TRIB2_MOUSE
ID TRIB2_MOUSE Reviewed; 343 AA.
AC Q8K4K3; Q8K017; Q8R2V8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tribbles homolog 2;
DE Short=TRB-2;
GN Name=Trib2 {ECO:0000312|MGI:MGI:2145021};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAM45477.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kiss-Toth E., Dempsey C., Jozsa V., Caunt J., Oxley K.M., Bagstaff S.M.,
RA Wyllie D.H., Harte M., O'Neill L.A.J., Qwarnstrom E.E., Dower S.K.;
RT "Mammalian homologs of Drosophila tribbles (htrb) control mitogen activated
RT protein kinase signaling.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAC32063.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC32063.1};
RC TISSUE=Aorta {ECO:0000312|EMBL:BAC37820.1},
RC Cerebellum {ECO:0000312|EMBL:BAC38467.1},
RC Colon {ECO:0000312|EMBL:BAE25758.1}, Retina {ECO:0000312|EMBL:BAC32063.1},
RC and Vein {ECO:0000312|EMBL:BAC37820.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH27159.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH27159.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH37387.1},
RC Kidney {ECO:0000312|EMBL:AAH34338.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH27159.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- 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; AF358867; AAM45477.1; -; mRNA.
DR EMBL; AK044747; BAC32063.1; -; mRNA.
DR EMBL; AK080064; BAC37820.1; -; mRNA.
DR EMBL; AK082329; BAC38467.1; -; mRNA.
DR EMBL; AK144192; BAE25758.1; -; mRNA.
DR EMBL; BC027159; AAH27159.1; -; mRNA.
DR EMBL; BC034338; AAH34338.1; -; mRNA.
DR EMBL; BC037387; AAH37387.1; -; mRNA.
DR CCDS; CCDS25821.1; -.
DR RefSeq; NP_653134.2; NM_144551.5.
DR RefSeq; XP_006515117.1; XM_006515054.1.
DR AlphaFoldDB; Q8K4K3; -.
DR SMR; Q8K4K3; -.
DR BioGRID; 229913; 2.
DR IntAct; Q8K4K3; 1.
DR STRING; 10090.ENSMUSP00000020922; -.
DR iPTMnet; Q8K4K3; -.
DR PhosphoSitePlus; Q8K4K3; -.
DR PaxDb; Q8K4K3; -.
DR PRIDE; Q8K4K3; -.
DR ProteomicsDB; 258845; -.
DR Antibodypedia; 674; 280 antibodies from 33 providers.
DR DNASU; 217410; -.
DR Ensembl; ENSMUST00000020922; ENSMUSP00000020922; ENSMUSG00000020601.
DR GeneID; 217410; -.
DR KEGG; mmu:217410; -.
DR UCSC; uc007nbq.1; mouse.
DR CTD; 28951; -.
DR MGI; MGI:2145021; Trib2.
DR VEuPathDB; HostDB:ENSMUSG00000020601; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00950000182986; -.
DR HOGENOM; CLU_000288_13_1_1; -.
DR InParanoid; Q8K4K3; -.
DR OMA; GHFNVPE; -.
DR OrthoDB; 1362510at2759; -.
DR PhylomeDB; Q8K4K3; -.
DR TreeFam; TF329785; -.
DR BioGRID-ORCS; 217410; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Trib2; mouse.
DR PRO; PR:Q8K4K3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8K4K3; protein.
DR Bgee; ENSMUSG00000020601; Expressed in humerus cartilage element and 255 other tissues.
DR ExpressionAtlas; Q8K4K3; baseline and differential.
DR Genevisible; Q8K4K3; MM.
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; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:0055106; F:ubiquitin-protein transferase regulator activity; IDA:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IC:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IC:BHF-UCL.
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_0000131864"
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 244
FT /note="L -> V (in Ref. 1; AAM45477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38773 MW; 9418B7AC19FCC23F CRC64;
MNIHRSTPIT IARYGRSRNK TQDFEELSSI RSAEPSQSFS PNLGSPSPPE TPNLSHCVSC
IGKYLLLEPL EGDHVFRAVH LHSGEELVCK VFEISCYQES LAPCFCLSAH SNINQITEIL
LGETKAYVFF ERSYGDMHSF VRTCKKLREE EAARLFYQIA SAVAHCHDGG LVLRDLKLRK
FIFKDEERTR VKLESLEDAY ILRGDDDSLS DKHGCPAYVS PEILNTSGSY SGKAADVWSL
GVMLYTMLVG RYPFHDIEPS SLFSKIRRGQ FNIPETLSPK AKCLIRSILR REPSERLTSQ
EILDHPWFST DFSVSNSGFG AKEACDQLVP DVNMEENLDP FFN
