Search Results
Overview
| Uniprot ID | P09382 |
|---|---|
| Protein Name | Galectin-1 |
| Gene Name | LGALS1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 108 | LPDGYEFKFPNRLNL |
| 128 | MAADGDFKIKCVAFD |
| 13 | VASNLNLKPGECLRV |
| 130 | ADGDFKIKCVAFD** |
| 29 | GEVAPDAKSFVLNLG |
| 37 | SFVLNLGKDSNNLCL |
| 64 | NTIVCNSKDGGAWGT |
Function
Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Plays a negative role in Th17 cell differentiation via activation of the receptor CD69 (PubMed:24752896)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Molecular Function | GO:0030395 | lactose binding |
| Molecular Function | GO:0043236 | laminin binding |
| Molecular Function | GO:0048018 | receptor ligand activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0098609 | cell-cell adhesion |
| Biological Process | GO:2000329 | negative regulation of T-helper 17 cell lineage commitment |
| Biological Process | GO:0043065 | positive regulation of apoptotic process |
| Biological Process | GO:0043123 | positive regulation of canonical NF-kappaB signal transduction |
| Biological Process | GO:0050729 | positive regulation of inflammatory response |
| Biological Process | GO:0046598 | positive regulation of viral entry into host cell |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031012 | extracellular matrix |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005886 | plasma membrane |
Reference
[1] 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.
[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[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.