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TRIB2_BOVIN
ID   TRIB2_BOVIN             Reviewed;         343 AA.
AC   Q5GLH2; A4FV13; Q864R4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Tribbles homolog 2;
DE            Short=TRB-2;
GN   Name=TRIB2 {ECO:0000250|UniProtKB:Q96RU7};
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] {ECO:0000305, ECO:0000312|EMBL:AAR12274.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15829623; DOI=10.1095/biolreprod.104.038026;
RA   Ndiaye K., Fayad T., Silversides D.W., Sirois J., Lussier J.G.;
RT   "Identification of downregulated messenger RNAs in bovine granulosa cells
RT   of dominant follicles following stimulation with human chorionic
RT   gonadotropin.";
RL   Biol. Reprod. 73:324-333(2005).
RN   [2] {ECO:0000312|EMBL:AAP04410.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Shan Y.X., Yu L.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:AAP04410.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interacts with MAPK kinases and regulates activation of MAP
CC       kinases. Does not display kinase activity (By similarity).
CC       {ECO:0000250|UniProtKB:Q28283, ECO:0000250|UniProtKB:Q96RU8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=May associate with the cytoskeleton. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in granulosa cells of the dominant
CC       follicles of the ovary and down-regulated in ovulatory follicles.
CC       {ECO:0000269|PubMed:15829623}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. Tribbles subfamily. {ECO:0000305}.
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DR   EMBL; AY360147; AAR12274.1; -; mRNA.
DR   EMBL; AY247741; AAP04410.1; -; mRNA.
DR   EMBL; BC123595; AAI23596.1; -; mRNA.
DR   RefSeq; NP_847887.2; NM_178317.3.
DR   AlphaFoldDB; Q5GLH2; -.
DR   SMR; Q5GLH2; -.
DR   STRING; 9913.ENSBTAP00000021347; -.
DR   PaxDb; Q5GLH2; -.
DR   PRIDE; Q5GLH2; -.
DR   Ensembl; ENSBTAT00000021347; ENSBTAP00000021347; ENSBTAG00000016045.
DR   Ensembl; ENSBTAT00000076875; ENSBTAP00000060498; ENSBTAG00000016045.
DR   GeneID; 352960; -.
DR   KEGG; bta:352960; -.
DR   CTD; 28951; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016045; -.
DR   VGNC; VGNC:36309; TRIB2.
DR   eggNOG; KOG0583; Eukaryota.
DR   GeneTree; ENSGT00950000182986; -.
DR   HOGENOM; CLU_000288_13_1_1; -.
DR   InParanoid; Q5GLH2; -.
DR   OMA; CQDQLVP; -.
DR   OrthoDB; 1362510at2759; -.
DR   TreeFam; TF329785; -.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000016045; Expressed in cumulus cell and 104 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IBA:GO_Central.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0055106; F:ubiquitin-protein transferase regulator activity; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043405; P:regulation of MAP kinase activity; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR   PANTHER; PTHR22961; PTHR22961; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Protein kinase inhibitor; Reference proteome.
FT   CHAIN           1..343
FT                   /note="Tribbles homolog 2"
FT                   /id="PRO_0000131861"
FT   DOMAIN          61..308
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        255
FT                   /note="H -> Q (in Ref. 2; AAP04410)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   343 AA;  38801 MW;  1F8D0E00D359CCAC CRC64;
     MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC
     IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFDISCYQES LAPCFCLSAH SNINQITEII
     LGETKAYVFF ERSYGDMHSF VRTCKKLREE EAARLFYQIA SAVAHCHDGG LVLRDLKLRK
     FIFKDEERTR VKLESLEDAY ILRGDDDSLS DKHGCPAYVS PEILNTNGSY SGKAADVWSL
     GVMLYTMLVG RYPFHDIEPS SLFSKIRRGQ FNIPETLSPK AKCLIRSILR REPSERLTSQ
     EILDHPWFST DFSVSNSGYG AKEVSDQLVP DVNMEETLDP FFN
 
 
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