CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011923
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle protein 20 homolog 
Protein Synonyms/Alias
 p55CDC 
Gene Name
 CDC20 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31PPARWQRKAKEAAGPubiquitination[1]
62TPGRTPGKSSSKVQTubiquitination[2, 3]
66TPGKSSSKVQTTPSKubiquitination[1, 2, 3, 4, 5]
73KVQTTPSKPGGDRYIubiquitination[1, 2, 3, 4]
97VASFLLSKENQPENSubiquitination[1, 2, 3, 4]
109ENSQTPTKKEHQKAWubiquitination[2, 3, 4]
110NSQTPTKKEHQKAWAubiquitination[1]
114PTKKEHQKAWALNLNubiquitination[1, 2, 4]
129GFDVEEAKILRLSGKubiquitination[1, 2, 3, 4, 6]
136KILRLSGKPQNAPEGubiquitination[1, 2, 3, 4, 6, 7, 8]
149EGYQNRLKVLYSQKAubiquitination[1, 7]
155LKVLYSQKATPGSSRubiquitination[1, 2, 3, 4, 5, 7]
259LWDVQQQKRLRNMTSubiquitination[1, 2, 3, 4, 5, 6]
435WKYPTMAKVAELKGHubiquitination[2]
440MAKVAELKGHTSRVLubiquitination[1, 2, 5]
485ARRREREKASAAKSSubiquitination[1, 2, 3, 4, 5, 8, 9, 10, 11]
490REKASAAKSSLIHQGubiquitination[1, 2, 3, 4, 5, 7, 8, 9, 10, 11]
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] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [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] 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]
 [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] 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]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] 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]
 [11] 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] 
Functional Description
 Required for full ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) and may confer substrate specificity upon the complex. Is regulated by MAD2L1: in metaphase the MAD2L1-CDC20-APC/C ternary complex is inactive and in anaphase the CDC20-APC/C binary complex is active in degrading substrates. The CDC20-APC/C complex positively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. CDC20-APC/C-induced degradation of NEUROD2 induces presynaptic differentiation. 
Sequence Annotation
 REPEAT 182 221 WD 1.
 REPEAT 224 263 WD 2.
 REPEAT 266 303 WD 3.
 REPEAT 307 346 WD 4.
 REPEAT 353 395 WD 5.
 REPEAT 397 438 WD 6.
 REPEAT 441 480 WD 7.
 MOD_RES 41 41 Phosphoserine.
 MOD_RES 70 70 Phosphothreonine.
 MOD_RES 72 72 Phosphoserine.
 MOD_RES 92 92 Phosphoserine.
 MOD_RES 106 106 Phosphothreonine.
 MOD_RES 153 153 Phosphoserine.
 MOD_RES 157 157 Phosphothreonine.
 MOD_RES 161 161 Phosphoserine.
 CROSSLNK 485 485 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 490 490 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Differentiation; Isopeptide bond; Mitosis; Neurogenesis; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 499 AA 
Protein Sequence
MAQFAFESDL HSLLQLDAPI PNAPPARWQR KAKEAAGPAP SPMRAANRSH SAGRTPGRTP 60
GKSSSKVQTT PSKPGGDRYI PHRSAAQMEV ASFLLSKENQ PENSQTPTKK EHQKAWALNL 120
NGFDVEEAKI LRLSGKPQNA PEGYQNRLKV LYSQKATPGS SRKTCRYIPS LPDRILDAPE 180
IRNDYYLNLV DWSSGNVLAV ALDNSVYLWS ASSGDILQLL QMEQPGEYIS SVAWIKEGNY 240
LAVGTSSAEV QLWDVQQQKR LRNMTSHSAR VGSLSWNSYI LSSGSRSGHI HHHDVRVAEH 300
HVATLSGHSQ EVCGLRWAPD GRHLASGGND NLVNVWPSAP GEGGWVPLQT FTQHQGAVKA 360
VAWCPWQSNV LATGGGTSDR HIRIWNVCSG ACLSAVDAHS QVCSILWSPH YKELISGHGF 420
AQNQLVIWKY PTMAKVAELK GHTSRVLSLT MSPDGATVAS AAADETLRLW RCFELDPARR 480
REREKASAAK SSLIHQGIR 499 
Gene Ontology
 GO:0005813; C:centrosome; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0005819; C:spindle; TAS:ProtInc.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0051488; P:activation of anaphase-promoting complex activity; IDA:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007094; P:mitotic spindle assembly checkpoint; TAS:Reactome.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0090129; P:positive regulation of synapse maturation; ISS:UniProtKB.
 GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0050773; P:regulation of dendrite development; IEA:Compara.
 GO:0040020; P:regulation of meiosis; IEA:Compara. 
Interpro
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS