Search Results
Overview
| Uniprot ID | P50402 |
|---|---|
| Protein Name | Emerin |
| Gene Name | EMD |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 37 | TRRLYEKKIFEYETQ |
| 79 | DMYDLPKKEDALLYQ |
Function
Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments (PubMed:15328537). Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway (PubMed:16858403). Links centrosomes to the nuclear envelope via a microtubule association (PubMed:17785515). Required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005637 | nuclear inner membrane |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005874 | microtubule |
| Cellular Component | GO:0005635 | nuclear envelope |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0005640 | nuclear outer membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005819 | spindle |
| Cellular Component | GO:0160045 | TMEM240-body |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0048487 | beta-tubulin binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Biological Process | GO:1990000 | amyloid fibril formation |
| Biological Process | GO:0071363 | cellular response to growth factor stimulus |
| Biological Process | GO:0006936 | muscle contraction |
| Biological Process | GO:0007517 | muscle organ development |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0048147 | negative regulation of fibroblast proliferation |
| Biological Process | GO:0071763 | nuclear membrane organization |
| Biological Process | GO:0046827 | positive regulation of protein export from nucleus |
| Biological Process | GO:0060828 | regulation of canonical Wnt signaling pathway |
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] 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.
[6] 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.