CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001626
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pericentrin 
Protein Synonyms/Alias
 Kendrin; Pericentrin-B 
Gene Name
 PCNT 
Gene Synonyms/Alias
 KIAA0402; PCNT2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
505VEDLEQLKQREKTQHubiquitination[1]
788EKQTIINKFELREAEubiquitination[1]
881ERKEITEKFSAEQDAubiquitination[2]
952RVAELQTKHAADLGAubiquitination[2]
1069KKTALHEKEETLRLQubiquitination[2]
1145ANLLSMLKADVNLSHubiquitination[2]
1293QIHSRFEKEFSFKNEubiquitination[2]
1705EEENTSLKVIYTRSSubiquitination[2]
1799LEAALEAKEALSRLLubiquitination[2]
1884IDALNQRKAAHSAELubiquitination[2]
2015LKDAPLCKQEGVMSVubiquitination[2, 3]
2038QSELLLVKNEMRLSLubiquitination[2, 3]
2050LSLEDGGKGKEKVLEubiquitination[2]
2052LEDGGKGKEKVLEDCubiquitination[2]
2054DGGKGKEKVLEDCQLubiquitination[2]
2504EQGDLQEKSLEHLRLubiquitination[2, 3]
2538THLQNQEKLQHLRTAubiquitination[2]
2570QVELLAYKVEQEKCIubiquitination[2]
2575AYKVEQEKCIAGDLQubiquitination[2]
2597EKANSVQKLLAAEQTubiquitination[2, 3]
2610QTVVRDLKSDLCESRubiquitination[2, 3]
2685QRESQSAKALEELRAubiquitination[2]
2709SRLCVALKHEQTAKDacetylation[3]
2709SRLCVALKHEQTAKDubiquitination[2]
2720TAKDNLQKELRIEHSubiquitination[2]
2745SQLSELQKDLAAEKSubiquitination[2]
2810DLQAMLEKVQQQALHubiquitination[2]
2828QLEAEAQKHCEALRRubiquitination[2]
2854VEALHTQKRELRCSLubiquitination[2]
2932QRDLHKIKQLQQTVRubiquitination[2, 3, 4]
2944TVRDLESKDEVPGSRubiquitination[2, 3]
3010DWTSSNEKAVMSLLHubiquitination[2]
3034SRPTSSQKKMAAELQubiquitination[2]
3035RPTSSQKKMAAELQFubiquitination[2]
3057KDNVSLTKALSTVTQubiquitination[1, 5]
3066LSTVTQEKLELSRAVubiquitination[2]
3099RSERSAWKPDETAPQubiquitination[2]
3229KGALAQGKAPRPGPRubiquitination[2]
3328LPDSTSKKSCHPMIKubiquitination[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] 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]
 [4] 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]
 [5] 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
 Integral component of the filamentous matrix of the centrosome involved in the initial establishment of organized microtubule arrays in both mitosis and meiosis. Plays a role, together with DISC1, in the microtubule network formation. Is an integral component of the pericentriolar material (PCM). May play an important role in preventing premature centrosome splitting during interphase by inhibiting NEK2 kinase activity at the centrosome. 
Sequence Annotation
 REGION 2983 3246 Interaction with NEK2.
 REGION 3195 3208 Calmodulin-binding.
 MOD_RES 191 191 Phosphothreonine.
 MOD_RES 366 366 Phosphoserine (By similarity).
 MOD_RES 682 682 Phosphoserine.
 MOD_RES 1712 1712 Phosphoserine (By similarity).
 MOD_RES 2044 2044 Phosphoserine.
 MOD_RES 2177 2177 Phosphoserine.
 MOD_RES 2327 2327 Phosphoserine.
 MOD_RES 2477 2477 Phosphoserine.
 MOD_RES 2486 2486 Phosphoserine.
 MOD_RES 3302 3302 Phosphoserine.  
Keyword
 Alternative splicing; Calmodulin-binding; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Dwarfism; Microtubule; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3336 AA 
Protein Sequence
MEVEQEQRRR KVEAGRTKLA HFRQRKTKGD SSHSEKKTAK RKGSAVDASV QEESPVTKED 60
SALCGGGDIC KSTSCDDTPD GAGGAFAAQP EDCDGEKRED LEQLQQKQVN DHPPEQCGMF 120
TVSDHPPEQH GMFTVGDHPP EQRGMFTVSD HPPEQHGMFT VSDHPPEQRG MFTISDHQPE 180
QRGMFTVSDH TPEQRGIFTI SDHPAEQRGM FTKECEQECE LAITDLESGR EDEAGLHQSQ 240
AVHGLELEAL RLSLSNMHTA QLELTQANLQ KEKETALTEL REMLNSRRAQ ELALLQSRQQ 300
HELELLREQH AREKEEVVLR CGQEAAELKE KLQSEMEKNA QIVKTLKEDW ESEKDLCLEN 360
LRKELSAKHQ SEMEDLQNQF QKELAEQRAE LEKIFQDKNQ AERALRNLES HHQAAIEKLR 420
EDLQSEHGRC LEDLEFKFKE SEKEKQLELE NLQASYEDLK AQSQEEIRRL WSQLDSARTS 480
RQELSELHEQ LLARTSRVED LEQLKQREKT QHESELEQLR IYFEKKLRDA EKTYQEDLTL 540
LQQRLQGARE DALLDSVEVG LSCVGLEEKP EKGRKDHVDE LEPERHKESL PRFQAELEES 600
HRHQLEALES PLCIQHEGHV SDRCCVETSA LGHEWRLEPS EGHSQELPWV HLQGVQDGDL 660
EADTERAARV LGLETEHKVQ LSLLQTELKE EIELLKIENR NLYGKLQHET RLKDDLEKVK 720
HNLIEDHQKE LNNAKQKTEL MKQEFQRKET DWKVMKEELQ REAEEKLTLM LLELREKAES 780
EKQTIINKFE LREAEMRQLQ DQQAAQILDL ERSLTEQQGR LQQLEQDLTS DDALHCSQCG 840
REPPTAQDGE LAALHVKEDC ALQLMLARSR FLEERKEITE KFSAEQDAFL QEAQEQHARE 900
LQLLQERHQQ QLLSVTAELE ARHQAALGEL TASLESKQGA LLAARVAELQ TKHAADLGAL 960
ETRHLSSLDS LESCYLSEFQ TIREEHRQAL ELLRADFEEQ LWKKDSLHQT ILTQELEKLK 1020
RKHEGELQSV RDHLRTEVST ELAGTVAHEL QGVHQGEFGS EKKTALHEKE ETLRLQSAQA 1080
QPFHQEEKES LSLQLQKKNH QVQQLKDQVL SLSHEIEECR SELEVLQQRR ERENREGANL 1140
LSMLKADVNL SHSERGALQD ALRRLLGLFG ETLRAAVTLR SRIGERVGLC LDDAGAGLAL 1200
STAPALEETW SDVALPELDR TLSECAEMSS VAEISSHMRE SFLMSPESVR ECEQPIRRVF 1260
QSLSLAVDGL MEMALDSSRQ LEEARQIHSR FEKEFSFKNE ETAQVVRKHQ ELLECLKEES 1320
AAKAELALEL HKTQGTLEGF KVETADLKEV LAGKEDSEHR LVLELESLRR QLQQAAQEQA 1380
ALREECTRLW SRGEATATDA EAREAALRKE VEDLTKEQSE TRKQAEKDRS ALLSQMKILE 1440
SELEEQLSQH RGCAKQAEAV TALEQQVASL DKHLRNQRQF MDEQAAEREH EREEFQQEIQ 1500
RLEGQLRQAA KPQPWGPRDS QQAPLDGEVE LLQQKLREKL DEFNELAIQK ESADRQVLMQ 1560
EEEIKRLEEM NINIRKKVAQ LQEEVEKQKN IVKGLEQDKE VLKKQQMSSL LLASTLQSTL 1620
DAGRCPEPPS GSPPEGPEIQ LEVTQRALLR RESEVLDLKE QLEKMKGDLE SKNEEILHLN 1680
LKLDMQNSQT AVSLRELEEE NTSLKVIYTR SSEIEELKAT IENLQENQKR LQKEKAEEIE 1740
QLHEVIEKLQ HELSLMGPVV HEVSDSQAGS LQSELLCSQA GGPRGQALQG ELEAALEAKE 1800
ALSRLLADQE RRHSQALEAL QQRLQGAEEA AELQLAELER NVALREAEVE DMASRIQEFE 1860
AALKAKEATI AERNLEIDAL NQRKAAHSAE LEAVLLALAR IRRALEQQPL AAGAAPPELQ 1920
WLRAQCARLS RQLQVLHQRF LRCQVELDRR QARRATAHTR VPGAHPQPRM DGGAKAQVTG 1980
DVEASHDAAL EPVVPDPQGD LQPVLVTLKD APLCKQEGVM SVLTVCQRQL QSELLLVKNE 2040
MRLSLEDGGK GKEKVLEDCQ LPKVDLVAQV KQLQEKLNRL LYSMTFQNVD AADTKSLWPM 2100
ASAHLLESSW SDDSCDGEEP DISPHIDTCD ANTATGGVTD VIKNQAIDAC DANTTPGGVT 2160
DVIKNWDSLI PDEMPDSPIQ EKSECQDMSL SSPTSVLGGS RHQSHTAEAG PRKSPVGMLD 2220
LSSWSSPEVL RKDWTLEPWP SLPVTPHSGA LSLCSADTSL GDRADTSLPQ TQGPGLLCSP 2280
GVSAAALALQ WAESPPADDH HVQRTAVEKD VEDFITTSFD SQETLSSPPP GLEGKADRSE 2340
KSDGSGFGAR LSPGSGGPEA QTAGPVTPAS ISGRFQPLPE AMKEKEVRPK HVKALLQMVR 2400
DESHQILALS EGLAPPSGEP HPPRKEDEIQ DISLHGGKTQ EVPTACPDWR GDLLQVVQEA 2460
FEKEQEMQGV ELQPRLSGSD LGGHSSLLER LEKIIREQGD LQEKSLEHLR LPDRSSLLSE 2520
IQALRAQLRM THLQNQEKLQ HLRTALTSAE ARGSQQEHQL RRQVELLAYK VEQEKCIAGD 2580
LQKTLSEEQE KANSVQKLLA AEQTVVRDLK SDLCESRQKS EQLSRSLCEV QQEVLQLRSM 2640
LSSKENELKA ALQELESEQG KGRALQSQLE EEQLRHLQRE SQSAKALEEL RASLETQRAQ 2700
SSRLCVALKH EQTAKDNLQK ELRIEHSRCE ALLAQERSQL SELQKDLAAE KSRTLELSEA 2760
LRHERLLTEQ LSQRTQEACV HQDTQAHHAL LQKLKEEKSR VVDLQAMLEK VQQQALHSQQ 2820
QLEAEAQKHC EALRREKEVS ATLKSTVEAL HTQKRELRCS LEREREKPAW LQAELEQSHP 2880
RLKEQEGRKA ARRSAEARQS PAAAEQWRKW QRDKEKLREL ELQRQRDLHK IKQLQQTVRD 2940
LESKDEVPGS RLHLGSARRA AGSDADHLRE QQRELEAMRQ RLLSAARLLT SFTSQAVDRT 3000
VNDWTSSNEK AVMSLLHTLE ELKSDLSRPT SSQKKMAAEL QFQFVDVLLK DNVSLTKALS 3060
TVTQEKLELS RAVSKLEKLL KHHLQKGCSP SRSERSAWKP DETAPQSSLR RPDPGRLPPA 3120
ASEEAHTSNV KMEKLYLHYL RAESFRKALI YQKKYLLLLI GGFQDSEQET LSMIAHLGVF 3180
PSKAERKITS RPFTRFRTAV RVVIAILRLR FLVKKWQEVD RKGALAQGKA PRPGPRARQP 3240
QSPPRTRESP PTRDVPSGHT RDPARGRRLA AAASPHSGGR ATPSPNSRLE RSLTASQDPE 3300
HSLTEYIHHL EVIQQRLGGV LPDSTSKKSC HPMIKQ 3336 
Gene Ontology
 GO:0005814; C:centriole; IEA:Compara.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0045171; C:intercellular bridge; IEA:Compara.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0048854; P:brain morphogenesis; IEA:Compara.
 GO:0021696; P:cerebellar cortex morphogenesis; IEA:Compara.
 GO:0042384; P:cilium assembly; IDA:MGI.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0035108; P:limb morphogenesis; IEA:Compara.
 GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0061351; P:neural precursor cell proliferation; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0021772; P:olfactory bulb development; IEA:Compara.
 GO:0007051; P:spindle organization; IEA:Compara. 
Interpro
 IPR019528; PACT_domain.
 IPR024151; Pericentrin. 
Pfam
 PF10495; PACT_coil_coil 
SMART
  
PROSITE
  
PRINTS