
DR   GO; GO:0097531; P:mast cell migration; ISO:RGD.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR   GO; GO:0033028; P:myeloid cell apoptotic process; ISO:RGD.
DR   GO; GO:0001779; P:natural killer cell differentiation; ISO:RGD.
DR   GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISO:RGD.
DR   GO; GO:0001787; P:natural killer cell proliferation; ISO:RGD.
DR   GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISO:RGD.
DR   GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:RGD.
DR   GO; GO:0048541; P:Peyer's patch development; ISO:RGD.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:RGD.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0090271; P:positive regulation of fibroblast growth factor production; IMP:RGD.
DR   GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD.
DR   GO; GO:0045621; P:positive regulation of lymphocyte differentiation; ISO:RGD.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:RGD.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR   GO; GO:0032825; P:positive regulation of natural killer cell differentiation; ISO:RGD.
DR   GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:RGD.
DR   GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:RGD.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0042448; P:progesterone metabolic process; ISO:RGD.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:RGD.
DR   GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:RGD.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; ISO:RGD.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR   GO; GO:0019218; P:regulation of steroid metabolic process; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0070672; P:response to interleukin-15; ISO:RGD.
DR   GO; GO:0070669; P:response to interleukin-2; ISO:RGD.
DR   GO; GO:0070670; P:response to interleukin-4; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IDA:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IDA:RGD.
DR   GO; GO:0007548; P:sex differentiation; ISO:RGD.
DR   GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR   GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
DR   GO; GO:0019530; P:taurine metabolic process; ISO:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IDA:RGD.
DR   CDD; cd10420; SH2_STAT5b; 1.
DR   CDD; cd16855; STAT5_CCD; 1.
DR   CDD; cd16849; STAT5_DBD; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.20.1050.20; STAT transcription factor, all-alpha domain; 1.
DR   Gene3D; 2.60.40.630; STAT transcription factor, DNA-binding domain; 1.
DR   Gene3D; 1.10.532.10; STAT transcription factor, N-terminal domain; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR046994; STAT5_CCD.
DR   InterPro; IPR035858; STAT5a/5b_DBD.
DR   InterPro; IPR035886; STAT5b_SH2.
DR   InterPro; IPR048988; STAT_linker.
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; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1.
DR   PANTHER; PTHR11801:SF39; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 5B; 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   Pfam; PF21354; STAT_linker; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF47655; STAT; 1.
DR   SUPFAM; SSF48092; Transcription factor STAT-4 N-domain; 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_0000182432"
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:0007744|PubMed:22673903"
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:22673903"
FT   CONFLICT        296
FT                   /note="L -> A (in Ref. 2; CAA66141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="S -> V (in Ref. 2; CAA66141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="R -> A (in Ref. 2; CAA66141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        690
FT                   /note="R -> P (in Ref. 2; CAA66141)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        716
FT                   /note="T -> A (in Ref. 2; CAA66141)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   786 AA;  90223 MW;  52250DE6ACC8DBE3 CRC64;
     MAMWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL
     LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
     REANNGSSPA GSLADAMSQK HLQINQTFEE LRLITQDTES ELKKLQQTQE YFIIQYQESL
     RIQAQFAQLA QLNPQERMSR ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL
     RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRLEHLC
     QQLPIPGPVE EMLAEVNATI TDIISALSTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
     NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC CVMEYHQATG TLSAHFRNMS
     LKRIKRSDRR GAESVTEEKF TILFDSQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA
     TVLWDNAFRE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS
     SSNHLEDYNS MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
     QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL
     GDLNYLIYVF PDRPKDEVYS KYYTPVPCER ATAKAADGYV KPQIKQVVPE FVNASTDAGS
     GATYMDQAPS PVVCPQAHYN MYPQNPDSVL DTDGDFDLED TMDVARRVEE LLGRPMDSQW
     IPHAQS
//