Search Results
Overview
| Uniprot ID | P43274 |
|---|---|
| Protein Name | Histone H1.4 |
| Gene Name | H1-4 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 34 | AAGGAKRKTSGPPVS |
| 90 | GLKSLVSKGTLVQTK |
| 97 | KGTLVQTKGTGASGS |
Function
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:12808097, PubMed:16377562). 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:12808097, PubMed:16377562). Ability to associate with nucleosomes and compact chromatin depends on linker DNA length and trajectory (By similarity). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:12808097, PubMed:16377562)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0043531 | ADP binding |
| Molecular Function | GO:0016208 | AMP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0005509 | calcium ion binding |
| Molecular Function | GO:0032564 | dATP binding |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0031492 | nucleosomal DNA binding |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Biological Process | GO:0030261 | chromosome condensation |
| Biological Process | GO:0045910 | negative regulation of DNA recombination |
| Biological Process | GO:0006334 | nucleosome assembly |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.
[2] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.