O43303 (CP110_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1012 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for centrosome duplication at different stages of procentriole formation. Collaborates with CEP97, being involved in the suppression of a cilia assembly program. 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.10 Ref.11
Subunit structure	Interacts with CALM1, CETN2, CEP76 and CEP97. Interacts with CCNF. Ref.8 Ref.10 Ref.13 Ref.16
Subcellular location	Cytoplasm › cytoskeleton › centrosome › centriole. Note: Recruited early and then associates with the growing distal tips. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.16
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 Ref.9 Ref.12 Ref.14 Ref.15 Ubiquitinated by the SCF(Cyclin F) during G2 phase, leading to its degradation by the proteasome and preventing centrosome reduplication. Ref.16
Sequence caution	The sequence BAA24849.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome centriole replication Inferred from mutant phenotype Ref.11. Source: UniProtKB regulation of cytokinesis Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular component	centriole Inferred from direct assay Ref.11Ref.16. Source: UniProtKB cytosol Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction Ref.8Ref.13Ref.16. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CALM1	P62158	9	EBI-1566217,EBI-397435
CEP97	Q8IW35	15	EBI-1566217,EBI-1566210
CETN2	P41208	3	EBI-1566217,EBI-1789926
KIF24	Q5T7B8	9	EBI-1566217,EBI-2556811

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1012	1012	Centriolar coiled-coil protein of 110 kDa		PRO_0000089460
Regions
	Region	1 – 223	223	CEP97 binding
	Region	64 – 82	19	Calmodulin-binding
	Region	350 – 565	216	Interaction with CEP76
	Region	781 – 821	41	Calmodulin-binding
	Region	909 – 924	16	Calmodulin-binding
	Coiled coil	49 – 90	42	Potential
	Coiled coil	640 – 709	70	Potential
Amino acid modifications
	Modified residue	366	1	Phosphoserine Ref.12
	Modified residue	370	1	Phosphoserine Ref.12 Ref.14
	Modified residue	372	1	Phosphoserine Ref.12 Ref.15
	Modified residue	641	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	968 – 1012	45	TPKTS…NVATI → SICRKNPKKAAKCCDNLRRQ HSLG in isoform 2.		VSP_011897
	Natural variant	69	1	R → S. Corresponds to variant rs16972129 [ dbSNP | Ensembl ].		VAR_056788
	Natural variant	171	1	P → L. Corresponds to variant rs3751821 [ dbSNP | Ensembl ].		VAR_056789
	Natural variant	252	1	I → M. Ref.1 Ref.2 Ref.3 Ref.5 Corresponds to variant rs226891 [ dbSNP | Ensembl ].		VAR_019823
	Natural variant	347	1	F → I. Ref.1 Corresponds to variant rs11645625 [ dbSNP | Ensembl ].		VAR_056790
	Natural variant	375	1	M → I. Corresponds to variant rs7190666 [ dbSNP | Ensembl ].		VAR_019824
Experimental info
	Mutagenesis	586 – 588	3	RRL → ARA: Abolishes interaction with CCNF. Ref.16
	Sequence conflict	628	1	V → F in AAH36654. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: 5459F655CFB9DFD0	FASTA	1,012	113,424
	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
	Isoform 2 [UniParc]. Checksum: CDEA157BFDBC92EA	FASTA	991	111,224
	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 RLLSRQGSIC RKNPKKAAKC CDNLRRQHSL G

References

	« Hide 'large scale' referencesShow '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: 9455477] [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: 17974005] [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: 10493829] [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. , 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: 15616553] [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: 15489334] [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: 12361598] [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: 14654843] [Abstract] Cited for: MASS SPECTROMETRY, 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: 16760425] [Abstract] Cited for: FUNCTION, INTERACTION WITH CALM1 AND CETN2, SUBCELLULAR LOCATION.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Cep97 and CP110 suppress a cilia assembly program." Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D. Cell 130:678-690(2007) [PubMed: 17719545] [Abstract] Cited for: FUNCTION, INTERACTION WITH CALM1 AND CEP97, SUBCELLULAR LOCATION.
[11]	"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: 17681131] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-370 AND SER-372, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19460342] [Abstract] Cited for: INTERACTION WITH CEP76.
[14]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, MASS SPECTROMETRY.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"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: 20596027] [Abstract] Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, MUTAGENESIS OF 586-ARG--LEU-588, INTERACTION WITH CCNF.
+	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.
IPI	IPI00011933. IPI00478736.
PIR	T01372.
RefSeq	NP_001185951.1. NM_001199022.1. NP_055526.3. NM_014711.4.
UniGene	Hs.279912.
3D structure databases
ProteinModelPortal	O43303.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43303. 12 interactions.
STRING	O43303.
PTM databases
PhosphoSite	O43303.
Proteomic databases
PRIDE	O43303.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219827; ENSP00000219827; ENSG00000103540. ENST00000381396; ENSP00000370803; ENSG00000103540. ENST00000396208; ENSP00000379511; ENSG00000103540. ENST00000396212; ENSP00000379515; ENSG00000103540.
GeneID	9738.
KEGG	hsa:9738.
UCSC	uc002dgk.2. human. uc002dgl.2. human.
Organism-specific databases
CTD	9738.
GeneCards	GC16P019536.
HGNC	HGNC:24342. CCP110.
HPA	HPA039402.
MIM	609544. gene.
neXtProt	NX_O43303.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05924.
GeneTree	ENSGT00390000004090.
HOGENOM	HBG278100.
HOVERGEN	HBG050873.
InParanoid	O43303.
OMA	KDTMEFI.
OrthoDB	EOG40ZQX3.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	O43303.
Bgee	O43303.
CleanEx	HS_CEP110.
Genevestigator	O43303.
GermOnline	ENSG00000103540. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

CP110_HUMAN

Accession

Primary (citable) accession number: O43303
Secondary accession number(s): B7WP23 , O43335, Q68DV9, Q8NE13

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.