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Q9BV73

- CP250_HUMAN

UniProt

Q9BV73 - CP250_HUMAN

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Protein
Centrosome-associated protein CEP250
Gene
CEP250, CEP2, CNAP1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Probably plays an important role in centrosome cohesion during interphase.

GO - Molecular functioni

  1. protein C-terminus binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

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

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. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole. Cytoplasmcytoskeletoncilium basal body
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.1 Publication

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
Complete GO annotation...

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 CEP250
PRO_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.3 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 Inferred. 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 CEP135.3 Publications

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.

Family & Domainsi

Coiled coil

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

Compositional bias

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

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.
VSP_007372Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201L → I in AAC06349. 1 Publication
Sequence conflicti136 – 1361E → A in AAC06349. 1 Publication
Sequence conflicti365 – 3651H → L in AAC06349. 1 Publication
Sequence conflicti372 – 3721D → E in AAC06349. 1 Publication
Sequence conflicti509 – 5091E → D in AAC07988. 1 Publication
Sequence conflicti552 – 5521S → I in AAC06349. 1 Publication
Sequence conflicti757 – 7571E → A in AAC06349. 1 Publication
Sequence conflicti784 – 7874EVTK → DEPQ in AAC06349. 1 Publication
Sequence conflicti1153 – 11531Q → H in AAC06349. 1 Publication
Sequence conflicti1246 – 12461H → L in AAC06349. 1 Publication
Sequence conflicti1513 – 15131L → P in AAC06349. 1 Publication
Sequence conflicti2082 – 20821Q → L in AAC06349. 1 Publication
Sequence conflicti2345 – 23451D → N in AAC06349. 1 Publication

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

EnsembliENST00000342580; ENSP00000341541; ENSG00000126001. [Q9BV73-2]
ENST00000397527; 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...

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 ENST00000342580 ; ENSP00000341541 ; ENSG00000126001 . [Q9BV73-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

Similar proteinsi