CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012509
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pericentriolar material 1 protein 
Protein Synonyms/Alias
 PCM-1; hPCM-1 
Gene Name
 PCM1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
51SSEKNKKKFGVESDKubiquitination[1, 2]
58KFGVESDKRVTNDISubiquitination[2]
78GVGRRRTKTPHTFPHubiquitination[2]
102PEQAELEKLKQRINFubiquitination[1, 2]
104QAELEKLKQRINFSDubiquitination[1, 2]
139RQLSENRKPFNFLPMubiquitination[1, 2]
152PMQINTNKSKDASTSubiquitination[1, 2]
154QINTNKSKDASTSPPubiquitination[2]
218QIRDYITKASSMREDubiquitination[1, 2]
229MREDLVEKNERSANVubiquitination[2]
247THLIDHLKEQEKSYMubiquitination[2]
251DHLKEQEKSYMKFLKubiquitination[2]
255EQEKSYMKFLKKILAubiquitination[1, 2]
258KSYMKFLKKILARDPubiquitination[2]
259SYMKFLKKILARDPQubiquitination[2]
277MEEIENLKKQHDLLKubiquitination[2, 3]
278EEIENLKKQHDLLKRubiquitination[2]
382REVSQSRKPSASERLubiquitination[2, 3]
393SERLPDEKVELFSKMubiquitination[1, 2, 3, 4]
399EKVELFSKMRVLQEKacetylation[5]
399EKVELFSKMRVLQEKubiquitination[1, 2]
409VLQEKKQKMDKLLGEubiquitination[1, 2]
412EKKQKMDKLLGELHTubiquitination[1, 2]
492NPSEKLQKLNEVRKRubiquitination[1, 2, 3]
658EDAEFEQKINRLMAAubiquitination[1, 2]
733VNEKAREKFYEAKLQubiquitination[1, 2]
738REKFYEAKLQQQQREubiquitination[1, 2, 3]
747QQQQRELKQLQEERKubiquitination[2]
754KQLQEERKKLIDIQEubiquitination[2]
755QLQEERKKLIDIQEKubiquitination[2]
762KLIDIQEKIQALQTAubiquitination[2, 3]
786SVGNCPTKKYMPAVTubiquitination[2, 3]
787VGNCPTKKYMPAVTSubiquitination[1, 2, 3]
807QHETSTSKSVFEPEDubiquitination[2]
841EELRQRRKQLEALMAubiquitination[1, 2, 3]
954KETKNRWKNNCPFSAubiquitination[1, 2]
970ENYRPLAKTRQQNISubiquitination[1, 2, 3]
996ELSYVEEKEQWQEQIubiquitination[2]
1007QEQINQLKKQLDFSVubiquitination[1, 2]
1076QNNVQRLKQMLNELMubiquitination[1, 2, 4, 6]
1181TEYMAFPKPFESSSSubiquitination[1, 2, 4]
1193SSSIGAEKPRNKKLPubiquitination[2, 4]
1197GAEKPRNKKLPEEEVubiquitination[2, 3]
1198AEKPRNKKLPEEEVEubiquitination[2, 3]
1221EQEGEVEKPFIKTGFubiquitination[1, 2]
1234GFSVSVEKSTSSNRKubiquitination[2]
1275VDPTTVTKTFKTRKAubiquitination[2]
1291AQASLASKDKTPKSKubiquitination[2]
1296ASKDKTPKSKSKKRNubiquitination[2]
1329SSTCEPCKSRNRHSAubiquitination[2]
1345TEEPVQAKVFSRKNHubiquitination[1, 2, 3]
1357KNHEQLEKIIKCNRSubiquitination[2]
1531MREYERMKTEAESNSubiquitination[2]
1602RQIKAIMKEVIPFLKubiquitination[1, 2]
1609KEVIPFLKEHMDEVCubiquitination[2]
1639TQQNDESKEFVKFFHubiquitination[2]
1643DESKEFVKFFHKQLGubiquitination[2]
1647EFVKFFHKQLGSILQubiquitination[1, 2]
1659ILQDSLAKFAGRKLKubiquitination[1, 2]
1701DNNSITVKQRCKRKIubiquitination[1, 2, 3]
1707VKQRCKRKIEATGVIubiquitination[2]
1850FKKTAESKNVPLEREubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] 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]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Required for centrosome assembly and function. Essential for the correct localization of several centrosomal proteins including CEP250, CETN3, PCNT and NEK2. Required to anchor microtubules to the centrosome. Involved in the biogenesis of cilia. 
Sequence Annotation
 REGION 1279 1799 Interaction with HAP1.
 REGION 1913 2024 Interaction with BBS4.
 MOD_RES 65 65 Phosphoserine.
 MOD_RES 68 68 Phosphoserine.
 MOD_RES 69 69 Phosphoserine.
 MOD_RES 93 93 Phosphoserine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 399 399 N6-acetyllysine.
 MOD_RES 431 431 Phosphoserine.
 MOD_RES 861 861 Phosphoserine.
 MOD_RES 866 866 Phosphoserine (By similarity).
 MOD_RES 960 960 Phosphoserine.
 MOD_RES 1185 1185 Phosphoserine.
 MOD_RES 1231 1231 Phosphoserine.
 MOD_RES 1257 1257 Phosphoserine.
 MOD_RES 1260 1260 Phosphoserine.
 MOD_RES 1263 1263 Phosphoserine.
 MOD_RES 1290 1290 Phosphoserine (By similarity).
 MOD_RES 1435 1435 Phosphoserine (By similarity).
 MOD_RES 1437 1437 Phosphoserine (By similarity).
 MOD_RES 1656 1656 Phosphoserine (By similarity).
 MOD_RES 1697 1697 Phosphoserine.
 MOD_RES 1730 1730 Phosphoserine.
 MOD_RES 1765 1765 Phosphoserine.
 MOD_RES 1768 1768 Phosphoserine.
 MOD_RES 1776 1776 Phosphoserine.
 MOD_RES 1958 1958 Phosphoserine.
 MOD_RES 1977 1977 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Chromosomal rearrangement; Cilium biogenesis/degradation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2024 AA 
Protein Sequence
MATGGGPFED GMNDQDLPNW SNENVDDRLN NMDWGAQQKK ANRSSEKNKK KFGVESDKRV 60
TNDISPESSP GVGRRRTKTP HTFPHSRYMS QMSVPEQAEL EKLKQRINFS DLDQRSIGSD 120
SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDASTSP PNRETIGSAQ CKELFASALS 180
NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT 240
HLIDHLKEQE KSYMKFLKKI LARDPQQEPM EEIENLKKQH DLLKRMLQQQ EQLRALQGRQ 300
AALLALQHKA EQAIAVMDDS VVAETAGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA 360
VPDNRRQAES LSLTREVSQS RKPSASERLP DEKVELFSKM RVLQEKKQKM DKLLGELHTL 420
RDQHLNNSSS SPQRSVDQRS TSAPSASVGL APVVNGESNS LTSSVPYPTA SLVSQNESEN 480
EGHLNPSEKL QKLNEVRKRL NELRELVHYY EQTSDMMTDA VNENRKDEET EESEYDSEHE 540
NSEPVTNIRN PQVASTWNEV NSHSNAQCVS NNRDGRTVNS NCEINNRSAA NIRALNMPPS 600
LDCRYNREGE QEIHVAQGED DEEEEEEAEE EGVSGASLSS HRSSLVDEHP EDAEFEQKIN 660
RLMAAKQKLR QLQDLVAMVQ DDDAAQGVIS ASASNLDDFY PAEEDTKQNS NNTRGNANKT 720
QKDTGVNEKA REKFYEAKLQ QQQRELKQLQ EERKKLIDIQ EKIQALQTAC PDLQLSAASV 780
GNCPTKKYMP AVTSTPTVNQ HETSTSKSVF EPEDSSIVDN ELWSEMRRHE MLREELRQRR 840
KQLEALMAEH QRRQGLAETA SPVAVSLRSD GSENLCTPQQ SRTEKTMATW GGSTQCALDE 900
EGDEDGYLSE GIVRTDEEEE EEQDASSNDN FSVCPSNSVN HNSYNGKETK NRWKNNCPFS 960
ADENYRPLAK TRQQNISMQR QENLRWVSEL SYVEEKEQWQ EQINQLKKQL DFSVSICQTL 1020
MQDQQTLSCL LQTLLTGPYS VMPSNVASPQ VHFIMHQLNQ CYTQLTWQQN NVQRLKQMLN 1080
ELMRQQNQHP EKPGGKERGS SASHPPSPSL FCPFSFPTQP VNLFNIPGFT NFSSFAPGMN 1140
FSPLFPSNFG DFSQNISTPS EQQQPLAQNS SGKTEYMAFP KPFESSSSIG AEKPRNKKLP 1200
EEEVESSRTP WLYEQEGEVE KPFIKTGFSV SVEKSTSSNR KNQLDTNGRR RQFDEESLES 1260
FSSMPDPVDP TTVTKTFKTR KASAQASLAS KDKTPKSKSK KRNSTQLKSR VKNIRYESAS 1320
MSSTCEPCKS RNRHSAQTEE PVQAKVFSRK NHEQLEKIIK CNRSTEISSE TGSDFSMFEA 1380
LRDTIYSEVA TLISQNESRP HFLIELFHEL QLLNTDYLRQ RALYALQDIV SRHISESHEK 1440
GENVKSVNSG TWIASNSELT PSESLATTDD ETFEKNFERE THKISEQNDA DNASVLSVSS 1500
NFEPFATDDL GNTVIHLDQA LARMREYERM KTEAESNSNM RCTCRIIEDG DGAGAGTTVN 1560
NLEETPVIEN RSSQQPVSEV STIPCPRIDT QQLDRQIKAI MKEVIPFLKE HMDEVCSSQL 1620
LTSVRRMVLT LTQQNDESKE FVKFFHKQLG SILQDSLAKF AGRKLKDCGE DLLVEISEVL 1680
FNELAFFKLM QDLDNNSITV KQRCKRKIEA TGVIQSCAKE AKRILEDHGS PAGEIDDEDK 1740
DKDETETVKQ TQTSEVYDGP KNVRSDISDQ EEDEESEGCP VSINLSKAET QALTNYGSGE 1800
DENEDEEMEE FEEGPVDVQT SLQANTEATE ENEHDEQVLQ RDFKKTAESK NVPLEREATS 1860
KNDQNNCPVK PCYLNILEDE QPLNSAAHKE SPPTVDSTQQ PNPLPLRLPE MEPLVPRVKE 1920
VKSAQETPES SLAGSPDTES PVLVNDYEAE SGNISQKSDE EDFVKVEDLP LKLTIYSEAD 1980
LRKKMVEEEQ KNHLSGEICE MQTEELAGNS ETLKEPETVG AQSI 2024 
Gene Ontology
 GO:0034451; C:centriolar satellite; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0000242; C:pericentriolar material; ISS:BHF-UCL.
 GO:0042802; F:identical protein binding; ISS:BHF-UCL.
 GO:0051297; P:centrosome organization; IMP:BHF-UCL.
 GO:0042384; P:cilium assembly; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0022027; P:interkinetic nuclear migration; ISS:BHF-UCL.
 GO:0034453; P:microtubule anchoring; ISS:BHF-UCL.
 GO:0034454; P:microtubule anchoring at centrosome; IEA:Compara.
 GO:0050768; P:negative regulation of neurogenesis; ISS:BHF-UCL.
 GO:0097150; P:neuronal stem cell maintenance; IEA:Compara.
 GO:0071539; P:protein localization to centrosome; ISS:BHF-UCL. 
Interpro
 IPR024138; Pericentriolar_Pcm1. 
Pfam
  
SMART
  
PROSITE
  
PRINTS