CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001262
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle protein 123 homolog 
Protein Synonyms/Alias
 Protein D123; HT-1080; PZ32 
Gene Name
 CDC123 
Gene Synonyms/Alias
 C10orf7; D123 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24FFRGVTIKSVILPLPubiquitination[1, 2, 3, 4, 5, 6]
35LPLPQNVKDYLLDDGubiquitination[2, 7]
104LGGSVFPKLNWSAPRubiquitination[2, 4]
135SDIFLLFKSSDFITRubiquitination[2, 8]
168EYELVLRKWCELIPGubiquitination[4]
186RCFVKENKLIGISQRubiquitination[4]
204QYYDHISKQKEEIRRubiquitination[1, 2, 3, 5]
206YDHISKQKEEIRRCIubiquitination[4]
218RCIQDFFKKHIQYKFubiquitination[4]
308YLSYRLPKDFVDLSTubiquitination[1, 2, 3, 4, 5, 6, 9]
321STGEDAHKLIDFLKLubiquitination[1, 2, 5, 6]
327HKLIDFLKLKRNQQEubiquitination[1, 2, 3, 4, 5, 7]
329LIDFLKLKRNQQEDDubiquitination[1, 4, 5]
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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
Functional Description
 Required for S phase entry of the cell cycle (By similarity). 
Sequence Annotation
 MOD_RES 60 60 Phosphoserine.  
Keyword
 Cell cycle; Cell division; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 336 AA 
Protein Sequence
MKKEHVLHCQ FSAWYPFFRG VTIKSVILPL PQNVKDYLLD DGTLVVSGRD DPPTHSQPDS 60
DDEAEEIQWS DDENTATLTA PEFPEFATKV QEAINSLGGS VFPKLNWSAP RDAYWIAMNS 120
SLKCKTLSDI FLLFKSSDFI TRDFTQPFIH CTDDSPDPCI EYELVLRKWC ELIPGAEFRC 180
FVKENKLIGI SQRDYTQYYD HISKQKEEIR RCIQDFFKKH IQYKFLDEDF VFDIYRDSRG 240
KVWLIDFNPF GEVTDSLLFT WEELISENNL NGDFSEVDAQ EQDSPAFRCT NSEVTVQPSP 300
YLSYRLPKDF VDLSTGEDAH KLIDFLKLKR NQQEDD 336 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0007050; P:cell cycle arrest; TAS:ProtInc.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0007346; P:regulation of mitotic cell cycle; ISS:HGNC. 
Interpro
 IPR016525; Cell_div_Cdc123.
 IPR009772; D123. 
Pfam
 PF07065; D123 
SMART
  
PROSITE
  
PRINTS