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Q9BV73

- CP250_HUMAN

UniProt

Q9BV73 - CP250_HUMAN

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Protein

Centrosome-associated protein CEP250

Gene

CEP250

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 domain specific binding Source: UniProtKB
  3. 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
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 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. protein complex Source: UniProtKB
  8. 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 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

BgeeiQ9BV73.
CleanExiHS_CEP250.
ExpressionAtlasiQ9BV73. baseline and differential.
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. 229 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.
GeneTreeiENSGT00730000110800.
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

        10         20         30         40         50
METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ
60 70 80 90 100
RQATLVRKLQ AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL
110 120 130 140 150
VRLEEEQQRC ESLAEVNTQL RLHMEKADVV NKALREDVEK LTVDWSRARD
160 170 180 190 200
ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL WREVVTFRRH FLEMKSATDR
210 220 230 240 250
DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG REPAQLLLLL
260 270 280 290 300
AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE
310 320 330 340 350
DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ
360 370 380 390 400
VMVEEGDNIA QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ
410 420 430 440 450
AVQDLRQQLA GCQEAVNLLQ QQHDQWEEEG KALRQRLQKL TGERDTLAGQ
460 470 480 490 500
TVDLQGEVDS LSKERELLQK AREELRQQLE VLEQEAWRLR RVNVELQLQG
510 520 530 540 550
DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS ELITLREALE
560 570 580 590 600
SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK
610 620 630 640 650
LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA
660 670 680 690 700
EKRREALWEK NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR
710 720 730 740 750
HQQEAATTQL EQLHQEAKRQ EEVLARAVQE KEALVREKAA LEVRLQAVER
760 770 780 790 800
DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN SVIEVTKGQL EVQIQTVTQA
810 820 830 840 850
KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG KTALEQQKAA
860 870 880 890 900
HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA
910 920 930 940 950
IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER
960 970 980 990 1000
LRQDMKVQKL KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS
1010 1020 1030 1040 1050
LLQDKMDLQK QVEDLKSQLV AQDDSQRLVE QEVQEKLRET QEYNRIQKEL
1060 1070 1080 1090 1100
EREKASLTLS LMEKEQRLLV LQEADSIRQQ ELSALRQDMQ EAQGEQKELS
1110 1120 1130 1140 1150
AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA SLWAQEAKAA
1160 1170 1180 1190 1200
QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR
1210 1220 1230 1240 1250
PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ
1260 1270 1280 1290 1300
DLWKTQQTRD VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE
1310 1320 1330 1340 1350
KSKWEGKQNS LESELMELHE TMASLQSRLR RAELQRMEAQ GERELLQAAK
1360 1370 1380 1390 1400
ENLTAQVEHL QAAVVEARAQ ASAAGILEED LRTARSALKL KNEEVESERE
1410 1420 1430 1440 1450
RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL RGQIQELEKQ
1460 1470 1480 1490 1500
REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE
1510 1520 1530 1540 1550
QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK
1560 1570 1580 1590 1600
QLVTLECLAL ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER
1610 1620 1630 1640 1650
SQELQAQSSQ IHDLESHSTV LARELQERDQ EVKSQREQIE ELQRQKEHLT
1660 1670 1680 1690 1700
QDLERRDQEL MLQKERIQVL EDQRTRQTKI LEEDLEQIKL SLRERGRELT
1710 1720 1730 1740 1750
TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC QQEHIHELQE
1760 1770 1780 1790 1800
LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS
1810 1820 1830 1840 1850
LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA
1860 1870 1880 1890 1900
HMTLKERHGE LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE
1910 1920 1930 1940 1950
KALLALQQQC AEQAQEHEVE TRALQDSWLQ AQAVLKERDQ ELEALRAESQ
1960 1970 1980 1990 2000
SSRHQEEAAR ARAEALQEAL GKAHAALQGK EQHLLEQAEL SRSLEASTAT
2010 2020 2030 2040 2050
LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL QQALAQRDEE
2060 2070 2080 2090 2100
LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ
2110 2120 2130 2140 2150
LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR
2160 2170 2180 2190 2200
ELERLQAALR QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS
2210 2220 2230 2240 2250
VLERDSEQQR LQDELELTRR ALEKERLHSP GATSTAELGS RGEQGVQLGE
2260 2270 2280 2290 2300
VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA RLEIDRSRLQ RHNVQLRSTL
2310 2320 2330 2340 2350
EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG QKNSDAKCVA
2360 2370 2380 2390 2400
ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ
2410 2420 2430 2440
APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 229 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.
GeneTreei ENSGT00730000110800.
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

Bgeei Q9BV73.
CleanExi HS_CEP250.
ExpressionAtlasi Q9BV73. baseline and differential.
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: October 29, 2014
This is version 119 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