Search Results

Overview

Uniprot IDP0C0S5
Protein NameHistone H2A.Z
Gene NameH2AZ1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
116 GVIPHIHKSLIGKKG
12 KAGKDSGKAKTKAVS
5 ***MAGGKAGKDSGK
8 MAGGKAGKDSGKAKT

Function

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division

Protein Sequence

10 MAGGKAGKDS 20 GKAKTKAVSR 30 SQRAGLQFPV 40 GRIHRHLKSR 50 TTSHGRVGAT 60 AAVYSAAILE 70 YLTAEVLELA 80 GNASKDLKVK 90 RITPRHLQLA 100 IRGDEELDSL 110 IKATIAGGGV 120 IPHIHKSLIG KKGQQKTV

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000791 euchromatin
Cellular Component GO:0070062 extracellular exosome
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:0031492 nucleosomal DNA binding
Molecular Function GO:0046982 protein heterodimerization activity
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0000979 RNA polymerase II core promoter sequence-specific DNA binding
Molecular Function GO:0030527 structural constituent of chromatin
Biological Process GO:0071392 cellular response to estradiol stimulus
Biological Process GO:0006325 chromatin organization
Biological Process GO:0031507 heterochromatin formation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II

Reference

[1] 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.

[2] 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.

[3] 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.