CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023292
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosomal protein of 164 kDa 
Protein Synonyms/Alias
 Cep164 
Gene Name
 CEP164 
Gene Synonyms/Alias
 KIAA1052; NPHP15 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1008LDELQARKLKLESQVubiquitination[1]
1038SLEAEAQKKQHLLREubiquitination[1]
1039LEAEAQKKQHLLREVubiquitination[1]
1076SLGTNQTKEVSSSLSubiquitination[2, 3]
1114GVALRSAKEFLVQQTubiquitination[1, 4]
1150ASAQEVAKDPPGIKAubiquitination[3]
1176TRHLDEMKSAMRKGHubiquitination[1]
1216TLGGSPTKKAVTFDLubiquitination[1]
1260TPSLTSRKIHGLSHSubiquitination[1]
1359VDDFLLEKWRKYFPSubiquitination[1, 3, 5]
1362FLLEKWRKYFPSGIPubiquitination[1]
1437PLFSSTPKPKATLSLubiquitination[1]
1439FSSTPKPKATLSLLQubiquitination[1, 3]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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
 Plays a role in microtubule organization and/or maintenance for the formation of primary cilia (PC), a microtubule-based structure that protrudes from the surface of epithelial cells. Plays a critical role in G2/M checkpoint and nuclear divisions. A key player in the DNA damage-activated ATR/ATM signaling cascade since it is required for the proper phosphorylation of H2AX, RPA, CHEK2 and CHEK1. Plays a critical role in chromosome segregation, acting as a mediator required for the maintenance of genomic stability through modulation of MDC1, RPA and CHEK1. 
Sequence Annotation
 DOMAIN 56 89 WW.
 REGION 1 194 Interaction with ATRIP.
 MOD_RES 186 186 Phosphoserine; by ATR and ATM.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Ciliopathy; Cilium biogenesis/degradation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; DNA damage; DNA repair; Mitosis; Nephronophthisis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1460 AA 
Protein Sequence
MAGRPLRIGD QLVLEEDYDE TYIPSEQEIL EFAREIGIDP IKEPELMWLA REGIVAPLPG 60
EWKPCQDITG DIYYFNFANG QSMWDHPCDE HYRSLVIQER AKLSTSGAIK KKKKKKEKKD 120
KKDRDPPKSS LALGSSLAPV HVPLGGLAPL RGLVDTPPSA LRGSQSVSLG SSVESGRQLG 180
ELMLPSQGLK TSAYTKGLLG SIYEDKTALS LLGLGEETNE EDEEESDNQS VHSSSEPLRN 240
LHLDIGALGG DFEYEESLRT SQPEEKKDVS LDSDAAGPPT PCKPSSPGAD SSLSSAVGKG 300
RQGSGARPGL PEKEENEKSE PKICRNLVTP KADPTGSEPA KASEKEAPED TVDAGEEGSR 360
REEAAKEPKK KASALEEGSS DASQELEISE HMKEPQLSDS IASDPKSFHG LDFGFRSRIS 420
EHLLDVDVLS PVLGGACRQA QQPLGIEDKD DSQSSQDELQ SKQSKGLEER LSPPLPHEER 480
AQSPPRSLAT EEEPPQGPEG QPEWKEAEEL GEDSAASLSL QLSLQREQAP SPPAACEKGK 540
EQHSQAEELG PGQEEAEDPE EKVAVSPTPP VSPEVRSTEP VAPPEQLSEA ALKAMEEAVA 600
QVLEQDQRHL LESKQEKMQQ LREKLCQEEE EEILRLHQQK EQSLSSLRER LQKAIEEEEA 660
RMREEESQRL SWLRAQVQSS TQADEDQIRA EQEASLQKLR EELESQQKAE RASLEQKNRQ 720
MLEQLKEEIE ASEKSEQAAL NAAKEKALQQ LREQLEGERK EAVATLEKEH SAELERLCSS 780
LEAKHREVVS SLQKKIQEAQ QKEEAQLQKC LGQVEHRVHQ KSYHVAGYEH ELSSLLREKR 840
QEVEGEHERR LDKMKEEHQQ VMAKAREQYE AEERKQRAEL LGHLTGELER LQRAHERELE 900
TVRQEQHKRL EDLRRRHREQ ERKLQDLELD LETRAKDVKA RLALLEVQEE TARREKQQLL 960
DVQRQVALKS EEATATHQQL EEAQKEHTHL LQSNQQLREI LDELQARKLK LESQVDLLQA 1020
QSQQLQKHFS SLEAEAQKKQ HLLREVTVEE NNASPHFEPD LHIEDLRKSL GTNQTKEVSS 1080
SLSQSKEDLY LDSLSSHNVW HLLSAEGVAL RSAKEFLVQQ TRSMRRRQTA LKAAQQHWRH 1140
ELASAQEVAK DPPGIKALED MRKNLEKETR HLDEMKSAMR KGHNLLKKKE EKLNQLESSL 1200
WEEASDEGTL GGSPTKKAVT FDLSDMDSLS SESSESFSPP HREWWRQQRI DSTPSLTSRK 1260
IHGLSHSLRQ ISSQLSSVLS ILDSLNPQSP PPLLASMPAQ LPPRDPKSTP TPTYYGSLAR 1320
FSALSSATPT STQWAWDSGQ GPRLPSSVAQ TVDDFLLEKW RKYFPSGIPL LSNSPTPLES 1380
RLGYMSASEQ LRLLQHSHSQ VPEAGSTTFQ GIIEANRRWL ERVKNDPRLP LFSSTPKPKA 1440
TLSLLQLGLD EHNRVKVYRF 1460 
Gene Ontology
 GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0042384; P:cilium assembly; IMP:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW. 
Interpro
 IPR001202; WW_dom. 
Pfam
  
SMART
 SM00456; WW 
PROSITE
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 
PRINTS