Phykpl Gene Summary [Mouse]
This gene overlaps in a tail-to-tail orientation the gene encoding heterogeneous nuclear ribonucleoprotein A/B. The terminal exon of this gene is interspersed with exons of heterogeneous nuclear ribonucleoprotein A/B. [provided by RefSeq, Jul 2008]
Details
| Type | Nonsense Mediated Decay |
| Official Symbol | Phykpl |
| Official Name | 5-phosphohydroxy-L-lysine phospholyase [Source:MGI Symbol;Acc:MGI:1920197] |
| Ensembl ID | ENSMUSG00000020359 |
| Bio databases IDs | |
| Aliases | 5-phosphohydroxy-L-lysine phospholyase |
| Synonyms | 2900006B13Rik, 5-phosphohydroxy-L-lysine phospho-lyase, AGXT2L2, LOC102547782, LOC103693322, PHLU |
| 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 Phykpl often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- adenosylmethionine-8-amino-7-oxononanoate transaminase
- 4-aminobutyrate aminotransferase, eukaryotic type
- Aminotransferase class-III
- transaminase, acetylornithine/succinylornithine family
- AAT_I
- enzyme
- protein binding
- identical protein binding
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
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
- mitochondrial matrix
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the mouse Phykpl gene, providing context for its role in the cell.
Cellular Component
Where in the cell the gene product is active
- mitochondrial matrix
Molecular Function
What the gene product does at the molecular level
- identical protein binding
- pyridoxal phosphate binding
- protein binding
- transaminase activity
- lyase activity