Search Results

Overview

Uniprot IDQ8WUI4
Protein NameHistone deacetylase 7
Gene NameHDAC7
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
160 TVSEPNLKLRYKPKK
389 KTHVQVIKRSAKPSE
603 RLKLDNGKLAGLLAQ
86 AVASSVVKQKLAEVI
88 ASSVVKQKLAEVILK
95 KLAEVILKKQQAALE
96 LAEVILKKQQAALER

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). 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). Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C (By similarity). During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors (By similarity). May be involved in Epstein-Barr virus (EBV) latency, possibly by repressing the viral BZLF1 gene (PubMed:12239305). Positively regulates the transcriptional repressor activity of FOXP3 (PubMed:17360565). Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). Also acetylates non-histone proteins, such as ALKBH5 (PubMed:37369679)

Protein Sequence

10 MDLRVGQRPP 20 VEPPPEPTLL 30 ALQRPQRLHH 40 HLFLAGLQQQ 50 RSVEPMRLSM 60 DTPMPELQVG 70 PQEQELRQLL 80 HKDKSKRSAV 90 ASSVVKQKLA 100 EVILKKQQAA 110 LERTVHPNSP 120 GIPYRTLEPL 130 ETEGATRSML 140 SSFLPPVPSL 150 PSDPPEHFPL 160 RKTVSEPNLK 170 LRYKPKKSLE 180 RRKNPLLRKE 190 SAPPSLRRRP 200 AETLGDSSPS 210 SSSTPASGCS 220 SPNDSEHGPN 230 PILGSEALLG 240 QRLRLQETSV 250 APFALPTVSL 260 LPAITLGLPA 270 PARADSDRRT 280 HPTLGPRGPI 290 LGSPHTPLFL 300 PHGLEPEAGG 310 TLPSRLQPIL 320 LLDPSGSHAP 330 LLTVPGLGPL 340 PFHFAQSLMT 350 TERLSGSGLH 360 WPLSRTRSEP 370 LPPSATAPPP 380 PGPMQPRLEQ 390 LKTHVQVIKR 400 SAKPSEKPRL 410 RQIPSAEDLE 420 TDGGGPGQVV 430 DDGLEHRELG 440 HGQPEARGPA 450 PLQQHPQVLL 460 WEQQRLAGRL 470 PRGSTGDTVL 480 LPLAQGGHRP 490 LSRAQSSPAA 500 PASLSAPEPA 510 SQARVLSSSE 520 TPARTLPFTT 530 GLIYDSVMLK 540 HQCSCGDNSR 550 HPEHAGRIQS 560 IWSRLQERGL 570 RSQCECLRGR 580 KASLEELQSV 590 HSERHVLLYG 600 TNPLSRLKLD 610 NGKLAGLLAQ 620 RMFVMLPCGG 630 VGVDTDTIWN 640 ELHSSNAARW 650 AAGSVTDLAF 660 KVASRELKNG 670 FAVVRPPGHH 680 ADHSTAMGFC 690 FFNSVAIACR 700 QLQQQSKASK 710 ILIVDWDVHH 720 GNGTQQTFYQ 730 DPSVLYISLH 740 RHDDGNFFPG 750 SGAVDEVGAG 760 SGEGFNVNVA 770 WAGGLDPPMG 780 DPEYLAAFRI 790 VVMPIAREFS 800 PDLVLVSAGF 810 DAAEGHPAPL 820 GGYHVSAKCF 830 GYMTQQLMNL 840 AGGAVVLALE 850 GGHDLTAICD 860 ASEACVAALL 870 GNRVDPLSEE 880 GWKQKPNLNA 890 IRSLEAVIRV 900 HSKYWGCMQR 910 LASCPDSWVP 920 RVPGADKEEV 930 EAVTALASLS 940 VGILAEDRPS 950 EQLVEEEEPM NL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000118 histone deacetylase complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0071889 14-3-3 protein binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0004407 histone deacetylase activity
Molecular Function GO:0141221 histone deacetylase activity, hydrolytic mechanism
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0005080 protein kinase C binding
Molecular Function GO:0033558 protein lysine deacetylase activity
Molecular Function GO:0019789 SUMO transferase activity
Molecular Function GO:0003714 transcription corepressor activity
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0040029 epigenetic regulation of gene expression
Biological Process GO:0032703 negative regulation of interleukin-2 production
Biological Process GO:1901223 negative regulation of non-canonical NF-kappaB signal transduction
Biological Process GO:0045668 negative regulation of osteoblast differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0090050 positive regulation of cell migration involved in sprouting angiogenesis
Biological Process GO:0006476 protein deacetylation
Biological Process GO:0016925 protein sumoylation
Biological Process GO:0050684 regulation of mRNA processing

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] 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.

[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.