CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023053
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle protein 23 homolog 
Protein Synonyms/Alias
 Anaphase-promoting complex subunit 8; APC8; Cyclosome subunit 8 
Gene Name
 CDC23 
Gene Synonyms/Alias
 ANAPC8 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
34SDLREIKKQLLLIAGubiquitination[1]
97AKAYFDVKEYDRAAHubiquitination[1, 2]
129RYLSGEKKKDDETVDubiquitination[1]
130YLSGEKKKDDETVDSubiquitination[1]
143DSLGPLEKGQVKNEAubiquitination[2, 3, 4]
147PLEKGQVKNEALRELubiquitination[1, 2, 3]
281HNIRDIDKALSIFNEubiquitination[2]
291SIFNELRKQDPYRIEubiquitination[1]
313LLYVRSMKSELSYLAubiquitination[1, 3]
328HNLCEIDKYRVETCCubiquitination[1]
349SLRSQHEKAALYFQRubiquitination[2, 3, 5]
359LYFQRALKLNPRYLGubiquitination[1, 2, 5]
396RHAIEVNKRDYRAWYubiquitination[1, 2, 5, 6]
445ALGECYEKLNQLVEAubiquitination[1, 3]
453LNQLVEAKKCYWRAYubiquitination[1, 2, 4, 5]
454NQLVEAKKCYWRAYAubiquitination[1, 5]
467YAVGDVEKMALVKLAacetylation[5, 7, 8]
467YAVGDVEKMALVKLAubiquitination[1, 2, 5, 9]
472VEKMALVKLAKLHEQubiquitination[1, 3, 6]
475MALVKLAKLHEQLTEubiquitination[1]
522YLAQYYFKCKLWDEAubiquitination[1]
535EASTCAQKCCAFNDTubiquitination[1, 3, 5]
547NDTREEGKALLRQILubiquitination[1, 2]
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] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] 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] 
Functional Description
 Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. 
Sequence Annotation
 REPEAT 83 116 TPR 1.
 REPEAT 169 202 TPR 2.
 REPEAT 228 261 TPR 3.
 REPEAT 263 296 TPR 4.
 REPEAT 331 364 TPR 5.
 REPEAT 366 398 TPR 6.
 REPEAT 400 432 TPR 7.
 REPEAT 433 466 TPR 8.
 REPEAT 468 500 TPR 9.
 MOD_RES 273 273 Phosphotyrosine.
 MOD_RES 467 467 N6-acetyllysine.
 MOD_RES 562 562 Phosphothreonine.
 MOD_RES 565 565 Phosphothreonine.
 MOD_RES 578 578 Phosphoserine.
 MOD_RES 582 582 Phosphothreonine.
 MOD_RES 588 588 Phosphoserine.
 MOD_RES 593 593 Phosphoserine.
 MOD_RES 596 596 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Mitosis; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 597 AA 
Protein Sequence
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF 60
SLPALPLAEL QPPPPITEED AQDMDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY 120
SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSK KHQARELDGF GLYLYGVVLR 180
KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE 240
LQLIEEALQK YQNLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM 300
DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL 360
NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY 420
YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKMAL VKLAKLHEQL 480
TESEQAAQCY IKYIQDIYSC GEIVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN 540
DTREEGKALL RQILQLRNQG ETPTTEVPAP FFLPASLSAN NTPTRRVSPL NLSSVTP 597 
Gene Ontology
 GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004842; F:ubiquitin-protein ligase activity; TAS:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000080; P:G1 phase of mitotic cell cycle; IDA:UniProtKB.
 GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; TAS:ProtInc.
 GO:0007080; P:mitotic metaphase plate congression; IDA:UniProtKB.
 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:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
 GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc. 
Interpro
 IPR007192; APC8.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF04049; APC8
 PF00515; TPR_1 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS