Search Results
Overview
| Uniprot ID | P62807 |
|---|---|
| Protein Name | Histone H2B type 1-C/E/F/G/I |
| Gene Name | H2BC4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 109 | LLPGELAKHAVSEGT |
| 117 | HAVSEGTKAVTKYTS |
| 121 | EGTKAVTKYTSSK** |
| 16 | PAPKKGSKKAVTKAQ |
| 21 | GSKKAVTKAQKKDGK |
| 35 | KKRKRSRKESYSVYV |
| 47 | VYVYKVLKQVHPDTG |
| 6 | **MPEPAKSAPAPKK |
| 86 | SRLAHYNKRSTITSR |
Function
Core component of nucleosome. 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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Biological Process | GO:0019731 | antibacterial humoral response |
| Biological Process | GO:0061844 | antimicrobial humoral immune response mediated by antimicrobial peptide |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0050830 | defense response to Gram-positive bacterium |
| Biological Process | GO:0002227 | innate immune response in mucosa |
| Biological Process | GO:0006334 | nucleosome assembly |
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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[5] 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.
[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[7] 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.