Search Results
Overview
| Uniprot ID | P07305 |
|---|---|
| Protein Name | Histone H1.0 |
| Gene Name | H1-0 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 149 | PVKKAKKKLAATPKK |
| 40 | VAAIQAEKNRAGSSR |
| 52 | SSRQSIQKYIKSHYK |
| 59 | KYIKSHYKVGENADS |
| 82 | LVTTGVLKQTKGVGA |
| 85 | TGVLKQTKGVGASGS |
Function
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:33238161). Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers and promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex (PubMed:33238161). The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division (PubMed:7374750)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0017053 | transcription repressor complex |
| Molecular Function | GO:0031490 | chromatin DNA binding |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0003680 | minor groove of adenine-thymine-rich DNA binding |
| Molecular Function | GO:0031492 | nucleosomal DNA binding |
| Molecular Function | GO:0031491 | nucleosome binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Biological Process | GO:0030261 | chromosome condensation |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0045910 | negative regulation of DNA recombination |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:2000679 | positive regulation of transcription regulatory region DNA binding |
Reference
[1] 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.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[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.