Search Results
Overview
| Uniprot ID | P20700 |
|---|---|
| Protein Name | Lamin-B1 |
| Gene Name | LMNB1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 102 | DTARERAKLQIELGK |
| 109 | KLQIELGKCKAEHDQ |
| 111 | QIELGKCKAEHDQLL |
| 123 | QLLLNYAKKESDLNG |
| 156 | LATALGDKKSLEGDL |
| 157 | ATALGDKKSLEGDLE |
| 182 | ASLAAAKKQLADETL |
| 261 | DAQVRLYKEELEQTY |
| 271 | LEQTYHAKLENARLS |
| 312 | SQLSNLQKESRACLE |
| 389 | EGEEERLKLSPSPSS |
| 474 | GGWEMIRKIGDTSVS |
| 483 | GDTSVSYKYTSRYVL |
| 49 | RLAVYIDKVRSLETE |
| 532 | EDVKVILKNSQGEEV |
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:28716252, PubMed:32910914). 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:28716252, PubMed:32910914). 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:28716252, PubMed:32910914). Plays a role in sperm morphological development during late stages of spermiogenesis, particularly the anchoring of the sperm head to the tail (PubMed:38870534). Component of the LMNB1/SUN5/SEPT12 bridge that connects the sperm proximal centriole to the implantation fossa, the bridge functions to prevent detachment of the proximal centriole from the posterior nucleus during spermiogenesis (PubMed:38870534)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005638 | lamin filament |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0005637 | nuclear inner membrane |
| Cellular Component | GO:0005652 | nuclear lamina |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0043274 | phospholipase binding |
| Molecular Function | GO:1990837 | sequence-specific double-stranded DNA binding |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0160123 | structural constituent of nuclear lamina |
| 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] 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.
[3] 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.