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Q9BV73

- CP250_HUMAN

UniProt

Q9BV73 - CP250_HUMAN

Protein

Centrosome-associated protein CEP250

Gene

CEP250

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (09 May 2003)
      Previous versions | rss
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    Functioni

    Probably plays an important role in centrosome cohesion during interphase.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein C-terminus binding Source: UniProtKB
    3. protein domain specific binding Source: UniProtKB
    4. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. centriole-centriole cohesion Source: UniProtKB
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. mitotic cell cycle Source: UniProtKB
    4. protein localization Source: UniProtKB
    5. protein localization to organelle Source: UniProtKB
    6. regulation of centriole-centriole cohesion Source: UniProtKB

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Centrosome-associated protein CEP250
    Alternative name(s):
    250 kDa centrosomal protein
    Short name:
    Cep250
    Centrosomal Nek2-associated protein 1
    Short name:
    C-Nap1
    Centrosomal protein 2
    Gene namesi
    Name:CEP250
    Synonyms:CEP2, CNAP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:1859. CEP250.

    Subcellular locationi

    Cytoplasmperinuclear region 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication. Cytoplasmcytoskeletoncilium basal body 1 Publication
    Note: Component of the core centrosome. In interphase cells, it specifically associates with the proximal ends of both mother and daughter centrioles. Associates with the centrosome in interphase cells. In mitotic cells, it dissociates from the mitotic spindle poles. At the end of cell division, it reaccumulates at centrosomes. In photoreceptors, found at the proximal ends of basal bodies.

    GO - Cellular componenti

    1. centriole Source: UniProtKB
    2. centrosome Source: UniProtKB
    3. cilium Source: UniProtKB-KW
    4. cytosol Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. microtubule organizing center Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    8. protein complex Source: UniProtKB
    9. spindle pole centrosome Source: Ensembl

    Keywords - Cellular componenti

    Cell projection, Cilium, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26415.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 24422442Centrosome-associated protein CEP250PRO_0000089487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2229 – 22291Phosphoserine1 Publication
    Modified residuei2252 – 22521Phosphoserine1 Publication
    Modified residuei2259 – 22591Phosphoserine1 Publication
    Modified residuei2417 – 24171Phosphoserine; by NEK21 Publication
    Modified residuei2421 – 24211Phosphoserine; by NEK21 Publication

    Post-translational modificationi

    Differentially phosphorylated during cell cycle. Phosphorylation may regulate association/dissociation from centrosome. During M phase of mitosis, C-terminal part is phosphorylated by NEK2, suggesting that it may trigger the dissociation from the mitotic centrosome. Dephosphorylated in vitro by the PP1 phosphatase.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BV73.
    PaxDbiQ9BV73.
    PRIDEiQ9BV73.

    PTM databases

    PhosphoSiteiQ9BV73.

    Expressioni

    Tissue specificityi

    Ubiquitously and weakly expressed.

    Gene expression databases

    ArrayExpressiQ9BV73.
    BgeeiQ9BV73.
    CleanExiHS_CEP250.
    GenevestigatoriQ9BV73.

    Interactioni

    Subunit structurei

    Monomer and homodimer Probable. Interacts with CROCC/rootletin By similarity. Forms a complex in vitro with both NEK2 kinase and the PPP1CC catalytic subunit of protein phosphatase 1 (PP1). Interacts with CEP135.By similarity3 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Axin2O885663EBI-1053100,EBI-7690990From a different organism.
    SIK2Q9H0K15EBI-1053100,EBI-1181664

    Protein-protein interaction databases

    BioGridi116360. 9 interactions.
    IntActiQ9BV73. 9 interactions.
    MINTiMINT-1191144.
    STRINGi9606.ENSP00000348401.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BV73.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili95 – 15864Sequence AnalysisAdd
    BLAST
    Coiled coili244 – 352109Sequence AnalysisAdd
    BLAST
    Coiled coili395 – 1172778Sequence AnalysisAdd
    BLAST
    Coiled coili1243 – 2227985Sequence AnalysisAdd
    BLAST
    Coiled coili2262 – 2376115Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi246 – 2505Poly-Leu
    Compositional biasi464 – 21711708Gln/Glu-richAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000246955.
    HOVERGENiHBG081320.
    InParanoidiQ9BV73.
    KOiK16464.
    OMAiMRLKEQQ.
    OrthoDBiEOG7W6WJX.
    PhylomeDBiQ9BV73.
    TreeFamiTF101138.

    Family and domain databases

    InterProiIPR026048. CEP250.
    [Graphical view]
    PANTHERiPTHR23159:SF1. PTHR23159:SF1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BV73-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ     50
    RQATLVRKLQ AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL 100
    VRLEEEQQRC ESLAEVNTQL RLHMEKADVV NKALREDVEK LTVDWSRARD 150
    ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL WREVVTFRRH FLEMKSATDR 200
    DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG REPAQLLLLL 250
    AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE 300
    DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ 350
    VMVEEGDNIA QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ 400
    AVQDLRQQLA GCQEAVNLLQ QQHDQWEEEG KALRQRLQKL TGERDTLAGQ 450
    TVDLQGEVDS LSKERELLQK AREELRQQLE VLEQEAWRLR RVNVELQLQG 500
    DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS ELITLREALE 550
    SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK 600
    LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA 650
    EKRREALWEK NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR 700
    HQQEAATTQL EQLHQEAKRQ EEVLARAVQE KEALVREKAA LEVRLQAVER 750
    DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN SVIEVTKGQL EVQIQTVTQA 800
    KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG KTALEQQKAA 850
    HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA 900
    IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER 950
    LRQDMKVQKL KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS 1000
    LLQDKMDLQK QVEDLKSQLV AQDDSQRLVE QEVQEKLRET QEYNRIQKEL 1050
    EREKASLTLS LMEKEQRLLV LQEADSIRQQ ELSALRQDMQ EAQGEQKELS 1100
    AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA SLWAQEAKAA 1150
    QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR 1200
    PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ 1250
    DLWKTQQTRD VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE 1300
    KSKWEGKQNS LESELMELHE TMASLQSRLR RAELQRMEAQ GERELLQAAK 1350
    ENLTAQVEHL QAAVVEARAQ ASAAGILEED LRTARSALKL KNEEVESERE 1400
    RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL RGQIQELEKQ 1450
    REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE 1500
    QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK 1550
    QLVTLECLAL ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER 1600
    SQELQAQSSQ IHDLESHSTV LARELQERDQ EVKSQREQIE ELQRQKEHLT 1650
    QDLERRDQEL MLQKERIQVL EDQRTRQTKI LEEDLEQIKL SLRERGRELT 1700
    TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC QQEHIHELQE 1750
    LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS 1800
    LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA 1850
    HMTLKERHGE LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE 1900
    KALLALQQQC AEQAQEHEVE TRALQDSWLQ AQAVLKERDQ ELEALRAESQ 1950
    SSRHQEEAAR ARAEALQEAL GKAHAALQGK EQHLLEQAEL SRSLEASTAT 2000
    LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL QQALAQRDEE 2050
    LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ 2100
    LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR 2150
    ELERLQAALR QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS 2200
    VLERDSEQQR LQDELELTRR ALEKERLHSP GATSTAELGS RGEQGVQLGE 2250
    VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA RLEIDRSRLQ RHNVQLRSTL 2300
    EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG QKNSDAKCVA 2350
    ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ 2400
    APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR 2442
    Length:2,442
    Mass (Da):281,137
    Last modified:May 9, 2003 - v2
    Checksum:iBC2B8A36E07B8272
    GO
    Isoform 2 (identifier: Q9BV73-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         863-918: Missing.

    Show »
    Length:2,386
    Mass (Da):274,380
    Checksum:iCE22E600206C2CE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201L → I in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti136 – 1361E → A in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti365 – 3651H → L in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti372 – 3721D → E in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti509 – 5091E → D in AAC07988. (PubMed:9647649)Curated
    Sequence conflicti552 – 5521S → I in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti757 – 7571E → A in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti784 – 7874EVTK → DEPQ in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti1153 – 11531Q → H in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti1246 – 12461H → L in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti1513 – 15131L → P in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti2082 – 20821Q → L in AAC06349. (PubMed:9506584)Curated
    Sequence conflicti2345 – 23451D → N in AAC06349. (PubMed:9506584)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti995 – 9951Q → H.
    Corresponds to variant rs2296403 [ dbSNP | Ensembl ].
    VAR_015649
    Natural varianti1072 – 10721Q → E.
    Corresponds to variant rs17092706 [ dbSNP | Ensembl ].
    VAR_050898
    Natural varianti1441 – 14411R → Q.
    Corresponds to variant rs3748433 [ dbSNP | Ensembl ].
    VAR_021858

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei863 – 91856Missing in isoform 2. 1 PublicationVSP_007372Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022655 mRNA. Translation: AAC06349.1.
    AF049105 mRNA. Translation: AAC07988.1.
    AL121586 Genomic DNA. Translation: CAB89415.1.
    CH471077 Genomic DNA. Translation: EAW76206.1.
    CH471077 Genomic DNA. Translation: EAW76207.1.
    CCDSiCCDS13255.1. [Q9BV73-1]
    PIRiT08621.
    RefSeqiNP_009117.2. NM_007186.4. [Q9BV73-1]
    XP_005260319.1. XM_005260262.2. [Q9BV73-1]
    XP_006723753.1. XM_006723690.1. [Q9BV73-1]
    XP_006723754.1. XM_006723691.1. [Q9BV73-1]
    XP_006723755.1. XM_006723692.1. [Q9BV73-1]
    XP_006723756.1. XM_006723693.1. [Q9BV73-1]
    XP_006723758.1. XM_006723695.1. [Q9BV73-2]
    UniGeneiHs.443976.

    Genome annotation databases

    EnsembliENST00000397527; ENSP00000380661; ENSG00000126001. [Q9BV73-1]
    GeneIDi11190.
    KEGGihsa:11190.
    UCSCiuc010zve.2. human. [Q9BV73-1]

    Polymorphism databases

    DMDMi30580364.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF022655 mRNA. Translation: AAC06349.1 .
    AF049105 mRNA. Translation: AAC07988.1 .
    AL121586 Genomic DNA. Translation: CAB89415.1 .
    CH471077 Genomic DNA. Translation: EAW76206.1 .
    CH471077 Genomic DNA. Translation: EAW76207.1 .
    CCDSi CCDS13255.1. [Q9BV73-1 ]
    PIRi T08621.
    RefSeqi NP_009117.2. NM_007186.4. [Q9BV73-1 ]
    XP_005260319.1. XM_005260262.2. [Q9BV73-1 ]
    XP_006723753.1. XM_006723690.1. [Q9BV73-1 ]
    XP_006723754.1. XM_006723691.1. [Q9BV73-1 ]
    XP_006723755.1. XM_006723692.1. [Q9BV73-1 ]
    XP_006723756.1. XM_006723693.1. [Q9BV73-1 ]
    XP_006723758.1. XM_006723695.1. [Q9BV73-2 ]
    UniGenei Hs.443976.

    3D structure databases

    ProteinModelPortali Q9BV73.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116360. 9 interactions.
    IntActi Q9BV73. 9 interactions.
    MINTi MINT-1191144.
    STRINGi 9606.ENSP00000348401.

    PTM databases

    PhosphoSitei Q9BV73.

    Polymorphism databases

    DMDMi 30580364.

    Proteomic databases

    MaxQBi Q9BV73.
    PaxDbi Q9BV73.
    PRIDEi Q9BV73.

    Protocols and materials databases

    DNASUi 11190.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397527 ; ENSP00000380661 ; ENSG00000126001 . [Q9BV73-1 ]
    GeneIDi 11190.
    KEGGi hsa:11190.
    UCSCi uc010zve.2. human. [Q9BV73-1 ]

    Organism-specific databases

    CTDi 11190.
    GeneCardsi GC20P034042.
    H-InvDB HIX0015764.
    HGNCi HGNC:1859. CEP250.
    MIMi 609689. gene.
    neXtProti NX_Q9BV73.
    PharmGKBi PA26415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000246955.
    HOVERGENi HBG081320.
    InParanoidi Q9BV73.
    KOi K16464.
    OMAi MRLKEQQ.
    OrthoDBi EOG7W6WJX.
    PhylomeDBi Q9BV73.
    TreeFami TF101138.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    ChiTaRSi CEP250. human.
    GeneWikii CEP250.
    GenomeRNAii 11190.
    NextBioi 42595.
    PROi Q9BV73.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BV73.
    Bgeei Q9BV73.
    CleanExi HS_CEP250.
    Genevestigatori Q9BV73.

    Family and domain databases

    InterProi IPR026048. CEP250.
    [Graphical view ]
    PANTHERi PTHR23159:SF1. PTHR23159:SF1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Autoantibodies to a group of centrosomal proteins in human autoimmune sera reactive with the centrosome."
      Mack G.J., Rees J., Sandblom O., Balczon R., Fritzler M.J., Rattner J.B.
      Arthritis Rheum. 41:551-558(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS AUTOANTIGEN IN AUTOIMMUNE DISEASES.
      Tissue: Cervix carcinoma.
    2. "C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of the cell cycle-regulated protein kinase Nek2."
      Fry A.M., Mayor T., Meraldi P., Stierhof Y.-D., Tanaka K., Nigg E.A.
      J. Cell Biol. 141:1563-1574(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH NEK2, SUBCELLULAR LOCATION DURING THE CELL CYCLE.
      Tissue: Placenta.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "NIMA-related kinase 2 (Nek2), a cell-cycle-regulated protein kinase localized to centrosomes, is complexed to protein phosphatase 1."
      Helps N.R., Luo X., Barker H.M., Cohen P.T.W.
      Biochem. J. 349:509-518(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH NEK2 AND PPP1CA.
    6. "The mechanism regulating the dissociation of the centrosomal protein C-Nap1 from mitotic spindle poles."
      Mayor T., Hacker U., Stierhof Y.-D., Nigg E.A.
      J. Cell Sci. 115:3275-3284(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION DURING CELL CYCLE.
    7. "A novel function of CEP135 as a platform protein of C-NAP1 for its centriolar localization."
      Kim K., Lee S., Chang J., Rhee K.
      Exp. Cell Res. 314:3692-3700(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CEP135.
    8. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2229; SER-2252 AND SER-2259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction."
      Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M., Schiebel E.
      Nat. Cell Biol. 12:1166-1176(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-2417 AND SER-2421.

    Entry informationi

    Entry nameiCP250_HUMAN
    AccessioniPrimary (citable) accession number: Q9BV73
    Secondary accession number(s): E1P5Q3
    , O14812, O60588, Q9H450
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: May 9, 2003
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    Antibodies against CEP2 are present in sera from patients with autoimmune diseases that developed autoantibodies against centrosomal proteins.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3