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UniProtKB/Swiss-Prot entry O43303


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CE110_HUMAN
Primary accession number O43303
Secondary accession numbers O43335 Q68DV9 Q8NE13
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on October 23, 2007 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 59)
Name and origin of the protein
Protein name Centrosomal protein of 110 kDa
Synonym Cep110
Gene name
Name: CEP110
Synonyms: CP110, KIAA0419
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-252.
TISSUE=Brain;
DOI=10.1093/dnares/4.5.307; PubMed=9455477 [NCBI, ExPASy, EBI, Israel, Japan]
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 GENOMIC DNA], AND VARIANT MET-252.
DOI=10.1006/geno.1999.5927; PubMed=10493829 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03187; PubMed=15616553 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-252.
TISSUE=Fetal kidney;
The German cDNA consortium;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-252.
TISSUE=Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S1534-5807(02)00258-7; PubMed=12361598 [NCBI, ExPASy, EBI, Israel, Japan]
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]
MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02166; PubMed=14654843 [NCBI, ExPASy, EBI, Israel, Japan]
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, AND INTERACTION WITH CALM1 AND CENTRIN.
DOI=10.1091/mbc.E06-04-0371; PubMed=16760425 [NCBI, ExPASy, EBI, Israel, Japan]
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
FUNCTION, INTERACTION WITH CALM1 AND CEP97, AND SUBCELLULAR LOCATION.
DOI=10.1016/j.cell.2007.06.027; PubMed=17719545 [NCBI, ExPASy, EBI, Israel, Japan]
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.;
"Cep97 and CP110 suppress a cilia assembly program.";
Cell 130:678-690(2007).
Comments
  • FUNCTION: Necessary for centrosome duplication. 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 centrin.
  • SUBUNIT: Interacts with CALM1, centrin and CEP97.
  • INTERACTION:
    P62158:CALM1; NbExp=5; IntAct=EBI-1566217, EBI-397435;
    Q8IW35:CEP97; NbExp=5; IntAct=EBI-1566217, EBI-1566210;
    P41208:CETN2; NbExp=2; IntAct=EBI-1566217, EBI-1789926;
  • SUBCELLULAR LOCATION: Centrosome.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO43303-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO43303-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_011897.
  • TISSUE SPECIFICITY: Highly expressed in testis. Detected at intermediate levels in spleen, thymus, prostate, small intestine, colon and peripheral blood leukocytes.
  • 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.
  • PTM: Phosphorylated by CDKs.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB007879; BAA24849.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC003108; AAC05804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012621; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
CR749255; CAH18111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036654; AAH36654.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T01372; T01372.
RefSeq NP_055526.3; -.
UniGene Hs.279912
3D structure databases
ModBase O43303.
Protein-protein interaction databases
IntAct O43303; 7.
PTM databases
PhosphoSite O43303; -.
Organism-specific databases
GeneCards GC16P019442; -.
H-InvDB HIX0019147; -.
MIM 609544; gene. [NCBI / EBI]
GeneCards O43303.
HUGE KIAA0419.
Gene expression databases
ArrayExpress O43303; -.
CleanEx HS_CEP110; -.
GermOnline ENSG00000103540; Homo sapiens.
Ontologies
GO
GO:0005813; Cellular component: centrosome (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0051298; Biological process: centrosome duplication (inferred from mutant phenotype from UniProtKB).
GO:0032465; Biological process: regulation of cytokinesis (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Genome annotation databases
Ensembl ENSG00000103540; Homo sapiens. [Contig view]
GeneID 9738; -.
Phylogenomic databases
HOGENOM O43303; -.
HOVERGEN O43303; -.
Other
LinkHub O43303; -.
SOURCE CEP110; Homo sapiens.
ProtoNet O43303.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Coiled coil; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1012  1012     Centrosomal protein of 110 kDa. PRO_0000089460
REGION   1    223  223     CEP97 binding. 
REGION   64     82  19     Calmodulin binding. 
REGION   781    821  41     Calmodulin binding. 
REGION   909    924  16     Calmodulin binding. 
COILED   49     90  42     Potential. 
COILED   640    709  70     Potential. 
MOD_RES   641    641        Phosphoserine. 
VAR_SEQ   968   1012        TPKTSVKGVVQNRQKPSQSRVPNRVPVSGVYAGKIQRKRP NVATI -> SICRKNPKKAAKCCDNLRRQHSLG (in isoform 2). VSP_011897
VARIANT   252    252  1     I -> M (in dbSNP:rs226891 [NCBI]). VAR_019823 
VARIANT   375    375  1     M -> I (in dbSNP:rs7190666 [NCBI]). VAR_019824 
CONFLICT   347    347        F -> I (in Ref. 1; BAA24849). 
CONFLICT   628    628        V -> F (in Ref. 5; AAH36654). 
Sequence information
Length: 1012 AA [This is the length of the unprocessed precursor] Molecular weight: 113424 Da [This is the MW of the unprocessed precursor] CRC64: 5459F655CFB9DFD0 [This is a checksum on the sequence]
        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 

O43303 in FASTA format

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