Ppm1a Gene Summary [Rat]
Enables phosphoprotein phosphatase activity and transmembrane transporter binding activity. Predicted to be involved in positive regulation of DNA-templated transcription; protein modification process; and regulation of signal transduction. Predicted to act upstream of or within cellular response to transforming growth factor beta stimulus; negative regulation of BMP signaling pathway; and positive regulation of protein export from nucleus. Located in neuron projection. Orthologous to human PPM1A (protein phosphatase, Mg2+/Mn2+ dependent 1A). [provided by Alliance of Genome Resources, Apr 2025]
Details
| Type | Protein Coding |
| Official Symbol | Ppm1a |
| Official Name | protein phosphatase, Mg2+/Mn2+ dependent, 1A [Source:RGD Symbol;Acc:3373] |
| Ensembl ID | ENSRNOG00000005916 |
| Bio databases IDs | |
| Aliases | protein phosphatase, Mg2+/Mn2+ dependent, 1A |
| Synonyms | 2310003C21RIK, 2900017D14Rik, MMPa-2, MPPa-1, Pp2c1, PP2CA, PP2C-ALPHA, PP2C-α, protein phosphatase 1A, magnesium dependent, alpha isoform, protein phosphatase 1A, magnesium dependent, α isoform, protein phosphatase, Mg2+/Mn2+ dependent 1A, protein phosphatase, Mg2+/Mn2+ dependent, 1A |
| Species | Rat, Rattus norvegicus |
| 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 rat Ppm1a often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- SMAD binding
- Protein phosphatase 2C
- protein serine/threonine phosphatase
- protein phosphatase
- phosphoprotein phosphatase
- calcium-dependent protein serine/threonine phosphatase
- phosphatase
- ion channel binding
- Protein serine/threonine phosphatase 2C, C-terminal domain
- protein binding
- Serine/threonine phosphatases, family 2C, catalytic domain
- PP2Cc
Pathways
Biological processes and signaling networks where the Ppm1a gene in rat 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
- acute inflammation
- dextran sodium sulfate-induced colitis
- renal agenesis
role in cell
- expression in
- proliferation
- growth
- apoptosis
- survival
- activation in
- phosphorylation in
- migration
- cell cycle progression
- G2/M phase
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
- cellular membrane
- Nucleus
- Plasma Membrane
- cytosol
- nucleoplasm
- neurites
- cytosolic fraction
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Ppm1a gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- peptidyl-threonine dephosphorylation
- positive regulation of protein export from nucleus
- protein dephosphorylation
- positive regulation of canonical Wnt receptor signaling pathway
- positive regulation of I-kappaB kinase/NF-kappaB cascade
- negative regulation of I-kappaB kinase/NF-kappaB cascade
- protein export from nucleus
- N-terminal protein myristoylation
- negative regulation of BMP signaling pathway
- negative regulation of transcription from RNA polymerase II promoter
- cellular response to transforming growth factor beta stimulus
- positive regulation of transcription, DNA-dependent
- regulation of cell cycle
- dephosphorylation
- negative regulation of transforming growth factor beta receptor signaling pathway
Cellular Component
Where in the cell the gene product is active
- nucleus
- membrane
- cytosol
- plasma membrane
- nucleoplasm
Molecular Function
What the gene product does at the molecular level
- protein serine/threonine phosphatase activity
- magnesium ion binding
- calmodulin-dependent protein phosphatase activity
- protein binding
- R-SMAD binding
- manganese ion binding
- myosin phosphatase activity