CE350_HUMAN
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 03-AUG-2022, entry version 165.
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 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 CENPJ
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:28625565, PubMed:28428259). 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). {ECO:0000250|UniProtKB:E9Q309,
CC ECO:0000269|PubMed:15615782, ECO:0000269|PubMed:16314388,
CC ECO:0000269|PubMed:17878239, ECO:0000269|PubMed:18412956,
CC ECO:0000269|PubMed:25134987, ECO:0000269|PubMed:28428259,
CC ECO:0000269|PubMed:28625565, ECO:0000269|PubMed:28659385}.
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 Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:28659385}. Note=Associated with mitotic spindles
CC (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_014810.4.
DR PDB; 2COZ; NMR; -; A=2473-2581.
DR PDBsum; 2COZ; -.
DR SMR; Q5VT06; -.
DR BioGRID; 115191; 134.
DR DIP; DIP-49946N; -.
DR IntAct; Q5VT06; 73.
DR MINT; Q5VT06; -.
DR STRING; 9606.ENSP00000356579; -.
DR GlyGen; Q5VT06; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q5VT06; -.
DR PhosphoSitePlus; Q5VT06; -.
DR BioMuta; CEP350; -.
DR DMDM; 74746869; -.
DR EPD; Q5VT06; -.
DR jPOST; Q5VT06; -.
DR MassIVE; Q5VT06; -.
DR MaxQB; Q5VT06; -.
DR PaxDb; Q5VT06; -.
DR PeptideAtlas; Q5VT06; -.
DR PRIDE; Q5VT06; -.
DR ProteomicsDB; 65290; -.
DR Antibodypedia; 34424; 79 antibodies from 21 providers.
DR DNASU; 9857; -.
DR Ensembl; ENST00000367607.8; ENSP00000356579.3; ENSG00000135837.16.
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 CTD; 9857; -.
DR DisGeNET; 9857; -.
DR GeneCards; CEP350; -.
DR HGNC; HGNC:24238; CEP350.
DR HPA; ENSG00000135837; Low tissue specificity.
DR MIM; 617870; gene.
DR neXtProt; NX_Q5VT06; -.
DR OpenTargets; ENSG00000135837; -.
DR PharmGKB; PA143485434; -.
DR VEuPathDB; HostDB:ENSG00000135837; -.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155130; -.
DR HOGENOM; CLU_000421_0_0_1; -.
DR InParanoid; Q5VT06; -.
DR OMA; DCYSDEQ; -.
DR PhylomeDB; Q5VT06; -.
DR TreeFam; TF329845; -.
DR PathwayCommons; Q5VT06; -.
DR SignaLink; Q5VT06; -.
DR SIGNOR; Q5VT06; -.
DR BioGRID-ORCS; 9857; 75 hits in 1092 CRISPR screens.
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 207 other tissues.
DR ExpressionAtlas; Q5VT06; baseline and differential.
DR Genevisible; Q5VT06; HS.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1905515; P:non-motile cilium assembly; IEA:Ensembl.
DR GO; GO:0071539; P:protein localization to centrosome; IEA:Ensembl.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR028750; CEP350.
DR InterPro; IPR025486; DUF4378.
DR PANTHER; PTHR13958; PTHR13958; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14309; DUF4378; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Nucleus; Phosphoprotein; 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 253..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2110..2128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2147..2164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2415..2432
FT /note="Polar 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"
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
