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O43303 (CP110_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centriolar coiled-coil protein of 110 kDa
Alternative name(s):
Centrosomal protein of 110 kDa
Short name=CP110
Short name=Cep110
Gene names
Name:CCP110
Synonyms:CEP110, CP110, KIAA0419
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1012 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Required for correct spindle formation and has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CETN2. Ref.6 Ref.8 Ref.9 Ref.10 Ref.18

Subunit structure

Interacts with CALM1, CETN2, CEP76 and CEP97. 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. Ref.8 Ref.9 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.14 Ref.15

Tissue specificity

Highly expressed in testis. Detected at intermediate levels in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes. Ref.6

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. Ref.6

Post-translational modification

Phosphorylated by CDKs. Ref.6

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. Ref.14 Ref.18

Sequence caution

The sequence BAA24849.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43303-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43303-2)

The sequence of this isoform differs from the canonical sequence as follows:
     968-1012: TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRPNVATI → SICRKNPKKAAKCCDNLRRQHSLG

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10121012Centriolar coiled-coil protein of 110 kDa
PRO_0000089460

Regions

Region1 – 223223CEP97 binding
Region64 – 8219Calmodulin-binding
Region350 – 565216Interaction with CEP76
Region781 – 82141Calmodulin-binding
Region909 – 92416Calmodulin-binding
Coiled coil49 – 9042 Potential
Coiled coil640 – 70970 Potential

Natural variations

Alternative sequence968 – 101245TPKTS…NVATI → SICRKNPKKAAKCCDNLRRQ HSLG in isoform 2.
VSP_011897
Natural variant691R → S.
Corresponds to variant rs16972129 [ dbSNP | Ensembl ].
VAR_056788
Natural variant1711P → L.
Corresponds to variant rs3751821 [ dbSNP | Ensembl ].
VAR_056789
Natural variant2521I → M. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs226891 [ dbSNP | Ensembl ].
VAR_019823
Natural variant3471F → I. Ref.1
Corresponds to variant rs11645625 [ dbSNP | Ensembl ].
VAR_056790
Natural variant3751M → I.
Corresponds to variant rs7190666 [ dbSNP | Ensembl ].
VAR_019824

Experimental info

Mutagenesis586 – 5883RRL → ARA: Abolishes interaction with CCNF. Ref.14
Sequence conflict6281V → F in AAH36654. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: 5459F655CFB9DFD0

FASTA1,012113,424
        10         20         30         40         50         60 
MEEYEKFCEK SLARIQEASL STESFLPAQS ESISLIRFHG VAILSPLLNI EKRKEMQQEK 

        70         80         90        100        110        120 
QKALDVEARK QVNRKKALLT RVQEILDNVQ VRKAPNASDF DQWEMETVYS NSEVRNLNVP 

       130        140        150        160        170        180 
ATFPNSFPSH TEHSTAAKLD KIAGILPLDN EDQCKTDGID LARDSEGFNS PKQCDSSNIS 

       190        200        210        220        230        240 
HVENEAFPKT SSATPQETLI SDGPFSVNEQ QDLPLLAEVI PDPYVMSLQN LMKKSKEYIE 

       250        260        270        280        290        300 
REQSRRSLRG SINRIVNESH LDKEHDAVEV ADCVKEKGQL TGKHCVSVIP DKPSLNKSNV 

       310        320        330        340        350        360 
LLQGASTQAS SMSMPVLASF SKVDIPIRTG HPTVLESNSD FKVIPTFVTE NNVIKSLTGS 

       370        380        390        400        410        420 
YAKLPSPEPS MSPKMHRRRS RTSSACHILI NNPINACELS PKGKEQAMDL IIQDTDENTN 

       430        440        450        460        470        480 
VPEIMPKLPT DLAGVCSSKV YVGKNTSEVK EDVVLGKSNQ VCQSSGNHLE NKVTHGLVTV 

       490        500        510        520        530        540 
EGQLTSDERG AHIMNSTCAA MPKLHEPYAS SQCIASPNFG TVSGLKPASM LEKNCSLQTE 

       550        560        570        580        590        600 
LNKSYDVKNP SPLLMQNQNT RQQMDTPMVS CGNEQFLDNS FEKVKRRLDL DIDGLQKENC 

       610        620        630        640        650        660 
PYVITSGITE QERQHLPEKR YPKGSGFVNK NKMLGTSSKE SEELLKSKML AFEEMRKRLE 

       670        680        690        700        710        720 
EQHAQQLSLL IAEQEREQER LQKEIEEQEK MLKEKKAMTA EASELDINNA VELEWRKISD 

       730        740        750        760        770        780 
SSLLETMLSQ ADSLHTSNSN SSGFTNSAMQ YSFVSANEAP FYLWGSSTSG LTKLSVTRPF 

       790        800        810        820        830        840 
GRAKTRWSQV FSLEIQAKFN KITAVAKGFL TRRLMQTDKL KQLRQTVKDT MEFIRSFQSE 

       850        860        870        880        890        900 
APLKRGIVSA QDASLQERVL AQLRAALYGI HDIFFVMDAA ERMSILHHDR EVRKEKMLRQ 

       910        920        930        940        950        960 
MDKMKSPRVA LSAATQKSLD RKKYMKAAEM GMPNKKFLVK QNPSETRVLQ PNQGQNAPVH 

       970        980        990       1000       1010 
RLLSRQGTPK TSVKGVVQNR QKPSQSRVPN RVPVSGVYAG KIQRKRPNVA TI 

« Hide

Isoform 2 [UniParc].

Checksum: CDEA157BFDBC92EA
Show »

FASTA991111,224

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS MET-252 AND ILE-347.
Tissue: Brain.
[2]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-252.
Tissue: Fetal kidney.
[3]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
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.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-252.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
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. expand/collapse author list , 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.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-252.
Tissue: Testis.
[6]"CP110, a cell cycle-dependent CDK substrate, regulates centrosome duplication in human cells."
Chen Z., Indjeian V.B., McManus M., Wang L., Dynlacht B.D.
Dev. Cell 3:339-350(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, PHOSPHORYLATION.
[7]"Proteomic characterization of the human centrosome by protein correlation profiling."
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Lymphoblast.
[8]"CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CALM1 AND CETN2, SUBCELLULAR LOCATION.
[9]"Cep97 and CP110 suppress a cilia assembly program."
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.
Cell 130:678-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CALM1 AND CEP97, SUBCELLULAR LOCATION.
[10]"Plk4-induced centriole biogenesis in human cells."
Kleylein-Sohn J., Westendorf J., Le Clech M., Habedanck R., Stierhof Y.-D., Nigg E.A.
Dev. Cell 13:190-202(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Cep76, a centrosomal protein that specifically restrains centriole reduplication."
Tsang W.Y., Spektor A., Vijayakumar S., Bista B.R., Li J., Sanchez I., Duensing S., Dynlacht B.D.
Dev. Cell 16:649-660(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP76.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"SCF(Cyclin F) controls centrosome homeostasis and mitotic fidelity through CP110 degradation."
D'Angiolella V., Donato V., Vijayakumar S., Saraf A., Florens L., Washburn M.P., Dynlacht B., Pagano M.
Nature 466:138-142(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 586-ARG--LEU-588, INTERACTION WITH CCNF.
[15]"Centriolar kinesin Kif24 interacts with CP110 to remodel microtubules and regulate ciliogenesis."
Kobayashi T., Tsang W.Y., Li J., Lane W., Dynlacht B.D.
Cell 145:914-925(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF24.
[16]"Neurl4, a novel daughter centriole protein, prevents formation of ectopic microtubule organizing centres."
Li J., Kim S., Kobayashi T., Liang F.X., Korzeniewski N., Duensing S., Dynlacht B.D.
EMBO Rep. 13:547-553(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NEURL4 AND CCNF.
[17]"Interaction proteomics identify NEURL4 and the HECT E3 ligase HERC2 as novel modulators of centrosome architecture."
Al-Hakim A.K., Bashkurov M., Gingras A.C., Durocher D., Pelletier L.
Mol. Cell. Proteomics 11:M111.014233.01-M111.014233.14(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CEP97; HERC2 AND NEURL4.
[18]"USP33 regulates centrosome biogenesis via deubiquitination of the centriolar protein CP110."
Li J., D'Angiolella V., Seeley E.S., Kim S., Kobayashi T., Fu W., Campos E.I., Pagano M., Dynlacht B.D.
Nature 495:255-259(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DEUBIQUITINATION, INTERACTION WITH USP20 AND USP33.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007879 mRNA. Translation: BAA24849.2. Different initiation.
CR749255 mRNA. Translation: CAH18111.1.
AC003108 Genomic DNA. Translation: AAC05804.1.
AC012621 Genomic DNA. No translation available.
BC036654 mRNA. Translation: AAH36654.1.
CCDSCCDS10579.1. [O43303-2]
CCDS55992.1. [O43303-1]
PIRT01372.
RefSeqNP_001185951.1. NM_001199022.1.
NP_055526.3. NM_014711.4.
XP_005255776.1. XM_005255719.1. [O43303-1]
XP_005255778.1. XM_005255721.1. [O43303-2]
UniGeneHs.279912.

3D structure databases

ProteinModelPortalO43303.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115087. 28 interactions.
DIPDIP-39892N.
IntActO43303. 19 interactions.
MINTMINT-7994609.

PTM databases

PhosphoSiteO43303.

Proteomic databases

MaxQBO43303.
PaxDbO43303.
PRIDEO43303.

Protocols and materials databases

DNASU9738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000381396; ENSP00000370803; ENSG00000103540. [O43303-1]
ENST00000396208; ENSP00000379511; ENSG00000103540. [O43303-2]
ENST00000396212; ENSP00000379515; ENSG00000103540. [O43303-2]
GeneID9738.
KEGGhsa:9738.
UCSCuc002dgk.4. human. [O43303-2]
uc002dgl.4. human. [O43303-1]

Organism-specific databases

CTD9738.
GeneCardsGC16P019536.
HGNCHGNC:24342. CCP110.
HPAHPA039402.
MIM609544. gene.
neXtProtNX_O43303.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82086.
HOVERGENHBG050873.
InParanoidO43303.
KOK16453.
OMAFYLWGSS.
OrthoDBEOG7SV0XP.
PhylomeDBO43303.
TreeFamTF332788.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressO43303.
BgeeO43303.
CleanExHS_CEP110.
GenevestigatorO43303.

Family and domain databases

ProtoNetSearch...

Other

GeneWikiCCP110.
GenomeRNAi9738.
NextBio36648.
PROO43303.
SOURCESearch...

Entry information

Entry nameCP110_HUMAN
AccessionPrimary (citable) accession number: O43303
Secondary accession number(s): B7WP23 expand/collapse secondary AC list , O43335, Q68DV9, Q8NE13
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: October 23, 2007
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM