CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004016
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Uracil-DNA glycosylase 
Protein Synonyms/Alias
 UDG 
Gene Name
 ung 
Gene Synonyms/Alias
 b2580; JW2564 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
15HDVLAEEKQQPYFLNacetylation[1]
42VTIYPPQKDVFNAFRacetylation[2]
147GWETFTDKVISLINQacetylation[2]
170LWGSHAQKKGAIIDKacetylation[2]
177KKGAIIDKQRHHVLKacetylation[2]
184KQRHHVLKAPHPSPLacetylation[2]
Reference
 [1] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111]
 [2] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618
Functional Description
 Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. 
Sequence Annotation
 ACT_SITE 64 64 Proton acceptor.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Glycosidase; Hydrolase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 229 AA 
Protein Sequence
MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI 60
LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL 120
LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH 180
HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE 229 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
 GO:0006284; P:base-excision repair; IEA:InterPro. 
Interpro
 IPR018085; Ura-DNA_Glyclase_AS.
 IPR002043; Ura_DNA_glycsylse.
 IPR005122; Uracil-DNA_glycosylase-like. 
Pfam
 PF03167; UDG 
SMART
 SM00986; UDG 
PROSITE
 PS00130; U_DNA_GLYCOSYLASE 
PRINTS