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Protein

Histone deacetylase 1

Gene

HDAC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity. 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. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.7 Publications

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • deacetylase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone deacetylase activity Source: UniProtKB
  • histone deacetylase binding Source: BHF-UCL
  • NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  • NF-kappaB binding Source: UniProtKB
  • protein deacetylase activity Source: UniProtKB
  • protein N-terminus binding Source: MGI
  • repressing transcription factor binding Source: ParkinsonsUK-UCL
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription corepressor activity Source: BHF-UCL
  • RNA polymerase II transcription factor binding Source: ParkinsonsUK-UCL
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: ParkinsonsUK-UCL
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • beta-catenin-TCF complex assembly Source: Reactome
  • blood coagulation Source: Reactome
  • chromatin modification Source: UniProtKB
  • chromatin remodeling Source: BHF-UCL
  • circadian regulation of gene expression Source: UniProtKB
  • embryonic digit morphogenesis Source: BHF-UCL
  • epidermal cell differentiation Source: BHF-UCL
  • eyelid development in camera-type eye Source: BHF-UCL
  • fungiform papilla formation Source: BHF-UCL
  • hair follicle placode formation Source: BHF-UCL
  • histone deacetylation Source: UniProtKB
  • histone H3 deacetylation Source: BHF-UCL
  • histone H4 deacetylation Source: BHF-UCL
  • methylation-dependent chromatin silencing Source: BHF-UCL
  • negative regulation by host of viral transcription Source: UniProtKB
  • negative regulation of androgen receptor signaling pathway Source: BHF-UCL
  • negative regulation of apoptotic process Source: BHF-UCL
  • negative regulation of canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of gene expression Source: CACAO
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • odontogenesis of dentin-containing tooth Source: BHF-UCL
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of receptor biosynthetic process Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein deacetylation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Biological rhythms, Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

BRENDAi3.5.1.98. 2681.
ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-193670. p75NTR negatively regulates cell cycle via SC1.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-4641265. Repression of WNT target genes.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKQ13547.
SIGNORiQ13547.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 1 (EC:3.5.1.98)
Short name:
HD1
Gene namesi
Name:HDAC1
Synonyms:RPD3L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:4852. HDAC1.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: ParkinsonsUK-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • histone deacetylase complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • NuRD complex Source: UniProtKB
  • protein complex Source: UniProtKB
  • Sin3 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1411H → A: Abolishes histone deacetylase activity. 1 Publication
Mutagenesisi287 – 2871F → Y: Abolishes interaction with CHFR; when associated with I-297. 1 Publication
Mutagenesisi297 – 2971M → I: Abolishes interaction with CHFR; when associated with Y-287. 1 Publication
Mutagenesisi391 – 48292Missing : Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. Add
BLAST
Mutagenesisi421 – 4211S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. 1 Publication
Mutagenesisi421 – 4211S → D or E: Slightly decreases deacetylase activity. 1 Publication
Mutagenesisi423 – 4231S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. 1 Publication
Mutagenesisi423 – 4231S → D or E: Decreases deacetylase activity. 1 Publication
Mutagenesisi424 – 4241E → A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesisi425 – 4251E → A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.
Mutagenesisi426 – 4261E → A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.

Organism-specific databases

PharmGKBiPA29226.

Chemistry

ChEMBLiCHEMBL2093865.
DrugBankiDB06603. Panobinostat.
DB06176. Romidepsin.
DB02546. Vorinostat.
GuidetoPHARMACOLOGYi2658.

Polymorphism and mutation databases

BioMutaiHDAC1.
DMDMi2498443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Histone deacetylase 1PRO_0000114687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysineCombined sources
Modified residuei220 – 2201N6-acetyllysineCombined sources
Modified residuei261 – 2611S-nitrosocysteineBy similarity
Modified residuei273 – 2731S-nitrosocysteineBy similarity
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei421 – 4211Phosphoserine; by CK2Combined sources1 Publication
Modified residuei423 – 4231Phosphoserine; by CK2Combined sources1 Publication
Modified residuei432 – 4321N6-methylated lysine; by EHMT21 Publication
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki457 – 457Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

Post-translational modificationi

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1.3 Publications
Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.1 Publication
Ubiquitinated by CHFR, leading to its degradation by the proteasome. Ubiquitinated by KCTD11, leading to proteasomal degradation.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiQ13547.
PaxDbiQ13547.
PeptideAtlasiQ13547.
PRIDEiQ13547.
TopDownProteomicsiQ13547.

PTM databases

iPTMnetiQ13547.
PhosphoSiteiQ13547.
SwissPalmiQ13547.

Expressioni

Tissue specificityi

Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.

Gene expression databases

BgeeiENSG00000116478.
CleanExiHS_HDAC1.
ExpressionAtlasiQ13547. baseline and differential.
GenevisibleiQ13547. HS.

Organism-specific databases

HPAiCAB005017.
CAB068191.
HPA029693.

Interactioni

Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylation (NuRD) complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A (By similarity). Interacts with DNTTIP1 (PubMed:25653165). Identified in a histone deacetylase complex that contains DNTTIP1, HDAC1 and ELMSAN1; this complex assembles into a tetramer that contains four copies of each protein chain (PubMed:25653165). Interacts with CCAR2 (PubMed:21030595). Interacts with PPHLN1 (PubMed:17963697). Found in a complex with YY1, SIN3A and GON4L (By similarity).By similarity45 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL1Q9UKG12EBI-301834,EBI-741243
ARID5BQ148655EBI-301834,EBI-1210388
BCL11BQ9C0K03EBI-301834,EBI-6597578
BICP0P291282EBI-301834,EBI-11292028From a different organism.
BRMS1Q9HCU94EBI-301834,EBI-714781
C16orf87Q6PH813EBI-301834,EBI-6598617
CHD4Q148396EBI-301834,EBI-372916
CSNK2A1P684002EBI-301834,EBI-347804
DAXXQ9UER72EBI-301834,EBI-77321
DDX17Q92841-43EBI-301834,EBI-5280703
DDX5P178444EBI-301834,EBI-351962
DHX30Q7L2E33EBI-301834,EBI-1211456
DNMT3LQ9UJW33EBI-301834,EBI-740967
E4F1Q66K893EBI-301834,EBI-1227043
EHMT2Q96KQ77EBI-301834,EBI-744366
EID3Q8N1402EBI-301834,EBI-744483
FAM60AQ9NP505EBI-301834,EBI-741906
GFI1Q996844EBI-301834,EBI-949368
HCFC1P516102EBI-301834,EBI-396176
HDAC2Q9276911EBI-301834,EBI-301821
HIST2H4BP628053EBI-301834,EBI-302023
LOXL2Q9Y4K02EBI-301834,EBI-7172227
MAGEA1P433552EBI-301834,EBI-740978
MBD1Q9UIS92EBI-301834,EBI-867196
MIER1Q8N1087EBI-301834,EBI-3504940
MTA1Q1333010EBI-301834,EBI-714236
NCOR2Q9Y6182EBI-301834,EBI-80830
NFKB1P198385EBI-301834,EBI-300010
NPM1P067482EBI-301834,EBI-78579
NR2E3Q9Y5X42EBI-301834,EBI-7216962
PRDM5Q9NQX13EBI-301834,EBI-4292031
PWWP2AQ96N645EBI-301834,EBI-6597774
RB1P064004EBI-301834,EBI-491274
RBBP4Q090286EBI-301834,EBI-620823
RBBP7Q165766EBI-301834,EBI-352227
RELAQ042066EBI-301834,EBI-73886
SAP18O004222EBI-301834,EBI-1044156
SNAI1O958633EBI-301834,EBI-1045459
SUV39H1O434633EBI-301834,EBI-349968
TP53P046377EBI-301834,EBI-366083

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: BHF-UCL
  • NF-kappaB binding Source: UniProtKB
  • protein N-terminus binding Source: MGI
  • repressing transcription factor binding Source: ParkinsonsUK-UCL
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription factor binding Source: ParkinsonsUK-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109315. 541 interactions.
DIPiDIP-24184N.
IntActiQ13547. 243 interactions.
MINTiMINT-90475.
STRINGi9606.ENSP00000362649.

Chemistry

BindingDBiQ13547.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 144Combined sources
Helixi19 – 213Combined sources
Helixi33 – 4412Combined sources
Helixi48 – 503Combined sources
Beta strandi51 – 566Combined sources
Helixi61 – 644Combined sources
Turni65 – 673Combined sources
Helixi70 – 789Combined sources
Turni83 – 864Combined sources
Helixi88 – 947Combined sources
Turni97 – 993Combined sources
Helixi106 – 12520Combined sources
Beta strandi130 – 1367Combined sources
Beta strandi151 – 1533Combined sources
Helixi155 – 1639Combined sources
Turni164 – 1663Combined sources
Beta strandi170 – 1745Combined sources
Beta strandi176 – 1783Combined sources
Helixi181 – 1866Combined sources
Turni187 – 1893Combined sources
Beta strandi191 – 20010Combined sources
Beta strandi205 – 2073Combined sources
Helixi217 – 2193Combined sources
Beta strandi223 – 2286Combined sources
Helixi234 – 25219Combined sources
Beta strandi255 – 2606Combined sources
Helixi263 – 2653Combined sources
Helixi278 – 28912Combined sources
Beta strandi295 – 2984Combined sources
Helixi305 – 31915Combined sources
Helixi334 – 3363Combined sources
Turni338 – 3403Combined sources
Helixi356 – 37116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYImodel-A1-482[»]
4BKXX-ray3.00B1-482[»]
5ICNX-ray3.30B1-376[»]
ProteinModelPortaliQ13547.
SMRiQ13547. Positions 8-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 321313Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ13547.
KOiK06067.
OMAiHASCVKF.
OrthoDBiEOG091G067J.
PhylomeDBiQ13547.
TreeFamiTF106171.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Complete.

Q13547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK
60 70 80 90 100
MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC
110 120 130 140 150
PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF
160 170 180 190 200
CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK
210 220 230 240 250
YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME
260 270 280 290 300
MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
310 320 330 340 350
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM
360 370 380 390 400
TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD
410 420 430 440 450
PDKRISICSS DKRIACEEEF SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE
460 470 480
KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK LA
Length:482
Mass (Da):55,103
Last modified:November 1, 1997 - v1
Checksum:i4D35B7C1ED7838D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti312 – 3121W → R in BAA08909 (PubMed:8646880).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.
CCDSiCCDS360.1.
RefSeqiNP_004955.2. NM_004964.2.
UniGeneiHs.88556.

Genome annotation databases

EnsembliENST00000373548; ENSP00000362649; ENSG00000116478.
GeneIDi3065.
KEGGihsa:3065.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.
CCDSiCCDS360.1.
RefSeqiNP_004955.2. NM_004964.2.
UniGeneiHs.88556.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TYImodel-A1-482[»]
4BKXX-ray3.00B1-482[»]
5ICNX-ray3.30B1-376[»]
ProteinModelPortaliQ13547.
SMRiQ13547. Positions 8-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109315. 541 interactions.
DIPiDIP-24184N.
IntActiQ13547. 243 interactions.
MINTiMINT-90475.
STRINGi9606.ENSP00000362649.

Chemistry

BindingDBiQ13547.
ChEMBLiCHEMBL2093865.
DrugBankiDB06603. Panobinostat.
DB06176. Romidepsin.
DB02546. Vorinostat.
GuidetoPHARMACOLOGYi2658.

PTM databases

iPTMnetiQ13547.
PhosphoSiteiQ13547.
SwissPalmiQ13547.

Polymorphism and mutation databases

BioMutaiHDAC1.
DMDMi2498443.

Proteomic databases

EPDiQ13547.
PaxDbiQ13547.
PeptideAtlasiQ13547.
PRIDEiQ13547.
TopDownProteomicsiQ13547.

Protocols and materials databases

DNASUi3065.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373548; ENSP00000362649; ENSG00000116478.
GeneIDi3065.
KEGGihsa:3065.

Organism-specific databases

CTDi3065.
GeneCardsiHDAC1.
HGNCiHGNC:4852. HDAC1.
HPAiCAB005017.
CAB068191.
HPA029693.
MIMi601241. gene.
neXtProtiNX_Q13547.
PharmGKBiPA29226.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1342. Eukaryota.
COG0123. LUCA.
GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ13547.
KOiK06067.
OMAiHASCVKF.
OrthoDBiEOG091G067J.
PhylomeDBiQ13547.
TreeFamiTF106171.

Enzyme and pathway databases

BRENDAi3.5.1.98. 2681.
ReactomeiR-HSA-1538133. G0 and Early G1.
R-HSA-193670. p75NTR negatively regulates cell cycle via SC1.
R-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-3214815. HDACs deacetylate histones.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-4641265. Repression of WNT target genes.
R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SABIO-RKQ13547.
SIGNORiQ13547.

Miscellaneous databases

ChiTaRSiHDAC1. human.
GeneWikiiHDAC1.
GenomeRNAii3065.
PROiQ13547.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000116478.
CleanExiHS_HDAC1.
ExpressionAtlasiQ13547. baseline and differential.
GenevisibleiQ13547. HS.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetiSearch...

Entry informationi

Entry nameiHDAC1_HUMAN
AccessioniPrimary (citable) accession number: Q13547
Secondary accession number(s): Q92534
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 198 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.