CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021265
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Anaphase-promoting complex subunit 1 
Protein Synonyms/Alias
 APC1; Cyclosome subunit 1; Mitotic checkpoint regulator; Testis-specific gene 24 protein 
Gene Name
 ANAPC1 
Gene Synonyms/Alias
 TSG24 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
29PFGRDHCKHHPNALNubiquitination[1]
69QEVTIHEKQKESWQLubiquitination[2]
71VTIHEKQKESWQLRKubiquitination[1]
107VIWSKGSKSQALAVYubiquitination[1]
140ISQDKSEKAYSSNEVubiquitination[2, 3]
184VANVWPTKYGLLFERubiquitination[4]
275VWTLRRVKSEEENVVubiquitination[1, 2, 5]
284EEENVVLKFSEQGGTubiquitination[3]
310AHLRSLSKGDSPVTSubiquitination[1, 2, 3, 5, 6, 7, 8]
379SSHNQSPKRHSISHSubiquitination[1]
429EKNSQASKVFITSDLubiquitination[1, 2, 3]
463KFQESNDKTQLIFGSubiquitination[2]
477SVTNIPAKDAAPVEKubiquitination[1, 2]
565PELRDSSKLHDSLYNubiquitination[1]
694LSPVIAPKKARPSETubiquitination[2]
695SPVIAPKKARPSETGubiquitination[1]
905RITIAPQKLQVEQEEubiquitination[1, 2, 7]
985IGRQDLSKQACEGNLubiquitination[1, 9]
1066DHEFIEEKENRLLQLubiquitination[1, 2]
1162SAWIVYNKPKHAELAubiquitination[1]
1648TQWYEQTKEELMAPTubiquitination[1]
1693HLKSILSKDGVLYVKubiquitination[1]
1700KDGVLYVKLRAGQLSubiquitination[1]
1709RAGQLSYKEDPMGWQubiquitination[1, 2, 7]
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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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] 
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 1297 1325 PC 1.
 REPEAT 1366 1404 PC 2.
 REPEAT 1467 1501 PC 3.
 REPEAT 1520 1552 PC 4.
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 60 60 Phosphoserine.
 MOD_RES 202 202 Phosphoserine.
 MOD_RES 286 286 Phosphoserine.
 MOD_RES 291 291 Phosphothreonine.
 MOD_RES 341 341 Phosphoserine.
 MOD_RES 355 355 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 373 373 Phosphoserine.
 MOD_RES 377 377 Phosphoserine.
 MOD_RES 537 537 Phosphothreonine.
 MOD_RES 547 547 Phosphoserine.
 MOD_RES 555 555 Phosphoserine.
 MOD_RES 571 571 Phosphotyrosine.
 MOD_RES 686 686 Phosphoserine.
 MOD_RES 688 688 Phosphoserine.  
Keyword
 Cell cycle; Cell division; Complete proteome; Mitosis; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1944 AA 
Protein Sequence
MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS 60
LQEVTIHEKQ KESWQLRKGV SEIGEDVDYD EELYVAGNMV IWSKGSKSQA LAVYKAFTVD 120
SPVQQALWCD FIISQDKSEK AYSSNEVEKC ICILQSSCIN MHSIEGKDYI ASLPFQVANV 180
WPTKYGLLFE RSASSHEVPP GSPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV 240
DHAMKIVFLN TDPSIVMTYD AVQNVHSVWT LRRVKSEEEN VVLKFSEQGG TPQNVATSSS 300
LTAHLRSLSK GDSPVTSPFQ NYSSIHSQSR STSSPSLHSR SPSISNMAAL SRAHSPALGV 360
HSFSGVQRFN ISSHNQSPKR HSISHSPNSN SNGSFLAPET EPIVPELCID HLWTETITNI 420
REKNSQASKV FITSDLCGQK FLCFLVESQL QLRCVKFQES NDKTQLIFGS VTNIPAKDAA 480
PVEKIDTMLV LEGSGNLVLY TGVVRVGKVF IPGLPAPSLT MSNTMPRPST PLDGVSTPKP 540
LSKLLGSLDE VVLLSPVPEL RDSSKLHDSL YNEDCTFQQL GTYIHSIRDP VHNRVTLELS 600
NGSMVRITIP EIATSELVQT CLQAIKFILP KEIAVQMLVK WYNVHSAPGG PSYHSEWNLF 660
VTCLMNMMGY NTDRLAWTRN FDFEGSLSPV IAPKKARPSE TGSDDDWEYL LNSDYHQNVE 720
SHLLNRSLCL SPSEASQMKD EDFSQNLSLD SSTLLFTHIP AIFFVLHLVY EELKLNTLMG 780
EGICSLVELL VQLARDLKLG PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE 840
PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVSD ESSQYLTRIT 900
IAPQKLQVEQ EENRFSFRHS TSVSSLAERL VVWMTNVGFT LRDLETLPFG IALPIRDAIY 960
HCREQPASDW PEAVCLLIGR QDLSKQACEG NLPKGKSVLS SDVPSGTETE EEDDGMNDMN 1020
HEVMSLIWSE DLRVQDVRRL LQSAHPVRVN VVQYPELSDH EFIEEKENRL LQLCQRTMAL 1080
PVGRGMFTLF SYHPVPTEPL PIPKLNLTGR APPRNTTVDL NSGNIDVPPN MTSWASFHNG 1140
VAAGLKIAPA SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG 1200
HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HIPALLPPTS TELDVPHNVQ VAAVVGIGLV 1260
YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL ALGMVCLGHG SNLIGMSDLN 1320
VPEQLYQYMV GGHRRFQTGM HREKHKSPSY QIKEGDTINV DVTCPGATLA LAMIYLKTNN 1380
RSIADWLRAP DTMYLLDFVK PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS 1440
LSEIELPCSE DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFNCLHK FAKDFMTYLS 1500
APNASVTGPH NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM NYGFHLAHHM 1560
ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR YHLQALRHLY VLAAEPRLLV 1620
PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL 1680
SKGTQHLKSI LSKDGVLYVK LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISA 1740
FTSDPALLSF AEYFCKPTVN MGQKQEILDL FSSVLYECVT QETPEMLPAY IAMDQAIRRL 1800
GRREMSETSE LWQIKLVLEF FSSRSHQERL QNHPKRGLFM NSEFLPVVKC TIDNTLDQWL 1860
QVGGDMCVHA YLSGQPLEES QLSMLACFLV YHSVPAPQHL PPIGLEGSTS FAELLFKFKQ 1920
LKMPVRALLR LAPLLLGNPQ PMVM 1944 
Gene Ontology
 GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 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: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. 
Interpro
 IPR024990; Apc1. 
Pfam
 PF12859; Apc1 
SMART
  
PROSITE
  
PRINTS