Search Results
Overview
| Uniprot ID | Q96N64 |
|---|---|
| Protein Name | PWWP domain-containing protein 2A |
| Gene Name | PWWP2A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 324 | PRQVLCDKCKNSVVA |
| 363 | ESVTTVNKKLKTDHK |
| 364 | SVTTVNKKLKTDHKV |
| 370 | KKLKTDHKVDGKNQN |
| 387 | QKRNAVVKVSNIAHS |
| 400 | HSRGRVVKVSAQANT |
| 409 | SAQANTSKAQLSTKK |
| 421 | TKKVLQSKNMDHAKA |
| 501 | LEKMRSGKMAPKPQS |
Function
Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260, PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation (By similarity). Essential for proper mitosis progression (PubMed:28645917)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0140003 | histone H3K36me3 reader activity |
| Molecular Function | GO:0120325 | NuRD complex binding |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0032968 | positive regulation of transcription elongation by RNA polymerase II |
| Biological Process | GO:0001178 | regulation of transcriptional start site selection at RNA polymerase II promoter |
Reference
[1] 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.
[2] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[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.