Uracil-DNA glycosylase
Matched no rule. Shown as-is rather than assigned a class by guesswork. Values below are reported as measured; because this is not a molecular target, they are not treated as affinities anywhere on this site.
- Measurements
- 2
- Compounds
- 2
- Binding constants
- 0
- Median pX
- —
I · Identity
What this target is
Its function as UniProt states it, where in a cell the protein is found, and which cell types and tissues transcribe its gene.
Uracil-DNA glycosylase
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 cytosine12958596,15967827,17101234,22521144,7671300,8900285,9016624,9776759. 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 lesion22521144. 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 mutations12958596. 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)12958596
Quoted from UniProt’s FUNCTION annotation for P13051 (reviewed). The superscript numbers are UniProt’s own PubMed citations, kept in the sentence and in order, each linking to the paper it names.
What it acts with
STRING’s highest-confidence human functional partners. The combined score mixes several kinds of evidence, so each channel is shown separately — a partner supported by experiment is a different claim from one supported only by text mining, and for a receptor this is where its coupling appears as evidence rather than as assertion.
Where it sits in the cell
- Nucleoplasm
- Mitochondriaadditional
Human Protein Atlas, by antibody immunofluorescence in cell lines — a different assay from the expression figures below, which are RNA.
UniProt, curated Mitochondrion · Nucleus
Expression by cell type
Single cell type RNA, the 5 highest of those the Human Protein Atlas reports for this gene. Transcript, not protein, and a cell type rather than a tissue.
- Oocytes170.4 nCPM
- Differentiating spermatogonia107.5 nCPM
- Migrating cytotrophoblasts84.8 nCPM
- Parietal cells79.6 nCPM
- Cytotrophoblasts76.2 nCPM
IV · Evidence
Every measurement at this target
Each row links to the ChEMBL assay it came from.
Other measurements 2
Everything else ChEMBL recorded for this compound — percentage inhibition, efficacy, half-life, cytotoxicity. Reported in the assay's own units, which is why no value is converted here.
| Target | Class | Type | Value (nM) | pX | Organism | Assay |
|---|---|---|---|---|---|---|
| Uracil-DNA glycosylase | Unclassified | Inhibition | — no normalized value | — value does not convert to pX | Homo sapiens | CHEMBL5665453 |
| Uracil-DNA glycosylase | Unclassified | Inhibition | — no normalized value | — value does not convert to pX | Homo sapiens | CHEMBL5665453 |