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Q9BV73 (CP250_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CEP250
Synonyms:CEP2, CNAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2442 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably plays an important role in centrosome cohesion during interphase.

Subunit structure

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. Ref.2 Ref.5 Ref.7

Subcellular location

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. Ref.2

Tissue specificity

Ubiquitously and weakly expressed.

Post-translational modification

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. Ref.5 Ref.6 Ref.9

Miscellaneous

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

Ontologies

Keywords
   Biological processCell cycle
   Cellular componentCell projection
Cilium
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

centriole-centriole cohesion

Inferred from mutant phenotype PubMed 11076968Ref.7. Source: UniProtKB

mitotic cell cycle

Inferred from direct assay Ref.6. Source: UniProtKB

protein localization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of centriole-centriole cohesion

Inferred from direct assay Ref.2. Source: UniProtKB

   Cellular_componentcentriole

Inferred from direct assay Ref.7. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614Ref.2. Source: UniProtKB

cilium

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microtubule organizing center

Non-traceable author statement Ref.2. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from mutant phenotype Ref.5. Source: UniProtKB

spindle pole centrosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein C-terminus binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Axin2O885663EBI-1053100,EBI-7690990From a different organism.
SIK2Q9H0K15EBI-1053100,EBI-1181664

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BV73-1)

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: Q9BV73-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 24422442Centrosome-associated protein CEP250
PRO_0000089487

Regions

Coiled coil95 – 15864 Potential
Coiled coil244 – 352109 Potential
Coiled coil395 – 1172778 Potential
Coiled coil1243 – 2227985 Potential
Coiled coil2262 – 2376115 Potential
Compositional bias246 – 2505Poly-Leu
Compositional bias464 – 21711708Gln/Glu-rich

Amino acid modifications

Modified residue22291Phosphoserine Ref.8
Modified residue22521Phosphoserine Ref.8
Modified residue22591Phosphoserine Ref.8
Modified residue24171Phosphoserine; by NEK2 Ref.9
Modified residue24211Phosphoserine; by NEK2 Ref.9

Natural variations

Alternative sequence863 – 91856Missing in isoform 2.
VSP_007372
Natural variant9951Q → H.
Corresponds to variant rs2296403 [ dbSNP | Ensembl ].
VAR_015649
Natural variant10721Q → E.
Corresponds to variant rs17092706 [ dbSNP | Ensembl ].
VAR_050898
Natural variant14411R → Q.
Corresponds to variant rs3748433 [ dbSNP | Ensembl ].
VAR_021858

Experimental info

Sequence conflict1201L → I in AAC06349. Ref.1
Sequence conflict1361E → A in AAC06349. Ref.1
Sequence conflict3651H → L in AAC06349. Ref.1
Sequence conflict3721D → E in AAC06349. Ref.1
Sequence conflict5091E → D in AAC07988. Ref.2
Sequence conflict5521S → I in AAC06349. Ref.1
Sequence conflict7571E → A in AAC06349. Ref.1
Sequence conflict784 – 7874EVTK → DEPQ in AAC06349. Ref.1
Sequence conflict11531Q → H in AAC06349. Ref.1
Sequence conflict12461H → L in AAC06349. Ref.1
Sequence conflict15131L → P in AAC06349. Ref.1
Sequence conflict20821Q → L in AAC06349. Ref.1
Sequence conflict23451D → N in AAC06349. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 9, 2003. Version 2.
Checksum: BC2B8A36E07B8272

FASTA2,442281,137
        10         20         30         40         50         60 
METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ 

        70         80         90        100        110        120 
AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL 

       130        140        150        160        170        180 
RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL 

       190        200        210        220        230        240 
WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG 

       250        260        270        280        290        300 
REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE 

       310        320        330        340        350        360 
DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA 

       370        380        390        400        410        420 
QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ 

       430        440        450        460        470        480 
QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE 

       490        500        510        520        530        540 
VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS 

       550        560        570        580        590        600 
ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK 

       610        620        630        640        650        660 
LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK 

       670        680        690        700        710        720 
NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ 

       730        740        750        760        770        780 
EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN 

       790        800        810        820        830        840 
SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG 

       850        860        870        880        890        900 
KTALEQQKAA HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA 

       910        920        930        940        950        960 
IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER LRQDMKVQKL 

       970        980        990       1000       1010       1020 
KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS LLQDKMDLQK QVEDLKSQLV 

      1030       1040       1050       1060       1070       1080 
AQDDSQRLVE QEVQEKLRET QEYNRIQKEL EREKASLTLS LMEKEQRLLV LQEADSIRQQ 

      1090       1100       1110       1120       1130       1140 
ELSALRQDMQ EAQGEQKELS AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA 

      1150       1160       1170       1180       1190       1200 
SLWAQEAKAA QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR 

      1210       1220       1230       1240       1250       1260 
PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ DLWKTQQTRD 

      1270       1280       1290       1300       1310       1320 
VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE KSKWEGKQNS LESELMELHE 

      1330       1340       1350       1360       1370       1380 
TMASLQSRLR RAELQRMEAQ GERELLQAAK ENLTAQVEHL QAAVVEARAQ ASAAGILEED 

      1390       1400       1410       1420       1430       1440 
LRTARSALKL KNEEVESERE RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL 

      1450       1460       1470       1480       1490       1500 
RGQIQELEKQ REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE 

      1510       1520       1530       1540       1550       1560 
QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK QLVTLECLAL 

      1570       1580       1590       1600       1610       1620 
ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER SQELQAQSSQ IHDLESHSTV 

      1630       1640       1650       1660       1670       1680 
LARELQERDQ EVKSQREQIE ELQRQKEHLT QDLERRDQEL MLQKERIQVL EDQRTRQTKI 

      1690       1700       1710       1720       1730       1740 
LEEDLEQIKL SLRERGRELT TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC 

      1750       1760       1770       1780       1790       1800 
QQEHIHELQE LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS 

      1810       1820       1830       1840       1850       1860 
LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA HMTLKERHGE 

      1870       1880       1890       1900       1910       1920 
LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE KALLALQQQC AEQAQEHEVE 

      1930       1940       1950       1960       1970       1980 
TRALQDSWLQ AQAVLKERDQ ELEALRAESQ SSRHQEEAAR ARAEALQEAL GKAHAALQGK 

      1990       2000       2010       2020       2030       2040 
EQHLLEQAEL SRSLEASTAT LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL 

      2050       2060       2070       2080       2090       2100 
QQALAQRDEE LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ 

      2110       2120       2130       2140       2150       2160 
LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR ELERLQAALR 

      2170       2180       2190       2200       2210       2220 
QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS VLERDSEQQR LQDELELTRR 

      2230       2240       2250       2260       2270       2280 
ALEKERLHSP GATSTAELGS RGEQGVQLGE VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA 

      2290       2300       2310       2320       2330       2340 
RLEIDRSRLQ RHNVQLRSTL EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG 

      2350       2360       2370       2380       2390       2400 
QKNSDAKCVA ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ 

      2410       2420       2430       2440 
APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR 

« Hide

Isoform 2 [UniParc].

Checksum: CE22E600206C2CE8
Show »

FASTA2,386274,380

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13255.1. [Q9BV73-1]
PIRT08621.
RefSeqNP_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]
UniGeneHs.443976.

3D structure databases

ProteinModelPortalQ9BV73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116360. 9 interactions.
IntActQ9BV73. 9 interactions.
MINTMINT-1191144.
STRING9606.ENSP00000348401.

PTM databases

PhosphoSiteQ9BV73.

Polymorphism databases

DMDM30580364.

Proteomic databases

MaxQBQ9BV73.
PaxDbQ9BV73.
PRIDEQ9BV73.

Protocols and materials databases

DNASU11190.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342580; ENSP00000341541; ENSG00000126001. [Q9BV73-2]
ENST00000397527; ENSP00000380661; ENSG00000126001. [Q9BV73-1]
GeneID11190.
KEGGhsa:11190.
UCSCuc010zve.2. human. [Q9BV73-1]

Organism-specific databases

CTD11190.
GeneCardsGC20P034042.
H-InvDBHIX0015764.
HGNCHGNC:1859. CEP250.
MIM609689. gene.
neXtProtNX_Q9BV73.
PharmGKBPA26415.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000246955.
HOVERGENHBG081320.
InParanoidQ9BV73.
KOK16464.
OMAMRLKEQQ.
OrthoDBEOG7W6WJX.
PhylomeDBQ9BV73.
TreeFamTF101138.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ9BV73.
BgeeQ9BV73.
CleanExHS_CEP250.
GenevestigatorQ9BV73.

Family and domain databases

InterProIPR026048. CEP250.
[Graphical view]
PANTHERPTHR23159:SF1. PTHR23159:SF1. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCEP250. human.
GeneWikiCEP250.
GenomeRNAi11190.
NextBio42595.
PROQ9BV73.
SOURCESearch...

Entry information

Entry nameCP250_HUMAN
AccessionPrimary (citable) accession number: Q9BV73
Secondary accession number(s): E1P5Q3 expand/collapse secondary AC list , O14812, O60588, Q9H450
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: May 9, 2003
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM