CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020226
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosome-associated protein CEP250 
Protein Synonyms/Alias
 250 kDa centrosomal protein; Cep250; Centrosomal Nek2-associated protein 1; C-Nap1; Centrosomal protein 2 
Gene Name
 CEP250 
Gene Synonyms/Alias
 CEP2; CNAP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
62LVRKLQAKVLQYRSWubiquitination[1]
75SWCQELEKRLEATGGubiquitination[1]
126QLRLHMEKADVVNKAubiquitination[1]
155ARDELMRKESQWQMEubiquitination[1]
206DRDLMELKAEHVRLSubiquitination[1]
252QLLLLLAKTQELEKEubiquitination[1]
1036VEQEVQEKLRETQEYubiquitination[1]
1048QEYNRIQKELEREKAacetylation[2, 3]
1048QEYNRIQKELEREKAubiquitination[4, 5]
1148SLWAQEAKAAQLQLRubiquitination[1, 4, 5, 6, 7]
1254KLHQDLWKTQQTRDVubiquitination[1]
1268VLRDQVQKLEERLTDubiquitination[1]
1280LTDTEAEKSQVHTELubiquitination[1]
1467LLSLDLKKRNQEVDLubiquitination[1]
1574HKMECQQKLIKELEGubiquitination[1]
1577ECQQKLIKELEGQREubiquitination[1, 4, 5, 7]
1679DQRTRQTKILEEDLEubiquitination[1]
2063EREQLLEKSLAQRVQubiquitination[1]
2265PSPDGMEKQSWRQRLubiquitination[1]
2327AGSLEISKATASSPTubiquitination[1]
2347GQKNSDAKCVAELQKubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Probably plays an important role in centrosome cohesion during interphase. 
Sequence Annotation
 MOD_RES 2229 2229 Phosphoserine.
 MOD_RES 2252 2252 Phosphoserine.
 MOD_RES 2259 2259 Phosphoserine.
 MOD_RES 2417 2417 Phosphoserine; by NEK2.
 MOD_RES 2421 2421 Phosphoserine; by NEK2.  
Keyword
 Alternative splicing; Cell cycle; Cell projection; Cilium; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2442 AA 
Protein Sequence
METRSPGLNN MKPQSLQLVL EEQVLALQQQ MAENQAASWR KLKNSQEAQQ RQATLVRKLQ 60
AKVLQYRSWC QELEKRLEAT GGPIPQRWEN VEEPNLDELL VRLEEEQQRC ESLAEVNTQL 120
RLHMEKADVV NKALREDVEK LTVDWSRARD ELMRKESQWQ MEQEFFKGYL KGEHGRLLSL 180
WREVVTFRRH FLEMKSATDR DLMELKAEHV RLSGSLLTCC LRLTVGAQSR EPNGSGRMDG 240
REPAQLLLLL AKTQELEKEA HERSQELIQL KSQGDLEKAE LQDRVTELSA LLTQSQKQNE 300
DYEKMIKALR ETVEILETNH TELMEHEASL SRNAQEEKLS LQQVIKDITQ VMVEEGDNIA 360
QGSGHENSLE LDSSIFSQFD YQDADKALTL VRSVLTRRRQ AVQDLRQQLA GCQEAVNLLQ 420
QQHDQWEEEG KALRQRLQKL TGERDTLAGQ TVDLQGEVDS LSKERELLQK AREELRQQLE 480
VLEQEAWRLR RVNVELQLQG DSAQGQKEEQ QEELHLAVRE RERLQEMLMG LEAKQSESLS 540
ELITLREALE SSHLEGELLR QEQTEVTAAL ARAEQSIAEL SSSENTLKTE VADLRAAAVK 600
LSALNEALAL DKVGLNQQLL QLEEENQSVC SRMEAAEQAR NALQVDLAEA EKRREALWEK 660
NTHLEAQLQK AEEAGAELQA DLRDIQEEKE EIQKKLSESR HQQEAATTQL EQLHQEAKRQ 720
EEVLARAVQE KEALVREKAA LEVRLQAVER DRQDLAEQLQ GLSSAKELLE SSLFEAQQQN 780
SVIEVTKGQL EVQIQTVTQA KEVIQGEVRC LKLELDTERS QAEQERDAAA RQLAQAEQEG 840
KTALEQQKAA HEKEVNQLRE KWEKERSWHQ QELAKALESL EREKMELEMR LKEQQTEMEA 900
IQAQREEERT QAESALCQMQ LETEKERVSL LETLLQTQKE LADASQQLER LRQDMKVQKL 960
KEQETTGILQ TQLQEAQREL KEAARQHRDD LAALQEESSS LLQDKMDLQK QVEDLKSQLV 1020
AQDDSQRLVE QEVQEKLRET QEYNRIQKEL EREKASLTLS LMEKEQRLLV LQEADSIRQQ 1080
ELSALRQDMQ EAQGEQKELS AQMELLRQEV KEKEADFLAQ EAQLLEELEA SHITEQQLRA 1140
SLWAQEAKAA QLQLRLRSTE SQLEALAAEQ QPGNQAQAQA QLASLYSALQ QALGSVCESR 1200
PELSGGGDSA PSVWGLEPDQ NGARSLFKRG PLLTALSAEA VASALHKLHQ DLWKTQQTRD 1260
VLRDQVQKLE ERLTDTEAEK SQVHTELQDL QRQLSQNQEE KSKWEGKQNS LESELMELHE 1320
TMASLQSRLR RAELQRMEAQ GERELLQAAK ENLTAQVEHL QAAVVEARAQ ASAAGILEED 1380
LRTARSALKL KNEEVESERE RAQALQEQGE LKVAQGKALQ ENLALLTQTL AEREEEVETL 1440
RGQIQELEKQ REMQKAALEL LSLDLKKRNQ EVDLQQEQIQ ELEKCRSVLE HLPMAVQERE 1500
QKLTVQREQI RELEKDRETQ RNVLEHQLLE LEKKDQMIES QRGQVQDLKK QLVTLECLAL 1560
ELEENHHKME CQQKLIKELE GQRETQRVAL THLTLDLEER SQELQAQSSQ IHDLESHSTV 1620
LARELQERDQ EVKSQREQIE ELQRQKEHLT QDLERRDQEL MLQKERIQVL EDQRTRQTKI 1680
LEEDLEQIKL SLRERGRELT TQRQLMQERA EEGKGPSKAQ RGSLEHMKLI LRDKEKEVEC 1740
QQEHIHELQE LKDQLEQQLQ GLHRKVGETS LLLSQREQEI VVLQQQLQEA REQGELKEQS 1800
LQSQLDEAQR ALAQRDQELE ALQQEQQQAQ GQEERVKEKA DALQGALEQA HMTLKERHGE 1860
LQDHKEQARR LEEELAVEGR RVQALEEVLG DLRAESREQE KALLALQQQC AEQAQEHEVE 1920
TRALQDSWLQ AQAVLKERDQ ELEALRAESQ SSRHQEEAAR ARAEALQEAL GKAHAALQGK 1980
EQHLLEQAEL SRSLEASTAT LQASLDACQA HSRQLEEALR IQEGEIQDQD LRYQEDVQQL 2040
QQALAQRDEE LRHQQEREQL LEKSLAQRVQ ENMIQEKQNL GQEREEEEIR GLHQSVRELQ 2100
LTLAQKEQEI LELRETQQRN NLEALPHSHK TSPMEEQSLK LDSLEPRLQR ELERLQAALR 2160
QTEAREIEWR EKAQDLALSL AQTKASVSSL QEVAMFLQAS VLERDSEQQR LQDELELTRR 2220
ALEKERLHSP GATSTAELGS RGEQGVQLGE VSGVEAEPSP DGMEKQSWRQ RLEHLQQAVA 2280
RLEIDRSRLQ RHNVQLRSTL EQVERERRKL KREAMRAAQA GSLEISKATA SSPTQQDGRG 2340
QKNSDAKCVA ELQKEVVLLQ AQLTLERKQK QDYITRSAQT SRELAGLHHS LSHSLLAVAQ 2400
APEATVLEAE TRRLDESLTQ SLTSPGPVLL HPSPSTTQAA SR 2442 
Gene Ontology
 GO:0005814; C:centriole; IDA:UniProtKB.
 GO:0005929; C:cilium; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0043234; C:protein complex; IMP:UniProtKB.
 GO:0031616; C:spindle pole centrosome; IEA:Compara.
 GO:0010457; P:centriole-centriole cohesion; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0008104; P:protein localization; IMP:UniProtKB.
 GO:0030997; P:regulation of centriole-centriole cohesion; IDA:UniProtKB. 
Interpro
 IPR026048; CEP250. 
Pfam
  
SMART
  
PROSITE
  
PRINTS