Search Results
Overview
| Uniprot ID | Q9BTC8 |
|---|---|
| Protein Name | Metastasis-associated protein MTA3 |
| Gene Name | MTA3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 459 | VRNTGSPKSAVKTRQ |
| 560 | SLQTPTTKRMLTTPN |
| 576 | TSLSILGKRNYSHHN |
Function
Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:12705869, PubMed:16428440, PubMed:28977666). Plays a role in maintenance of the normal epithelial architecture through the repression of SNAI1 transcription in a histone deacetylase-dependent manner, and thus the regulation of E-cadherin levels (PubMed:12705869). Contributes to transcriptional repression by BCL6 (PubMed:15454082)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016581 | NuRD complex |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0043565 | sequence-specific DNA binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0042659 | regulation of cell fate specification |
| Biological Process | GO:2000736 | regulation of stem cell differentiation |
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] 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.
[3] 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.
[4] 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.