CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023055
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Anaphase-promoting complex subunit 7 
Protein Synonyms/Alias
 APC7; Cyclosome subunit 7 
Gene Name
 ANAPC7 
Gene Synonyms/Alias
 APC7 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99EYRNAVSKYTMALQQubiquitination[1, 2, 3, 4, 5, 6, 7]
107YTMALQQKKALSKTSubiquitination[2]
115KALSKTSKVRPSTGNubiquitination[5]
139LPSEIEVKYKMAECYubiquitination[5]
153YTMLKQDKDAIAILDubiquitination[2, 5]
181MLANLYKKAGQERPSubiquitination[5]
193RPSVTSYKEVLRQCPubiquitination[2, 5]
263STICSLEKKSLLRDNacetylation[8, 9, 10]
263STICSLEKKSLLRDNubiquitination[5]
264TICSLEKKSLLRDNVubiquitination[5]
288YFRAGDNKNSVLKFEubiquitination[2, 3, 6, 10]
293DNKNSVLKFEQAQMLubiquitination[1, 2, 3, 5, 6, 7, 10]
306MLDPYLIKGMDVYGYubiquitination[2]
353GCHSFYSKRYSRALYubiquitination[5]
364RALYLGAKAIQLNSNubiquitination[2, 5, 11]
379SVQALLLKGAALRNMubiquitination[1, 2, 5, 7, 11, 12]
460EDPVTQEKAKTLLDKubiquitination[5]
462PVTQEKAKTLLDKALubiquitination[5]
467KAKTLLDKALTQRPDubiquitination[1, 2, 5, 7, 12]
477TQRPDYIKAVVKKAEubiquitination[1, 2, 5, 7, 12]
482YIKAVVKKAELLSREubiquitination[5]
491ELLSREQKYEDGIALubiquitination[1, 2, 5, 7]
551KSLEGMQKMEKEESPubiquitination[2, 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] 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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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 77 110 TPR 1.
 REPEAT 169 202 TPR 2.
 REPEAT 271 304 TPR 3.
 REPEAT 373 406 TPR 4.
 REPEAT 441 475 TPR 5.
 REPEAT 476 508 TPR 6.
 REPEAT 509 542 TPR 7.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Mitosis; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 599 AA 
Protein Sequence
MDPGDAAILE SSLRILYRLF ESVLPPLPAA LQSRMNVIDH VRDMAAAGLH SNVRLLSSLL 60
LTMSNNNPEL FSPPQKYQLL VYHADSLFHD KEYRNAVSKY TMALQQKKAL SKTSKVRPST 120
GNSASTPQSQ CLPSEIEVKY KMAECYTMLK QDKDAIAILD GIPSRQRTPK INMMLANLYK 180
KAGQERPSVT SYKEVLRQCP LALDAILGLL SLSVKGAEVA SMTMNVIQTV PNLDWLSVWI 240
KAYAFVHTGD NSRAISTICS LEKKSLLRDN VDLLGSLADL YFRAGDNKNS VLKFEQAQML 300
DPYLIKGMDV YGYLLAREGR LEDVENLGCR LFNISDQHAE PWVVSGCHSF YSKRYSRALY 360
LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI RLAPCRLDCY EGLIECYLAS 420
NSIREAMVMA NNVYKTLGAN AQTLTLLATV CLEDPVTQEK AKTLLDKALT QRPDYIKAVV 480
KKAELLSREQ KYEDGIALLR NALANQSDCV LHRILGDFLV AVNEYQEAMD QYSIALSLDP 540
NDQKSLEGMQ KMEKEESPTD ATQEEDVDDM EGSGEEGDLE GSDSEAAQWA DQEQWFGMQ 599 
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
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR013105; TPR_2.
 IPR019734; TPR_repeat. 
Pfam
 PF07719; TPR_2 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS