Shmt2 Gene Summary [Mouse]
Enables glycine hydroxymethyltransferase activity. Involved in several processes, including formate biosynthetic process; regulation of oxidative phosphorylation; and tetrahydrofolate interconversion. Acts upstream of or within dTMP biosynthetic process. Located in mitochondrial inner membrane. Is active in mitochondrial matrix and nucleus. Is expressed in several structures, including future brain; hepatic primordium; placenta; skeleton; and submandibular gland primordium. Human ortholog(s) of this gene implicated in neurodevelopmental disorder with cardiomyopathy, spasticity, and brain abnormalities. Orthologous to human SHMT2 (serine hydroxymethyltransferase 2). [provided by Alliance of Genome Resources, Jul 2025]
Details
| Type | Protein Coding |
| Official Symbol | Shmt2 |
| Official Name | serine hydroxymethyltransferase 2 (mitochondrial) [Source:MGI Symbol;Acc:MGI:1277989] |
| Ensembl ID | ENSMUSG00000025403 |
| Bio databases IDs | |
| Aliases | serine hydroxymethyltransferase 2 (mitochondrial) |
| Synonyms | 2700043D08Rik, GLYA, HEL-S-51e, mSHMT, NEDCASB, Serine Hydroxymethyltransferase2, serine hydroxymethyltransferase 2 (mitochondrial), SHMT |
| 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 Shmt2 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- pyridoxal phosphate binding
- L-allo-threonine aldolase
- AAT_I
- chromatin binding
- enzyme
- protein binding
- Aminotransferase class I and II
- glycine hydroxymethyltransferase
- identical protein binding
- amino acid binding
Top Findings
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
disease
- breast cancer
- lung cancer
- neoplasia
- small cell lung cancer
- hepatic fibrosis
- prostate cancer
- ovarian cancer
- organismal death
- neurodevelopmental disorder with cardiomyopathy, spasticity, and brain abnormalities
- non-small cell lung cancer
role in cell
- migration
- expression in
- phosphorylation in
- proliferation
- colony formation
- production in
- invasion by
- colony formation by
- glycolysis in
- oxidative phosphorylation in
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
- detergent resistant lipid raft fraction
- microtubule cytoskeleton
- Nucleus
- Mitochondria
- mitochondrial matrix
- mitochondrial nucleoids
- mitochondrial inner membrane
- nuclear envelope
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the mouse Shmt2 gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- regulation of oxidative phosphorylation
- response to type I interferon
- positive regulation of cell proliferation
- L-serine metabolic process
- L-serine biosynthetic process
- tetrahydrofolate metabolic process
- one-carbon metabolic process
- glycine metabolic process
- protein homotetramerization
- protein tetramerization
- glycine biosynthetic process from serine
- tetrahydrofolate interconversion
- protein K63-linked deubiquitination
- regulation of mitochondrial translation
Cellular Component
Where in the cell the gene product is active
- nucleus
- microtubule cytoskeleton
- extracellular vesicular exosome
- mitochondrial matrix
- cytoplasm
- BRISC complex
- mitochondrion
- mitochondrial inner membrane
- mitochondrial nucleoid
Molecular Function
What the gene product does at the molecular level
- pyridoxal phosphate binding
- identical protein binding
- protein binding
- glycine hydroxymethyltransferase activity
- chromatin binding
- amino acid binding
- L-allo-threonine aldolase activity