Asph Gene Summary [Mouse]
Predicted to enable calcium ion binding activity and peptidyl-aspartic acid 3-dioxygenase activity. Involved in regulation of protein depolymerization and regulation of protein stability. Acts upstream of or within several processes, including face morphogenesis; limb morphogenesis; and peptidyl-aspartic acid hydroxylation. Located in cytoplasm. Is expressed in several structures, including cerebellum; eye; face; heart; and limb. Human ortholog(s) of this gene implicated in cholangiocarcinoma. Orthologous to human ASPH (aspartate beta-hydroxylase). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Processed Transcript |
| Official Symbol | Asph |
| Official Name | aspartate-beta-hydroxylase [Source:MGI Symbol;Acc:MGI:1914186] |
| Ensembl ID | ENSMUSG00000028207 |
| Bio databases IDs | |
| Aliases | aspartate-beta-hydroxylase |
| Synonyms | 2310005F16Rik, 3110001L23Rik, AAH, aspartate-beta-hydroxylase, aspartate-β-hydroxylase, Aspartyl beta Hydroxylase, Aspartyl β Hydroxylase, BAH, C79816, CASQ2BP1, cI-37, D7Mgi29, FDLAB, HAAH, JCTN, Junctin, LOC100910356 |
| Species | Mouse, Mus musculus |
| 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 mouse Asph often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- EF-Hand
- Aspartyl beta-hydroxylase N-terminal region
- electron carrier
- TPR repeat
- peptide-aspartate beta-dioxygenase
- 2-oxoglutarate:oxygen oxidoreductase
- calcium ion binding
- enzyme
- protein binding
- endoplasmic reticulum lumenal domain
- structural constituent of muscle
- tol-pal system protein YbgF
- transmembrane domain
- ion channel binding
- structural molecule
- tetratricopeptide repeat
- Aspartyl/Asparaginyl beta-hydroxylase
Pathways
Biological processes and signaling networks where the Asph gene in mouse plays a role, providing insight into its function and relevance in health or disease.
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- neoplasia
- intestinal gastric adenocarcinoma
- intestinal gastric cancer
- exertional heat stroke
- ectopia lentis, spontaneous filtering blebs, and craniofacial dysmorphism
- organismal death
- liver cancer
- epithelial cancer
- hepatocellular carcinoma
- colorectal cancer
role in cell
- expression in
- growth
- migration
- proliferation
- activation in
- function
- transformation
- invasion by
- angiogenesis by
- response by
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
- Cytoplasm
- pH resistant lipid raft fraction
- detergent resistant lipid raft fraction
- cortical endoplasmic reticulum
- cellular membrane
- Plasma Membrane
- sarcoplasmic reticulum
- Endoplasmic Reticulum
- endoplasmic reticulum membrane
- myofibrils
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the mouse Asph gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- cell proliferation
- regulation of protein stability
- activation of cysteine-type endopeptidase activity
- muscle contraction
- negative regulation of cell proliferation
- palate development
- peptidyl-aspartic acid hydroxylation
- limb morphogenesis
- pattern specification process
- positive regulation of proteolysis
- face morphogenesis
Cellular Component
Where in the cell the gene product is active
- endoplasmic reticulum membrane
- endoplasmic reticulum
- cortical endoplasmic reticulum
- plasma membrane
- sarcoplasmic reticulum membrane
Molecular Function
What the gene product does at the molecular level
- protein binding
- structural constituent of muscle
- electron carrier activity
- calcium ion binding
- structural molecule activity