Search Results
Overview
| Uniprot ID | Q92769 |
|---|---|
| Protein Name | Histone deacetylase 2 |
| Gene Name | HDAC2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 439 | RRNVADHKKGAKKAR |
| 451 | KARIEEDKKETEDKK |
| 452 | ARIEEDKKETEDKKT |
| 478 | SGEKTDTKGTKSEQL |
| 481 | KTDTKGTKSEQLSNP |
Function
Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Component of the SIN3B complex that represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (PubMed:19343227). May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity). Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:35044827)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0035098 | ESC/E(Z) complex |
| Cellular Component | GO:0000118 | histone deacetylase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016581 | NuRD complex |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0070822 | Sin3-type complex |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0031072 | heat shock protein binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0004407 | histone deacetylase activity |
| Molecular Function | GO:0141221 | histone deacetylase activity, hydrolytic mechanism |
| Molecular Function | GO:0042826 | histone deacetylase binding |
| Molecular Function | GO:0160009 | histone decrotonylase activity |
| Molecular Function | GO:0051059 | NF-kappaB binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0160010 | protein de-2-hydroxyisobutyrylase activity |
| Molecular Function | GO:0033558 | protein lysine deacetylase activity |
| Molecular Function | GO:0160216 | protein lysine delactylase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Molecular Function | GO:0001221 | transcription coregulator binding |
| Biological Process | GO:0048149 | behavioral response to ethanol |
| Biological Process | GO:0003300 | cardiac muscle hypertrophy |
| Biological Process | GO:1903351 | cellular response to dopamine |
| Biological Process | GO:0034605 | cellular response to heat |
| Biological Process | GO:0070301 | cellular response to hydrogen peroxide |
| Biological Process | GO:0071300 | cellular response to retinoic acid |
| Biological Process | GO:0071560 | cellular response to transforming growth factor beta stimulus |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0016358 | dendrite development |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0042733 | embryonic digit morphogenesis |
| Biological Process | GO:0009913 | epidermal cell differentiation |
| Biological Process | GO:0061029 | eyelid development in camera-type eye |
| Biological Process | GO:0061198 | fungiform papilla formation |
| Biological Process | GO:0060789 | hair follicle placode formation |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0030336 | negative regulation of cell migration |
| Biological Process | GO:0061000 | negative regulation of dendritic spine development |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0010977 | negative regulation of neuron projection development |
| Biological Process | GO:1902455 | negative regulation of stem cell population maintenance |
| Biological Process | GO:0010944 | negative regulation of transcription by competitive promoter binding |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:0030512 | negative regulation of transforming growth factor beta receptor signaling pathway |
| Biological Process | GO:0042475 | odontogenesis of dentin-containing tooth |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0010718 | positive regulation of epithelial to mesenchymal transition |
| Biological Process | GO:0032732 | positive regulation of interleukin-1 production |
| Biological Process | GO:0033148 | positive regulation of intracellular estrogen receptor signaling pathway |
| Biological Process | GO:1902437 | positive regulation of male mating behavior |
| Biological Process | GO:0048714 | positive regulation of oligodendrocyte differentiation |
| Biological Process | GO:0045862 | positive regulation of proteolysis |
| Biological Process | GO:1902459 | positive regulation of stem cell population maintenance |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0032760 | positive regulation of tumor necrosis factor production |
| Biological Process | GO:0050847 | progesterone receptor signaling pathway |
| Biological Process | GO:0042659 | regulation of cell fate specification |
| Biological Process | GO:0045995 | regulation of embryonic development |
| Biological Process | GO:2000736 | regulation of stem cell differentiation |
| Biological Process | GO:0001975 | response to amphetamine |
| Biological Process | GO:1904645 | response to amyloid-beta |
| Biological Process | GO:0031000 | response to caffeine |
| Biological Process | GO:0042220 | response to cocaine |
| Biological Process | GO:0055093 | response to hyperoxia |
| Biological Process | GO:0032496 | response to lipopolysaccharide |
| Biological Process | GO:0035094 | response to nicotine |
| Biological Process | GO:0009410 | response to xenobiotic stimulus |
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] 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.
[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] 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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[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.