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   27-MAR-2024, entry version 157.
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}, Cerebellum
RC   {ECO:0000312|EMBL:BAC38467.1}, Colon {ECO:0000312|EMBL:BAE25758.1},
RC   Retina {ECO:0000312|EMBL:BAC32063.1}, and Vein
RC   {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}, Kidney
RC   {ECO:0000312|EMBL:AAH34338.1}, and Mammary gland
RC   {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; 10090-ENSMUSP00000020922; -.
DR   ProteomicsDB; 258845; -.
DR   Antibodypedia; 674; 297 antibodies from 33 providers.
DR   DNASU; 217410; -.
DR   Ensembl; ENSMUST00000020922.8; ENSMUSP00000020922.8; ENSMUSG00000020601.9.
DR   GeneID; 217410; -.
DR   KEGG; mmu:217410; -.
DR   UCSC; uc007nbq.1; mouse.
DR   AGR; MGI:2145021; -.
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; PLEGDHI; -.
DR   OrthoDB; 2937186at2759; -.
DR   PhylomeDB; Q8K4K3; -.
DR   TreeFam; TF329785; -.
DR   BioGRID-ORCS; 217410; 1 hit in 80 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 257 other cell types or tissues.
DR   ExpressionAtlas; Q8K4K3; baseline and differential.
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   CDD; cd14022; PK_TRB2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR   PANTHER; PTHR22961; SER/THR PROTEIN KINASE-TRB; 1.
DR   PANTHER; PTHR22961:SF15; TRIBBLES HOMOLOG 2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   Genevisible; Q8K4K3; MM.
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
//