GCLC
Gene Ontology Biological Process
- cell redox homeostasis [IDA]
- cellular nitrogen compound metabolic process [TAS]
- cysteine metabolic process [IDA]
- glutamate metabolic process [IDA]
- glutathione biosynthetic process [IDA, IMP, TAS]
- glutathione derivative biosynthetic process [TAS]
- negative regulation of apoptotic process [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- regulation of blood vessel size [IMP]
- response to heat [IDA]
- response to hormone [IDA]
- response to oxidative stress [IDA]
- small molecule metabolic process [TAS]
- sulfur amino acid metabolic process [TAS]
- xenobiotic metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GCLM
Gene Ontology Biological Process
- cellular nitrogen compound metabolic process [TAS]
- glutamate metabolic process [IDA]
- glutathione biosynthetic process [IDA, IMP, TAS]
- glutathione derivative biosynthetic process [TAS]
- positive regulation of glutamate-cysteine ligase activity [IBA]
- regulation of blood vessel size [IMP]
- response to drug [IDA]
- response to oxidative stress [IDA]
- small molecule metabolic process [TAS]
- sulfur amino acid metabolic process [TAS]
- xenobiotic metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Identification of an important cysteine residue in human glutamate-cysteine ligase catalytic subunit by site-directed mutagenesis.
Glutamate-cysteine ligase (GLCL) catalyses the rate-limiting step in glutathione biosynthesis. To identify cysteine residues in GLCL that are involved in its activity, eight conserved cysteine residues in human GLCL catalytic subunit (hGLCLC) were replaced with glycine residues by PCR-based site-directed mutagenesis. Both recombinant hGLCLC and hGLCL holoenzyme were expressed and purified with a baculovirus expression system. The activity of purified ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| GCLC GCLM | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 1 | BioGRID | 2218607 | |
| GCLM GCLC | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 1 | BioGRID | 3188796 | |
| GCLC GCLM | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 1 | BioGRID | 3038331 | |
| GCLM GCLC | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 1 | BioGRID | 1262423 | |
| GCLC GCLM | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | 858424 |
Curated By
- BioGRID