CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018072
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosomal protein of 192 kDa 
Protein Synonyms/Alias
 Cep192 
Gene Name
 CEP192 
Gene Synonyms/Alias
 KIAA1569; PP8407 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
101DTFFMSNKPQRYKDKubiquitination[1]
547WSKDPSSKSGNLLETubiquitination[1]
1294NLILEGVKKLSDSYMubiquitination[1]
1379SDRGINNKTATELSTubiquitination[1]
1482EFLQPSSKASLESTSubiquitination[1]
1496SDLGASGKHGGNVSLubiquitination[1]
Reference
 [1] 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
Functional Description
 Required for mitotic centrosome and spindle assembly. Appears to be a major regulator of pericentriolar material (PCM) recruitment, centrosome maturation, and centriole duplication. 
Sequence Annotation
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 1159 1159 Phosphoserine.
 MOD_RES 1502 1502 Phosphoserine.
 MOD_RES 1514 1514 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1941 AA 
Protein Sequence
MKTSDLVPSF GYFIRSPEKR EPIALIRKSD VSRGNLEKEM AHLNHDLYSG DLNEQSQAQL 60
SEGSITLQVE AVESTSQVDE NDVTLTADKG KTEDTFFMSN KPQRYKDKLP DSGDSMLRIS 120
TIASAIAEAS VNTDPSQLAA MIKALSNKTR DKTFQEDEKQ KDYSHVRHFL PNDLEKSNGS 180
NALDMEKYLK KTEVSRYESA LENFSRASMS DTWDLSLPKE QTTQDIHPVD LSATSVSVRA 240
PEENTAAIVY VENGESENQE SFRTINSSNS VTNRENNSAV VDVKTCSIDN KLQDVGNDEK 300
ATSISTPSDS YSSVRNPRIT SLCLLKDCEE IRDNRENQRQ NECVSEISNS EKHVTFENHR 360
IVSPKNSDLK NTSPEHGGRG SEDEQESFRP STSPLSHSSP SEISGTSSSG CALESFGSAA 420
QQQQPPCEQE LSPLVCSPAG VSRLTYVSEP ESSYPTTATD DALEDRKSDI TSELSTTIIQ 480
GSPAALEERA MEKLREKVPF QNRGKGTLSS IIQNNSDTRK ATETTSLSSK PEYVKPDFRW 540
SKDPSSKSGN LLETSEVGWT SNPEELDPIR LALLGKSGLS CQVGSATSHP VSCQEPIDED 600
QRISPKDKST AGREFSGQVS HQTTSENQCT PIPSSTVHSS VADMQNMPAA VHALLTQPSL 660
SAAPFAQRYL GTLPSTGSTT LPQCHAGNAT VCGFSGGLPY PAVAGEPVQN SVAVGICLGS 720
NIGSGWMGTS SLCNPYSNTL NQNLLSTTKP FPVPSVGTNC GIEPWDSGVT SGLGSVRVPE 780
ELKLPHACCV GIASQTLLSV LNPTDRWLQV SIGVLSISVN GEKVDLSTYR CLVFKNKAII 840
RPHATEEIKV LFIPSSPGVF RCTFSVASWP CSTDAETIVQ AEALASTVTL TAIAESPVIE 900
VETEKKDVLD FGDLTYGGWK ALPLKLINRT HATVPIRLII NANAVAWRCF TFSKESVRAP 960
VEVAPCADVV TRLAGPSVVN HMMPASYDGQ DPEFLMIWVL FHSPKKQISS SDILDSAEEF 1020
SAKVDIEVDS PNPTPVLRSV SLRARAGIAR IHAPRDLQTM HFLAKVASSR KQHLPLKNAG 1080
NIEVYLDIKV PEQGSHFSVD PKNLLLKPGE EHEVIVSFTP KDPEACEERI LKIFVQPFGP 1140
QYEVVLKGEV ISSGSKPLSP GPCLDIPSIL SNKQFLAWGG VPLGRTQLQK LALRNNSAST 1200
TQHLRLLIRG QDQDCFQLQN TFGSEQRLTS NCEIRIHPKE DIFISVLFAP TRLSCMLARL 1260
EIKQLGNRSQ PGIKFTIPLS GYGGTSNLIL EGVKKLSDSY MVTVNGLVPG KESKIVFSVR 1320
NTGSRAAFVK AVGFKDSQKK VLLDPKVLRI FPDKFVLKER TQENVTLIYN PSDRGINNKT 1380
ATELSTVYLF GGDEISRQQY RRALLHKPEM IKQILPEHSV LQNINFVEAF QDELLVTEVY 1440
DLPQRPNDVQ LFYGSMCKII LSVIGEFRDC ISSREFLQPS SKASLESTSD LGASGKHGGN 1500
VSLDVLPVKG PQGSPLLSRA ARPPLDQLAS EEPWTVLPEH LILVAPSPCD MAKTGRFQIV 1560
NNSVRLLRFE LCWPAHCLTV TPQHGCVAPE SKLQILVSPN SSLSTKQSMF PWSGLIYIHC 1620
DDGQKKIVKV QIREDLTQVE LLTRLTSKPF GILSPVSEPS VSHLVKPMTK PPSTKVEIRN 1680
KSITFPTTEP GETSESCLEL ENHGTTDVKW HLSSLAPPYV KGVDESGDVF RATYAAFRCS 1740
PISGLLESHG IQKVSITFLP RGRGDYAQFW DVECHPLKEP HMKHTLRFQL SGQSIEAENE 1800
PENACLSTDS LIKIDHLVKP RRQAVSEASA RIPEQLDVTA RGVYAPEDVY RFRPTSVGES 1860
RTLKVNLRNN SFITHSLKFL SPREPFYVKH SKYSLRAQHY INMPVQFKPK SAGKFEALLV 1920
IQTDEGKSIA IRLIGEALGK N 1941 
Gene Ontology
 GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0019902; F:phosphatase binding; IDA:UniProtKB.
 GO:0051298; P:centrosome duplication; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
 GO:0051225; P:spindle assembly; IMP:UniProtKB. 
Interpro
  
Pfam
  
SMART
  
PROSITE
  
PRINTS