Search Results
Overview
| Uniprot ID | Q9HCK8 |
|---|---|
| Protein Name | ATP-dependent chromatin remodeler CHD8 |
| Gene Name | CHD8 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 2241 | TAAAQFTKLRRGMDE |
| 2286 | GHPLFHKKKGNRKKL |
| 2416 | PIAPESSKKRARRMR |
| 2417 | IAPESSKKRARRMRP |
| 532 | SKTKGKSKLNTITPV |
| 542 | TITPVVGKKRKRNTS |
| 543 | ITPVVGKKRKRNTSS |
| 573 | DEESSIQKRRSNRQV |
| 965 | CKLLDSLKHMDLEHK |
Function
ATP-dependent chromatin-remodeling factor, it slides nucleosomes along DNA; nucleosome sliding requires ATP (PubMed:28533432). Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. Regulates alternative splicing of a core group of genes involved in neuronal differentiation, cell cycle and DNA repair. Enables H3K36me3-coupled transcription elongation and co-transcriptional RNA processing likely via interaction with HNRNPL
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0071339 | MLL1 complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| 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:0008013 | beta-catenin binding |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0003678 | DNA helicase activity |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0140002 | histone H3K4me3 reader activity |
| Molecular Function | GO:0002039 | p53 binding |
| Biological Process | GO:0007420 | brain development |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0048565 | digestive tract development |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| 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:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0045945 | positive regulation of transcription by RNA polymerase III |
| Biological Process | GO:0016055 | 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] 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.
[5] 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.