Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Centriolar coiled-coil protein of 110 kDa (Centrosomal protein of 110 kDa) (CP110) (Cep110)

 CP110_HUMAN             Reviewed;        1012 AA.
O43303; B7WP23; O43335; Q68DV9; Q8NE13;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
23-OCT-2007, sequence version 3.
18-JUL-2018, entry version 158.
RecName: Full=Centriolar coiled-coil protein of 110 kDa;
AltName: Full=Centrosomal protein of 110 kDa;
Short=CP110;
Short=Cep110;
Name=CCP110; Synonyms=CEP110, CP110, KIAA0419;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
MET-252 AND ILE-347.
TISSUE=Brain;
PubMed=9455477; DOI=10.1093/dnares/4.5.307;
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VIII.
78 new cDNA clones from brain which code for large proteins in
vitro.";
DNA Res. 4:307-313(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
MET-252.
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-252.
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
MET-252.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
PHOSPHORYLATION.
PubMed=12361598; DOI=10.1016/S1534-5807(02)00258-7;
Chen Z., Indjeian V.B., McManus M., Wang L., Dynlacht B.D.;
"CP110, a cell cycle-dependent CDK substrate, regulates centrosome
duplication in human cells.";
Dev. Cell 3:339-350(2002).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[8]
FUNCTION, INTERACTION WITH CALM1 AND CETN2, AND SUBCELLULAR LOCATION.
PubMed=16760425; DOI=10.1091/mbc.E06-04-0371;
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z.,
Salisbury J.L., Sanchez I., Dynlacht B.D.;
"CP110 cooperates with two calcium-binding proteins to regulate
cytokinesis and genome stability.";
Mol. Biol. Cell 17:3423-3434(2006).
[9]
FUNCTION, INTERACTION WITH CALM1 AND CEP97, AND SUBCELLULAR LOCATION.
PubMed=17719545; DOI=10.1016/j.cell.2007.06.027;
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
"Cep97 and CP110 suppress a cilia assembly program.";
Cell 130:678-690(2007).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17681131; DOI=10.1016/j.devcel.2007.07.002;
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R.,
Stierhof Y.-D., Nigg E.A.;
"Plk4-induced centriole biogenesis in human cells.";
Dev. Cell 13:190-202(2007).
[11]
INTERACTION WITH CEP290.
PubMed=18694559; DOI=10.1016/j.devcel.2008.07.004;
Tsang W.Y., Bossard C., Khanna H., Peraenen J., Swaroop A.,
Malhotra V., Dynlacht B.D.;
"CP110 suppresses primary cilia formation through its interaction with
CEP290, a protein deficient in human ciliary disease.";
Dev. Cell 15:187-197(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
INTERACTION WITH CEP76.
PubMed=19460342; DOI=10.1016/j.devcel.2009.03.004;
Tsang W.Y., Spektor A., Vijayakumar S., Bista B.R., Li J., Sanchez I.,
Duensing S., Dynlacht B.D.;
"Cep76, a centrosomal protein that specifically restrains centriole
reduplication.";
Dev. Cell 16:649-660(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 586-ARG--LEU-588,
AND INTERACTION WITH CCNF.
PubMed=20596027; DOI=10.1038/nature09140;
D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L.,
Washburn M.P., Dynlacht B., Pagano M.;
"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity
through CP110 degradation.";
Nature 466:138-142(2010).
[16]
SUBCELLULAR LOCATION, AND INTERACTION WITH KIF24.
PubMed=21620453; DOI=10.1016/j.cell.2011.04.028;
Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.;
"Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules
and regulate ciliogenesis.";
Cell 145:914-925(2011).
[17]
INTERACTION WITH CEP104.
PubMed=22885064; DOI=10.1016/j.cub.2012.07.047;
Jiang K., Toedt G., Montenegro Gouveia S., Davey N.E., Hua S.,
van der Vaart B., Grigoriev I., Larsen J., Pedersen L.B.,
Bezstarosti K., Lince-Faria M., Demmers J., Steinmetz M.O.,
Gibson T.J., Akhmanova A.;
"A proteome-wide screen for mammalian SxIP motif-containing
microtubule plus-end tracking proteins.";
Curr. Biol. 22:1800-1807(2012).
[18]
INTERACTION WITH NEURL4 AND CCNF.
PubMed=22441691; DOI=10.1038/embor.2012.40;
Li J., Kim S., Kobayashi T., Liang F.X., Korzeniewski N., Duensing S.,
Dynlacht B.D.;
"Neurl4, a novel daughter centriole protein, prevents formation of
ectopic microtubule organizing centres.";
EMBO Rep. 13:547-553(2012).
[19]
INTERACTION WITH CEP97; HERC2 AND NEURL4.
PubMed=22261722; DOI=10.1074/mcp.M111.014233;
Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.;
"Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2
as novel modulators of centrosome architecture.";
Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-551, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
FUNCTION, DEUBIQUITINATION, AND INTERACTION WITH USP20 AND USP33.
PubMed=23486064; DOI=10.1038/nature11941;
Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W.,
Campos E.I., Pagano M., Dynlacht B.D.;
"USP33 regulates centrosome biogenesis via deubiquitination of the
centriolar protein CP110.";
Nature 495:255-259(2013).
[22]
INTERACTION WITH TALPID3.
PubMed=24421332; DOI=10.1083/jcb.201304153;
Kobayashi T., Kim S., Lin Y.C., Inoue T., Dynlacht B.D.;
"The CP110-interacting proteins Talpid3 and Cep290 play overlapping
and distinct roles in cilia assembly.";
J. Cell Biol. 204:215-229(2014).
[23]
PHOSPHORYLATION AT SER-170 AND THR-194, AND MUTAGENESIS OF SER-170 AND
THR-194.
PubMed=26304236; DOI=10.1158/1535-7163.MCT-15-0443;
Hu S., Lu Y., Orr B., Godek K., Mustachio L.M., Kawakami M.,
Sekula D., Compton D.A., Freemantle S., Dmitrovsky E.;
"Specific CP110 phosphorylation sites mediate anaphase catastrophe
after CDK2 inhibition: evidence for cooperation with USP33
knockdown.";
Mol. Cancer Ther. 14:2576-2585(2015).
-!- FUNCTION: Necessary for centrosome duplication at different stages
of procentriole formation. Acts as a key negative regulator of
ciliogenesis in collaboration with CEP97 by capping the mother
centriole thereby preventing cilia formation (PubMed:17719545
PubMed:17681131, PubMed:23486064). Also involved in promoting
ciliogenesis. May play a role in the assembly of the mother
centriole subdistal appendages (SDA) thereby effecting the fusion
of recycling endosomes to basal bodies during cilia formation (By
similarity). Required for correct spindle formation and has a role
in regulating cytokinesis and genome stability via cooperation
with CALM1 and CETN2 (PubMed:16760425).
{ECO:0000250|UniProtKB:Q7TSH4, ECO:0000269|PubMed:12361598,
ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131,
ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:23486064}.
-!- SUBUNIT: Interacts with CALM1, CETN2, CEP76, CEP97, CEP104,
CEP290, TALPID3. Seems to associate with discrete CETN2, CEP97 and
CEP290-containing complexes. Interacts with NEURL4 and CCNF; these
interactions are not mutually exclusive and both lead to CCP110
ubiquitination and proteasome-dependent degradation. Via its
interaction with NEURL4, may indirectly interact with HERC2.
Interacts with KIF24, leading to its recruitment to centrioles.
Interacts with USP20 and USP33. {ECO:0000269|PubMed:16760425,
ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:18694559,
ECO:0000269|PubMed:19460342, ECO:0000269|PubMed:20596027,
ECO:0000269|PubMed:21620453, ECO:0000269|PubMed:22261722,
ECO:0000269|PubMed:22441691, ECO:0000269|PubMed:22885064,
ECO:0000269|PubMed:23486064, ECO:0000269|PubMed:24421332}.
-!- INTERACTION:
P62158:CALM3; NbExp=15; IntAct=EBI-1566217, EBI-397435;
P41002:CCNF; NbExp=9; IntAct=EBI-1566217, EBI-1207574;
O15078:CEP290; NbExp=15; IntAct=EBI-1566217, EBI-1811944;
Q8IW35:CEP97; NbExp=25; IntAct=EBI-1566217, EBI-1566210;
P41208:CETN2; NbExp=3; IntAct=EBI-1566217, EBI-1789926;
Q5T7B8:KIF24; NbExp=9; IntAct=EBI-1566217, EBI-2556811;
Q96JN8:NEURL4; NbExp=9; IntAct=EBI-1566217, EBI-1053406;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome, centriole
{ECO:0000269|PubMed:12361598, ECO:0000269|PubMed:14654843,
ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:17681131,
ECO:0000269|PubMed:17719545, ECO:0000269|PubMed:20596027,
ECO:0000269|PubMed:21620453}. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q7TSH4}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000250|UniProtKB:Q7TSH4}. Note=Recruited early and then
associates with the growing distal tips. Recruited to the mother
centriole by KIF24. Removed from centrioles by TTBK2, leading to
initiation of ciliogenesis and localizes only to the daughter
centriole in ciliated cells. In cytotoxic T lymphocytes remains
associated with the mother centriole during docking of the
centrosome at the immunological synapse upon target contact.
{ECO:0000250|UniProtKB:Q7TSH4, ECO:0000269|PubMed:21620453}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43303-1; Sequence=Displayed;
Name=2;
IsoId=O43303-2; Sequence=VSP_011897;
-!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at
intermediate levels in spleen, thymus, prostate, small intestine,
colon and peripheral blood leukocytes.
{ECO:0000269|PubMed:12361598}.
-!- INDUCTION: Up-regulated during the transition from G1 to S phase
of the cell cycle. The highest levels are observed in S phase,
after which the levels decrease markedly.
{ECO:0000269|PubMed:12361598}.
-!- PTM: Phosphorylated by CDKs. {ECO:0000269|PubMed:12361598}.
-!- PTM: Ubiquitinated by the SCF(CCNF) during G2 phase, leading to
its degradation by the proteasome and preventing centrosome
reduplication. Deubiquitinated by USP33 in S and G2/M phase,
leading to stabilize CCP110 during the period which centrioles
duplicate and elongate. {ECO:0000269|PubMed:20596027,
ECO:0000269|PubMed:23486064}.
-!- SEQUENCE CAUTION:
Sequence=BAA24849.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AB007879; BAA24849.2; ALT_INIT; mRNA.
EMBL; CR749255; CAH18111.1; -; mRNA.
EMBL; AC003108; AAC05804.1; -; Genomic_DNA.
EMBL; AC012621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036654; AAH36654.1; -; mRNA.
CCDS; CCDS10579.1; -. [O43303-2]
CCDS; CCDS55992.1; -. [O43303-1]
PIR; T01372; T01372.
RefSeq; NP_001185951.2; NM_001199022.2. [O43303-1]
RefSeq; NP_001310498.1; NM_001323569.1. [O43303-1]
RefSeq; NP_001310499.1; NM_001323570.1. [O43303-2]
RefSeq; NP_001310500.1; NM_001323571.1. [O43303-2]
RefSeq; NP_001310501.1; NM_001323572.1. [O43303-2]
RefSeq; NP_055526.4; NM_014711.5. [O43303-2]
RefSeq; XP_011544293.1; XM_011545991.2. [O43303-1]
RefSeq; XP_011544294.1; XM_011545992.2. [O43303-1]
RefSeq; XP_016879397.1; XM_017023908.1. [O43303-1]
UniGene; Hs.279912; -.
ProteinModelPortal; O43303; -.
SMR; O43303; -.
BioGrid; 115087; 73.
CORUM; O43303; -.
DIP; DIP-39892N; -.
IntAct; O43303; 67.
MINT; O43303; -.
STRING; 9606.ENSP00000370803; -.
iPTMnet; O43303; -.
PhosphoSitePlus; O43303; -.
BioMuta; CCP110; -.
EPD; O43303; -.
MaxQB; O43303; -.
PaxDb; O43303; -.
PeptideAtlas; O43303; -.
PRIDE; O43303; -.
ProteomicsDB; 48877; -.
ProteomicsDB; 48878; -. [O43303-2]
DNASU; 9738; -.
Ensembl; ENST00000381396; ENSP00000370803; ENSG00000103540. [O43303-1]
Ensembl; ENST00000396208; ENSP00000379511; ENSG00000103540. [O43303-2]
Ensembl; ENST00000396212; ENSP00000379515; ENSG00000103540. [O43303-2]
GeneID; 9738; -.
KEGG; hsa:9738; -.
UCSC; uc002dgk.5; human. [O43303-1]
CTD; 9738; -.
DisGeNET; 9738; -.
EuPathDB; HostDB:ENSG00000103540.16; -.
GeneCards; CCP110; -.
HGNC; HGNC:24342; CCP110.
HPA; HPA039402; -.
MIM; 609544; gene.
neXtProt; NX_O43303; -.
OpenTargets; ENSG00000103540; -.
eggNOG; ENOG410IF00; Eukaryota.
eggNOG; ENOG410XP98; LUCA.
GeneTree; ENSGT00390000004090; -.
HOVERGEN; HBG050873; -.
InParanoid; O43303; -.
KO; K16453; -.
OMA; PSMSPKM; -.
OrthoDB; EOG091G0NCE; -.
PhylomeDB; O43303; -.
TreeFam; TF332788; -.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; O43303; -.
ChiTaRS; CCP110; human.
GeneWiki; CCP110; -.
GenomeRNAi; 9738; -.
PRO; PR:O43303; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103540; -.
CleanEx; HS_CEP110; -.
ExpressionAtlas; O43303; baseline and differential.
Genevisible; O43303; HS.
GO; GO:0005814; C:centriole; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0007099; P:centriole replication; IMP:UniProtKB.
GO; GO:0051298; P:centrosome duplication; IDA:UniProtKB.
GO; GO:0032053; P:ciliary basal body organization; ISS:UniProtKB.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
GO; GO:0045724; P:positive regulation of cilium assembly; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
InterPro; IPR033207; CCP110.
PANTHER; PTHR13594; PTHR13594; 1.
1: Evidence at protein level;
Alternative splicing; Cell projection; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 1012 Centriolar coiled-coil protein of 110
kDa.
/FTId=PRO_0000089460.
REGION 1 223 CEP97 binding.
REGION 64 82 Calmodulin-binding.
REGION 67 82 Required for interaction with CEP290.
{ECO:0000269|PubMed:18694559}.
REGION 350 565 Interaction with CEP76.
{ECO:0000269|PubMed:19460342}.
REGION 781 821 Calmodulin-binding.
REGION 909 924 Calmodulin-binding.
COILED 49 90 {ECO:0000255}.
COILED 640 709 {ECO:0000255}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000305|PubMed:26304236}.
MOD_RES 194 194 Phosphothreonine.
{ECO:0000305|PubMed:26304236}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TSH4}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TSH4}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 968 1012 TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPN
VATI -> SICRKNPKKAAKCCDNLRRQHSLG (in
isoform 2). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9455477}.
/FTId=VSP_011897.
VARIANT 69 69 R -> S (in dbSNP:rs16972129).
/FTId=VAR_056788.
VARIANT 171 171 P -> L (in dbSNP:rs3751821).
/FTId=VAR_056789.
VARIANT 252 252 I -> M (in dbSNP:rs226891).
{ECO:0000269|PubMed:10493829,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:9455477}.
/FTId=VAR_019823.
VARIANT 347 347 F -> I (in dbSNP:rs11645625).
{ECO:0000269|PubMed:9455477}.
/FTId=VAR_056790.
VARIANT 375 375 M -> I (in dbSNP:rs7190666).
/FTId=VAR_019824.
MUTAGEN 170 170 S->A: Loss of centrosome clustering and
protection from anaphase catastrophe upon
CDK2 inhibition in lung cancer cells.
{ECO:0000269|PubMed:26304236}.
MUTAGEN 194 194 T->A: Loss of centrosome clustering and
protection from anaphase catastrophe upon
CDK2 inhibition in lung cancer cells.
{ECO:0000269|PubMed:26304236}.
MUTAGEN 586 588 RRL->ARA: Abolishes interaction with
CCNF. {ECO:0000269|PubMed:20596027}.
CONFLICT 628 628 V -> F (in Ref. 5; AAH36654).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
EIAAB08836 CCP110,Centriolar coiled-coil protein of 110 kDa,Centrosomal protein of 110 kDa,Cep110,CEP110,CP110,CP110,Homo sapiens,Human,KIAA0419
EIAAB08837 Ccp110,Centriolar coiled-coil protein of 110 kDa,Centrosomal protein of 110 kDa,Cep110,Cep110,Cp110,Cp110,Kiaa0419,Mouse,Mus musculus
EIAAB08340 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,CEP1,Cep110,CEP110,CNTRL,Homo sapiens,Human
EIAAB08339 Centriolin,Centrosomal protein 1,Centrosomal protein of 110 kDa,Cep1,Cep110,Cep110,Cntrl,Mouse,Mus musculus
CP110_HUMAN ELISA Kit FOR Centriolar coiled-coil protein of 110 kDa; organism: Human; gene name: CCP110 96T
CP110_MOUSE ELISA Kit FOR Centriolar coiled-coil protein of 110 kDa; organism: Mouse; gene name: Ccp110 96T
EIAAB06663 Ccdc46,Centrosomal protein of 112 kDa,Cep112,Coiled-coil domain-containing protein 46,Mouse,Mus musculus
EIAAB06867 Ccdc45,Centrosomal protein of 95 kDa,Cep95,Coiled-coil domain-containing protein 45,Rat,Rattus norvegicus
EIAAB06863 Ccdc123,Centrosomal protein of 89 kDa,Cep89,Coiled-coil domain-containing protein 123,Mouse,Mus musculus
EIAAB06866 Ccdc45,Centrosomal protein of 95 kDa,Cep95,Coiled-coil domain-containing protein 45,Mouse,Mus musculus
EIAAB06861 Ccdc21,Centrosomal protein of 85 kDa,Cep85,Coiled-coil domain-containing protein 21,Mouse,Mus musculus
EIAAB06862 CCDC21,Centrosomal protein of 85 kDa,CEP85,Coiled-coil domain-containing protein 21,Homo sapiens,Human
EIAAB06864 CCDC123,Centrosomal protein of 89 kDa,CEP89,Coiled-coil domain-containing protein 123,Homo sapiens,Human
EIAAB06662 CCDC46,Centrosomal protein of 112 kDa,CEP112,Coiled-coil domain-containing protein 46,Homo sapiens,Human
EIAAB06865 CCDC45,Centrosomal protein of 95 kDa,CEP45,CEP95,Coiled-coil domain-containing protein 45,Homo sapiens,Human
EIAAB06664 CCDC100,Centrosomal protein of 120 kDa,Cep120,CEP120,Coiled-coil domain-containing protein 100,Homo sapiens,Human
EIAAB06666 Bos taurus,Bovine,CCDC100,Centrosomal protein of 120 kDa,Cep120,CEP120,Coiled-coil domain-containing protein 100
EIAAB06665 Ccdc100,Centrosomal protein of 120 kDa,Cep120,Cep120,Coiled-coil domain-containing protein 100,Mouse,Mus musculus
EIAAB05061 Calcium-binding and coiled-coil domain-containing protein 1,Calcoco1,CocoA,Coiled-coil coactivator protein,Kiaa1536,Mouse,Mus musculus
EIAAB46890 CCDC131,Coiled-coil domain-containing protein 131,Homo sapiens,Human,KIAA0546,Proline_serine-rich coiled-coil protein 2,PSRC2,ZFC3H1,Zinc finger C3H1 domain-containing protein
EIAAB07114 AAG10,Aging-associated gene 10 protein,C7orf17,CHCHD2,Coiled-coil-helix-coiled-coil-helix domain-containing protein 2, mitochondrial,HCV NS2 trans-regulated protein,Homo sapiens,Human,NS2TP
EIAAB07128 C9orf49,CHCHD2P9,CHCHD9,Coiled-coil-helix-coiled-coil-helix domain-containing 2 pseudogene 9,Homo sapiens,Human,Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitocho
EIAAB33921 Cc1,Coiled-coil-forming protein 1,Kiaa0203,LaXp180,Mouse,Mus musculus,Rb1cc1,RB1-inducible coiled-coil protein 1
EIAAB05058 Calcium-binding and coiled-coil domain-containing protein 1,CALCOCO1,Calphoglin,Coiled-coil coactivator protein,Homo sapiens,Human,KIAA1536,PP13275,Sarcoma antigen NY-SAR-3,UNQ2436_PRO4996
EIAAB05742 Ccdc115,Ccp1,Coiled-coil domain-containing protein 115,Coiled-coil protein 1,Mouse,Mus musculus


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur