Search Results
Overview
| Uniprot ID | P16402 |
|---|---|
| Protein Name | Histone H1.3 |
| Gene Name | H1-3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 107 | TGASGSFKLNKKAAS |
| 141 | GAAKKPKKVAGAATP |
| 149 | VAGAATPKKSIKKTP |
| 161 | KTPKKVKKPATAAGT |
| 35 | GATAGKRKASGPPVS |
| 47 | PVSELITKAVAASKE |
| 53 | TKAVAASKERSGVSL |
| 76 | AAGYDVEKNNSRIKL |
| 86 | SRIKLGLKSLVSKGT |
| 91 | GLKSLVSKGTLVQTK |
| 98 | KGTLVQTKGTGASGS |
Function
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:37922872). 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:40516528). 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 (PubMed:37922872). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0031490 | chromatin DNA binding |
| Molecular Function | GO:0003690 | double-stranded DNA binding |
| Molecular Function | GO:0031492 | nucleosomal DNA binding |
| Molecular Function | GO:0003723 | RNA 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] 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] 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.