TRIB1_HUMAN
ID TRIB1_HUMAN Reviewed; 372 AA.
AC Q96RU8; B4DMM6; C5HU08; O15180; Q9H2Y8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Tribbles homolog 1;
DE Short=TRB-1;
DE AltName: Full=G-protein-coupled receptor-induced gene 2 protein;
DE Short=GIG-2;
DE AltName: Full=SKIP1;
GN Name=TRIB1 {ECO:0000312|HGNC:HGNC:16891};
GN Synonyms=C8FW {ECO:0000312|EMBL:CAA04119.1},
GN GIG2 {ECO:0000312|EMBL:AAG35663.1}, TRB1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK58174.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH MAP2K1 AND MAP2K4.
RX PubMed=15299019; DOI=10.1074/jbc.m407732200;
RA Kiss-Toth E., Bagstaff S.M., Sung H.Y., Jozsa V., Dempsey C., Caunt J.C.,
RA Oxley K.M., Wyllie D.H., Polgar T., Harte M., O'Neill L.A.J.,
RA Qwarnstrom E.E., Dower S.K.;
RT "Human tribbles, a protein family controlling mitogen-activated protein
RT kinase cascades.";
RL J. Biol. Chem. 279:42703-42708(2004).
RN [2] {ECO:0000312|EMBL:AAG35663.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Mayhaus M., von der Kammer H., Klaudiny J., Albrecht C., Hoffmann B.,
RA Nitsch R.M.;
RT "Identification of a novel nuclear factor Gig2, as an m1-acetylcholine
RT receptor-induced gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5] {ECO:0000312|EMBL:AAG35663.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7] {ECO:0000312|EMBL:AAG35663.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000312|EMBL:AAH63292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta {ECO:0000312|EMBL:AAH63292.1};
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).
RN [9] {ECO:0000305, ECO:0000312|EMBL:CAA04119.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-372 (ISOFORM 1).
RC TISSUE=Thyroid {ECO:0000312|EMBL:CAA04119.1};
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).
RN [10]
RP INTERACTION WITH CEBPA AND COP1.
RX PubMed=20410507; DOI=10.1182/blood-2009-07-229450;
RA Dedhia P.H., Keeshan K., Uljon S., Xu L., Vega M.E., Shestova O.,
RA Zaks-Zilberman M., Romany C., Blacklow S.C., Pear W.S.;
RT "Differential ability of Tribbles family members to promote degradation of
RT C/EBPalpha and induce acute myelogenous leukemia.";
RL Blood 116:1321-1328(2010).
RN [11] {ECO:0007744|PDB:5CEK, ECO:0007744|PDB:5CEM}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 83-371, FUNCTION, INTERACTION
RP WITH CEBPA, AND SUBUNIT.
RX PubMed=26455797; DOI=10.1016/j.str.2015.08.017;
RA Murphy J.M., Nakatani Y., Jamieson S.A., Dai W., Lucet I.S., Mace P.D.;
RT "Molecular mechanism of CCAAT-enhancer binding protein recruitment by the
RT TRIB1 pseudokinase.";
RL Structure 23:2111-2121(2015).
RN [12] {ECO:0007744|PDB:5IGO, ECO:0007744|PDB:5IGQ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 354-361, INTERACTION WITH COP1,
RP DOMAIN, AND MUTAGENESIS OF ASP-355; GLN-356; ILE-357; VAL-358; PRO-359;
RP GLU-360 AND TYR-361.
RX PubMed=27041596; DOI=10.1016/j.str.2016.03.002;
RA Uljon S., Xu X., Durzynska I., Stein S., Adelmant G., Marto J.A.,
RA Pear W.S., Blacklow S.C.;
RT "Structural basis for substrate selectivity of the E3 ligase COP1.";
RL Structure 24:687-696(2016).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] ARG-173; MET-215; ILE-267; CYS-298;
RP ALA-360; ASP-360 AND LEU-371.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Adapter protein involved in protein degradation by
CC interacting with COP1 ubiquitin ligase (PubMed:27041596). The COP1-
CC binding motif is masked by autoinhibitory interactions with the protein
CC kinase domain (PubMed:26455797). Serves to alter COP1 substrate
CC specificity by directing the activity of COP1 toward CEBPA
CC (PubMed:27041596). Binds selectively the recognition sequence of CEBPA
CC (PubMed:26455797). Regulates myeloid cell differentiation by altering
CC the expression of CEBPA in a COP1-dependent manner (By similarity).
CC Controls macrophage, eosinophil and neutrophil differentiation via the
CC COP1-binding domain (By similarity). Interacts with MAPK kinases and
CC regulates activation of MAP kinases, but has no kinase activity
CC (PubMed:15299019, PubMed:26455797). {ECO:0000250|UniProtKB:Q8K4K4,
CC ECO:0000269|PubMed:15299019, ECO:0000269|PubMed:26455797,
CC ECO:0000305|PubMed:27041596}.
CC -!- SUBUNIT: Monomer (PubMed:26455797). Interacts (via protein kinase
CC domain) with CEBPA (PubMed:20410507, PubMed:26455797). Interacts with
CC COP1 (PubMed:20410507, PubMed:27041596). {ECO:0000269|PubMed:20410507,
CC ECO:0000269|PubMed:26455797, ECO:0000269|PubMed:27041596}.
CC -!- INTERACTION:
CC Q96RU8; Q8N2I9: STK40; NbExp=4; IntAct=EBI-492555, EBI-716112;
CC Q96RU8-1; P49715-1: CEBPA; NbExp=2; IntAct=EBI-16180744, EBI-16180754;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96RU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RU8-2; Sequence=VSP_054894;
CC -!- TISSUE SPECIFICITY: Expressed in most human tissues with the highest
CC levels in skeletal muscle, thyroid gland, pancreas, peripheral blood
CC leukocytes, and bone marrow. {ECO:0000269|PubMed:15299019}.
CC -!- DOMAIN: The protein kinase active site is incompatible with ATP binding
CC and is inactive (PubMed:26455797). {ECO:0000269|PubMed:26455797}.
CC -!- DOMAIN: The C-terminus (351-372) is required for interaction with COP1
CC (PubMed:27041596). {ECO:0000269|PubMed:27041596}.
CC -!- DOMAIN: The COP1-binding motif (355-360) is required for regulation
CC activity (By similarity). {ECO:0000250|UniProtKB:Q8K4K4}.
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; AF250310; AAK58174.1; -; mRNA.
DR EMBL; AF205437; AAG35663.1; -; mRNA.
DR EMBL; AK297539; BAG59938.1; -; mRNA.
DR EMBL; AL832388; CAI46181.1; -; mRNA.
DR EMBL; FJ515869; ACS13752.1; -; Genomic_DNA.
DR EMBL; AC091114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW92085.1; -; Genomic_DNA.
DR EMBL; BC063292; AAH63292.1; -; mRNA.
DR EMBL; AJ000480; CAA04119.1; -; mRNA.
DR CCDS; CCDS6357.1; -. [Q96RU8-1]
DR CCDS; CCDS64971.1; -. [Q96RU8-2]
DR RefSeq; NP_001269914.1; NM_001282985.1. [Q96RU8-2]
DR RefSeq; NP_079471.1; NM_025195.3. [Q96RU8-1]
DR PDB; 5CEK; X-ray; 2.80 A; A=83-343.
DR PDB; 5CEM; X-ray; 2.10 A; A=83-371.
DR PDB; 5IGO; X-ray; 1.60 A; U/V/W/X=354-361.
DR PDB; 5IGQ; X-ray; 3.90 A; U=354-364, V/W/X/Y/Z=354-361.
DR PDB; 6DC0; X-ray; 2.80 A; A/B=90-343.
DR PDBsum; 5CEK; -.
DR PDBsum; 5CEM; -.
DR PDBsum; 5IGO; -.
DR PDBsum; 5IGQ; -.
DR PDBsum; 6DC0; -.
DR AlphaFoldDB; Q96RU8; -.
DR SMR; Q96RU8; -.
DR BioGRID; 115516; 40.
DR DIP; DIP-34542N; -.
DR IntAct; Q96RU8; 26.
DR MINT; Q96RU8; -.
DR STRING; 9606.ENSP00000312150; -.
DR ChEMBL; CHEMBL4524042; -.
DR iPTMnet; Q96RU8; -.
DR PhosphoSitePlus; Q96RU8; -.
DR BioMuta; TRIB1; -.
DR DMDM; 83305929; -.
DR EPD; Q96RU8; -.
DR jPOST; Q96RU8; -.
DR MassIVE; Q96RU8; -.
DR MaxQB; Q96RU8; -.
DR PaxDb; Q96RU8; -.
DR PeptideAtlas; Q96RU8; -.
DR PRIDE; Q96RU8; -.
DR ProteomicsDB; 4625; -.
DR ProteomicsDB; 78041; -. [Q96RU8-1]
DR Antibodypedia; 27210; 389 antibodies from 32 providers.
DR DNASU; 10221; -.
DR Ensembl; ENST00000311922.4; ENSP00000312150.3; ENSG00000173334.4. [Q96RU8-1]
DR Ensembl; ENST00000520847.1; ENSP00000429063.1; ENSG00000173334.4. [Q96RU8-2]
DR GeneID; 10221; -.
DR KEGG; hsa:10221; -.
DR MANE-Select; ENST00000311922.4; ENSP00000312150.3; NM_025195.4; NP_079471.1.
DR UCSC; uc003yrx.4; human. [Q96RU8-1]
DR CTD; 10221; -.
DR DisGeNET; 10221; -.
DR GeneCards; TRIB1; -.
DR HGNC; HGNC:16891; TRIB1.
DR HPA; ENSG00000173334; Tissue enhanced (bone).
DR MIM; 609461; gene.
DR neXtProt; NX_Q96RU8; -.
DR OpenTargets; ENSG00000173334; -.
DR PharmGKB; PA134963922; -.
DR VEuPathDB; HostDB:ENSG00000173334; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00950000182986; -.
DR HOGENOM; CLU_000288_13_1_1; -.
DR InParanoid; Q96RU8; -.
DR OMA; KEPWERL; -.
DR OrthoDB; 1362510at2759; -.
DR PhylomeDB; Q96RU8; -.
DR TreeFam; TF329785; -.
DR PathwayCommons; Q96RU8; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; Q96RU8; -.
DR BioGRID-ORCS; 10221; 35 hits in 1115 CRISPR screens.
DR ChiTaRS; TRIB1; human.
DR GeneWiki; TRIB1; -.
DR GenomeRNAi; 10221; -.
DR Pharos; Q96RU8; Tbio.
DR PRO; PR:Q96RU8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96RU8; protein.
DR Bgee; ENSG00000173334; Expressed in mucosa of urinary bladder and 196 other tissues.
DR ExpressionAtlas; Q96RU8; baseline and differential.
DR Genevisible; Q96RU8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IDA:BHF-UCL.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IMP:BHF-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:BHF-UCL.
DR GO; GO:0055106; F:ubiquitin-protein transferase regulator activity; ISS:BHF-UCL.
DR GO; GO:0007254; P:JNK cascade; IMP:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045659; P:negative regulation of neutrophil differentiation; IEA:Ensembl.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:BHF-UCL.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:0045645; P:positive regulation of eosinophil differentiation; IEA:Ensembl.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:BHF-UCL.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR024105; TRB1.
DR InterPro; IPR024104; Tribbles/Ser_Thr_kinase_40.
DR PANTHER; PTHR22961; PTHR22961; 1.
DR PANTHER; PTHR22961:SF17; PTHR22961:SF17; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Protein kinase inhibitor;
KW Reference proteome.
FT CHAIN 1..372
FT /note="Tribbles homolog 1"
FT /id="PRO_0000131859"
FT DOMAIN 1..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 355..360
FT /note="COP1-binding"
FT /evidence="ECO:0000250|UniProtKB:Q8K4K4"
FT COMPBIAS 59..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054894"
FT VARIANT 173
FT /note="S -> R (in dbSNP:rs56285697)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042364"
FT VARIANT 215
FT /note="T -> M (in dbSNP:rs34349706)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042365"
FT VARIANT 267
FT /note="V -> I (in dbSNP:rs56056430)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042366"
FT VARIANT 298
FT /note="R -> C (in dbSNP:rs55953723)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042367"
FT VARIANT 360
FT /note="E -> A (in dbSNP:rs35454769)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042368"
FT VARIANT 360
FT /note="E -> D (in dbSNP:rs16900603)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042369"
FT VARIANT 371
FT /note="F -> L (in a lung large cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042370"
FT MUTAGEN 355
FT /note="D->A: Decreased interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 356
FT /note="Q->A: Decreased interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 357
FT /note="I->A: Decreased interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 358
FT /note="V->I,A: Loss of interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 359
FT /note="P->A: Strongly decreased interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 360
FT /note="E->A: Decreased interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT MUTAGEN 361
FT /note="Y->A: No effect on interaction with COP1."
FT /evidence="ECO:0000269|PubMed:27041596"
FT CONFLICT 149..150
FT /note="VI -> SV (in Ref. 9; CAA04119)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="D -> S (in Ref. 1 and 9)"
FT /evidence="ECO:0000305"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:5CEK"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5CEM"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5CEK"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:5CEK"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 179..198
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6DC0"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5CEK"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:5CEM"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:5CEM"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5CEM"
SQ SEQUENCE 372 AA; 41009 MW; 5F54E50924B1365B CRC64;
MRVGPVRSAM SGASQPRGPA LLFPATRGVP AKRLLDADDA AAVAAKCPRL SECSSPPDYL
SPPGSPCSPQ PPPAAPGAGG GSGSAPGPSR IADYLLLPLA EREHVSRALC IHTGRELRCK
VFPIKHYQDK IRPYIQLPSH SNITGIVEVI LGETKAYVFF EKDFGDMHSY VRSRKRLREE
EAARLFKQIV SAVAHCHQSA IVLGDLKLRK FVFSTEERTQ LRLESLEDTH IMKGEDDALS
DKHGCPAYVS PEILNTTGTY SGKAADVWSL GVMLYTLLVG RYPFHDSDPS ALFSKIRRGQ
FCIPEHISPK ARCLIRSLLR REPSERLTAP EILLHPWFES VLEPGYIDSE IGTSDQIVPE
YQEDSDISSF FC
