Search Results
Overview
| Uniprot ID | Q13547 |
|---|---|
| Protein Name | Histone deacetylase 1 |
| Gene Name | HDAC1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 220 | DIGAGKGKYYAVNYP |
| 412 | ISICSSDKRIACEEE |
| 432 | EEGEGGRKNSSNFKK |
| 438 | RKNSSNFKKAKRVKT |
| 439 | KNSSNFKKAKRVKTE |
| 444 | FKKAKRVKTEDEKEK |
| 451 | KTEDEKEKDPEEKKE |
| 457 | EKDPEEKKEVTEEEK |
| 473 | KEEKPEAKGVKEEVK |
| 476 | KPEAKGVKEEVKLA* |
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:16762839, PubMed:17704056, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:16762839, PubMed:17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:16762839, PubMed:17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3, ZNF76 and TSHZ3 (PubMed:12837748, PubMed:16285960, PubMed:16337145, PubMed:16478997, PubMed:17996965, PubMed:19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed:12837748, PubMed:16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed:19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed:19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed:19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed:17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed:17996965). 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). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed:28497810, PubMed:35044827)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0000792 | heterochromatin |
| Cellular Component | GO:0000118 | histone deacetylase complex |
| Cellular Component | GO:0043025 | neuronal cell body |
| 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:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:0070822 | Sin3-type complex |
| Cellular Component | GO:0017053 | transcription repressor complex |
| Molecular Function | GO:0001046 | core promoter sequence-specific DNA binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0070888 | E-box binding |
| Molecular Function | GO:0019899 | enzyme 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:0035851 | Krueppel-associated box domain binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0051059 | NF-kappaB binding |
| Molecular Function | GO:0002039 | p53 binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0033558 | protein lysine deacetylase activity |
| Molecular Function | GO:0160216 | protein lysine delactylase 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:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Molecular Function | GO:0001222 | transcription corepressor binding |
| Biological Process | GO:0036120 | cellular response to platelet-derived growth factor stimulus |
| Biological Process | GO:0006325 | chromatin organization |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0006346 | DNA methylation-dependent constitutive heterochromatin formation |
| 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:0043922 | host-mediated suppression of viral transcription |
| Biological Process | GO:0060766 | negative regulation of androgen receptor signaling pathway |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0030336 | negative regulation of cell migration |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0045814 | negative regulation of gene expression, epigenetic |
| Biological Process | GO:1902455 | negative regulation of stem cell population maintenance |
| 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:0010628 | positive regulation of gene expression |
| Biological Process | GO:0033148 | positive regulation of intracellular estrogen receptor signaling pathway |
| Biological Process | GO:0048661 | positive regulation of smooth muscle cell proliferation |
| 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: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:0006357 | regulation of transcription by RNA polymerase II |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] 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.
[6] 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.
[7] 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.
[8] 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.
[9] 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.
[10] 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.
[11] 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.
[12] 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.