Search Results
Overview
| Uniprot ID | Q03252 |
|---|---|
| Protein Name | Lamin-B2 |
| Gene Name | LMNB2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 133 | AELDEVNKSAKKREG |
| 150 | TVAQGRVKDLESLFH |
| 186 | ELRAQLAKAEDGHAV |
| 195 | EDGHAVAKKQLEKET |
| 223 | QEELDFRKSVFEEEV |
| 290 | QAKLDSAKLSSDQND |
| 298 | LSSDQNDKAASAARE |
| 81 | LLLKISEKEEVTTRE |
Function
Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:33033404). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:33033404). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:33033404)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005882 | intermediate filament |
| Cellular Component | GO:0005652 | nuclear lamina |
| Cellular Component | GO:0031965 | nuclear membrane |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0006998 | nuclear envelope organization |
| Biological Process | GO:0007097 | nuclear migration |
| Biological Process | GO:0051664 | nuclear pore localization |
| Biological Process | GO:0090435 | protein localization to nuclear envelope |
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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] 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.
[4] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[5] 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.