Search Results
Overview
| Uniprot ID | Q96A08 |
|---|---|
| Protein Name | Histone H2B type 1-A |
| Gene Name | H2BC1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 110 | LLPGELAKHAVSEGT |
| 118 | HAVSEGTKAVTKYTS |
| 36 | KKRKRTRKESYSIYI |
| 45 | SYSIYIYKVLKQVHP |
| 48 | IYIYKVLKQVHPDTG |
| 7 | *MPEVSSKGATISKK |
| 87 | SRLAHYSKRSTISSR |
Function
Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells (By similarity). Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones (By similarity). Core component of nucleosome (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Also found in fat cells, its function and the presence of post-translational modifications specific to such cells are still unclear (PubMed:21249133)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:0006337 | nucleosome disassembly |
| Biological Process | GO:0035092 | sperm DNA condensation |
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] 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.
[3] 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.
[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.