ADO Back

2-aminoethanethiol (cysteamine) dioxygenase

External References:      Wikipedia GeneCards HUGO COSMIC Google Scholar

NCBI Description of ADO

Human thiol dioxygenases include cysteine dioxygenase (CDO; MIM 603943) and cysteamine (2-aminoethanethiol) dioxygenase (ADO; EC 1.13.11.19). CDO adds 2 oxygen atoms to free cysteine, whereas ADO adds 2 oxygen atoms to free cysteamine to form hypotaurine (Dominy et al., 2007 [PubMed 17581819]).[supplied by OMIM, Mar 2008].

Community Annotation of ADO Add / Edit ADO: Annotations

No community annotations yet for ADO.
Sort mutations by: Tumor type  Mutation type  Position  
Straightedge cursor Expand

Figure notes


• "Mouse over" a mutation to see details.
• Missense green saturation indicates evolutionary conservation of the mutated positions.
• Red hashes in protein strip are splice sites.
• Blue-white-red bars are log2 copy ratio distributions (–1 to +1) from Zack et al. (2013).


Legend

ADO is highly significantly mutated in
(none)
ADO is significantly mutated in
(none)
ADO is near significance in
(none)

Click on a tumor type to see its full list of significant genes.

Data details


Mutation list for ADO