UniProt Accession

 UNG_HUMAN; P13051; A8K5M6; B2R8Y1; O00637; O00719; Q93028 

Genbank Protein ID

 X15653; X89398; X89398; Y09008; AF526277; AK291341; AK313552; CH471054; CH471054; BC015205; BC050634 

Genbank Nucleotide ID

 CAA33679.1; CAA61578.1; CAA61579.1; CAA70211.1; AAM77695.1; BAF84030.1; BAG36328.1; EAW97846.1; EAW97847.1; AAH15205.1; AAH50634.1 

Protein Name

 Uracil-DNA glycosylase 

Protein Synonyms/Alias

 UDG 

Gene Name

 UNG 

Gene Synonyms/Alias

 DGU; UNG1; UNG15 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MIGQKTLYSFFS	acetylation	[1]
5	***MIGQKTLYSFFS	ubiquitination	[2, 3, 4, 5]
49	DAAAIPAKKAPAGQE	ubiquitination	[6]
78	LDRIQRNKAAALLRL	ubiquitination	[3, 4]
108	HLSGEFGKPYFIKLM	ubiquitination	[4]
295	FGCRHFSKTNELLQK	acetylation	[1]
295	FGCRHFSKTNELLQK	ubiquitination	[6]
302	KTNELLQKSGKKPID	ubiquitination	[6]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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] 

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

 REGION 1 25 FAM72A-binding.
 ACT_SITE 154 154 Proton acceptor (By similarity).
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 23 23 Phosphoserine.
 MOD_RES 60 60 Phosphothreonine.
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 295 295 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; DNA damage; DNA repair; Glycosidase; Host-virus interaction; Hydrolase; Mitochondrion; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 313 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0004844; F:uracil DNA N-glycosylase activity; NAS:UniProtKB.
 GO:0006284; P:base-excision repair; TAS:ProtInc.
 GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Compara.
 GO:0016447; P:somatic recombination of immunoglobulin gene segments; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

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