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Overview

Uniprot IDP16401
Protein NameHistone H1.5
Gene NameH1-5
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 KGTLVQTKGTGASGS
168 KPAAAGVKKVAKSPK
188 AKPKKATKSPAKPKA
199 KPKAVKPKAAKPKAA
27 AKKKATKKAAGAGAA
35 AAGAGAAKRKATGPP
37 GAGAAKRKATGPPVS
49 PVSELITKAVAASKE
67 LSLAALKKALAAGGY
78 AGGYDVEKNNSRIKL
93 GLKSLVSKGTLVQTK

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (By similarity). 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). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity)

Protein Sequence

10 MSETAPAETA 20 TPAPVEKSPA 30 KKKATKKAAG 40 AGAAKRKATG 50 PPVSELITKA 60 VAASKERNGL 70 SLAALKKALA 80 AGGYDVEKNN 90 SRIKLGLKSL 100 VSKGTLVQTK 110 GTGASGSFKL 120 NKKAASGEAK 130 PKAKKAGAAK 140 AKKPAGATPK 150 KAKKAAGAKK 160 AVKKTPKKAK 170 KPAAAGVKKV 180 AKSPKKAKAA 190 AKPKKATKSP 200 AKPKAVKPKA 210 AKPKAAKPKA 220 AKPKAAKAKK AAAKKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005654 nucleoplasm
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:0042826 histone deacetylase 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:0006325 chromatin organization
Biological Process GO:0030261 chromosome condensation
Biological Process GO:0071169 establishment of protein localization to chromatin
Biological Process GO:0045910 negative regulation of DNA recombination
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0006334 nucleosome assembly
Biological Process GO:0050821 protein stabilization

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] 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] 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.