Search Results
Overview
| Uniprot ID | Q13111 |
|---|---|
| Protein Name | Chromatin assembly factor 1 subunit A |
| Gene Name | CHAF1A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 30 | DRPAFPVKKLIQARL |
| 327 | RITKKFVKGSTEKNK |
| 467 | TLAGSCGKFAPFEIK |
| 47 | KRLNLVPKGKADDMS |
| 49 | LNLVPKGKADDMSDD |
| 870 | QGTPISLKRKSAGSM |
| 95 | RPKLVNGKGPLDNFL |
Function
Acts as a component of the histone chaperone complex chromatin assembly factor 1 (CAF-1), which assembles histone octamers onto DNA during replication and repair. CAF-1 performs the first step of the nucleosome assembly process, bringing newly synthesized histones H3 and H4 to replicating DNA; histones H2A/H2B can bind to this chromatin precursor subsequent to DNA replication to complete the histone octamer. It may play a role in heterochromatin maintenance in proliferating cells by bringing newly synthesized cbx proteins to heterochromatic DNA replication foci
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0033186 | CAF-1 complex |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0070087 | chromo shadow domain binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0006335 | DNA replication-dependent chromatin assembly |
| Biological Process | GO:0006334 | nucleosome assembly |
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] 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.