ADPRH Gene Summary [Human]
The enzyme encoded by this gene catalyzes removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. Unlike the rat and mouse enzymes that require DTT for maximal activity, the human enzyme is DTT-independent. Alternatively spliced transcript variants that encode different protein isoforms have been described. [provided by RefSeq, May 2014]
Details
| Type | Protein Coding |
| Official Symbol | ADPRH |
| Official Name | ADP-ribosylarginine hydrolase [Source:HGNC Symbol;Acc:HGNC:269] |
| Ensembl ID | ENSG00000144843 |
| Bio databases IDs | |
| Aliases | ADP-ribosylarginine hydrolase, [Protein ADP-ribosylarginine] hydrolase |
| Synonyms | ADPRHA, ADP-ribosylarginine hydrolase, ARH1, hARH1 |
| Species | Human, Homo sapiens |
| Orthologies |
Protein Domains
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in human ADPRH often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- ADPribosylarginine hydrolase
- ADP-ribosylglycohydrolase
- metal ion binding
- enzyme
- protein binding
- DraG
- magnesium ion binding
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Extracellular Space
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human ADPRH gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- protein modification process
- protein de-ADP-ribosylation
Cellular Component
Where in the cell the gene product is active
- extracellular space
Molecular Function
What the gene product does at the molecular level
- magnesium ion binding
- ADP-ribosylarginine hydrolase activity
- protein binding
- potassium ion binding