Search Results
Overview
| Uniprot ID | P56524 |
|---|---|
| Protein Name | Histone deacetylase 4 |
| Gene Name | HDAC4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 174 | ASTEVKMKLQEFVLN |
| 182 | LQEFVLNKKKALAHR |
| 272 | SSPLLRRKDGPVVTA |
| 282 | PVVTALKKRPLDVTD |
Function
Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. Deacetylates HSPA1A and HSPA1B at 'Lys-77' leading to their preferential binding to co-chaperone STUB1 (PubMed:27708256)
Protein Sequence
10
MSSQSHPDGL
20
SGRDQPVELL
30
NPARVNHMPS
40
TVDVATALPL
50
QVAPSAVPMD
60
LRLDHQFSLP
70
VAEPALREQQ
80
LQQELLALKQ
90
KQQIQRQILI
100
AEFQRQHEQL
110
SRQHEAQLHE
120
HIKQQQEMLA
130
MKHQQELLEH
140
QRKLERHRQE
150
QELEKQHREQ
160
KLQQLKNKEK
170
GKESAVASTE
180
VKMKLQEFVL
190
NKKKALAHRN
200
LNHCISSDPR
210
YWYGKTQHSS
220
LDQSSPPQSG
230
VSTSYNHPVL
240
GMYDAKDDFP
250
LRKTASEPNL
260
KLRSRLKQKV
270
AERRSSPLLR
280
RKDGPVVTAL
290
KKRPLDVTDS
300
ACSSAPGSGP
310
SSPNNSSGSV
320
SAENGIAPAV
330
PSIPAETSLA
340
HRLVAREGSA
350
APLPLYTSPS
360
LPNITLGLPA
370
TGPSAGTAGQ
380
QDAERLTLPA
390
LQQRLSLFPG
400
THLTPYLSTS
410
PLERDGGAAH
420
SPLLQHMVLL
430
EQPPAQAPLV
440
TGLGALPLHA
450
QSLVGADRVS
460
PSIHKLRQHR
470
PLGRTQSAPL
480
PQNAQALQHL
490
VIQQQHQQFL
500
EKHKQQFQQQ
510
QLQMNKIIPK
520
PSEPARQPES
530
HPEETEEELR
540
EHQALLDEPY
550
LDRLPGQKEA
560
HAQAGVQVKQ
570
EPIESDEEEA
580
EPPREVEPGQ
590
RQPSEQELLF
600
RQQALLLEQQ
610
RIHQLRNYQA
620
SMEAAGIPVS
630
FGGHRPLSRA
640
QSSPASATFP
650
VSVQEPPTKP
660
RFTTGLVYDT
670
LMLKHQCTCG
680
SSSSHPEHAG
690
RIQSIWSRLQ
700
ETGLRGKCEC
710
IRGRKATLEE
720
LQTVHSEAHT
730
LLYGTNPLNR
740
QKLDSKKLLG
750
SLASVFVRLP
760
CGGVGVDSDT
770
IWNEVHSAGA
780
ARLAVGCVVE
790
LVFKVATGEL
800
KNGFAVVRPP
810
GHHAEESTPM
820
GFCYFNSVAV
830
AAKLLQQRLS
840
VSKILIVDWD
850
VHHGNGTQQA
860
FYSDPSVLYM
870
SLHRYDDGNF
880
FPGSGAPDEV
890
GTGPGVGFNV
900
NMAFTGGLDP
910
PMGDAEYLAA
920
FRTVVMPIAS
930
EFAPDVVLVS
940
SGFDAVEGHP
950
TPLGGYNLSA
960
RCFGYLTKQL
970
MGLAGGRIVL
980
ALEGGHDLTA
990
ICDASEACVS
1000
ALLGNELDPL
1010
PEKVLQQRPN
1020
ANAVRSMEKV
1030
MEIHSKYWRC
1040
LQRTTSTAGR
1050
SLIEAQTCEN
1060
EEAETVTAMA
1070
SLSVGVKPAE
1080
KRPDEEPMEE
EPPL
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0000118 | histone deacetylase complex |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0017053 | transcription repressor complex |
| Molecular Function | GO:0001216 | DNA-binding transcription activator activity |
| 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:0042826 | histone deacetylase binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0060090 | molecular adaptor activity |
| Molecular Function | GO:0030955 | potassium ion binding |
| Molecular Function | GO:0033558 | protein lysine deacetylase activity |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Molecular Function | GO:0019789 | SUMO transferase activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0042113 | B cell activation |
| Biological Process | GO:0030183 | B cell differentiation |
| Biological Process | GO:0014898 | cardiac muscle hypertrophy in response to stress |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0040029 | epigenetic regulation of gene expression |
| Biological Process | GO:0006954 | inflammatory response |
| Biological Process | GO:0045814 | negative regulation of gene expression, epigenetic |
| Biological Process | GO:0045820 | negative regulation of glycolytic process |
| Biological Process | GO:0010832 | negative regulation of myotube differentiation |
| Biological Process | GO:0061084 | negative regulation of protein refolding |
| 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:0007399 | nervous system development |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0033235 | positive regulation of protein sumoylation |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0016925 | protein sumoylation |
| Biological Process | GO:0014894 | response to denervation involved in regulation of muscle adaptation |
| Biological Process | GO:0070555 | response to interleukin-1 |
| Biological Process | GO:0060337 | type I interferon-mediated signaling pathway |
Reference
[1] 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.
[2] 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.