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Database: UniProt
Entry: STA5B_PIG
LinkDB: STA5B_PIG
Original site: STA5B_PIG 
ID   STA5B_PIG               Reviewed;         787 AA.
AC   Q9TUZ0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-JUN-2019, entry version 132.
DE   RecName: Full=Signal transducer and activator of transcription 5B;
GN   Name=STAT5B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Large white; TISSUE=Mammary gland;
RA   Palin M.-F., Beaudry D., Roberge C., Farmer C.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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
CC       element and activates PRL-induced transcription. Positively
CC       regulates hematopoietic/erythroid differentiation.
CC       {ECO:0000250|UniProtKB:P51692}.
CC   -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC       member. Binds NR3C1. Interacts with NCOA1. Interacts with NMI.
CC       Interacts with SOCS7. Interacts (via SH2 domain) with INSR.
CC       Interacts with CPEB3; this inhibits STAT5B-mediated
CC       transcriptional activation. {ECO:0000250|UniProtKB:P42232,
CC       ECO:0000250|UniProtKB:P51692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42232}.
CC       Nucleus {ECO:0000250|UniProtKB:P42232}. Note=Translocated into the
CC       nucleus in response to phosphorylation. {ECO:0000250}.
CC   -!- PTM: Tyrosine phosphorylated in response to signaling via
CC       activated KIT, resulting in translocation to the nucleus. Tyrosine
CC       phosphorylated in response to signaling via activated FLT3; wild-
CC       type FLT3 results in much weaker phosphorylation than
CC       constitutively activated mutant FLT3. Alternatively, can be
CC       phosphorylated by JAK2. Phosphorylation at Tyr-699 by PTK6 or HCK
CC       leads to an increase of its transcriptional activity.
CC       {ECO:0000250|UniProtKB:P51692}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
DR   EMBL; AF135123; AAD46164.1; -; mRNA.
DR   RefSeq; NP_999333.1; NM_214168.1.
DR   SMR; Q9TUZ0; -.
DR   STRING; 9823.ENSSSCP00000018443; -.
DR   PaxDb; Q9TUZ0; -.
DR   PeptideAtlas; Q9TUZ0; -.
DR   PRIDE; Q9TUZ0; -.
DR   GeneID; 397340; -.
DR   KEGG; ssc:397340; -.
DR   CTD; 6777; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   eggNOG; ENOG410XPN8; LUCA.
DR   HOGENOM; HOG000230988; -.
DR   InParanoid; Q9TUZ0; -.
DR   KO; K11224; -.
DR   OrthoDB; 327469at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
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; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IBA:GO_Central.
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:0006952; P:defense response; IBA:GO_Central.
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; IBA:GO_Central.
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:0045086; P:positive regulation of interleukin-2 biosynthetic process; 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:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
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:0043434; P:response to peptide hormone; IBA:GO_Central.
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; Complete proteome; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; SH2 domain;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    787       Signal transducer and activator of
FT                                transcription 5B.
FT                                /FTId=PRO_0000182431.
FT   DOMAIN      589    686       SH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00191}.
FT   MOD_RES      90     90       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P51692}.
FT   MOD_RES     128    128       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51692}.
FT   MOD_RES     682    682       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P42229}.
FT   MOD_RES     699    699       Phosphotyrosine; by HCK, JAK and PTK6.
FT                                {ECO:0000250|UniProtKB:P51692}.
FT   VARIANT     153    153       P -> L.
FT   VARIANT     378    378       R -> Q.
FT   VARIANT     392    392       C -> Y.
SQ   SEQUENCE   787 AA;  89902 MW;  042D731ED607A0D3 CRC64;
     MAVWIQAQQL QGDALHQMQA LYGQHFPIEV RHYLSQWIES QAWDSIDLDN PQENIKATQL
     LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
     REANNGTSPA GSLADAMSQK HLQINQTFEE LRPVTQDTEN ELKKLQQTQE YFIIQYQESL
     RIQAQFAQLA QLNPQERLSR ETALQQKQVT LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
     RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
     QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
     NVHMNPPQVK ATIISEQRAK SLLKNESTRN DCSGEILNNC CVMEYHQATG TLSAHFRNMS
     LKRIKRSDRR GAESVTEEKF TILFESQFSV GGNELVFQVK TLSLPVVVIV HGSQDNNATA
     TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS
     SSSHLEDYSG MSVSWSQFNR ENLPGRNYTF WQWFDGVMEV LKKHLKPHWN DGAILGFVNK
     QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSQERMF WNLMPFTTRD FSIRSLADRL
     GDLNYLIYVF PDRPKDEVYS KYYTPVPCEP ATAKAVDGYV KPQIKQVVPE FVSASSDSAG
     GNATYMDQAP SPAVCPQAHY SIYPQNPDPV LDNDGDFDLD DTMDVARRVE ELLGRPMDSQ
     WIPHAQS
//
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