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PIM1_BOVIN
ID   PIM1_BOVIN              Reviewed;         313 AA.
AC   Q9N0P9;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Serine/threonine-protein kinase pim-1;
DE            EC=2.7.11.1;
GN   Name=PIM1;
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 [MRNA].
RX   PubMed=11182156; DOI=10.1016/s0165-2427(00)00259-2;
RA   Wang Z., Petersen K., Weaver M.S., Magnuson N.S.;
RT   "cDNA cloning, sequencing and characterization of bovine pim-1.";
RL   Vet. Immunol. Immunopathol. 78:177-195(2001).
CC   -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity involved
CC       in cell survival and cell proliferation and thus providing a selective
CC       advantage in tumorigenesis. Exerts its oncogenic activity through: the
CC       regulation of MYC transcriptional activity, the regulation of cell
CC       cycle progression and by phosphorylation and inhibition of proapoptotic
CC       proteins (BAD, MAP3K5). Phosphorylation of MYC leads to an increase of
CC       MYC protein stability and thereby an increase of transcriptional
CC       activity. The stabilization of MYC exerted by PIM1 might explain partly
CC       the strong synergism between these two oncogenes in tumorigenesis.
CC       Mediates survival signaling through phosphorylation of BAD, which
CC       induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1.
CC       Phosphorylation of MAP3K5, another proapoptotic protein, by PIM1,
CC       significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-
CC       mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing
CC       caspase-3 activation and cell apoptosis. Stimulates cell cycle
CC       progression at the G1-S and G2-M transitions by phosphorylation of
CC       CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle
CC       progression at G1, results in the relocation of CDKN1A to the cytoplasm
CC       and enhanced CDKN1A protein stability. Promotes cell cycle progression
CC       and tumorigenesis by down-regulating expression of a regulator of cell
CC       cycle progression, CDKN1B, at both transcriptional and post-
CC       translational levels. Phosphorylation of CDKN1B, induces 14-3-3 protein
CC       binding, nuclear export and proteasome-dependent degradation. May
CC       affect the structure or silencing of chromatin by phosphorylating HP1
CC       gamma/CBX3. Acts also as a regulator of homing and migration of bone
CC       marrow cells involving functional interaction with the CXCL12-CXCR4
CC       signaling axis. Also phosphorylates and activates the ATP-binding
CC       cassette transporter ABCG2, allowing resistance to drugs through their
CC       excretion from cells. Promotes brown adipocyte differentiation (By
CC       similarity). {ECO:0000250|UniProtKB:P06803,
CC       ECO:0000250|UniProtKB:P11309}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Binds to RP9. Interacts with CDKN1B and FOXO3. Interacts with
CC       BAD. Interacts with PPP2CA; this interaction promotes dephosphorylation
CC       of PIM1, ubiquitination and proteasomal degradation. Interacts with
CC       HSP90, this interaction stabilizes PIM1 protein levels. Interacts
CC       (ubiquitinated form) with HSP70 and promotes its proteosomal
CC       degradation. Interacts with CDKN1A. Interacts with CDC25C. Interacts
CC       (via N-terminal 96 residues) with CDC25A. Interacts with MAP3K5.
CC       Interacts with MYC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- PTM: Autophosphorylated (By similarity). Phosphorylated. Interaction
CC       with PPP2CA promotes dephosphorylation (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PIM subfamily. {ECO:0000305}.
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DR   EMBL; AF259078; AAF67200.1; -; mRNA.
DR   RefSeq; NP_776569.1; NM_174144.2.
DR   AlphaFoldDB; Q9N0P9; -.
DR   SMR; Q9N0P9; -.
DR   STRING; 9913.ENSBTAP00000000511; -.
DR   PaxDb; Q9N0P9; -.
DR   PRIDE; Q9N0P9; -.
DR   Ensembl; ENSBTAT00000000511; ENSBTAP00000000511; ENSBTAG00000000396.
DR   GeneID; 281402; -.
DR   KEGG; bta:281402; -.
DR   CTD; 5292; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000396; -.
DR   VGNC; VGNC:32899; PIM1.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00940000153394; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q9N0P9; -.
DR   OMA; QDIHLEP; -.
DR   OrthoDB; 930292at2759; -.
DR   TreeFam; TF320810; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000000396; Expressed in esophagus and 106 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:1990748; P:cellular detoxification; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:1905062; P:positive regulation of cardioblast proliferation; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR   GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0070561; P:vitamin D receptor signaling pathway; IEA:Ensembl.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017348; PIM1/2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; ATP-binding; Cell cycle; Cytoplasm; Kinase; Magnesium;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN           1..313
FT                   /note="Serine/threonine-protein kinase pim-1"
FT                   /id="PRO_0000086528"
FT   DOMAIN          38..290
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        167
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         44..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11309"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11309"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11309"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11309"
SQ   SEQUENCE   313 AA;  35630 MW;  9EF40229A847AD47 CRC64;
     MLLSKINSLA HLRAAPCSDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG SVYSGIRVAD
     NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF SGVIRLLDWF ERPDSFVLIL
     ERPEPVQDLF DFITERGALQ EELARSFFWQ VLEAVRHCHD CGVLHRDIKD ENILIDLNRG
     ELKLIDFGSG ALLKDTVYTD FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI
     PFEHDEEIVR GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA
     EIHLHSLSPG PSK
 
 
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