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Overview

Uniprot IDP16403
Protein NameHistone H1.2
Gene NameH1-2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
140 GAAKKPKKAAGGATP
168 PAAATVTKKVAKSPK
17 AAAPPAEKAPVKKKA
191 KAAKSAAKAVKPKAA
201 KPKAAKPKVVKPKKA
27 VKKKAAKKAGGTPRK
34 KAGGTPRKASGPPVS
52 TKAVAASKERSGVSL
64 VSLAALKKALAAAGY
90 GLKSLVSKGTLVQTK
97 KGTLVQTKGTGASGS

Function

Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber (PubMed:26581166, PubMed:38530350). Histone H1-2 is required for the condensation of nucleosome chains into higher-order structured fibers (PubMed:38530350). Compared to other histone H1 variants, H1-2 plays an essential role in nucleosome condensation: its absence leads to global chromatin decompaction, which is not observed when depleting other histone H1 variants (PubMed:38530350). Histone H1-2 also acts as a histone reader: specifically recognizes and binds histone H3 trimethylated at 'lys-27' (H3K27me3) (PubMed:26581166). Histones H1 also promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 complex, possibly by facilitating restoration of H3K27me3 post-replication (PubMed:37429872, PubMed:40516528). Together with histone H1-3, histone H1-2 acts as a regulator of splicing, most specifically exon skipping and intron retention events: histone H1-2 has a high affinity for exons 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 (PubMed:38530350)

Protein Sequence

10 MSETAPAAPA 20 AAPPAEKAPV 30 KKKAAKKAGG 40 TPRKASGPPV 50 SELITKAVAA 60 SKERSGVSLA 70 ALKKALAAAG 80 YDVEKNNSRI 90 KLGLKSLVSK 100 GTLVQTKGTG 110 ASGSFKLNKK 120 AASGEAKPKV 130 KKAGGTKPKK 140 PVGAAKKPKK 150 AAGGATPKKS 160 AKKTPKKAKK 170 PAAATVTKKV 180 AKSPKKAKVA 190 KPKKAAKSAA 200 KAVKPKAAKP 210 KVVKPKKAAP KKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005730 nucleolus
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:0061628 histone H3K27me3 reader activity
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:0140718 facultative heterochromatin formation
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] 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.

[2] 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.

[3] 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.