CE152_HUMAN
ID CE152_HUMAN Reviewed; 1710 AA.
AC O94986; E7ER66; Q17RV1; Q6NTA0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Centrosomal protein of 152 kDa {ECO:0000305};
DE Short=Cep152;
GN Name=CEP152 {ECO:0000312|HGNC:HGNC:29298}; Synonyms=KIAA0912;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Heart, Lung, and Testis;
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 [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 IDENTIFICATION BY MASS 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK4.
RX PubMed=21059844; DOI=10.1083/jcb.201007107;
RA Cizmecioglu O., Arnold M., Bahtz R., Settele F., Ehret L.,
RA Haselmann-Weiss U., Antony C., Hoffmann I.;
RT "Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the
RT centrosome.";
RL J. Cell Biol. 191:731-739(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH PLK4 AND CENPJ.
RX PubMed=20852615; DOI=10.1038/nature09445;
RA Dzhindzhev N.S., Yu Q.D., Weiskopf K., Tzolovsky G., Cunha-Ferreira I.,
RA Riparbelli M., Rodrigues-Martins A., Bettencourt-Dias M., Callaini G.,
RA Glover D.M.;
RT "Asterless is a scaffold for the onset of centriole assembly.";
RL Nature 467:714-718(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22020124; DOI=10.1038/emboj.2011.378;
RA Tang C.J., Lin S.Y., Hsu W.B., Lin Y.N., Wu C.T., Lin Y.C., Chang C.W.,
RA Wu K.S., Tang T.K.;
RT "The human microcephaly protein STIL interacts with CPAP and is required
RT for procentriole formation.";
RL EMBO J. 30:4790-4804(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CINP, AND VARIANT SCKL5
RP ARG-667.
RX PubMed=21131973; DOI=10.1038/ng.725;
RA Kalay E., Yigit G., Aslan Y., Brown K.E., Pohl E., Bicknell L.S.,
RA Kayserili H., Li Y., Tuysuz B., Nurnberg G., Kiess W., Koegl M.,
RA Baessmann I., Buruk K., Toraman B., Kayipmaz S., Kul S., Ikbal M.,
RA Turner D.J., Taylor M.S., Aerts J., Scott C., Milstein K., Dollfus H.,
RA Wieczorek D., Brunner H.G., Hurles M., Jackson A.P., Rauch A., Nurnberg P.,
RA Karaguzel A., Wollnik B.;
RT "CEP152 is a genome maintenance protein disrupted in Seckel syndrome.";
RL Nat. Genet. 43:23-26(2011).
RN [10]
RP INTERACTION WITH CEP63, AND SUBCELLULAR LOCATION.
RX PubMed=21983783; DOI=10.1038/ng.971;
RA Sir J.H., Barr A.R., Nicholas A.K., Carvalho O.P., Khurshid M., Sossick A.,
RA Reichelt S., D'Santos C., Woods C.G., Gergely F.;
RT "A primary microcephaly protein complex forms a ring around parental
RT centrioles.";
RL Nat. Genet. 43:1147-1153(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1241, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 CDK5RAP2.
RX PubMed=24613305; DOI=10.1016/j.cub.2014.01.067;
RA Firat-Karalar E.N., Rauniyar N., Yates J.R. III, Stearns T.;
RT "Proximity interactions among centrosome components identify regulators of
RT centriole duplication.";
RL Curr. Biol. 24:664-670(2014).
RN [13]
RP FUNCTION, INTERACTION WITH CDK5RAP2; WDR62; CEP63 AND CEP131, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26297806; DOI=10.7554/elife.07519;
RA Kodani A., Yu T.W., Johnson J.R., Jayaraman D., Johnson T.L., Al-Gazali L.,
RA Sztriha L., Partlow J.N., Kim H., Krup A.L., Dammermann A., Krogan N.,
RA Walsh C.A., Reiter J.F.;
RT "Centriolar satellites assemble centrosomal microcephaly proteins to
RT recruit CDK2 and promote centriole duplication.";
RL Elife 4:0-0(2015).
RN [14]
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 [15]
RP SUBCELLULAR LOCATION.
RX PubMed=30804208; DOI=10.1074/jbc.ra118.004867;
RA Denu R.A., Sass M.M., Johnson J.M., Potts G.K., Choudhary A., Coon J.J.,
RA Burkard M.E.;
RT "Polo-like kinase 4 maintains centriolar satellite integrity by
RT phosphorylation of centrosomal protein 131 (CEP131).";
RL J. Biol. Chem. 294:6531-6549(2019).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=32060285; DOI=10.1038/s41467-020-14767-2;
RA Atorino E.S., Hata S., Funaya C., Neuner A., Schiebel E.;
RT "CEP44 ensures the formation of bona fide centriole wall, a requirement for
RT the centriole-to-centrosome conversion.";
RL Nat. Commun. 11:903-903(2020).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-60 IN COMPLEX WITH PLK4,
RP FUNCTION, AND MUTAGENESIS OF GLU-21.
RX PubMed=24997597; DOI=10.1038/nsmb.2846;
RA Park S.Y., Park J.E., Kim T.S., Kim J.H., Kwak M.J., Ku B., Tian L.,
RA Murugan R.N., Ahn M., Komiya S., Hojo H., Kim N.H., Kim B.Y., Bang J.K.,
RA Erikson R.L., Lee K.W., Kim S.J., Oh B.H., Yang W., Lee K.S.;
RT "Molecular basis for unidirectional scaffold switching of human Plk4 in
RT centriole biogenesis.";
RL Nat. Struct. Mol. Biol. 21:696-703(2014).
RN [18]
RP VARIANT MCPH9 PRO-265, AND SUBCELLULAR LOCATION.
RX PubMed=20598275; DOI=10.1016/j.ajhg.2010.06.003;
RA Guernsey D.L., Jiang H., Hussin J., Arnold M., Bouyakdan K., Perry S.,
RA Babineau-Sturk T., Beis J., Dumas N., Evans S.C., Ferguson M., Matsuoka M.,
RA Macgillivray C., Nightingale M., Patry L., Rideout A.L., Thomas A., Orr A.,
RA Hoffmann I., Michaud J.L., Awadalla P., Meek D.C., Ludman M., Samuels M.E.;
RT "Mutations in centrosomal protein CEP152 in primary microcephaly families
RT linked to MCPH4.";
RL Am. J. Hum. Genet. 87:40-51(2010).
RN [19]
RP VARIANT ILE-793.
RX PubMed=20547088; DOI=10.1016/j.legalmed.2010.04.001;
RA Yuasa I., Umetsu K., Matsusue A., Nishimukai H., Harihara S., Fukumori Y.,
RA Saitou N., Jin F., Chattopadhyay P.K., Henke L., Henke J.;
RT "A Japanese-specific allele in the GALNT11 gene.";
RL Leg. Med. 12:208-211(2010).
CC -!- FUNCTION: Necessary for centrosome duplication; the function seems also
CC to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled
CC complex at the centrosome that recruits CDK2 required for centriole
CC duplication (PubMed:26297806). Acts as a molecular scaffold
CC facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in
CC centriole formation (PubMed:21059844, PubMed:20852615). Proposed to
CC snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter
CC centriole and to reposition PLK4 at the outer boundary of a newly
CC forming CEP152 ring structure (PubMed:24997597). Also plays a key role
CC in deuterosome-mediated centriole amplification in multiciliated that
CC can generate more than 100 centrioles (By similarity). Overexpression
CC of CEP152 can drive amplification of centrioles (PubMed:20852615).
CC {ECO:0000250|UniProtKB:A2AUM9, ECO:0000250|UniProtKB:Q498G2,
CC ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844,
CC ECO:0000269|PubMed:21131973}.
CC -!- SUBUNIT: Interacts (via N-terminus) with PLK4; the interaction is
CC mutally exclusive with a PLK4:CEP192 interaction (PubMed:21059844,
CC PubMed:20852615, PubMed:24997597). Interacts (via C-terminus) with
CC CENPJ (via-N-terminus) (PubMed:20852615). Interacts with CINP
CC (PubMed:21131973). Interacts with CDK5RAP2, WDR62, CEP63 and CEP131
CC (PubMed:21983783, PubMed:24613305, PubMed:26297806). CEP63, CDK5RAP2,
CC CEP152, WDR62 are proposed to form a stepwise assembled complex at the
CC centrosome forming a ring near parental centrioles (PubMed:26297806).
CC Interacts with DEUP1; this interaction recruits CEP152 to the
CC deuterosome. The interactions with CEP63 and DEUP1 are mutually
CC exclusive (By similarity). {ECO:0000250|UniProtKB:A2AUM9,
CC ECO:0000269|PubMed:20852615, ECO:0000269|PubMed:21059844,
CC ECO:0000269|PubMed:21131973, ECO:0000269|PubMed:21983783,
CC ECO:0000269|PubMed:24613305, ECO:0000269|PubMed:26297806}.
CC -!- INTERACTION:
CC O94986; Q9UPN4: CEP131; NbExp=3; IntAct=EBI-311012, EBI-2558372;
CC O94986; O00444: PLK4; NbExp=7; IntAct=EBI-311012, EBI-746202;
CC O94986-3; Q66GS9: CEP135; NbExp=2; IntAct=EBI-15878364, EBI-1046993;
CC O94986-3; O00444: PLK4; NbExp=16; IntAct=EBI-15878364, EBI-746202;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:20598275, ECO:0000269|PubMed:21059844,
CC ECO:0000269|PubMed:21131973, ECO:0000269|PubMed:21983783,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:30804208}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:21983783, ECO:0000269|PubMed:22020124,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26337392,
CC ECO:0000269|PubMed:32060285}. Note=Colocalizes with CDK5RAP2, WDR62 and
CC CEP63 in a discrete ring around the proximal end of the parental
CC centriole. At this site, a cohesive structure is predicted to engage
CC parental centrioles and procentrioles (PubMed:21983783,
CC PubMed:26297806). Localizes to the deuterosome (By similarity).
CC Localizes to pericentriolar material (PCM) (PubMed:26337392).
CC {ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:21983783,
CC ECO:0000269|PubMed:26297806, ECO:0000269|PubMed:26337392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=O94986-4; Sequence=Displayed;
CC Name=1;
CC IsoId=O94986-1; Sequence=VSP_035981, VSP_035983, VSP_035984;
CC Name=2;
CC IsoId=O94986-2; Sequence=VSP_035983, VSP_035984;
CC Name=3;
CC IsoId=O94986-3; Sequence=VSP_047002;
CC -!- DISEASE: Microcephaly 9, primary, autosomal recessive (MCPH9)
CC [MIM:614852]: A disease defined as a head circumference more than 3
CC standard deviations below the age-related mean. Brain weight is
CC markedly reduced and the cerebral cortex is disproportionately small.
CC Despite this marked reduction in size, the gyral pattern is relatively
CC well preserved, with no major abnormality in cortical architecture.
CC Affected individuals are mentally retarded. Primary microcephaly is
CC further defined by the absence of other syndromic features or
CC significant neurological deficits due to degenerative brain disorder.
CC {ECO:0000269|PubMed:20598275}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Seckel syndrome 5 (SCKL5) [MIM:613823]: A rare autosomal
CC recessive disorder characterized by proportionate dwarfism of prenatal
CC onset associated with low birth weight, growth retardation, severe
CC microcephaly with a bird-headed like appearance, and intellectual
CC disability. {ECO:0000269|PubMed:21131973}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CEP152 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69186.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA74935.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB020719; BAA74935.1; ALT_INIT; mRNA.
DR EMBL; AC012379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069186; AAH69186.1; ALT_SEQ; mRNA.
DR EMBL; BC117182; AAI17183.1; -; mRNA.
DR CCDS; CCDS42033.1; -. [O94986-3]
DR CCDS; CCDS58361.1; -. [O94986-4]
DR RefSeq; NP_001181927.1; NM_001194998.1. [O94986-4]
DR RefSeq; NP_055800.2; NM_014985.3. [O94986-3]
DR RefSeq; XP_006720500.1; XM_006720437.3. [O94986-4]
DR PDB; 4N7V; X-ray; 2.76 A; C=1-60.
DR PDB; 6CSU; X-ray; 2.50 A; B/D=1261-1313.
DR PDB; 6CSV; X-ray; 2.50 A; A/B/C/D=1261-1306.
DR PDBsum; 4N7V; -.
DR PDBsum; 6CSU; -.
DR PDBsum; 6CSV; -.
DR AlphaFoldDB; O94986; -.
DR SMR; O94986; -.
DR BioGRID; 116642; 175.
DR ComplexPortal; CPX-1299; CEP152-PLK4 complex.
DR DIP; DIP-31701N; -.
DR IntAct; O94986; 116.
DR MINT; O94986; -.
DR STRING; 9606.ENSP00000370337; -.
DR GlyGen; O94986; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O94986; -.
DR PhosphoSitePlus; O94986; -.
DR BioMuta; CEP152; -.
DR EPD; O94986; -.
DR jPOST; O94986; -.
DR MassIVE; O94986; -.
DR MaxQB; O94986; -.
DR PaxDb; O94986; -.
DR PeptideAtlas; O94986; -.
DR PRIDE; O94986; -.
DR ProteomicsDB; 17727; -.
DR ProteomicsDB; 50610; -. [O94986-4]
DR ProteomicsDB; 50611; -. [O94986-1]
DR ProteomicsDB; 50612; -. [O94986-2]
DR Antibodypedia; 50528; 188 antibodies from 27 providers.
DR DNASU; 22995; -.
DR Ensembl; ENST00000325747.9; ENSP00000321000.5; ENSG00000103995.14. [O94986-1]
DR Ensembl; ENST00000380950.7; ENSP00000370337.2; ENSG00000103995.14. [O94986-4]
DR Ensembl; ENST00000399334.7; ENSP00000382271.3; ENSG00000103995.14. [O94986-3]
DR GeneID; 22995; -.
DR KEGG; hsa:22995; -.
DR MANE-Select; ENST00000380950.7; ENSP00000370337.2; NM_001194998.2; NP_001181927.1.
DR UCSC; uc001zwy.4; human. [O94986-4]
DR CTD; 22995; -.
DR DisGeNET; 22995; -.
DR GeneCards; CEP152; -.
DR HGNC; HGNC:29298; CEP152.
DR HPA; ENSG00000103995; Tissue enhanced (bone).
DR MalaCards; CEP152; -.
DR MIM; 613529; gene.
DR MIM; 613823; phenotype.
DR MIM; 614852; phenotype.
DR neXtProt; NX_O94986; -.
DR OpenTargets; ENSG00000103995; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR Orphanet; 808; Seckel syndrome.
DR PharmGKB; PA142672126; -.
DR VEuPathDB; HostDB:ENSG00000103995; -.
DR eggNOG; ENOG502QT0E; Eukaryota.
DR GeneTree; ENSGT00950000182870; -.
DR HOGENOM; CLU_003346_0_0_1; -.
DR InParanoid; O94986; -.
DR OMA; HHKADIL; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; O94986; -.
DR TreeFam; TF332017; -.
DR PathwayCommons; O94986; -.
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; O94986; -.
DR BioGRID-ORCS; 22995; 162 hits in 1079 CRISPR screens.
DR ChiTaRS; CEP152; human.
DR GeneWiki; CEP152; -.
DR GenomeRNAi; 22995; -.
DR Pharos; O94986; Tbio.
DR PRO; PR:O94986; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O94986; protein.
DR Bgee; ENSG00000103995; Expressed in secondary oocyte and 140 other tissues.
DR ExpressionAtlas; O94986; baseline and differential.
DR Genevisible; O94986; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098536; C:deuterosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
DR GO; GO:0120098; C:procentriole; IDA:ComplexPortal.
DR GO; GO:0120099; C:procentriole replication complex; IPI:ComplexPortal.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0007099; P:centriole replication; IDA:ComplexPortal.
DR GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
DR GO; GO:0098535; P:de novo centriole assembly involved in multi-ciliated epithelial cell differentiation; ISS:UniProtKB.
DR InterPro; IPR029598; Cep152.
DR PANTHER; PTHR10337:SF6; PTHR10337:SF6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Dwarfism;
KW Intellectual disability; Phosphoprotein; Primary microcephaly;
KW Reference proteome.
FT CHAIN 1..1710
FT /note="Centrosomal protein of 152 kDa"
FT /id="PRO_0000089462"
FT REGION 1..60
FT /note="Interaction with PLK4"
FT /evidence="ECO:0000269|PubMed:24997597"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 234..490
FT /evidence="ECO:0000255"
FT COILED 615..664
FT /evidence="ECO:0000255"
FT COILED 700..772
FT /evidence="ECO:0000255"
FT COILED 902..993
FT /evidence="ECO:0000255"
FT COILED 1170..1241
FT /evidence="ECO:0000255"
FT COMPBIAS 108..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1241
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 89..181
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10048485"
FT /id="VSP_035981"
FT VAR_SEQ 1156..1211
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047002"
FT VAR_SEQ 1365..1368
FT /note="ALPL -> GMSK (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485"
FT /id="VSP_035983"
FT VAR_SEQ 1369..1710
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:10048485"
FT /id="VSP_035984"
FT VARIANT 54
FT /note="S -> L (in dbSNP:rs2289181)"
FT /id="VAR_047932"
FT VARIANT 265
FT /note="Q -> P (in MCPH9; dbSNP:rs267606717)"
FT /evidence="ECO:0000269|PubMed:20598275"
FT /id="VAR_063813"
FT VARIANT 667
FT /note="K -> R (in SCKL5; dbSNP:rs200879436)"
FT /evidence="ECO:0000269|PubMed:21131973"
FT /id="VAR_065258"
FT VARIANT 793
FT /note="S -> I (in dbSNP:rs2289178)"
FT /evidence="ECO:0000269|PubMed:20547088"
FT /id="VAR_050779"
FT VARIANT 914
FT /note="L -> V (in dbSNP:rs16961560)"
FT /id="VAR_050780"
FT VARIANT 1106
FT /note="V -> A (in dbSNP:rs16961557)"
FT /id="VAR_050781"
FT MUTAGEN 21
FT /note="E->K: Impairs interaction with PLK4; impaired
FT procentriole assembly and chromosome segregation."
FT /evidence="ECO:0000269|PubMed:24997597"
FT CONFLICT 558
FT /note="S -> P (in Ref. 3; AAH69186)"
FT /evidence="ECO:0000305"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:4N7V"
FT HELIX 1262..1310
FT /evidence="ECO:0007829|PDB:6CSU"
SQ SEQUENCE 1710 AA; 195626 MW; 1727BDA921E1F6BD CRC64;
MSLDFGSVAL PVQNEDEEYD EEDYEREKEL QQLLTDLPHD MLDDDLSSPE LQYSDCSEDG
TDGQPHHPEQ LEMSWNEQML PKSQSVNGYN EIQSLYAGEK CGNVWEENRS KTEDRHPVYH
PEEGGDEGGS GYSPPSKCEQ TDLYHLPENF RPYTNGQKQE FNNQATNVIK FSDPQWNHFQ
GPSCQGLEPY NKVTYKPYQS SAQNNGSPAQ EITGSDTFEG LQQQFLGANE NSAENMQIIQ
LQVLNKAKER QLENLIEKLN ESERQIRYLN HQLVIIKDEK DGLTLSLRES QKLFQNGKER
EIQLEAQIKA LETQIQALKV NEEQMIKKSR TTEMALESLK QQLVDLHHSE SLQRAREQHE
SIVMGLTKKY EEQVLSLQKN LDATVTALKE QEDICSRLKD HVKQLERNQE AIKLEKTEII
NKLTRSLEES QKQCAHLLQS GSVQEVAQLQ FQLQQAQKAH AMSANMNKAL QEELTELKDE
ISLYESAAKL GIHPSDSEGE LNIELTESYV DLGIKKVNWK KSKVTSIVQE EDPNEELSKD
EFILKLKAEV QRLLGSNSMK RHLVSQLQND LKDCHKKIED LHQVKKDEKS IEVETKTDTS
EKPKNQLWPE SSTSDVVRDD ILLLKNEIQV LQQQNQELKE TEGKLRNTNQ DLCNQMRQMV
QDFDHDKQEA VDRCERTYQQ HHEAMKTQIR ESLLAKHALE KQQLFEAYER THLQLRSELD
KLNKEVTAVQ ECYLEVCREK DNLELTLRKT TEKEQQTQEK IKEKLIQQLE KEWQSKLDQT
IKAMKKKTLD CGSQTDQVTT SDVISKKEMA IMIEEQKCTI QQNLEQEKDI AIKGAMKKLE
IELELKHCEN ITKQVEIAVQ NAHQRWLGEL PELAEYQALV KAEQKKWEEQ HEVSVNKRIS
FAVSEAKEKW KSELENMRKN ILPGKELEEK IHSLQKELEL KNEEVPVVIR AELAKARSEW
NKEKQEEIHR IQEQNEQDYR QFLDDHRNKI NEVLAAAKED FMKQKTELLL QKETELQTCL
DQSRREWTMQ EAKRIQLEIY QYEEDILTVL GVLLSDTQKE HISDSEDKQL LEIMSTCSSK
WMSVQYFEKL KGCIQKAFQD TLPLLVENAD PEWKKRNMAE LSKDSASQGT GQGDPGPAAG
HHAQPLALQA TEAEADKKKV LEIKDLCCGH CFQELEKAKQ ECQDLKGKLE KCCRHLQHLE
RKHKAVVEKI GEENNKVVEE LIEENNDMKN KLEELQTLCK TPPRSLSAGA IENACLPCSG
GALEELRGQY IKAVKKIKCD MLRYIQESKE RAAEMVKAEV LRERQETARK MRKYYLICLQ
QILQDDGKEG AEKKIMNAAS KLATMAKLLE TPISSKSQSK TTQSALPLTS EMLIAVKKSK
RNDVNQKIPC CIESKSNSVN TITRTLCEQA PKRRAACNLQ RLLENSEHQS IKHVGSKETH
LEFQFGDGSC KHLNSLPRNV SPEFVPCEGE GGFGLHKKKD LLSDNGSESL PHSAAYPFLG
TLGNKPSPRC TPGPSESGCM HITFRDSNER LGLKVYKCNP LMESENAASE KSQGLDVQEP
PVKDGGDLSD CLGWPSSSAT LSFDSREASF VHGRPQGTLE IPSESVKSKQ FSPSGYLSDT
EESNMICQTM KCQRYQTPYL SEETTYLEPG KISVNCGHPS RHKADRLKSD FKKLSSTLPS
SVCQQPSRKL IVPLSSQQDS GFDSPFVNLD
