CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014089
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosome-associated protein 350 
Protein Synonyms/Alias
 Cep350; Centrosome-associated protein of 350 kDa 
Gene Name
 CEP350 
Gene Synonyms/Alias
 CAP350; KIAA0480; GM133 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
237KGSENNLKLSVNNMAubiquitination[1]
250MAHDTDPKALRLTDSubiquitination[1, 2, 3]
274SQRLDILKRRQHDVKubiquitination[1]
291KLKERIRKQWEHSEEubiquitination[1]
339APPAPAYKGFNPSETubiquitination[1]
347GFNPSETKIRTPDGKubiquitination[1]
354KIRTPDGKVWQEAEFubiquitination[1, 4]
404KPVRKVQKVAQLSSTubiquitination[1]
512ASSLPDNKQEENTALubiquitination[1, 4]
521EENTALNKDFLPIEIubiquitination[1, 5]
545DSTAHTAKQDTVELQubiquitination[1]
555TVELQNQKSSAPVHAubiquitination[1]
663RLQETYSKLLLEKTLubiquitination[1, 5]
686VTQETQAKPGYQPSGubiquitination[2, 3]
726PPQPLARKDLMESTWubiquitination[1]
829LDRIEALKATAASLSubiquitination[1, 2, 3, 5, 6]
882KAVTPPVKDDNEDVFubiquitination[5]
895VFSARIQKMLGSCVSubiquitination[1]
921GNLSEFKKLPEMIRPubiquitination[1]
1013LKVAEILKEKEFCPGubiquitination[1, 5]
1015VAEILKEKEFCPGERubiquitination[1, 5]
1029RNSYEPIKEFQKEAEubiquitination[1, 2, 3]
1033EPIKEFQKEAEKFLPubiquitination[1]
1037EFQKEAEKFLPLFGHubiquitination[1]
1051HIGGTQSKGPWEELAubiquitination[1]
1059GPWEELAKGSPHSVIubiquitination[1]
1078KSYQLYGKGFEDKLDubiquitination[1]
1083YGKGFEDKLDRGTSTubiquitination[1]
1122GTGTSTEKKSTLEPHubiquitination[1]
1123TGTSTEKKSTLEPHSubiquitination[1]
1318MAPIPGSKRFSPAGLubiquitination[1, 4, 5, 7]
1370VSLAQIIKAQQQRHEubiquitination[1]
1384ERDLALLKLKAEQEAubiquitination[1]
1386DLALLKLKAEQEALEubiquitination[1, 4, 5]
1404QLEETRNKAAQVHAEubiquitination[1]
1433VLQEATCKIAAQQSEubiquitination[1]
1906AWDKELIKPKTPKKEubiquitination[1]
3110VLNQISEKQGRMLLVacetylation[8]
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] 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]
 [3] 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]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] 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
 Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CENPJ. Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network. Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity. 
Sequence Annotation
 DOMAIN 2517 2559 CAP-Gly.
 MOD_RES 878 878 Phosphothreonine.
 MOD_RES 1061 1061 Phosphoserine.
 MOD_RES 1253 1253 Phosphothreonine.
 MOD_RES 1256 1256 Phosphoserine.
 MOD_RES 1259 1259 Phosphoserine.
 MOD_RES 2204 2204 Phosphothreonine.
 MOD_RES 2206 2206 Phosphoserine.
 MOD_RES 2460 2460 Phosphoserine.
 MOD_RES 2839 2839 Phosphoserine.  
Keyword
 3D-structure; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3117 AA 
Protein Sequence
MRSSKSKEVP LPNPRNSQSK DTVQADITTS WDALSQTKAA LRHIENKLEV APTSTAVCDS 60
VMDTKKSSTS ATRKISRKDG RYLDDSWVNA PISKSTKSRK EKSRSPLRAT TLESNVKKNN 120
RVEFREPLVS YREIHGAPSN FSSSHLESKH VYCVDVNEEK TESGNWMIGS REERNIRSCD 180
FESSQSSVIN DTVVRFLNDR PAIDALQNSE CLIRMGASMR TEEEMPNRTK GSENNLKLSV 240
NNMAHDTDPK ALRLTDSSPS STSTSNSQRL DILKRRQHDV KLEKLKERIR KQWEHSEETN 300
GRGQKLGHID HPVMVVNVDN SVTAKVRKVA TAPPAPAYKG FNPSETKIRT PDGKVWQEAE 360
FQNMSRELYR DLALHFADDI SIKEKPAEKS KEKKVVKPVR KVQKVAQLSS TECRTGSSHL 420
ISTSSWRDGQ KLVKKILGPA PRMEPKEQRT ASSDRGGRER TAKSGGHIGR AESDPRLDVL 480
HRHLQRNSER SRSKSRSENN IKKLASSLPD NKQEENTALN KDFLPIEIRG ILDDLQLDST 540
AHTAKQDTVE LQNQKSSAPV HAPRSHSPVK RKPDKITANE DPPVISKRRH YDTDEVRQYI 600
VRQQEERKRK QNEEKKAQKE ATEQKNKRLQ ELYRKQKEAF TKVKNVPPSE PSATRRLQET 660
YSKLLLEKTL LEEPSHQHVT QETQAKPGYQ PSGESDKENK VQERPPSASS SSDMSLSEPP 720
QPLARKDLME STWMQPERLS PQVHHSQPQP FAGTAGSLLS HLLSLEHVGI LHKDFESILP 780
TRKNHNMASR PLTFTPQPYV TSPAAYTDAL LKPSASQYKS KLDRIEALKA TAASLSSRIE 840
SEAKKLAGAS INYGSAWNTE YDVQQAPQED GPWTKAVTPP VKDDNEDVFS ARIQKMLGSC 900
VSHATFDDDL PGVGNLSEFK KLPEMIRPQS AISSFRVRSP GPKPEGLLAQ LCKRQTDSSS 960
SDMQACSQDK AKISLGSSID SVSEGPLLSE GSLSEEEGDQ DGQPLLKVAE ILKEKEFCPG 1020
ERNSYEPIKE FQKEAEKFLP LFGHIGGTQS KGPWEELAKG SPHSVINIFT KSYQLYGKGF 1080
EDKLDRGTST SRPLNATATP LSGVSYEDDF VSSPGTGTST EKKSTLEPHS TLSPQEDHSN 1140
RKSAYDPSSV DVTSQHSSGA QSAASSRSST SSKGKKGKKE KTEWLDSFTG NVQNSLLDEE 1200
KAERGSHQGK KSGTSSKLSV KDFEQTLDTD STLEDLSGHS VSVSSDKGRS QKTPTSPLSP 1260
SSQKSLQFDV AGTSSERSKS SVMPPTITGF KPNAPLTDLN PAASRTTTEN MAPIPGSKRF 1320
SPAGLHHRMA AELSYLNAIE ESVRQLSDVE RVRGISLAQQ ESVSLAQIIK AQQQRHERDL 1380
ALLKLKAEQE ALESQRQLEE TRNKAAQVHA ESLQQVVQSQ REVTEVLQEA TCKIAAQQSE 1440
TARLTTDAAR QICEMAELTR THISDAVVAS GAPLAILYDH QRQHLPDFVK QLRTRTETDR 1500
KSPSVSLSQS KEGTLDSKHQ KYSASYDSYS ESSGYKNHDR RSSSGSSRQE SPSVPSCKEN 1560
EKKLNGEKIE SSIDEQVQTA ADDSLRSDSV PSLPDEKDST SIATEYSLKF DESMTEDEIE 1620
EQSFRSLLPS ESHRRFNMEK RRGHHDDSDE EASPEKTTLS TAKELNMPFS GGQDSFSKFT 1680
MEMVRQYMKE EEMRAAHQSS LLRLREKALK EKTKAELAWL EHQKKHLRDK GEDDKMPPLR 1740
KKQRGLLLRL QQEKAEIKRL QEANKAARKE RQLILKQQEE IEKIRQTTIK LQEKLKSAGE 1800
SKLDSHSDDD TKDNKATSPG PTDLETRSPS PISISSSETS SIMQKLKKMR SRMDEKFLTK 1860
REQKLMQRRQ HAEELLEWKR RLDAEEAEIR QMEKQALAAW DKELIKPKTP KKELEDQRTE 1920
QKEIASEEES PVPLYSHLNS ESSIPEELGS PAVEYVPSES IGQEQPGSPD HSILTEEMIC 1980
SQELESSTSP SKHSLPKSCT SVSKQESSKG SHRTGGQCHL PIKSHQHCYS WSDESLSMTQ 2040
SETTSDQSDI EGRIRALKDE LRKRKSVVNQ LKKEQKKRQK ERLKAQEASL IKQLESYDEF 2100
IKKTEAELSQ DLETSPTAKP QIKTLSSASE KPKIKPLTPL HRSETAKNWK SLTESERSRG 2160
SLESIAEHVD ASLSGSERSV SERSLSAYAK RVNEWDSRTE DFQTPSPVLR SSRKIREESG 2220
DSLENVPALH LLKELNATSR ILDMSDGKVG ESSKKSEIKE IEYTKLKKSK IEDAFSKEGK 2280
SDVLLKLVLE QGDSSEILSK KDLPLDSENV QKDLVGLAIE NLHKSEEMLK ERQSDQDMNH 2340
SPNIQSGKDI HEQKNTKEKD LSWSEHLFAP KEIPYSEDFE VSSFKKEISA ELYKDDFEVS 2400
SLLSLRKDSQ SCRDKPQPMR SSTSGATSFG SNEEISECLS EKSLSIHSNV HSDRLLELKS 2460
PTELMKSKER SDVEHEQQVT ESPSLASVPT ADELFDFHIG DRVLIGNVQP GILRFKGETS 2520
FAKGFWAGVE LDKPEGNNNG TYDGIAYFEC KEKHGIFAPP QKISHIPENF DDYVDINEDE 2580
DCYSDERYQC YNQEQNDTEG PKDREKDVSE YFYEKSLPSV NDIEASVNRS RSLKIETDNV 2640
QDISGVLEAH VHQQSSVDSQ ISSKENKDLI SDATEKVSIA AEDDTLDNTF SEELEKQQQF 2700
TEEEDNLYAE ASEKLCTPLL DLLTREKNQL EAQLKSSLNE EKKSKQQLEK ISLLTDSLLK 2760
VFVKDTVNQL QQIKKTRDEK IQLSNQELLG DDQKKVTPQD LSQNVEEQSP SISGCFLSSE 2820
LEDEKEEISS PDMCPRPESP VFGASGQEEL AKRLAELELS REFLSALGDD QDWFDEDFGL 2880
SSSHKIQKNK AEETIVPLMA EPKRVTQQPC ETLLAVPHTA EEVEILVHNA AEELWKWKEL 2940
GHDLHSISIP TKLLGCASKG LDIESTSKRV YKQAVFDLTK EIFEEIFAED PNLNQPVWMK 3000
PCRINSSYFR RVKNPNNLDE IKSFIASEVL KLFSLKKEPN HKTDWQKMMK FGRKKRDRVD 3060
HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT IDVLNQISEK QGRMLLV 3117 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell. 
Interpro
 IPR000938; CAP-Gly_domain. 
Pfam
 PF01302; CAP_GLY 
SMART
 SM01052; CAP_GLY 
PROSITE
 PS00845; CAP_GLY_1
 PS50245; CAP_GLY_2 
PRINTS