CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013496
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-acetyltransferase ESCO2 
Protein Synonyms/Alias
 Establishment of cohesion 1 homolog 2; ECO1 homolog 2 
Gene Name
 ESCO2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
111ESRSTCLKTNDEDKSacetylation[1]
237LGRTQKSKSEVIEDSubiquitination[2]
252DVETVSEKKTFATRQubiquitination[2]
303SKEHKVDKNEAFSSEubiquitination[2]
498CLIAEPIKQAFRVLSubiquitination[3]
Reference
 [1] 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]
 [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
Functional Description
 Acetyltransferase required for the establishment of sister chromatid cohesion. Couples the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during the S phase. Acetylates the cohesin component SMC3. 
Sequence Annotation
 ZN_FING 387 411 CCHH-type.
 MOD_RES 29 29 Phosphoserine.
 MOD_RES 75 75 Phosphoserine.
 MOD_RES 244 244 Phosphoserine.  
Keyword
 Acyltransferase; Cell cycle; Chromosome; Complete proteome; Disease mutation; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 601 AA 
Protein Sequence
MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS QQEHFVLSAL 60
KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK LIKESRSTCL KTNDEDKSFP 120
IVTEKMQGKP VCSKKNNKKP QKSLTAKYQP KYRHIKPVSR NSRNSKQNRV IYKPIVEKEN 180
NCHSAENNSN APRVLSQKIK PQVTLQGGAA FFVRKKSSLR KSSLENEPSL GRTQKSKSEV 240
IEDSDVETVS EKKTFATRQV PKCLVLEEKL KIGLLSASSK NKEKLIKDSS DDRVSSKEHK 300
VDKNEAFSSE DSLGENKTIS PKSTVYPIFS ASSVNSKRSL GEEQFSVGSV NFMKQTNIQK 360
NTNTRDTSKK TKDQLIIDAG QKHFGATVCK SCGMIYTASN PEDEMQHVQH HHRFLEGIKY 420
VGWKKERVVA EFWDGKIVLV LPHDPSFAIK KVEDVQELVD NELGFQQVVP KCPNKIKTFL 480
FISDEKRVVG CLIAEPIKQA FRVLSEPIGP ESPSSTECPR AWQCSDVPEP AVCGISRIWV 540
FRLKRRKRIA RRLVDTLRNC FMFGCFLSTD EIAFSDPTPD GKLFATKYCN TPNFLVYNFN 600
S 601 
Gene Ontology
 GO:0000785; C:chromatin; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0034421; P:post-translational protein acetylation; IMP:UniProtKB.
 GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. 
Interpro
 IPR026656; AcTrfase_ESCO. 
Pfam
  
SMART
  
PROSITE
  
PRINTS