CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014782
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cell division cycle-associated protein 2 
Protein Synonyms/Alias
 Recruits PP1 onto mitotic chromatin at anaphase protein; Repo-Man 
Gene Name
 CDCA2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
182EMTDLTRKEGLSACQubiquitination[1, 2]
284VADCVVGKGSSDAVSubiquitination[2]
323RRDLPTPKTFVLRSVubiquitination[1, 3]
575KGKKSVQKSLYGERDubiquitination[1]
622GYFSSNGKLEEVKTPacetylation[4]
627NGKLEEVKTPKNPVKacetylation[4]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Regulator of chromosome structure during mitosis required for condensin-depleted chromosomes to retain their compact architecture through anaphase. Acts by mediating the recruitment of phopsphatase PP1-gamma subunit (PPP1CC) to chromatin at anaphase and into the following interphase. At anaphase onset, its association with chromatin targets a pool of PPP1CC to dephosphorylate substrates. 
Sequence Annotation
 MOTIF 392 395 PP1-binding motif.
 MOD_RES 98 98 Phosphoserine.
 MOD_RES 120 120 Phosphoserine.
 MOD_RES 126 126 Phosphoserine.
 MOD_RES 131 131 Phosphoserine.
 MOD_RES 291 291 Phosphoserine.
 MOD_RES 309 309 Phosphoserine.
 MOD_RES 312 312 Phosphothreonine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 407 407 Phosphoserine.
 MOD_RES 412 412 Phosphothreonine.
 MOD_RES 437 437 Phosphoserine.
 MOD_RES 591 591 Phosphoserine.
 MOD_RES 756 756 Phosphoserine.
 MOD_RES 936 936 Phosphoserine.
 MOD_RES 977 977 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1023 AA 
Protein Sequence
MDANSKDKPP ETKESAMNNA GNASFILGTG KIVTPQKHAE LPPNPCTPDT FKSPLNFSTV 60
TVEQLGITPE SFVRNSAGKS SSYLKKCRRR SAVGARGSPE TNHLIRFIAR QQNIKNARKS 120
PLAQDSPSQG SPALYRNVNT LRERISAFQS AFHSIKENEK MTGCLEFSEA GKESEMTDLT 180
RKEGLSACQQ SGFPAVLSSK RRRISYQRDS DENLTDAEGK VIGLQIFNID TDRACAVETS 240
VDLSEISSKL GSTQSGFLVE ESLPLSELTE TSNALKVADC VVGKGSSDAV SPDTFTAEVS 300
SDAVPDVRSP ATPACRRDLP TPKTFVLRSV LKKPSVKMCL ESLQEHCNNL YDDDGTHPSL 360
ISNLPNCCKE KEAEDEENFE APAFLNMRKR KRVTFGEDLS PEVFDESLPA NTPLRKGGTP 420
VCKKDFSGLS SLLLEQSPVP EPLPQPDFDD KGENLENIEP LQVSFAVLSS PNKSSISETL 480
SGTDTFSSSN NHEKISSPKV GRITRTSNRR NQLVSVVEES VCNLLNTEVQ PCKEKKINRR 540
KSQETKCTKR ALPKKSQVLK SCRKKKGKGK KSVQKSLYGE RDIASKKPLL SPIPELPEVP 600
EMTPSIPSIR RLGSGYFSSN GKLEEVKTPK NPVKRKDLLR HDPDLHMHQG YDKYDVSEFC 660
SYIKSSSSLG NATSDEDPNT NIMNINENKN IPKAKNKSES ENEPKAGTDS PVSCASVTEE 720
RVASDSPKPA LTLQQGQEFS AGGQNAENLC QFFKISPDLN IKCERKDDFL GAAEGKLQCN 780
RLMPNSQKDC HCLGDVLIEN TKESKSQSED LGRKPMESSS VVSCRDRKDR RRSMCYSDGR 840
SLHLEKNGNH TPSSSVGSSV EISLENSELF KDLSDAIEQT FQRRNSETKV RRSTRLQKDL 900
ENEGLVWISL PLPSTSQKAK RRTICTFDSS GFESMSPIKE TVSSRQKPQM APPVSDPENS 960
QGPAAGSSDE PGKRRKSFCI STLANTKATS QFKGYRRRSS LNGKGESSLT ALERIEHNGE 1020
RKQ 1023 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW. 
Interpro
 IPR026149; Cdca2. 
Pfam
  
SMART
  
PROSITE
  
PRINTS