CP110_HUMAN
ID CP110_HUMAN Reviewed; 1012 AA.
AC O43303; B7WP23; O43335; Q68DV9; Q8NE13;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Centriolar coiled-coil protein of 110 kDa;
DE AltName: Full=Centrosomal protein of 110 kDa;
DE Short=CP110;
DE Short=Cep110;
GN Name=CCP110; Synonyms=CEP110, CP110, KIAA0419;
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 2), AND VARIANTS MET-252
RP AND ILE-347.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-252.
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-252.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-252.
RC TISSUE=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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP PHOSPHORYLATION.
RX PubMed=12361598; DOI=10.1016/s1534-5807(02)00258-7;
RA Chen Z., Indjeian V.B., McManus M., Wang L., Dynlacht B.D.;
RT "CP110, a cell cycle-dependent CDK substrate, regulates centrosome
RT duplication in human cells.";
RL Dev. Cell 3:339-350(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 FUNCTION, INTERACTION WITH CALM1 AND CETN2, AND SUBCELLULAR LOCATION.
RX PubMed=16760425; DOI=10.1091/mbc.e06-04-0371;
RA Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
RA Salisbury J.L., Sanchez I., Dynlacht B.D.;
RT "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis
RT and genome stability.";
RL Mol. Biol. Cell 17:3423-3434(2006).
RN [9]
RP FUNCTION, INTERACTION WITH CALM1 AND CEP97, AND SUBCELLULAR LOCATION.
RX PubMed=17719545; DOI=10.1016/j.cell.2007.06.027;
RA Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
RT "Cep97 and CP110 suppress a cilia assembly program.";
RL Cell 130:678-690(2007).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
RA Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D.,
RA Nigg E.A.;
RT "Plk4-induced centriole biogenesis in human cells.";
RL Dev. Cell 13:190-202(2007).
RN [11]
RP INTERACTION WITH CEP290.
RX PubMed=18694559; DOI=10.1016/j.devcel.2008.07.004;
RA Tsang W.Y., Bossard C., Khanna H., Peraenen J., Swaroop A., Malhotra V.,
RA Dynlacht B.D.;
RT "CP110 suppresses primary cilia formation through its interaction with
RT CEP290, a protein deficient in human ciliary disease.";
RL Dev. Cell 15:187-197(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 INTERACTION WITH CEP76.
RX PubMed=19460342; DOI=10.1016/j.devcel.2009.03.004;
RA Tsang W.Y., Spektor A., Vijayakumar S., Bista B.R., Li J., Sanchez I.,
RA Duensing S., Dynlacht B.D.;
RT "Cep76, a centrosomal protein that specifically restrains centriole
RT reduplication.";
RL Dev. Cell 16:649-660(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [15]
RP UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 586-ARG--LEU-588, AND
RP INTERACTION WITH CCNF.
RX PubMed=20596027; DOI=10.1038/nature09140;
RA D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
RA Washburn M.P., Dynlacht B., Pagano M.;
RT "SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through
RT CP110 degradation.";
RL Nature 466:138-142(2010).
RN [16]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KIF24.
RX PubMed=21620453; DOI=10.1016/j.cell.2011.04.028;
RA Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.;
RT "Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and
RT regulate ciliogenesis.";
RL Cell 145:914-925(2011).
RN [17]
RP INTERACTION WITH CEP104.
RX PubMed=22885064; DOI=10.1016/j.cub.2012.07.047;
RA Jiang K., Toedt G., Montenegro Gouveia S., Davey N.E., Hua S.,
RA van der Vaart B., Grigoriev I., Larsen J., Pedersen L.B., Bezstarosti K.,
RA Lince-Faria M., Demmers J., Steinmetz M.O., Gibson T.J., Akhmanova A.;
RT "A proteome-wide screen for mammalian SxIP motif-containing microtubule
RT plus-end tracking proteins.";
RL Curr. Biol. 22:1800-1807(2012).
RN [18]
RP INTERACTION WITH NEURL4 AND CCNF.
RX PubMed=22441691; DOI=10.1038/embor.2012.40;
RA Li J., Kim S., Kobayashi T., Liang F.X., Korzeniewski N., Duensing S.,
RA Dynlacht B.D.;
RT "Neurl4, a novel daughter centriole protein, prevents formation of ectopic
RT microtubule organizing centres.";
RL EMBO Rep. 13:547-553(2012).
RN [19]
RP INTERACTION WITH CEP97; HERC2 AND NEURL4.
RX PubMed=22261722; DOI=10.1074/mcp.m111.014233;
RA Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.;
RT "Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as
RT novel modulators of centrosome architecture.";
RL Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-551, AND
RP IDENTIFICATION BY 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 [21]
RP FUNCTION, DEUBIQUITINATION, AND INTERACTION WITH USP20 AND USP33.
RX PubMed=23486064; DOI=10.1038/nature11941;
RA Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W.,
RA Campos E.I., Pagano M., Dynlacht B.D.;
RT "USP33 regulates centrosome biogenesis via deubiquitination of the
RT centriolar protein CP110.";
RL Nature 495:255-259(2013).
RN [22]
RP INTERACTION WITH TALPID3.
RX PubMed=24421332; DOI=10.1083/jcb.201304153;
RA Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.;
RT "The CP110-interacting proteins Talpid3 and Cep290 play overlapping and
RT distinct roles in cilia assembly.";
RL J. Cell Biol. 204:215-229(2014).
RN [23]
RP PHOSPHORYLATION AT SER-170 AND THR-194, AND MUTAGENESIS OF SER-170 AND
RP THR-194.
RX PubMed=26304236; DOI=10.1158/1535-7163.mct-15-0443;
RA Hu S., Lu Y., Orr B., Godek K., Mustachio L.M., Kawakami M., Sekula D.,
RA Compton D.A., Freemantle S., Dmitrovsky E.;
RT "Specific CP110 phosphorylation sites mediate anaphase catastrophe after
RT CDK2 inhibition: evidence for cooperation with USP33 knockdown.";
RL Mol. Cancer Ther. 14:2576-2585(2015).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MPHOSPH9.
RX PubMed=30375385; DOI=10.1038/s41467-018-06990-9;
RA Huang N., Zhang D., Li F., Chai P., Wang S., Teng J., Chen J.;
RT "M-Phase Phosphoprotein 9 regulates ciliogenesis by modulating CP110-CEP97
RT complex localization at the mother centriole.";
RL Nat. Commun. 9:4511-4511(2018).
CC -!- FUNCTION: Necessary for centrosome duplication at different stages of
CC procentriole formation. Acts as a key negative regulator of
CC ciliogenesis in collaboration with CEP97 by capping the mother
CC centriole thereby preventing cilia formation (PubMed:17719545,
CC PubMed:17681131, PubMed:23486064, PubMed:30375385). Also involved in
CC promoting ciliogenesis. May play a role in the assembly of the mother
CC centriole subdistal appendages (SDA) thereby effecting the fusion of
CC recycling endosomes to basal bodies during cilia formation (By
CC similarity). Required for correct spindle formation and has a role in
CC regulating cytokinesis and genome stability via cooperation with CALM1
CC and CETN2 (PubMed:16760425). {ECO:0000250|UniProtKB:Q7TSH4,
CC ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:16760425,
CC ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545,
CC ECO:0000269|PubMed:23486064, ECO:0000269|PubMed:30375385}.
CC -!- SUBUNIT: Interacts with CALM1, CETN2, CEP76, CEP97, CEP104, CEP290,
CC TALPID3. Seems to associate with discrete CETN2, CEP97 and CEP290-
CC containing complexes. Interacts with NEURL4 and CCNF; these
CC interactions are not mutually exclusive and both lead to CCP110
CC ubiquitination and proteasome-dependent degradation. Via its
CC interaction with NEURL4, may indirectly interact with HERC2. Interacts
CC with KIF24, leading to its recruitment to centrioles. Interacts with
CC USP20 and USP33 (PubMed:23486064). Interacts with MPHOSPH9
CC (PubMed:30375385). {ECO:0000269|PubMed:16760425,
CC ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:18694559,
CC ECO:0000269|PubMed:19460342, ECO:0000269|PubMed:20596027,
CC ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:22261722,
CC ECO:0000269|PubMed:22441691, ECO:0000269|PubMed:22885064,
CC ECO:0000269|PubMed:23486064, ECO:0000269|PubMed:24421332,
CC ECO:0000269|PubMed:30375385}.
CC -!- INTERACTION:
CC O43303; P62158: CALM3; NbExp=14; IntAct=EBI-1566217, EBI-397435;
CC O43303; P41002: CCNF; NbExp=9; IntAct=EBI-1566217, EBI-1207574;
CC O43303; O15078: CEP290; NbExp=18; IntAct=EBI-1566217, EBI-1811944;
CC O43303; Q8IW35: CEP97; NbExp=27; IntAct=EBI-1566217, EBI-1566210;
CC O43303; P41208: CETN2; NbExp=3; IntAct=EBI-1566217, EBI-1789926;
CC O43303; Q9BVV6: KIAA0586; NbExp=6; IntAct=EBI-1566217, EBI-11286926;
CC O43303; Q5T7B8: KIF24; NbExp=12; IntAct=EBI-1566217, EBI-2556811;
CC O43303; Q96JN8: NEURL4; NbExp=9; IntAct=EBI-1566217, EBI-1053406;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:12361598,
CC ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:16760425,
CC ECO:0000269|PubMed:17681131, ECO:0000269|PubMed:17719545,
CC ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:21620453,
CC ECO:0000269|PubMed:30375385}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:30375385}. Cytoplasm,
CC cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q7TSH4}.
CC Note=Recruited early and then associates with the growing distal tips.
CC Recruited to the mother centriole by KIF24 (PubMed:21620453). Removed
CC from centrioles by TTBK2, leading to initiation of ciliogenesis and
CC localizes only to the daughter centriole in ciliated cells. In
CC cytotoxic T lymphocytes remains associated with the mother centriole
CC during docking of the centrosome at the immunological synapse upon
CC target contact (By similarity). Recruited at the distal end of the
CC mother centriole by MPHOSPH9 (PubMed:30375385).
CC {ECO:0000250|UniProtKB:Q7TSH4, ECO:0000269|PubMed:21620453,
CC ECO:0000269|PubMed:30375385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43303-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43303-2; Sequence=VSP_011897;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at
CC intermediate levels in spleen, thymus, prostate, small intestine, colon
CC and peripheral blood leukocytes. {ECO:0000269|PubMed:12361598}.
CC -!- INDUCTION: Up-regulated during the transition from G1 to S phase of the
CC cell cycle. The highest levels are observed in S phase, after which the
CC levels decrease markedly. {ECO:0000269|PubMed:12361598}.
CC -!- PTM: Phosphorylated by CDKs. {ECO:0000269|PubMed:12361598}.
CC -!- PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to its
CC degradation by the proteasome and preventing centrosome reduplication.
CC Deubiquitinated by USP33 in S and G2/M phase, leading to stabilize
CC CCP110 during the period which centrioles duplicate and elongate.
CC {ECO:0000269|PubMed:20596027, ECO:0000269|PubMed:23486064}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24849.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB007879; BAA24849.2; ALT_INIT; mRNA.
DR EMBL; CR749255; CAH18111.1; -; mRNA.
DR EMBL; AC003108; AAC05804.1; -; Genomic_DNA.
DR EMBL; AC012621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036654; AAH36654.1; -; mRNA.
DR CCDS; CCDS10579.1; -. [O43303-2]
DR CCDS; CCDS55992.1; -. [O43303-1]
DR PIR; T01372; T01372.
DR RefSeq; NP_001185951.2; NM_001199022.2. [O43303-1]
DR RefSeq; NP_001310498.1; NM_001323569.1. [O43303-1]
DR RefSeq; NP_001310499.1; NM_001323570.1. [O43303-2]
DR RefSeq; NP_001310500.1; NM_001323571.1. [O43303-2]
DR RefSeq; NP_001310501.1; NM_001323572.1. [O43303-2]
DR RefSeq; NP_055526.4; NM_014711.5. [O43303-2]
DR RefSeq; XP_011544293.1; XM_011545991.2. [O43303-1]
DR RefSeq; XP_011544294.1; XM_011545992.2. [O43303-1]
DR RefSeq; XP_016879397.1; XM_017023908.1. [O43303-1]
DR AlphaFoldDB; O43303; -.
DR SASBDB; O43303; -.
DR SMR; O43303; -.
DR BioGRID; 115087; 159.
DR CORUM; O43303; -.
DR DIP; DIP-39892N; -.
DR IntAct; O43303; 78.
DR MINT; O43303; -.
DR STRING; 9606.ENSP00000370803; -.
DR GlyGen; O43303; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43303; -.
DR PhosphoSitePlus; O43303; -.
DR BioMuta; CCP110; -.
DR EPD; O43303; -.
DR jPOST; O43303; -.
DR MassIVE; O43303; -.
DR MaxQB; O43303; -.
DR PaxDb; O43303; -.
DR PeptideAtlas; O43303; -.
DR PRIDE; O43303; -.
DR ProteomicsDB; 48877; -. [O43303-1]
DR ProteomicsDB; 48878; -. [O43303-2]
DR Antibodypedia; 42931; 192 antibodies from 35 providers.
DR DNASU; 9738; -.
DR Ensembl; ENST00000381396.9; ENSP00000370803.5; ENSG00000103540.16. [O43303-1]
DR Ensembl; ENST00000396208.3; ENSP00000379511.2; ENSG00000103540.16. [O43303-2]
DR Ensembl; ENST00000396212.6; ENSP00000379515.2; ENSG00000103540.16. [O43303-2]
DR GeneID; 9738; -.
DR KEGG; hsa:9738; -.
DR UCSC; uc002dgk.5; human. [O43303-1]
DR CTD; 9738; -.
DR DisGeNET; 9738; -.
DR GeneCards; CCP110; -.
DR HGNC; HGNC:24342; CCP110.
DR HPA; ENSG00000103540; Tissue enhanced (brain).
DR MIM; 609544; gene.
DR neXtProt; NX_O43303; -.
DR OpenTargets; ENSG00000103540; -.
DR VEuPathDB; HostDB:ENSG00000103540; -.
DR eggNOG; ENOG502QUVS; Eukaryota.
DR GeneTree; ENSGT00390000004090; -.
DR HOGENOM; CLU_302049_0_0_1; -.
DR InParanoid; O43303; -.
DR OMA; TDCVKEK; -.
DR OrthoDB; 408678at2759; -.
DR PhylomeDB; O43303; -.
DR TreeFam; TF332788; -.
DR PathwayCommons; O43303; -.
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-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; O43303; -.
DR SIGNOR; O43303; -.
DR BioGRID-ORCS; 9738; 168 hits in 1089 CRISPR screens.
DR ChiTaRS; CCP110; human.
DR GeneWiki; CCP110; -.
DR GenomeRNAi; 9738; -.
DR Pharos; O43303; Tbio.
DR PRO; PR:O43303; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O43303; protein.
DR Bgee; ENSG00000103540; Expressed in cranial nerve II and 194 other tissues.
DR ExpressionAtlas; O43303; baseline and differential.
DR Genevisible; O43303; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
DR GO; GO:0051298; P:centrosome duplication; IDA:UniProtKB.
DR GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
DR GO; GO:1903723; P:negative regulation of centriole elongation; IBA:GO_Central.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR InterPro; IPR033207; CCP110.
DR PANTHER; PTHR13594; PTHR13594; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1012
FT /note="Centriolar coiled-coil protein of 110 kDa"
FT /id="PRO_0000089460"
FT REGION 1..223
FT /note="CEP97 binding"
FT REGION 64..82
FT /note="Calmodulin-binding"
FT REGION 67..82
FT /note="Required for interaction with CEP290"
FT /evidence="ECO:0000269|PubMed:18694559"
FT REGION 350..565
FT /note="Interaction with CEP76"
FT /evidence="ECO:0000269|PubMed:19460342"
FT REGION 611..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..821
FT /note="Calmodulin-binding"
FT REGION 909..924
FT /note="Calmodulin-binding"
FT REGION 949..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..90
FT /evidence="ECO:0000255"
FT COILED 640..709
FT /evidence="ECO:0000255"
FT COMPBIAS 949..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:26304236"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:26304236"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSH4"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TSH4"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 968..1012
FT /note="TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI -> SIC
FT RKNPKKAAKCCDNLRRQHSLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455477"
FT /id="VSP_011897"
FT VARIANT 69
FT /note="R -> S (in dbSNP:rs16972129)"
FT /id="VAR_056788"
FT VARIANT 171
FT /note="P -> L (in dbSNP:rs3751821)"
FT /id="VAR_056789"
FT VARIANT 252
FT /note="I -> M (in dbSNP:rs226891)"
FT /evidence="ECO:0000269|PubMed:10493829,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9455477"
FT /id="VAR_019823"
FT VARIANT 347
FT /note="F -> I (in dbSNP:rs11645625)"
FT /evidence="ECO:0000269|PubMed:9455477"
FT /id="VAR_056790"
FT VARIANT 375
FT /note="M -> I (in dbSNP:rs7190666)"
FT /id="VAR_019824"
FT MUTAGEN 170
FT /note="S->A: Loss of centrosome clustering and protection
FT from anaphase catastrophe upon CDK2 inhibition in lung
FT cancer cells."
FT /evidence="ECO:0000269|PubMed:26304236"
FT MUTAGEN 194
FT /note="T->A: Loss of centrosome clustering and protection
FT from anaphase catastrophe upon CDK2 inhibition in lung
FT cancer cells."
FT /evidence="ECO:0000269|PubMed:26304236"
FT MUTAGEN 586..588
FT /note="RRL->ARA: Abolishes interaction with CCNF."
FT /evidence="ECO:0000269|PubMed:20596027"
FT CONFLICT 628
FT /note="V -> F (in Ref. 5; AAH36654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 113424 MW; 5459F655CFB9DFD0 CRC64;
MEEYEKFCEK SLARIQEASL STESFLPAQS ESISLIRFHG VAILSPLLNI EKRKEMQQEK
QKALDVEARK QVNRKKALLT RVQEILDNVQ VRKAPNASDF DQWEMETVYS NSEVRNLNVP
ATFPNSFPSH TEHSTAAKLD KIAGILPLDN EDQCKTDGID LARDSEGFNS PKQCDSSNIS
HVENEAFPKT SSATPQETLI SDGPFSVNEQ QDLPLLAEVI PDPYVMSLQN LMKKSKEYIE
REQSRRSLRG SINRIVNESH LDKEHDAVEV ADCVKEKGQL TGKHCVSVIP DKPSLNKSNV
LLQGASTQAS SMSMPVLASF SKVDIPIRTG HPTVLESNSD FKVIPTFVTE NNVIKSLTGS
YAKLPSPEPS MSPKMHRRRS RTSSACHILI NNPINACELS PKGKEQAMDL IIQDTDENTN
VPEIMPKLPT DLAGVCSSKV YVGKNTSEVK EDVVLGKSNQ VCQSSGNHLE NKVTHGLVTV
EGQLTSDERG AHIMNSTCAA MPKLHEPYAS SQCIASPNFG TVSGLKPASM LEKNCSLQTE
LNKSYDVKNP SPLLMQNQNT RQQMDTPMVS CGNEQFLDNS FEKVKRRLDL DIDGLQKENC
PYVITSGITE QERQHLPEKR YPKGSGFVNK NKMLGTSSKE SEELLKSKML AFEEMRKRLE
EQHAQQLSLL IAEQEREQER LQKEIEEQEK MLKEKKAMTA EASELDINNA VELEWRKISD
SSLLETMLSQ ADSLHTSNSN SSGFTNSAMQ YSFVSANEAP FYLWGSSTSG LTKLSVTRPF
GRAKTRWSQV FSLEIQAKFN KITAVAKGFL TRRLMQTDKL KQLRQTVKDT MEFIRSFQSE
APLKRGIVSA QDASLQERVL AQLRAALYGI HDIFFVMDAA ERMSILHHDR EVRKEKMLRQ
MDKMKSPRVA LSAATQKSLD RKKYMKAAEM GMPNKKFLVK QNPSETRVLQ PNQGQNAPVH
RLLSRQGTPK TSVKGVVQNR QKPSQSRVPN RVPVSGVYAG KIQRKRPNVA TI
