Search Results
Overview
| Uniprot ID | P43277 |
|---|---|
| Protein Name | Histone H1.3 |
| Gene Name | H1-3 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 35 | GAAAGKRKASGPPVS |
| 65 | VSLAALKKALAAAGY |
Function
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:12808097). 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). Together with histone H1-3, histone H1-3 acts as a regulator of splicing, most specifically exon skipping and intron retention events: histone H1-3 has a high affinity for introns and regulates splicing by affecting RNA polymerase II (RNAPII) elongation (By similarity). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:12808097)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003690 | double-stranded DNA 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 |
| Biological Process | GO:0048024 | regulation of mRNA splicing, via spliceosome |
Reference
[1] 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.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.