CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001515
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosomal protein of 152 kDa 
Protein Synonyms/Alias
 Cep152 
Gene Name
 CEP152 
Gene Synonyms/Alias
 KIAA0912 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
413ERNQEAIKLEKTEIIubiquitination[1]
422EKTEIINKLTRSLEEubiquitination[1]
432RSLEESQKQCAHLLQubiquitination[1]
523KVNWKKSKVTSIVQEubiquitination[1]
539DPNEELSKDEFILKLubiquitination[1]
547DEFILKLKAEVQRLLubiquitination[1]
560LLGSNSMKRHLVSQLubiquitination[1]
577DLKDCHKKIEDLHQVubiquitination[1]
596KSIEVETKTDTSEKPubiquitination[1]
644ELKETEGKLRNTNQDubiquitination[1]
686QQHHEAMKTQIRESLubiquitination[1]
701LAKHALEKQQLFEAYubiquitination[1]
740YLEVCREKDNLELTLubiquitination[1]
771KLIQQLEKEWQSKLDubiquitination[1]
776LEKEWQSKLDQTIKAubiquitination[1]
782SKLDQTIKAMKKKTLubiquitination[1]
786QTIKAMKKKTLDCGSubiquitination[1]
787TIKAMKKKTLDCGSQubiquitination[1]
807TSDVISKKEMAIMIEubiquitination[1]
828QQNLEQEKDIAIKGAubiquitination[1]
833QEKDIAIKGAMKKLEubiquitination[1]
853KHCENITKQVEIAVQubiquitination[1]
881AEYQALVKAEQKKWEubiquitination[1]
897QHEVSVNKRISFAVSubiquitination[1]
907SFAVSEAKEKWKSELubiquitination[1]
909AVSEAKEKWKSELENubiquitination[1]
919SELENMRKNILPGKEubiquitination[1]
925RKNILPGKELEEKIHubiquitination[1]
930PGKELEEKIHSLQKEubiquitination[1]
936EKIHSLQKELELKNEubiquitination[1, 2]
941LQKELELKNEEVPVVubiquitination[1]
989FLDDHRNKINEVLAAubiquitination[1]
998NEVLAAAKEDFMKQKubiquitination[1, 3]
1005KEDFMKQKTELLLQKubiquitination[1]
1012KTELLLQKETELQTCubiquitination[1]
1033EWTMQEAKRIQLEIYubiquitination[1]
1068HISDSEDKQLLEIMSubiquitination[1]
1089MSVQYFEKLKGCIQKubiquitination[1]
1114ENADPEWKKRNMAELubiquitination[1, 3]
1115NADPEWKKRNMAELSubiquitination[1, 2]
1157ATEAEADKKKVLEIKubiquitination[1]
1158TEAEADKKKVLEIKDubiquitination[1]
1159EAEADKKKVLEIKDLubiquitination[1]
1164KKKVLEIKDLCCGHCubiquitination[1]
1240EELQTLCKTPPRSLSubiquitination[1, 2]
1272ELRGQYIKAVKKIKCacetylation[4]
1272ELRGQYIKAVKKIKCubiquitination[1]
1276QYIKAVKKIKCDMLRacetylation[4]
1278IKAVKKIKCDMLRYIacetylation[4]
1278IKAVKKIKCDMLRYIubiquitination[1]
1297ERAAEMVKAEVLRERubiquitination[1, 2]
1333DGKEGAEKKIMNAASubiquitination[1]
1334GKEGAEKKIMNAASKubiquitination[1]
1341KIMNAASKLATMAKLubiquitination[1]
1347SKLATMAKLLETPISubiquitination[1]
1356LETPISSKSQSKTTQubiquitination[1]
1360ISSKSQSKTTQSALPubiquitination[1]
1377SEMLIAVKKSKRNDVubiquitination[3]
1387KRNDVNQKIPCCIESubiquitination[1, 2]
1395IPCCIESKSNSVNTIubiquitination[1, 2, 3]
1412TLCEQAPKRRAACNLubiquitination[1]
1432NSEHQSIKHVGSKETubiquitination[1, 2]
1437SIKHVGSKETHLEFQubiquitination[1]
1451QFGDGSCKHLNSLPRubiquitination[1]
1478GGFGLHKKKDLLSDNubiquitination[1]
1479GFGLHKKKDLLSDNGubiquitination[1]
1505FLGTLGNKPSPRCTPubiquitination[1]
1534SNERLGLKVYKCNPLubiquitination[1, 2]
1537RLGLKVYKCNPLMESubiquitination[1]
1607EIPSESVKSKQFSPSubiquitination[1]
1609PSESVKSKQFSPSGYubiquitination[1]
1631NMICQTMKCQRYQTPubiquitination[1]
1651TTYLEPGKISVNCGHubiquitination[1]
1673RLKSDFKKLSSTLPSubiquitination[1, 2]
1689VCQQPSRKLIVPLSSubiquitination[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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Regulator of genomic integrity and cellular response to DNA damage acting through ATR-mediated checkpoint signaling. Necessary for centrosome duplication. It functions as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, two molecules involved in centriole formation. 
Sequence Annotation
  
Keyword
 Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Dwarfism; Mental retardation; Polymorphism; Primary microcephaly; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1710 AA 
Protein Sequence
MSLDFGSVAL PVQNEDEEYD EEDYEREKEL QQLLTDLPHD MLDDDLSSPE LQYSDCSEDG 60
TDGQPHHPEQ LEMSWNEQML PKSQSVNGYN EIQSLYAGEK CGNVWEENRS KTEDRHPVYH 120
PEEGGDEGGS GYSPPSKCEQ TDLYHLPENF RPYTNGQKQE FNNQATNVIK FSDPQWNHFQ 180
GPSCQGLEPY NKVTYKPYQS SAQNNGSPAQ EITGSDTFEG LQQQFLGANE NSAENMQIIQ 240
LQVLNKAKER QLENLIEKLN ESERQIRYLN HQLVIIKDEK DGLTLSLRES QKLFQNGKER 300
EIQLEAQIKA LETQIQALKV NEEQMIKKSR TTEMALESLK QQLVDLHHSE SLQRAREQHE 360
SIVMGLTKKY EEQVLSLQKN LDATVTALKE QEDICSRLKD HVKQLERNQE AIKLEKTEII 420
NKLTRSLEES QKQCAHLLQS GSVQEVAQLQ FQLQQAQKAH AMSANMNKAL QEELTELKDE 480
ISLYESAAKL GIHPSDSEGE LNIELTESYV DLGIKKVNWK KSKVTSIVQE EDPNEELSKD 540
EFILKLKAEV QRLLGSNSMK RHLVSQLQND LKDCHKKIED LHQVKKDEKS IEVETKTDTS 600
EKPKNQLWPE SSTSDVVRDD ILLLKNEIQV LQQQNQELKE TEGKLRNTNQ DLCNQMRQMV 660
QDFDHDKQEA VDRCERTYQQ HHEAMKTQIR ESLLAKHALE KQQLFEAYER THLQLRSELD 720
KLNKEVTAVQ ECYLEVCREK DNLELTLRKT TEKEQQTQEK IKEKLIQQLE KEWQSKLDQT 780
IKAMKKKTLD CGSQTDQVTT SDVISKKEMA IMIEEQKCTI QQNLEQEKDI AIKGAMKKLE 840
IELELKHCEN ITKQVEIAVQ NAHQRWLGEL PELAEYQALV KAEQKKWEEQ HEVSVNKRIS 900
FAVSEAKEKW KSELENMRKN ILPGKELEEK IHSLQKELEL KNEEVPVVIR AELAKARSEW 960
NKEKQEEIHR IQEQNEQDYR QFLDDHRNKI NEVLAAAKED FMKQKTELLL QKETELQTCL 1020
DQSRREWTMQ EAKRIQLEIY QYEEDILTVL GVLLSDTQKE HISDSEDKQL LEIMSTCSSK 1080
WMSVQYFEKL KGCIQKAFQD TLPLLVENAD PEWKKRNMAE LSKDSASQGT GQGDPGPAAG 1140
HHAQPLALQA TEAEADKKKV LEIKDLCCGH CFQELEKAKQ ECQDLKGKLE KCCRHLQHLE 1200
RKHKAVVEKI GEENNKVVEE LIEENNDMKN KLEELQTLCK TPPRSLSAGA IENACLPCSG 1260
GALEELRGQY IKAVKKIKCD MLRYIQESKE RAAEMVKAEV LRERQETARK MRKYYLICLQ 1320
QILQDDGKEG AEKKIMNAAS KLATMAKLLE TPISSKSQSK TTQSALPLTS EMLIAVKKSK 1380
RNDVNQKIPC CIESKSNSVN TITRTLCEQA PKRRAACNLQ RLLENSEHQS IKHVGSKETH 1440
LEFQFGDGSC KHLNSLPRNV SPEFVPCEGE GGFGLHKKKD LLSDNGSESL PHSAAYPFLG 1500
TLGNKPSPRC TPGPSESGCM HITFRDSNER LGLKVYKCNP LMESENAASE KSQGLDVQEP 1560
PVKDGGDLSD CLGWPSSSAT LSFDSREASF VHGRPQGTLE IPSESVKSKQ FSPSGYLSDT 1620
EESNMICQTM KCQRYQTPYL SEETTYLEPG KISVNCGHPS RHKADRLKSD FKKLSSTLPS 1680
SVCQQPSRKL IVPLSSQQDS GFDSPFVNLD 1710 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0051298; P:centrosome duplication; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS