Aliases:This biomarker is also known as:
- Alcohol dehydrogenase 5,
- formaldehyde dehydrogenase,
- Alcohol dehydrogenase class-III,
- Alcohol dehydrogenase class chi chain,
- alcohol dehydrogenase class-III,
- Glutathione-dependent formaldehyde dehydrogenase,
- alcohol dehydrogenase class chi chain,
- glutathione-dependent formaldehyde dehydrogenase,
- alcohol dehydrogenase (class III), chi polypeptide,
- alcohol dehydrogenase class-3,
- alcohol dehydrogenase 5 (class III), chi polypeptide,
- EC 126.96.36.199,EC 1.1.1.-,EC 188.8.131.524,
- S-(hydroxymethyl)glutathione dehydrogenase,
ADH5 is a member of the alcohol dehydrogenase family. This protein forms a homodimer. ADH5 is ineffective in oxidizing ethanol, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. There are several non-transcribed pseuodogenes related to this gene.
There are no datasets associated with this biomarker.
The following organs have data associated with this biomarker…
|QA State:||Under Review|
No additional breast data available.
ADH5 was one of numerous potential early detection biomarkers specific to triple-negative breast cancer in multiple pathways identified.
- Discovery and preliminary confirmation of novel early detection biomarkers for triple-negative breast cancer using preclinical plasma samples from the Women's Health Initiative observational study.
- Plasma biomarker profiles differ depending on breast cancer subtype but RANTES is consistently increased.
|UniProt Accession #:||P11766|
|Mutated Sites Count:||37|
|Associated Pubmed ID Count||4|
|Affected Protein Function Sites Count:||5|