GCLM Gene Summary [Human]
Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase, is the first rate limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. Gamma glutamylcysteine synthetase deficiency has been implicated in some forms of hemolytic anemia. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Apr 2015]
Details
| Type | Protein Coding |
| Official Symbol | GCLM |
| Official Name | glutamate-cysteine ligase modifier subunit [Source:HGNC Symbol;Acc:HGNC:4312] |
| Ensembl ID | ENSG00000023909 |
| Bio databases IDs | |
| Aliases | glutamate-cysteine ligase modifier subunit, gamma-glutamylcysteine synthetase |
| Synonyms | AI649393, Gamma gclm, gamma GCS LIGHT CHAIN, Gamma glutamylcysteine synthase (regulatory), gamma GLUTAMYLCYSTEINE SYNTHETASE, gamma-glutamylcysteine synthetase light (regulatory) subunit, Gcmc, Gcs-ls, Gcs, Regulatory, GLCLR, glutamat-cystein ligase, regulatory subunit, glutamate-cysteine ligase modifier subunit, Glutamate-Cysteine Ligase, Modifier Subunit, γ gclm, γ-GCS, γ GCS LIGHT CHAIN, γ glutamylcysteine synthase (regulatory), γ GLUTAMYLCYSTEINE SYNTHETASE, γ-glutamylcysteine synthetase light (regulatory) subunit |
| 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 GCLM often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
- glutamate-cysteine ligase
- binding protein
- enzyme binding
- enzyme
- protein binding
Pathways
Biological processes and signaling networks where the GCLM gene in human 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
- liver cirrhosis
- susceptibility to myocardial infarction
- gastric adenocarcinoma
- gastric epithelial cancer
- atherosclerosis
- androgenic alopecia
- septic shock
- premature ovarian failure
- hyperzincemia and hypercalprotectinemia autoinflammatory syndrome
role in cell
- apoptosis
- morphology
- depolarization
- activation in
- formation in
- excitotoxicity
- toxicity
- sensitivity
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
- cytosol
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the human GCLM gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
- glutathione biosynthetic process
- cellular response to fibroblast growth factor stimulus
- response to nutrient
- response to xenobiotic stimulus
- cysteine metabolic process
- negative regulation of neuron apoptotic process
- cellular response to follicle-stimulating hormone stimulus
- response to oxidative stress
- cellular response to thyroxine stimulus
- glutamate metabolic process
- apoptotic mitochondrial changes
- cellular response to glucose stimulus
- cellular response to hepatocyte growth factor stimulus
- response to nitrosative stress
- positive regulation of glutamate-cysteine ligase activity
- negative regulation of extrinsic apoptotic signaling pathway
- response to activity
- regulation of mitochondrial depolarization
- hepatic stellate cell activation
Cellular Component
Where in the cell the gene product is active
- glutamate-cysteine ligase complex
- cytosol
Molecular Function
What the gene product does at the molecular level
- protein binding
- enzyme regulator activity
- glutamate-cysteine ligase activity
- glutamate-cysteine ligase catalytic subunit binding