STA5B_BOVIN
ID STA5B_BOVIN Reviewed; 787 AA.
AC Q9TUM3; O77702; Q2KIP0; Q9TUM2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Signal transducer and activator of transcription 5B;
GN Name=STAT5B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 185-560.
RC TISSUE=Blood;
RX PubMed=10050298; DOI=10.1046/j.1365-2052.1999.00323-9.x;
RA Meyer L., Brockmann G., Schwerin M., Seyfert H.-M.;
RT "A highly polymorphic GT-repeat in the bovine STAT5B encoding gene on
RT BTA19.";
RL Anim. Genet. 30:72-72(1999).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ237933; CAB51845.1; -; mRNA.
DR EMBL; AJ237934; CAB52172.1; -; Genomic_DNA.
DR EMBL; AJ237935; CAB52172.1; JOINED; Genomic_DNA.
DR EMBL; AJ237936; CAB52172.1; JOINED; Genomic_DNA.
DR EMBL; BC112568; AAI12569.1; -; mRNA.
DR EMBL; AJ005638; CAA06641.1; -; Genomic_DNA.
DR RefSeq; NP_777042.2; NM_174617.4.
DR RefSeq; XP_005220730.1; XM_005220673.3.
DR RefSeq; XP_005220731.1; XM_005220674.3.
DR AlphaFoldDB; Q9TUM3; -.
DR SMR; Q9TUM3; -.
DR STRING; 9913.ENSBTAP00000012497; -.
DR PaxDb; Q9TUM3; -.
DR PRIDE; Q9TUM3; -.
DR GeneID; 282376; -.
DR KEGG; bta:282376; -.
DR CTD; 6777; -.
DR eggNOG; KOG3667; Eukaryota.
DR HOGENOM; CLU_014189_2_2_1; -.
DR InParanoid; Q9TUM3; -.
DR OrthoDB; 327469at2759; -.
DR TreeFam; TF318648; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:AgBase.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; ISS:AgBase.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; ISS:AgBase.
DR GO; GO:0007565; P:female pregnancy; ISS:AgBase.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IEA:InterPro.
DR GO; GO:0007595; P:lactation; ISS:AgBase.
DR GO; GO:0019915; P:lipid storage; ISS:AgBase.
DR GO; GO:0001553; P:luteinization; ISS:AgBase.
DR GO; GO:0001779; P:natural killer cell differentiation; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:AgBase.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:AgBase.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:AgBase.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:AgBase.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:AgBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISS:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
DR GO; GO:0042448; P:progesterone metabolic process; ISS:AgBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:AgBase.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:AgBase.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISS:AgBase.
DR GO; GO:0019218; P:regulation of steroid metabolic process; ISS:AgBase.
DR GO; GO:0043029; P:T cell homeostasis; ISS:AgBase.
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 2: Evidence at transcript level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT CHAIN 1..787
FT /note="Signal transducer and activator of transcription 5B"
FT /id="PRO_0000182428"
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; by HCK, JAK and PTK6"
FT /evidence="ECO:0000250|UniProtKB:P51692"
FT CONFLICT 133
FT /note="L -> F (in Ref. 1; CAB51845)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="L -> V (in Ref. 1; CAB51845 and 2; AAI12569)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="F -> L (in Ref. 1; CAB51845 and 2; AAI12569)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="P -> S (in Ref. 1; CAB51845)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="Missing (in Ref. 1; CAB52172)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="Missing (in Ref. 1; CAB52172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 89991 MW; 121C9CD9794E3A9A CRC64;
MAVWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIEG QAWDSIDLDN PQENIKATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNGTSPA GSLADAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLA QLNPQERLSR ETALQQKQLS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHFC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN DYSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRSDRR GAESVTEEKF TILFESQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS
SSSHLEDYNG MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL
GDLSYLIYVF PDRPKDEVYS KYYTPVPCEP ATAKAVDGYV KPQIKQVVPE FVSASADSAG
GSATYMDQAP SPAVCPQPHY NMYPQNPDPV LDNDGDFDLD DTIDVARRVE ELLGRPMDSQ
WIPHAQS
