Search Results
Overview
| Uniprot ID | P49321 |
|---|---|
| Protein Name | Nuclear autoantigenic sperm protein |
| Gene Name | NASP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 405 | IERLTETKDGSGLEE |
| 413 | DGSGLEEKVRAKLVP |
| 417 | LEEKVRAKLVPSQEE |
| 450 | VAQGATEKSPEDKVQ |
| 52 | KLLGLGQKHLVMGDI |
| 698 | VSMIASRKPTDGASS |
Function
Component of the histone chaperone network (PubMed:22195965). Binds and stabilizes histone H3-H4 not bound to chromatin to maintain a soluble reservoir and modulate degradation by chaperone-mediated autophagy (PubMed:22195965). Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and H1 linker histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0001824 | blastocyst development |
| Biological Process | GO:0034080 | CENP-A containing chromatin assembly |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0006335 | DNA replication-dependent chromatin assembly |
| Biological Process | GO:0008584 | male gonad development |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0033574 | response to testosterone |
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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] 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.
[6] 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.