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Reviewed, UniProtKB/Swiss-Prot O43303 (CE110_HUMAN)

Last modified February 9, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Centrosomal protein of 110 kDa
      Short name=Cep110
Gene names
Name: CEP110
Synonyms: CP110, KIAA0419
OrganismHomo sapiens (Human) [Complete 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. 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. Ref.8 Ref.10 Ref.13

Subcellular location

Cytoplasmcytoskeletoncentrosomecentriole. Note: Recruited early and then associates with the growing distal tips. Ref.6 Ref.8 Ref.10 Ref.11 Ref.7

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.15

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcentriole replication Ref.11

Inferred from mutant phenotype. Source: UniProtKB

regulation of cytokinesis Ref.8

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentcentriole Ref.11

Inferred from direct assay. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

   Molecular functionprotein binding Ref.6 Ref.8 Ref.10 Ref.13

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 – 10121012Centrosomal 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

Amino acid modifications

Modified residue3661Phosphoserine Ref.12
Modified residue3701Phosphoserine Ref.12
Modified residue3721Phosphoserine Ref.12 Ref.15
Modified residue6411Phosphoserine Ref.9

Natural variations

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

Experimental info

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.

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: 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. 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: 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].
[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: Epithelium.
[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.
[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: T-cell.
+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.
IPIIPI00011933.
IPI00478736.
PIRT01372.
RefSeqNP_055526.3.
UniGeneHs.279912

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO43303. 6 interactions.
STRINGO43303.

PTM databases

PhosphoSiteO43303.

Genome annotation databases

EnsemblENST00000219827; ENSP00000219827; ENSG00000103540; Homo sapiens. [Genome view]
ENST00000381396; ENSP00000370803; ENSG00000103540; Homo sapiens. [Genome view]
ENST00000396208; ENSP00000379511; ENSG00000103540; Homo sapiens. [Genome view]
ENST00000396212; ENSP00000379515; ENSG00000103540; Homo sapiens. [Genome view]
GeneID9738.
KEGGhsa:9738.
UCSCuc002dgk.2. human.
uc002dgl.2. human.

Organism-specific databases

CTD9738.
GeneCardsGC09P122877.
GC16P019442.
H-InvDBHIX0019147.
MIM609544. gene.
HUGESearch...

Phylogenomic databases

eggNOGprNOG05924.
HOGENOMHBG278100.
HOVERGENO43303.
InParanoidO43303.
OMAPSPLLMQ.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressO43303.
BgeeO43303.
CleanExHS_CEP110.
GenevestigatorO43303.
GermOnlineENSG00000103540. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameCE110_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: February 9, 2010
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 16

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents