Overview
| Uniprot ID | P13051 |
|---|
| Protein Name | Uracil-DNA glycosylase |
|---|
| Gene Name | UNG |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 78 |
LDRIQRNKAAALLRL |
Function
Uracil-DNA glycosylase that hydrolyzes the N-glycosidic bond between uracil and deoxyribose in single- and double-stranded DNA (ssDNA and dsDNA) to release a free uracil residue and form an abasic (apurinic/apyrimidinic; AP) site. Excises uracil residues arising as a result of misincorporation of dUMP residues by DNA polymerase during replication or due to spontaneous or enzymatic deamination of cytosine (PubMed:12958596, PubMed:15967827, PubMed:17101234, PubMed:22521144, PubMed:7671300, PubMed:8900285, PubMed:9016624, PubMed:9776759). Mediates error-free base excision repair (BER) of uracil at replication forks. According to the model, it is recruited by PCNA to S-phase replication forks to remove misincorporated uracil at U:A base mispairs in nascent DNA strands. Via trimeric RPA it is recruited to ssDNA stretches ahead of the polymerase to allow detection and excision of deaminated cytosines prior to replication. The resultant AP sites temporarily stall replication, allowing time to repair the lesion (PubMed:22521144). Mediates mutagenic uracil processing involved in antibody affinity maturation. Processes AICDA-induced U:G base mispairs at variable immunoglobulin (Ig) regions leading to the generation of transversion mutations (PubMed:12958596). Operates at switch sites of Ig constant regions where it mediates Ig isotype class switch recombination. Excises AICDA-induced uracil residues forming AP sites that are subsequently nicked by APEX1 endonuclease. The accumulation of staggered nicks in opposite strands results in double strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity) (PubMed:12958596)
Protein Sequence
10
MIGQKTLYSF
20
FSPSPARKRH
30
APSPEPAVQG
40
TGVAGVPEES
50
GDAAAIPAKK
60
APAGQEEPGT
70
PPSSPLSAEQ
80
LDRIQRNKAA
90
ALLRLAARNV
100
PVGFGESWKK
110
HLSGEFGKPY
120
FIKLMGFVAE
130
ERKHYTVYPP
140
PHQVFTWTQM
150
CDIKDVKVVI
160
LGQDPYHGPN
170
QAHGLCFSVQ
180
RPVPPPPSLE
190
NIYKELSTDI
200
EDFVHPGHGD
210
LSGWAKQGVL
220
LLNAVLTVRA
230
HQANSHKERG
240
WEQFTDAVVS
250
WLNQNSNGLV
260
FLLWGSYAQK
270
KGSAIDRKRH
280
HVLQTAHPSP
290
LSVYRGFFGC
300
RHFSKTNELL
310
QKSGKKPIDW
KEL
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0003684 |
damaged DNA binding |
| Molecular Function |
GO:0043024 |
ribosomal small subunit binding |
| Molecular Function |
GO:0004844 |
uracil DNA N-glycosylase activity |
| Biological Process |
GO:0006284 |
base-excision repair |
| Biological Process |
GO:0097510 |
base-excision repair, AP site formation via deaminated base removal |
| Biological Process |
GO:0045008 |
depyrimidination |
| Biological Process |
GO:0043066 |
negative regulation of apoptotic process |
| Biological Process |
GO:0000012 |
single strand break repair |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.