TRIB2_CANLF
ID TRIB2_CANLF Reviewed; 343 AA.
AC Q28283;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Tribbles homolog 2;
DE Short=TRB-2;
GN Name=TRIB2 {ECO:0000250|UniProtKB:Q96RU7};
GN Synonyms=C5FW {ECO:0000312|EMBL:CAA67581.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA67581.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Thyroid {ECO:0000312|EMBL:CAA67581.1};
RX PubMed=8910471; DOI=10.1074/jbc.271.45.28451;
RA Wilkin F., Savonet V., Radulescu A., Petermans J., Dumont J.E.,
RA Maenhaut C.;
RT "Identification and characterization of novel genes modulated in the
RT thyroid of dogs treated with methimazole and propylthiouracil.";
RL J. Biol. Chem. 271:28451-28457(1996).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA67581.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Thyroid {ECO:0000312|EMBL:CAA67581.1};
RX PubMed=9342215; DOI=10.1111/j.1432-1033.1997.t01-1-00660.x;
RA Wilkin F., Suarez-Huerta N., Robaye B., Peetermans J., Libert F.,
RA Dumont J.E., Maenhaut C.;
RT "Characterization of a phosphoprotein whose mRNA is regulated by the
RT mitogenic pathways in dog thyroid cells.";
RL Eur. J. Biochem. 248:660-668(1997).
CC -!- FUNCTION: Interacts with MAPK kinases and regulates activation of MAP
CC kinases. Does not display kinase activity.
CC {ECO:0000250|UniProtKB:Q96RU8, ECO:0000269|PubMed:9342215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9342215}.
CC Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9342215}. Note=May
CC associate with the cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in the thyroid, also present in
CC ovary and cerebrum. {ECO:0000269|PubMed:8910471}.
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; X99144; CAA67581.1; -; mRNA.
DR RefSeq; NP_001003218.1; NM_001003218.1.
DR RefSeq; XP_005630124.1; XM_005630067.2.
DR RefSeq; XP_005630125.1; XM_005630068.2.
DR AlphaFoldDB; Q28283; -.
DR SMR; Q28283; -.
DR STRING; 9612.ENSCAFP00000043023; -.
DR PaxDb; Q28283; -.
DR Ensembl; ENSCAFT00030016960; ENSCAFP00030014821; ENSCAFG00030009154.
DR Ensembl; ENSCAFT00040018623; ENSCAFP00040016155; ENSCAFG00040010048.
DR Ensembl; ENSCAFT00845051570; ENSCAFP00845040463; ENSCAFG00845029138.
DR GeneID; 403884; -.
DR KEGG; cfa:403884; -.
DR CTD; 28951; -.
DR VEuPathDB; HostDB:ENSCAFG00845029138; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00950000182986; -.
DR InParanoid; Q28283; -.
DR OrthoDB; 1362510at2759; -.
DR Proteomes; UP000002254; Chromosome 17.
DR Bgee; ENSCAFG00000029053; Expressed in ovary and 48 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA: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_0000131862"
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"
SQ SEQUENCE 343 AA; 38787 MW; BF8D1300DACB84FA CRC64;
MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC
IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFDISCYQES LAPCFCLSAH SNINQITEII
LGETKAYVFF ERSYGDMHSF VRTCKKLREE EAARLFYQIA SAVAHCHDGG LVLRDLKLRK
FIFKDEERTR VKLESLEDAY ILRGDDDSLS DKHGCPAYVS PEILNTSGSY SGKAADVWSL
GVMLYTMLVG RYPFHDIEPS SLFSKIRRGQ FNIPETLSPK AKCLIRSILR REPSERLTSQ
EILDHPWFST DFSVSNSGYG AKEVSDQLVP DVNMEENLDP FFN
