Search Results
Overview
| Uniprot ID | Q12873 |
|---|---|
| Protein Name | ATP-dependent chromatin remodeler CHD3 |
| Gene Name | CHD3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 295 | KMAPLKIKLGLLGGK |
| 302 | KLGLLGGKRKKGGSY |
| 48 | LPSALGVKKRKRGPK |
| 644 | INHSVDKKGNYHYLV |
Function
ATP-dependent chromatin-remodeling factor that binds and distorts nucleosomal DNA (PubMed:28977666). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666, PubMed:30397230, PubMed:9804427). Involved in transcriptional repression as part of the NuRD complex (PubMed:27068747). Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity (PubMed:17626165)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016581 | NuRD complex |
| Cellular Component | GO:0016605 | PML body |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0140658 | ATP-dependent chromatin remodeler activity |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0004386 | helicase activity |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000976 | transcription cis-regulatory region binding |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0007098 | centrosome cycle |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006351 | DNA-templated transcription |
| 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:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:2000736 | regulation of stem cell differentiation |
| Biological Process | GO:0007051 | spindle organization |
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] 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.
[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.