ID CE350_HUMAN Reviewed; 3117 AA. AC Q5VT06; O75068; Q8TDK3; Q8WY20; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 02-SEP-2026, entry version 184. DE RecName: Full=Centrosome-associated protein 350 {ECO:0000305}; DE Short=Cep350; DE AltName: Full=Centrosome-associated protein of 350 kDa {ECO:0000303|Ref.1}; GN Name=CEP350 {ECO:0000312|HGNC:HGNC:24238}; GN Synonyms=CAP350 {ECO:0000303|Ref.1}, KIAA0480; GN ORFNames=GM133 {ECO:0000303|PubMed:11891061}; 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] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLN-945. RA Klein-Hitpass L., Esser F., Michels D., Schwerk C., Vassen L.; RT "Cloning and characterization of a cDNA encoding a protein of 350 kDa RT (CAP350) associated with centrosomes."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-131, IDENTIFICATION, AND TISSUE RP SPECIFICITY. RX PubMed=11891061; DOI=10.1016/s0378-1119(01)00897-6; RA Makalowska I., Sood R., Faruque M.U., Hu P., Robbins C.M., Eddings E.M., RA Mestre J.D., Baxevanis A.D., Carpten J.D.; RT "Identification of six novel genes by experimental validation of RT GeneMachine predicted genes."; RL Gene 284:203-213(2002). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE RP ANALYSIS]. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF RP 762-LEU-LEU-763, AND INTERACTION WITH NR1H3; PPARA; PPARD AND PPARG. RX PubMed=15615782; DOI=10.1242/jcs.01600; RA Patel H., Truant R., Rachubinski R.A., Capone J.P.; RT "Activity and subcellular compartmentalization of peroxisome proliferator- RT activated receptor alpha are altered by the centrosome-associated protein RT CAP350."; RL J. Cell Sci. 118:175-186(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2839, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH RP CEP43. RX PubMed=16314388; DOI=10.1091/mbc.e05-08-0810; RA Yan X., Habedanck R., Nigg E.A.; RT "A complex of two centrosomal proteins, CAP350 and FOP, cooperates with EB1 RT in microtubule anchoring."; RL Mol. Biol. Cell 17:634-644(2006). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MICROTUBULE. RX PubMed=17878239; DOI=10.1242/jcs.013102; RA Hoppeler-Lebel A., Celati C., Bellett G., Mogensen M.M., Klein-Hitpass L., RA Bornens M., Tassin A.-M.; RT "Centrosomal CAP350 protein stabilises microtubules associated with the RT Golgi complex."; RL J. Cell Sci. 120:3299-3308(2007). RN [9] RP INTERACTION WITH CEP43-FGFR1 FUSION PROTEIN. RX PubMed=18412956; DOI=10.1186/1476-4598-7-30; RA Lelievre H., Chevrier V., Tassin A.-M., Birnbaum D.; RT "Myeloproliferative disorder FOP-FGFR1 fusion kinase recruits RT phosphoinositide-3 kinase and phospholipase Cgamma at the centrosome."; RL Mol. Cancer 7:30-30(2008). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19052644; DOI=10.1371/journal.pone.0003855; RA Le Clech M.; RT "Role of CAP350 in centriolar tubule stability and centriole assembly."; RL PLoS ONE 3:E3855-E3855(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-878; THR-1253; SER-1256; RP SER-1259; THR-2204; SER-2206 AND SER-2460, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-139; SER-142; RP SER-218; SER-473; SER-507; THR-878; SER-939; SER-1061; SER-1259; SER-1648; RP SER-1653; SER-1818; SER-2115; SER-2206; SER-2460 AND THR-2689, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP INTERACTION WITH CYLD. RX PubMed=25134987; DOI=10.1038/ncomms5585; RA Eguether T., Ermolaeva M.A., Zhao Y., Bonnet M.C., Jain A., Pasparakis M., RA Courtois G., Tassin A.M.; RT "The deubiquitinating enzyme CYLD controls apical docking of basal bodies RT in ciliated epithelial cells."; RL Nat. Commun. 5:4585-4585(2014). RN [18] RP INTERACTION WITH CEP43, SUBCELLULAR LOCATION, AND PHYLOGENETIC ANALYSIS. RX PubMed=28625565; DOI=10.1016/j.devcel.2017.05.016; RA Kanie T., Abbott K.L., Mooney N.A., Plowey E.D., Demeter J., Jackson P.K.; RT "The CEP19-RABL2 GTPase complex binds IFT-B to initiate intraflagellar RT transport at the ciliary base."; RL Dev. Cell 42:1-15(2017). RN [19] RP INTERACTION WITH CEP43. RX PubMed=28428259; DOI=10.1091/mbc.e17-01-0017; RA Nishijima Y., Hagiya Y., Kubo T., Takei R., Katoh Y., Nakayama K.; RT "RABL2 interacts with the intraflagellar transport-B complex and CEP19 and RT participates in ciliary assembly."; RL Mol. Biol. Cell 28:1652-1666(2017). RN [20] RP FUNCTION, INTERACTION WITH CEP19, AND SUBCELLULAR LOCATION. RX PubMed=28659385; DOI=10.1098/rsob.170114; RA Mojarad B.A., Gupta G.D., Hasegan M., Goudiam O., Basto R., Gingras A.C., RA Pelletier L.; RT "CEP19 cooperates with FOP and CEP350 to drive early steps in the RT ciliogenesis programme."; RL Open Biol. 7:0-0(2017). RN [21] RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP78. RX PubMed=36756949; DOI=10.7554/elife.76157; RA Zhu T., Zhang Y., Sheng X., Zhang X., Chen Y., Zhu H., Guo Y., Qi Y., RA Zhao Y., Zhou Q., Chen X., Guo X., Zhao C.; RT "Absence of CEP78 causes photoreceptor and sperm flagella impairments in RT mice and a human individual."; RL Elife 12:0-0(2023). RN [22] RP STRUCTURE BY NMR OF 2473-2581. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the CAP-Gly domain in human centrosome-associated RT protein CAP350."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Plays an essential role in centriole growth by stabilizing a CC procentriolar seed composed of at least, SASS6 and CPAP CC (PubMed:19052644). Required for anchoring microtubules to the CC centrosomes and for the integrity of the microtubule network CC (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to CC discrete subcellular compartments and thereby modulates PPARA activity CC (PubMed:15615782). Required for ciliation (PubMed:28659385). CC {ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388, CC ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:19052644, CC ECO:0000269|PubMed:28659385}. CC -!- SUBUNIT: Part of a ternary complex that contains CEP350, CEP43 and CC MAPRE1. Interacts (via C-terminus) directly with CEP43 (via N-terminus) CC (PubMed:16314388, PubMed:28428259, PubMed:28625565). Interacts with CC NR1H3, PPARA, PPARD and PPARG (PubMed:15615782). Interacts directly CC with microtubules (PubMed:17878239). Interacts with the fusion protein CC CEP43-FGFR1, and by doing so recruits and activates PI3K and PLC-gamma CC (PubMed:18412956). Interacts with CYLD (PubMed:25134987). Interacts CC with CFAP157 (By similarity). Interacts with CEP19 (via C-terminus) CC (PubMed:28659385). Interacts with CEP78; promoting CEP78 localization CC to centrosome and centriole (PubMed:36756949). CC {ECO:0000250|UniProtKB:E9Q309, ECO:0000269|PubMed:15615782, CC ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:17878239, CC ECO:0000269|PubMed:18412956, ECO:0000269|PubMed:25134987, CC ECO:0000269|PubMed:28428259, ECO:0000269|PubMed:28625565, CC ECO:0000269|PubMed:28659385, ECO:0000269|PubMed:36756949}. CC -!- INTERACTION: CC Q5VT06; P35221: CTNNA1; NbExp=5; IntAct=EBI-947346, EBI-701918; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:14654843, CC ECO:0000269|PubMed:16314388, ECO:0000269|PubMed:19052644, CC ECO:0000269|PubMed:28659385}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:16314388}. Nucleus {ECO:0000269|PubMed:15615782}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, CC centriole {ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385, CC ECO:0000269|PubMed:36756949}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000269|PubMed:28659385}. Note=Associated with mitotic CC spindles (PubMed:16314388). Nuclear, in discrete foci. Associated with CC intermediate filaments (PubMed:15615782). Also present in the CC pericentrosomal area (PubMed:17878239). Localizes on both mother and CC daughter centrioles. Localizes to an axial position on the mother CC centriole (PubMed:28625565). Localizes to the distal end of the CC centriole on the subdistal appendage region (PubMed:28659385). CC {ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388, CC ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:28625565, CC ECO:0000269|PubMed:28659385}. CC -!- TISSUE SPECIFICITY: Detected in heart, brain, skeletal muscle, testis, CC placenta, lung, liver, kidney and pancreas. CC {ECO:0000269|PubMed:11891061, ECO:0000269|PubMed:15615782}. CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:16314388}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF287356; AAL55733.1; -; mRNA. DR EMBL; AL645487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590632; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL390718; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF387614; AAL91355.1; -; mRNA. DR CCDS; CCDS1336.1; -. DR PIR; T00263; T00263. DR RefSeq; NP_055625.4; NM_014810.5. DR RefSeq; XP_047291362.1; XM_047435406.1. DR PDB; 2COZ; NMR; -; A=2473-2581. DR SMR; Q5VT06; -. DR BioGRID; 115191; 187. DR CORUM; Q5VT06; -. DR DIP; DIP-49946N; -. DR FunCoup; Q5VT06; 1887. DR IntAct; Q5VT06; 109. DR MINT; Q5VT06; -. DR NDEx; IQUERY-CP-CEP350; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000356579; -. DR GlyCosmos; Q5VT06; 2 sites, 1 glycan. DR GlyGen; Q5VT06; 9 sites, 1 O-linked glycan (8 sites). DR iPTMnet; Q5VT06; -. DR PhosphoSitePlus; Q5VT06; -. DR BioMuta; CEP350; -. DR DMDM; 74746869; -. DR jPOST; Q5VT06; -. DR MassIVE; Q5VT06; -. DR PaxDb; 9606-ENSP00000356579; -. DR PeptideAtlas; Q5VT06; -. DR ProteomicsDB; 65290; -. DR Pumba; Q5VT06; -. DR Antibodypedia; 34424; 84 antibodies from 24 providers. DR DNASU; 9857; -. DR Ensembl; ENST00000367607.8; ENSP00000356579.3; ENSG00000135837.19. DR GeneID; 9857; -. DR KEGG; hsa:9857; -. DR MANE-Select; ENST00000367607.8; ENSP00000356579.3; NM_014810.5; NP_055625.4. DR UCSC; uc001gnt.4; human. DR AGR; HGNC:24238; -. DR ClinPGx; PA143485434; -. DR CTD; 9857; -. DR DisGeNET; 9857; -. DR GeneCards; CEP350; -. DR HGNC; HGNC:24238; CEP350. DR HPA; ENSG00000135837; Low tissue specificity. DR MIM; 617870; gene. DR OpenTargets; ENSG00000135837; -. DR VEuPathDB; HostDB:ENSG00000135837; -. DR eggNOG; KOG4568; Eukaryota. DR GeneTree; ENSGT00940000155130; -. DR HOGENOM; CLU_000421_0_0_1; -. DR InParanoid; Q5VT06; -. DR OMA; ESKHIYC; -. DR OrthoDB; 306254at2759; -. DR PAN-GO; Q5VT06; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q5VT06; -. DR PathwayCommons; Q5VT06; -. DR SignaLink; Q5VT06; -. DR SIGNOR; Q5VT06; -. DR Agora; ENSG00000135837; -. DR BioGRID-ORCS; 9857; 77 hits in 1174 CRISPR screens. DR CD-CODE; 8C2F96ED; Centrosome. DR ChiTaRS; CEP350; human. DR EvolutionaryTrace; Q5VT06; -. DR GeneWiki; CEP350; -. DR GenomeRNAi; 9857; -. DR Pharos; Q5VT06; Tbio. DR PRO; PR:Q5VT06; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5VT06; protein. DR Bgee; ENSG00000135837; Expressed in sperm and 209 other cell types or tissues. DR ExpressionAtlas; Q5VT06; baseline and differential. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0036064; C:ciliary basal body; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0008017; F:microtubule binding; IEA:InterPro. DR GO; GO:0034453; P:microtubule anchoring; IEA:InterPro. DR GO; GO:0071539; P:protein localization to centrosome; IDA:UniProtKB. DR FunFam; 2.30.30.190:FF:000010; centrosome-associated protein 350 isoform X2; 1. DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1. DR InterPro; IPR036859; CAP-Gly_dom_sf. DR InterPro; IPR000938; CAP-Gly_domain. DR InterPro; IPR028750; CEP350/CC187. DR InterPro; IPR025486; LNG1/2-like_C. DR PANTHER; PTHR13958; CENTROSOME-ASSOCIATED PROTEIN 350; 1. DR PANTHER; PTHR13958:SF4; CENTROSOME-ASSOCIATED PROTEIN 350; 1. DR Pfam; PF01302; CAP_GLY; 1. DR Pfam; PF14309; DUF4378; 1. DR SMART; SM01052; CAP_GLY; 1. DR SUPFAM; SSF74924; Cap-Gly domain; 1. DR PROSITE; PS00845; CAP_GLY_1; 1. DR PROSITE; PS50245; CAP_GLY_2; 1. DR PDBsum; 2COZ; -. PE 1: Evidence at protein level; KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome. FT CHAIN 1..3117 FT /note="Centrosome-associated protein 350" FT /id="PRO_0000233291" FT DOMAIN 2517..2559 FT /note="CAP-Gly" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..275 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 436..514 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 548..625 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 671..722 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 981..1002 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1081..1298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1494..1674 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1794..1854 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1903..2020 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2107..2221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2329..2356 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2407..2432 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2465..2485 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 598..645 FT /evidence="ECO:0000255" FT COILED 1369..1411 FT /evidence="ECO:0000255" FT COILED 1707..1800 FT /evidence="ECO:0000255" FT COILED 1856..1899 FT /evidence="ECO:0000255" FT COILED 2051..2110 FT /evidence="ECO:0000255" FT COILED 2719..2752 FT /evidence="ECO:0000255" FT COMPBIAS 14..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..267 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 469..501 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 563..573 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 591..625 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..703 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 705..718 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 981..992 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1087..1102 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1135..1144 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1153..1172 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1251..1267 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1272..1283 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1503..1512 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1522..1535 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1543..1556 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1558..1571 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1631..1647 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1794..1815 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1827..1841 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1903..1925 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1983..2005 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2111..2129 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2141..2170 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2173..2184 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2191..2201 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2329..2338 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2407..2417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2419..2432 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2465..2478 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 218 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 473 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 507 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 878 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 939 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1061 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1253 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1613 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q309" FT MOD_RES 1648 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1653 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1818 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1936 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q309" FT MOD_RES 2115 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2204 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 2206 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2431 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q309" FT MOD_RES 2460 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2689 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2830 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q309" FT MOD_RES 2839 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT VARIANT 892 FT /note="R -> T (in dbSNP:rs6692219)" FT /id="VAR_059202" FT VARIANT 945 FT /note="E -> Q (in dbSNP:rs2477120)" FT /evidence="ECO:0000269|Ref.1" FT /id="VAR_026126" FT VARIANT 1213 FT /note="G -> V (in dbSNP:rs12125245)" FT /id="VAR_059203" FT VARIANT 1445 FT /note="T -> A (in dbSNP:rs16855164)" FT /id="VAR_048671" FT VARIANT 1446 FT /note="T -> A (in dbSNP:rs16855164)" FT /id="VAR_059204" FT VARIANT 1517 FT /note="S -> A (in dbSNP:rs12124336)" FT /id="VAR_059205" FT VARIANT 2044 FT /note="T -> P (in dbSNP:rs56173179)" FT /id="VAR_061092" FT MUTAGEN 762..763 FT /note="LL->AA: Abolishes recruitment of PPARA to specific FT nuclear foci. No effect on interaction with PPARA (in FT vitro)." FT /evidence="ECO:0000269|PubMed:15615782" FT CONFLICT 25 FT /note="Missing (in Ref. 3; AAL91355)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="S -> G (in Ref. 1; AAL55733)" FT /evidence="ECO:0000305" FT CONFLICT 459 FT /note="E -> R (in Ref. 1; AAL55733)" FT /evidence="ECO:0000305" FT CONFLICT 2164 FT /note="S -> P (in Ref. 1; AAL55733)" FT /evidence="ECO:0000305" FT STRAND 2483..2486 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2501..2505 FT /evidence="ECO:0007829|PDB:2COZ" FT TURN 2506..2508 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2509..2518 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2520..2533 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2536..2538 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2540..2542 FT /evidence="ECO:0007829|PDB:2COZ" FT STRAND 2555..2558 FT /evidence="ECO:0007829|PDB:2COZ" FT HELIX 2560..2562 FT /evidence="ECO:0007829|PDB:2COZ" FT HELIX 2565..2567 FT /evidence="ECO:0007829|PDB:2COZ" SQ SEQUENCE 3117 AA; 350930 MW; DD0E03EA96DA319E CRC64; MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV APTSTAVCDS VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK EKSRSPLRAT TLESNVKKNN RVEFREPLVS YREIHGAPSN FSSSHLESKH VYCVDVNEEK TESGNWMIGS REERNIRSCD FESSQSSVIN DTVVRFLNDR PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV NNMAHDTDPK ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT PDGKVWQEAE FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR KVQKVAQLSS TECRTGSSHL ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT ASSDRGGRER TAKSGGHIGR AESDPRLDVL HRHLQRNSER SRSKSRSENN IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST AHTAKQDTVE LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE PSATRRLQET YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK VQERPPSASS SSDMSLSEPP QPLARKDLME STWMQPERLS PQVHHSQPQP FAGTAGSLLS HLLSLEHVGI LHKDFESILP TRKNHNMASR PLTFTPQPYV TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE SEAKKLAGAS INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ LCKRQTDSSS SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ DGQPLLKVAE ILKEKEFCPG ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS KGPWEELAKG SPHSVINIFT KSYQLYGKGF EDKLDRGTST SRPLNATATP LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN RKSAYDPSSV DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS QKTPTSPLSP SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN PAASRTTTEN MAPIPGSKRF SPAGLHHRMA AELSYLNAIE ESVRQLSDVE RVRGISLAQQ ESVSLAQIIK AQQQRHERDL ALLKLKAEQE ALESQRQLEE TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE TARLTTDAAR QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE SPSVPSCKEN EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST SIATEYSLKF DESMTEDEIE EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE EASPEKTTLS TAKELNMPFS GGQDSFSKFT MEMVRQYMKE EEMRAAHQSS LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR KKQRGLLLRL QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR SRMDEKFLTK REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW DKELIKPKTP KKELEDQRTE QKEIASEEES PVPLYSHLNS ESSIPEELGS PAVEYVPSES IGQEQPGSPD HSILTEEMIC SQELESSTSP SKHSLPKSCT SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ SETTSDQSDI EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK SLTESERSRG SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE DFQTPSPVLR SSRKIREESG DSLENVPALH LLKELNATSR ILDMSDGKVG ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK SDVLLKLVLE QGDSSEILSK KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH SPNIQSGKDI HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV HSDRLLELKS PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG DRVLIGNVQP GILRFKGETS FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC KEKHGIFAPP QKISHIPENF DDYVDINEDE DCYSDERYQC YNQEQNDTEG PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV QDISGVLEAH VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK ISLLTDSLLK VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD LSQNVEEQSP SISGCFLSSE LEDEKEEISS PDMCPRPESP VFGASGQEEL AKRLAELELS REFLSALGDD QDWFDEDFGL SSSHKIQKNK AEETIVPLMA EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL GHDLHSISIP TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK FGRKKRDRVD HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT IDVLNQISEK QGRMLLV //