Search Results

Overview

Uniprot IDP10412
Protein NameHistone H1.4
Gene NameH1-4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
106 TGASGSFKLNKKAAS
117 KAASGEAKPKAKKAG
140 GAAKKPKKATGAATP
169 AAAAGAKKAKSPKKA
17 AAPAPAEKTPVKKKA
192 PKSPAKAKAVKPKAA
197 KAKAVKPKAAKPKTA
34 SAGAAKRKASGPPVS
46 PVSELITKAVAASKE
52 TKAVAASKERSGVSL
63 GVSLAALKKALAAAG
64 VSLAALKKALAAAGY
75 AAGYDVEKNNSRIKL
85 SRIKLGLKSLVSKGT
90 GLKSLVSKGTLVQTK
97 KGTLVQTKGTGASGS

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:35581345, PubMed:40240600). 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:35581345, PubMed:40240600, PubMed:40516528). Ability to associate with nucleosomes and compact chromatin depends on linker DNA length and trajectory (PubMed:35581345). Also acts as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (PubMed:40240600)

Protein Sequence

10 MSETAPAAPA 20 APAPAEKTPV 30 KKKARKSAGA 40 AKRKASGPPV 50 SELITKAVAA 60 SKERSGVSLA 70 ALKKALAAAG 80 YDVEKNNSRI 90 KLGLKSLVSK 100 GTLVQTKGTG 110 ASGSFKLNKK 120 AASGEAKPKA 130 KKAGAAKAKK 140 PAGAAKKPKK 150 ATGAATPKKS 160 AKKTPKKAKK 170 PAAAAGAKKA 180 KSPKKAKAAK 190 PKKAPKSPAK 200 AKAVKPKAAK 210 PKTAKPKAAK PKKAAAKKK

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: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:0030261 chromosome condensation
Biological Process GO:0045910 negative regulation of DNA recombination
Biological Process GO:0006334 nucleosome assembly

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] 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.