Search Results
Overview
| Uniprot ID | P48507 |
|---|---|
| Protein Name | Glutamate--cysteine ligase regulatory subunit |
| Gene Name | GCLM |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 158 | ENLVQSKKIVAIGTS |
| 263 | SRGIIKSKGYILQAK |
| 34 | NWGRLRKKCPSTHSE |
Function
No function data available.
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0017109 | glutamate-cysteine ligase complex |
| Molecular Function | GO:0004357 | glutamate-cysteine ligase activity |
| Molecular Function | GO:0035226 | glutamate-cysteine ligase catalytic subunit binding |
| Molecular Function | GO:1990609 | glutamate-cysteine ligase regulator activity |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0097746 | blood vessel diameter maintenance |
| Biological Process | GO:0044344 | cellular response to fibroblast growth factor stimulus |
| Biological Process | GO:0071372 | cellular response to follicle-stimulating hormone stimulus |
| Biological Process | GO:0071333 | cellular response to glucose stimulus |
| Biological Process | GO:0035729 | cellular response to hepatocyte growth factor stimulus |
| Biological Process | GO:0097069 | cellular response to thyroxine stimulus |
| Biological Process | GO:0006536 | glutamate metabolic process |
| Biological Process | GO:0006750 | glutathione biosynthetic process |
| Biological Process | GO:0035733 | hepatic stellate cell activation |
| Biological Process | GO:0043524 | negative regulation of neuron apoptotic process |
| Biological Process | GO:0014823 | response to activity |
| Biological Process | GO:0044752 | response to human chorionic gonadotropin |
| Biological Process | GO:0051409 | response to nitrosative stress |
| Biological Process | GO:0007584 | response to nutrient |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0009410 | response to xenobiotic stimulus |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.