Search Results
Overview
| Uniprot ID | P55209 |
|---|---|
| Protein Name | Nucleosome assembly protein 1-like 1 |
| Gene Name | NAP1L1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 105 | EVHDLERKYAVLYQP |
| 116 | LYQPLFDKRFEIINA |
| 266 | QIDWKKGKNVTLKTI |
| 271 | KGKNVTLKTIKKKQK |
| 82 | KRRVNALKNLQVKCA |
| 87 | ALKNLQVKCAQIEAK |
Function
Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Biological Process | GO:0007399 | nervous system development |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:2000179 | positive regulation of neural precursor cell proliferation |
| Biological Process | GO:0050769 | positive regulation of neurogenesis |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0042470 | melanosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0140713 | histone chaperone activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0006260 | DNA replication |
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] 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] 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.