CP250_HUMAN
ID CP250_HUMAN Reviewed; 2442 AA.
AC Q9BV73; E1P5Q3; O14812; O60588; Q9H450;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Centrosome-associated protein CEP250;
DE AltName: Full=250 kDa centrosomal protein;
DE Short=Cep250;
DE AltName: Full=Centrosomal Nek2-associated protein 1;
DE Short=C-Nap1;
DE AltName: Full=Centrosomal protein 2;
GN Name=CEP250; Synonyms=CEP2, CNAP1;
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] (ISOFORM 1), AND IDENTIFICATION AS AUTOANTIGEN
RP IN AUTOIMMUNE DISEASES.
RC TISSUE=Cervix carcinoma;
RX PubMed=9506584;
RX DOI=10.1002/1529-0131(199803)41:3<551::aid-art22>3.0.co;2-x;
RA Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J., Rattner J.B.;
RT "Autoantibodies to a group of centrosomal proteins in human autoimmune sera
RT reactive with the centrosome.";
RL Arthritis Rheum. 41:551-558(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH NEK2, AND
RP SUBCELLULAR LOCATION DURING THE CELL CYCLE.
RC TISSUE=Placenta;
RX PubMed=9647649; DOI=10.1083/jcb.141.7.1563;
RA Fry A.M., Mayor T., Meraldi P., Stierhof Y.-D., Tanaka K., Nigg E.A.;
RT "C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of
RT the cell cycle-regulated protein kinase Nek2.";
RL J. Cell Biol. 141:1563-1574(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION, AND INTERACTION WITH NEK2 AND PPP1CA.
RX PubMed=10880350; DOI=10.1042/0264-6021:3490509;
RA Helps N.R., Luo X., Barker H.M., Cohen P.T.W.;
RT "NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase
RT localized to centrosomes, is complexed to protein phosphatase 1.";
RL Biochem. J. 349:509-518(2000).
RN [6]
RP PHOSPHORYLATION DURING CELL CYCLE.
RX PubMed=12140259; DOI=10.1242/jcs.115.16.3275;
RA Mayor T., Hacker U., Stierhof Y.-D., Nigg E.A.;
RT "The mechanism regulating the dissociation of the centrosomal protein C-
RT Nap1 from mitotic spindle poles.";
RL J. Cell Sci. 115:3275-3284(2002).
RN [7]
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 [8]
RP INTERACTION WITH CEP135.
RX PubMed=18851962; DOI=10.1016/j.yexcr.2008.09.016;
RA Kim K., Lee S., Chang J., Rhee K.;
RT "A novel function of CEP135 as a platform protein of C-NAP1 for its
RT centriolar localization.";
RL Exp. Cell Res. 314:3692-3700(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2229 AND SER-2252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP PHOSPHORYLATION AT SER-2417 AND SER-2421.
RX PubMed=21076410; DOI=10.1038/ncb2120;
RA Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M.,
RA Schiebel E.;
RT "Components of the Hippo pathway cooperate with Nek2 kinase to regulate
RT centrosome disjunction.";
RL Nat. Cell Biol. 12:1166-1176(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138; THR-2218; SER-2229 AND
RP SER-2322, AND 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 [12]
RP INTERACTION WITH CNTLN.
RX PubMed=24554434; DOI=10.1242/jcs.139451;
RA Fang G., Zhang D., Yin H., Zheng L., Bi X., Yuan L.;
RT "Centlein mediates an interaction between C-Nap1 and Cep68 to maintain
RT centrosome cohesion.";
RL J. Cell Sci. 127:1631-1639(2014).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT duplication.";
RL Mol. Biol. Cell 26:3788-3802(2015).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=31974111; DOI=10.1242/jcs.239616;
RA Hossain D., Shih S.Y., Xiao X., White J., Tsang W.Y.;
RT "Cep44 functions in centrosome cohesion by stabilizing rootletin.";
RL J. Cell Sci. 133:0-0(2020).
RN [15]
RP INVOLVEMENT IN CRDHL2, AND VARIANT CRDHL2 1155-ARG--ARG-2442 DEL.
RX PubMed=24780881; DOI=10.1136/jmedgenet-2014-102287;
RA Khateb S., Zelinger L., Mizrahi-Meissonnier L., Ayuso C., Koenekoop R.K.,
RA Laxer U., Gross M., Banin E., Sharon D.;
RT "A homozygous nonsense CEP250 mutation combined with a heterozygous
RT nonsense C2orf71 mutation is associated with atypical Usher syndrome.";
RL J. Med. Genet. 51:460-469(2014).
RN [16]
RP FUNCTION, VARIANT VAL-609, AND CHARACTERIZATION OF VARIANT VAL-609.
RX PubMed=28005958; DOI=10.1371/journal.pone.0168966;
RA de Castro-Miro M., Tonda R., Escudero-Ferruz P., Andres R.,
RA Mayor-Lorenzo A., Castro J., Ciccioli M., Hidalgo D.A.,
RA Rodriguez-Ezcurra J.J., Farrando J., Perez-Santonja J.J., Cormand B.,
RA Marfany G., Gonzalez-Duarte R.;
RT "Novel candidate genes and a wide spectrum of structural and point
RT mutations responsible for inherited retinal dystrophies revealed by exome
RT sequencing.";
RL PLoS ONE 11:E0168966-E0168966(2016).
RN [17]
RP INVOLVEMENT IN CRDHL2, AND VARIANTS CRDHL2 121-ARG--ARG-2442 DEL AND
RP 188-ARG--ARG-2442 DEL.
RX PubMed=29718797; DOI=10.1080/13816810.2018.1466338;
RA Kubota D., Gocho K., Kikuchi S., Akeo K., Miura M., Yamaki K.,
RA Takahashi H., Kameya S.;
RT "CEP250 mutations associated with mild cone-rod dystrophy and sensorineural
RT hearing loss in a Japanese family.";
RL Ophthalmic Genet. 39:500-507(2018).
RN [18]
RP VARIANTS CRDHL2 1113-LYS--ARG-2442 DEL AND 1336-ARG--ARG-2442 DEL.
RX PubMed=30459346; DOI=10.1038/s41598-018-35085-0;
RA Fuster-Garcia C., Garcia-Garcia G., Jaijo T., Fornes N., Ayuso C.,
RA Fernandez-Burriel M., Sanchez-De la Morena A., Aller E., Millan J.M.;
RT "High-throughput sequencing for the molecular diagnosis of Usher syndrome
RT reveals 42 novel mutations and consolidates CEP250 as Usher-like disease
RT causative.";
RL Sci. Rep. 8:17113-17113(2018).
RN [19]
RP VARIANT CRDHL2 188-ARG--ARG-2442 DEL.
RX PubMed=30998843; DOI=10.1002/humu.23759;
RA Huang X.F., Xiang L., Fang X.L., Liu W.Q., Zhuang Y.Y., Chen Z.J.,
RA Shen R.J., Cheng W., Han R.Y., Zheng S.S., Chen X.J., Liu X., Jin Z.B.;
RT "Functional characterization of CEP250 variant identified in nonsyndromic
RT retinitis pigmentosa.";
RL Hum. Mutat. 40:1039-1045(2019).
CC -!- FUNCTION: May be involved in ciliogenesis (PubMed:28005958). Probably
CC plays an important role in centrosome cohesion during interphase.
CC {ECO:0000269|PubMed:28005958}.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Forms a complex in vitro
CC with both NEK2 kinase and the PPP1CC catalytic subunit of protein
CC phosphatase 1 (PP1) (PubMed:9647649, PubMed:10880350). Interacts with
CC CEP135 (PubMed:18851962). Interacts with CROCC/rootletin (By
CC similarity). Interacts with CNTLN (PubMed:24554434). Interacts with NIN
CC (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q60952,
CC ECO:0000269|PubMed:10880350, ECO:0000269|PubMed:18851962,
CC ECO:0000269|PubMed:24554434, ECO:0000269|PubMed:9647649, ECO:0000305}.
CC -!- INTERACTION:
CC Q9BV73; Q96CV9: OPTN; NbExp=3; IntAct=EBI-1053100, EBI-748974;
CC Q9BV73; Q9H0K1: SIK2; NbExp=5; IntAct=EBI-1053100, EBI-1181664;
CC Q9BV73; O88566: Axin2; Xeno; NbExp=3; IntAct=EBI-1053100, EBI-7690990;
CC Q9BV73; PRO_0000449631 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-1053100, EBI-25475920;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392,
CC ECO:0000269|PubMed:9647649}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:31974111}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:9647649}. Cell projection, cilium,
CC photoreceptor outer segment {ECO:0000250|UniProtKB:Q60952}.
CC Photoreceptor inner segment {ECO:0000250|UniProtKB:Q60952}.
CC Note=Component of the core centrosome. In interphase cells, it
CC specifically associates with the proximal ends of both mother and
CC daughter centrioles. Associates with the centrosome in interphase
CC cells. In mitotic cells, it dissociates from the mitotic spindle poles.
CC At the end of cell division, it reaccumulates at centrosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BV73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BV73-2; Sequence=VSP_007372;
CC -!- TISSUE SPECIFICITY: Ubiquitously and weakly expressed.
CC -!- PTM: Differentially phosphorylated during cell cycle. Phosphorylation
CC may regulate association/dissociation from centrosome. During M phase
CC of mitosis, C-terminal part is phosphorylated by NEK2, suggesting that
CC it may trigger the dissociation from the mitotic centrosome.
CC Dephosphorylated in vitro by the PP1 phosphatase.
CC {ECO:0000269|PubMed:10880350, ECO:0000269|PubMed:12140259,
CC ECO:0000269|PubMed:21076410}.
CC -!- DISEASE: Cone-rod dystrophy and hearing loss 2 (CRDHL2) [MIM:618358]:
CC An autosomal recessive disease defined by the association of
CC progressive cone-rod dystrophy with sensorineural hearing loss. Cone-
CC rod dystrophy is characterized by retinal pigment deposits visible on
CC fundus examination, predominantly in the macular region, and initial
CC loss of cone photoreceptors followed by rod degeneration. This leads to
CC decreased visual acuity and sensitivity in the central visual field,
CC followed by loss of peripheral vision. Severe loss of vision occurs
CC earlier than in retinitis pigmentosa, due to cone photoreceptors
CC degenerating at a higher rate than rod photoreceptors.
CC {ECO:0000269|PubMed:24780881, ECO:0000269|PubMed:29718797,
CC ECO:0000269|PubMed:30459346, ECO:0000269|PubMed:30998843}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Antibodies against CEP2 are present in sera from
CC patients with autoimmune diseases that developed autoantibodies against
CC centrosomal proteins.
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; AF022655; AAC06349.1; -; mRNA.
DR EMBL; AF049105; AAC07988.1; -; mRNA.
DR EMBL; AL121586; CAB89415.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76206.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76207.1; -; Genomic_DNA.
DR CCDS; CCDS13255.1; -. [Q9BV73-1]
DR PIR; T08621; T08621.
DR RefSeq; NP_001305148.1; NM_001318219.1.
DR RefSeq; NP_009117.2; NM_007186.5. [Q9BV73-1]
DR RefSeq; XP_005260319.1; XM_005260262.4. [Q9BV73-1]
DR RefSeq; XP_006723753.1; XM_006723690.3. [Q9BV73-1]
DR RefSeq; XP_006723754.1; XM_006723691.1. [Q9BV73-1]
DR RefSeq; XP_006723755.1; XM_006723692.3. [Q9BV73-1]
DR RefSeq; XP_006723756.1; XM_006723693.3. [Q9BV73-1]
DR PDB; 6OQA; X-ray; 2.20 A; C/D/G/H=2134-2231.
DR PDBsum; 6OQA; -.
DR AlphaFoldDB; Q9BV73; -.
DR SMR; Q9BV73; -.
DR BioGRID; 116360; 273.
DR DIP; DIP-39406N; -.
DR IntAct; Q9BV73; 35.
DR MINT; Q9BV73; -.
DR STRING; 9606.ENSP00000380661; -.
DR iPTMnet; Q9BV73; -.
DR PhosphoSitePlus; Q9BV73; -.
DR BioMuta; CEP250; -.
DR DMDM; 30580364; -.
DR EPD; Q9BV73; -.
DR jPOST; Q9BV73; -.
DR MassIVE; Q9BV73; -.
DR MaxQB; Q9BV73; -.
DR PaxDb; Q9BV73; -.
DR PeptideAtlas; Q9BV73; -.
DR PRIDE; Q9BV73; -.
DR ProteomicsDB; 79175; -. [Q9BV73-1]
DR ProteomicsDB; 79176; -. [Q9BV73-2]
DR Antibodypedia; 26072; 85 antibodies from 20 providers.
DR DNASU; 11190; -.
DR Ensembl; ENST00000397527.6; ENSP00000380661.1; ENSG00000126001.16. [Q9BV73-1]
DR GeneID; 11190; -.
DR KEGG; hsa:11190; -.
DR MANE-Select; ENST00000397527.6; ENSP00000380661.1; NM_007186.6; NP_009117.2.
DR UCSC; uc032pib.2; human. [Q9BV73-1]
DR CTD; 11190; -.
DR DisGeNET; 11190; -.
DR GeneCards; CEP250; -.
DR HGNC; HGNC:1859; CEP250.
DR HPA; ENSG00000126001; Low tissue specificity.
DR MalaCards; CEP250; -.
DR MIM; 609689; gene.
DR MIM; 618358; phenotype.
DR neXtProt; NX_Q9BV73; -.
DR OpenTargets; ENSG00000126001; -.
DR PharmGKB; PA26415; -.
DR VEuPathDB; HostDB:ENSG00000126001; -.
DR eggNOG; ENOG502QTBY; Eukaryota.
DR GeneTree; ENSGT00940000161056; -.
DR HOGENOM; CLU_000920_0_0_1; -.
DR InParanoid; Q9BV73; -.
DR OMA; KQPWRQR; -.
DR OrthoDB; 76868at2759; -.
DR PhylomeDB; Q9BV73; -.
DR TreeFam; TF101138; -.
DR PathwayCommons; Q9BV73; -.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9BV73; -.
DR SIGNOR; Q9BV73; -.
DR BioGRID-ORCS; 11190; 18 hits in 1089 CRISPR screens.
DR ChiTaRS; CEP250; human.
DR GeneWiki; CEP250; -.
DR GenomeRNAi; 11190; -.
DR Pharos; Q9BV73; Tbio.
DR PRO; PR:Q9BV73; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BV73; protein.
DR Bgee; ENSG00000126001; Expressed in sural nerve and 115 other tissues.
DR ExpressionAtlas; Q9BV73; baseline and differential.
DR Genevisible; Q9BV73; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; NAS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:GO_Central.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB.
DR GO; GO:0030997; P:regulation of centriole-centriole cohesion; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cone-rod dystrophy; Cytoplasm;
KW Cytoskeleton; Deafness; Disease variant; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..2442
FT /note="Centrosome-associated protein CEP250"
FT /id="PRO_0000089487"
FT REGION 1273..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1820..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2223..2244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2307..2345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2416..2442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..158
FT /evidence="ECO:0000255"
FT COILED 244..352
FT /evidence="ECO:0000255"
FT COILED 395..1172
FT /evidence="ECO:0000255"
FT COILED 1243..2227
FT /evidence="ECO:0000255"
FT COILED 2262..2376
FT /evidence="ECO:0000255"
FT COMPBIAS 2324..2342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2218
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 2322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2417
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000269|PubMed:21076410"
FT MOD_RES 2421
FT /note="Phosphoserine; by NEK2"
FT /evidence="ECO:0000269|PubMed:21076410"
FT VAR_SEQ 863..918
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9647649"
FT /id="VSP_007372"
FT VARIANT 121..2442
FT /note="Missing (in CRDHL2)"
FT /evidence="ECO:0000269|PubMed:29718797"
FT /id="VAR_081745"
FT VARIANT 188..2442
FT /note="Missing (in CRDHL2; also found in a family with non-
FT syndromic retinitis pigmentosa)"
FT /evidence="ECO:0000269|PubMed:29718797,
FT ECO:0000269|PubMed:30998843"
FT /id="VAR_081746"
FT VARIANT 609
FT /note="A -> V (found in autosomal recessive retinitis
FT pigmentosa; unknown pathological significance; results in
FT increased ciliary length; dbSNP:rs145878385)"
FT /evidence="ECO:0000269|PubMed:28005958"
FT /id="VAR_081747"
FT VARIANT 995
FT /note="Q -> H (in dbSNP:rs2296403)"
FT /id="VAR_015649"
FT VARIANT 1072
FT /note="Q -> E (in dbSNP:rs17092706)"
FT /id="VAR_050898"
FT VARIANT 1113..2442
FT /note="Missing (in CRDHL2)"
FT /evidence="ECO:0000269|PubMed:30459346"
FT /id="VAR_081748"
FT VARIANT 1155..2442
FT /note="Missing (in CRDHL2; the retinal involvement is more
FT severe in double homozygotes also carrying a PCARE
FT truncating variant)"
FT /evidence="ECO:0000269|PubMed:24780881"
FT /id="VAR_081749"
FT VARIANT 1336..2442
FT /note="Missing (in CRDHL2)"
FT /evidence="ECO:0000269|PubMed:30459346"
FT /id="VAR_081750"
FT VARIANT 1441
FT /note="R -> Q (in dbSNP:rs3748433)"
FT /id="VAR_021858"
FT CONFLICT 120
FT /note="L -> I (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="E -> A (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="H -> L (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="D -> E (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="E -> D (in Ref. 2; AAC07988)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="S -> I (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="E -> A (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 784..787
FT /note="EVTK -> DEPQ (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="Q -> H (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="H -> L (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 1513
FT /note="L -> P (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 2082
FT /note="Q -> L (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT CONFLICT 2345
FT /note="D -> N (in Ref. 1; AAC06349)"
FT /evidence="ECO:0000305"
FT HELIX 2148..2227
FT /evidence="ECO:0007829|PDB:6OQA"
SQ SEQUENCE 2442 AA; 281137 MW; BC2B8A36E07B8272 CRC64;
METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ
AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL
RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL
WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG
REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE
DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA
QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ
QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE
VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS
ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK
LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK
NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ
EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN
SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG
KTALEQQKAA HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA
IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER LRQDMKVQKL
KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS LLQDKMDLQK QVEDLKSQLV
AQDDSQRLVE QEVQEKLRET QEYNRIQKEL EREKASLTLS LMEKEQRLLV LQEADSIRQQ
ELSALRQDMQ EAQGEQKELS AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA
SLWAQEAKAA QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR
PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ DLWKTQQTRD
VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE KSKWEGKQNS LESELMELHE
TMASLQSRLR RAELQRMEAQ GERELLQAAK ENLTAQVEHL QAAVVEARAQ ASAAGILEED
LRTARSALKL KNEEVESERE RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL
RGQIQELEKQ REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE
QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK QLVTLECLAL
ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER SQELQAQSSQ IHDLESHSTV
LARELQERDQ EVKSQREQIE ELQRQKEHLT QDLERRDQEL MLQKERIQVL EDQRTRQTKI
LEEDLEQIKL SLRERGRELT TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC
QQEHIHELQE LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS
LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA HMTLKERHGE
LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE KALLALQQQC AEQAQEHEVE
TRALQDSWLQ AQAVLKERDQ ELEALRAESQ SSRHQEEAAR ARAEALQEAL GKAHAALQGK
EQHLLEQAEL SRSLEASTAT LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL
QQALAQRDEE LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ
LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR ELERLQAALR
QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS VLERDSEQQR LQDELELTRR
ALEKERLHSP GATSTAELGS RGEQGVQLGE VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA
RLEIDRSRLQ RHNVQLRSTL EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG
QKNSDAKCVA ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ
APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR
