PHYHD1 Gene Summary [Human]
Enables 2-oxoglutarate-dependent dioxygenase activity. [provided by Alliance of Genome Resources, Apr 2022]
Details
| Type | Protein Coding |
| Official Symbol | PHYHD1 |
| Official Name | phytanoyl-CoA dioxygenase domain containing 1 [Source:HGNC Symbol;Acc:HGNC:23396] |
| Ensembl ID | ENSG00000175287 |
| Bio databases IDs | |
| Aliases | phytanoyl-CoA dioxygenase domain containing 1 |
| Synonyms | phytanoyl-CoA dioxygenase domain containing 1 |
| 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 PHYHD1 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- 2-oxoglutarate:oxygen oxidoreductase
- enzyme
- protein binding
- 2OG-Fe(II) oxygenase superfamily
- Phytanoyl-CoA dioxygenase (PhyH)
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
regulated by
disease
- epithelial cancer
- rectum cancer
- colon adenocarcinoma
- liver cancer
- prostate cancer
- colon epithelial cancer
- urothelial bladder carcinoma
- transitional cell bladder cancer
- hepatocellular carcinoma
- renal clear cell adenocarcinoma
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Unknown
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human PHYHD1 gene, providing context for its role in the cell.
Molecular Function
What the gene product does at the molecular level
- protein binding
- metal ion binding
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors