CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005852
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle protein 27 homolog 
Protein Synonyms/Alias
 Anaphase-promoting complex subunit 3; APC3; CDC27 homolog; CDC27Hs; H-NUC 
Gene Name
 CDC27 
Gene Synonyms/Alias
 ANAPC3; D0S1430E; D17S978E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
99LSGGVFNKQKSHDDIubiquitination[1, 2]
330RIGQTGTKSVFSQSGubiquitination[2, 3]
415KTKSKTNKGGITQPNubiquitination[2]
431NDSLEITKLDSSIISubiquitination[2, 4]
441SSIISEGKISTITPQubiquitination[2]
557VALSVLSKDLTDMDKubiquitination[2]
588REHDIAIKFFQRAIQubiquitination[1]
694KALDTLNKAIVIDPKubiquitination[1, 2]
718SVLFANEKYKSALQEubiquitination[2]
720LFANEKYKSALQELEubiquitination[2]
730LQELEELKQIVPKESubiquitination[2]
735ELKQIVPKESLVYFLubiquitination[1]
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] 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]
 [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
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 84 114 TPR 1.
 REPEAT 115 148 TPR 2.
 REPEAT 499 532 TPR 3.
 REPEAT 567 600 TPR 4.
 REPEAT 602 634 TPR 5.
 REPEAT 635 668 TPR 6.
 REPEAT 670 702 TPR 7.
 REPEAT 704 736 TPR 8.
 REPEAT 737 770 TPR 9.
 MOD_RES 205 205 Phosphothreonine.
 MOD_RES 209 209 Phosphothreonine.
 MOD_RES 244 244 Phosphothreonine.
 MOD_RES 291 291 Phosphoserine.
 MOD_RES 313 313 Phosphothreonine.
 MOD_RES 339 339 Phosphoserine.
 MOD_RES 366 366 Phosphothreonine.
 MOD_RES 386 386 Phosphoserine.
 MOD_RES 426 426 Phosphoserine.
 MOD_RES 430 430 Phosphothreonine.
 MOD_RES 435 435 Phosphoserine.
 MOD_RES 438 438 Phosphoserine.
 MOD_RES 446 446 Phosphothreonine.
 MOD_RES 821 821 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 824 AA 
Protein Sequence
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL 60
LKGHSCTTPQ CKYLLAKCCV DLSKLAEGEQ ILSGGVFNKQ KSHDDIVTEF GDSACFTLSL 120
LGHVYCKTDR LAKGSECYQK SLSLNPFLWS PFESLCEIGE KPDPDQTFKF TSLQNFSNCL 180
PNSCTTQVPN HSLSHRQPET VLTETPQDTI ELNRLNLESS NSKYSLNTDS SVSYIDSAVI 240
SPDTVPLGTG TSILSKQVQN KPKTGRSLLG GPAALSPLTP SFGILPLETP SPGDGSYLQN 300
YTNTPPVIDV PSTGAPSKKS VARIGQTGTK SVFSQSGNSR EVTPILAQTQ SSGPQTSTTP 360
QVLSPTITSP PNALPRRSSR LFTSDSSTTK ENSKKLKMKF PPKIPNRKTK SKTNKGGITQ 420
PNINDSLEIT KLDSSIISEG KISTITPQIQ AFNLQKAAAE GLMSLLREMG KGYLALCSYN 480
CKEAINILSH LPSHHYNTGW VLCQIGRAYF ELSEYMQAER IFSEVRRIEN YRVEGMEIYS 540
TTLWHLQKDV ALSVLSKDLT DMDKNSPEAW CAAGNCFSLQ REHDIAIKFF QRAIQVDPNY 600
AYAYTLLGHE FVLTEELDKA LACFRNAIRV NPRHYNAWYG LGMIYYKQEK FSLAEMHFQK 660
ALDINPQSSV LLCHIGVVQH ALKKSEKALD TLNKAIVIDP KNPLCKFHRA SVLFANEKYK 720
SALQELEELK QIVPKESLVY FLIGKVYKKL GQTHLALMNF SWAMDLDPKG ANNQIKEAID 780
KRYLPDDEEP ITQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF 824 
Gene Ontology
 GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
 GO:0005813; C:centrosome; IDA:MGI.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005876; C:spindle microtubule; IDA:MGI.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
 GO:0008283; P:cell proliferation; TAS:ProtInc.
 GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:MGI.
 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
 IPR026803; CDC27.
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR013105; TPR_2.
 IPR019734; TPR_repeat. 
Pfam
 PF00515; TPR_1
 PF07719; TPR_2 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS