HDAC3

Functionⁱ

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. 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. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (PubMed:21444723, PubMed:23911289). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI₃K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803).3 Publications

Catalytic activityⁱ

Hydrolysis of an N₆-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	135	By similarity		1

GO - Molecular functionⁱ

chromatin binding
Source: UniProtKB
Inferred from direct assayⁱ
- 16569215
- 18417529
cyclin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 18417529
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 11641274
histone deacetylase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16924111
- 18326024
histone deacetylase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 23867755
NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
NF-kappaB binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17785205
protein deacetylase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 17172643
transcription corepressor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16569215
- 18417529
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16569215

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to fluid shear stress
Source: UniProtKB
Inferred from direct assayⁱ
- 25190803
chromatin organization
Source: UniProtKB
Traceable author statementⁱ
- 12711221
circadian rhythm Source: Reactome
histone H3 deacetylation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
histone H4 deacetylation
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of apoptotic process
Source: ProtInc
Traceable author statementⁱ
- 10777477
negative regulation of JNK cascade
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 11931768
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16924111
negative regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 16569215
- 18417529
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from sequence or structural similarityⁱ
- 28614293
positive regulation of protein import into nucleus
Source: UniProtKB
Inferred from direct assayⁱ
- 25190803
positive regulation of protein phosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 25190803
positive regulation of TOR signaling
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 25190803
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 25190803
protein deacetylation
Source: UniProtKB
Inferred from direct assayⁱ
- 17172643
- 21030595
regulation of lipid metabolic process Source: Reactome
regulation of protein stability
Source: UniProtKB
Inferred from direct assayⁱ
- 25190803
spindle assembly
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 18326024

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Chromatin regulator, Hydrolase, Repressor
Biological process	Transcription, Transcription regulation

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1368071 NR1D1 (REV-ERBA) represses gene expression R-HSA-193670 p75NTR negatively regulates cell cycle via SC1 R-HSA-1989781 PPARA activates gene expression R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis 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-381340 Transcriptional regulation of white adipocyte differentiation R-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis R-HSA-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) R-HSA-400253 Circadian Clock R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis R-HSA-8940973 RUNX2 regulates osteoblast differentiation R-HSA-8943724 Regulation of PTEN gene transcription
SABIO-RKⁱ	O15379
SignaLinkⁱ	O15379
SIGNORⁱ	O15379

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histone deacetylase 3 (EC:3.5.1.98) Short name: HD3 Alternative name(s): RPD3-2 SMAP45
Gene namesⁱ	Name:HDAC3
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 5

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000171720.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:4854 HDAC3
MIMⁱ	605166 gene
neXtProtⁱ	NX_O15379

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8841
Open Targets More...OpenTargetsⁱ	ENSG00000171720
PharmGKBⁱ	PA29228

Chemistry databases

ChEMBLⁱ	CHEMBL1829
Drug and drug target database More...DrugBankⁱ	DB05015 Belinostat DB05651 MGCD-0103 DB06603 Panobinostat DB05223 SB939 DB02546 Vorinostat
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2617

Polymorphism and mutation databases

BioMutaⁱ	HDAC3

BioMutaⁱ

HDAC3

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000114696	1 – 428	Histone deacetylase 3Add BLAST		428

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	424	PhosphoserineCombined sources		1

Post-translational modificationⁱ

Sumoylated in vitro.1 Publication

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	O15379
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O15379
PaxDbⁱ	O15379
PeptideAtlas More...PeptideAtlasⁱ	O15379
PRIDEⁱ	O15379
ProteomicsDBⁱ	48618 48619 [O15379-2]

PTM databases

iPTMnetⁱ	O15379
PhosphoSitePlusⁱ	O15379

Miscellaneous databases

PMAP-CutDBⁱ	O15379

PMAP-CutDBⁱ

O15379

Expressionⁱ

Tissue specificityⁱ

Widely expressed.

Inductionⁱ

Up-regulated by disturbed flow in umbilical vein endothelial cells in vitro (PubMed:25190803).

Gene expression databases

Bgeeⁱ	ENSG00000171720 Expressed in 225 organ(s), highest expression level in right hemisphere of cerebellum
CleanExⁱ	HS_HDAC3
ExpressionAtlasⁱ	O15379 baseline and differential
Genevisibleⁱ	O15379 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB005583 HPA052052

HPAⁱ

CAB005583
HPA052052

Interactionⁱ

Subunit structureⁱ

Interacts with HDAC7 and HDAC9. Forms a heterologous complex at least with YY1. Interacts with DAXX, HDAC10 and DACH1. Found in a complex with NCOR1 and NCOR2. Component of the N-Cor repressor complex, at least composed of NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with BCOR, MJD2A/JHDM3A, NRIP1, PRDM6 and SRY. Interacts with BTBD14B. Interacts with GLIS2. Interacts (via the DNA-binding domain) with NR2C1; the interaction recruits phosphorylated NR2C1 to PML bodies for sumoylation. Component of the Notch corepressor complex. Interacts with CBFA2T3 and NKAP. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with and deacetylates MAPK14. Interacts with ZMYND15. Interacts with SMRT/NCOR2 and BCL6 on DNA enhancer elements. Interacts with INSM1 (PubMed:10655483, PubMed:10669754, PubMed:10860984, PubMed:10898795, PubMed:11006275, PubMed:11466315, PubMed:11533236, PubMed:11861901, PubMed:14525983, PubMed:14633989, PubMed:15297880, PubMed:15927959, PubMed:16569215, PubMed:18417529, PubMed:19409814, PubMed:23911289). Interacts with XBP1 isoform 1; the interaction occurs in endothelial cell (EC) under disturbed flow (PubMed:25190803). Interacts (via C-terminus) with CCAR2 (via N-terminus). Interacts with and deacetylates MEF2D. Interacts with BEND3. Interacts with NKAPL (By similarity). Interacts with DHX36; this interaction occurs in a RNA-dependent manner (PubMed:18279852).By similarity20 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
AKAP8	O43823	10	EBI-607682,EBI-1237481
AKAP8L	Q9ULX6	5	EBI-607682,EBI-357530
APPL1	Q9UKG1	2	EBI-607682,EBI-741243
CCND1	P24385	3	EBI-607682,EBI-375001
GATA3	P23771	7	EBI-607682,EBI-6664760
GPS2	Q13227	6	EBI-607682,EBI-713355
ICP0	P08393	3	EBI-607682,EBI-6148881	From Human herpesvirus 1 (strain 17).
KDM1A	O60341	4	EBI-607682,EBI-710124
L3MBTL2	Q969R5	6	EBI-607682,EBI-739909
MAGEA2B	P43356	4	EBI-607682,EBI-5650739
MBD1	Q9UIS9	3	EBI-607682,EBI-867196
MYC	P01106	6	EBI-607682,EBI-447544
NCOR1	O75376	5	EBI-607682,EBI-347233
Ncor1	Q60974	2	EBI-607682,EBI-349004	From Mus musculus.
NCOR2	Q9Y618	13	EBI-607682,EBI-80830
NR0B2	Q15466	2	EBI-607682,EBI-3910729
NRIP1	P48552	2	EBI-607682,EBI-746484
Nrip1	Q8CBD1	2	EBI-607682,EBI-1771626	From Mus musculus.
PGK1	P00558	2	EBI-607682,EBI-709599
PGK1	P00558-1	3	EBI-607682,EBI-16177310
PPP4C	P60510	2	EBI-607682,EBI-1046072
SUZ12	Q15022	7	EBI-607682,EBI-1264675
vif	P12504	2	EBI-607682,EBI-779991	From Human immunodeficiency virus type 1 group M subtype B (isolate NY5).

GO - Molecular functionⁱ

cyclin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 18417529
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 11641274
histone deacetylase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 23867755
NF-kappaB binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17785205
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16569215

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	114368, 222 interactors
CORUMⁱ	O15379
Database of interacting proteins More...DIPⁱ	DIP-24253N
IntActⁱ	O15379, 83 interactors
Molecular INTeraction database More...MINTⁱ	O15379
STRINGⁱ	9606.ENSP00000302967

Chemistry databases

BindingDBⁱ

O15379

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 8	Combined sources	4
Turnⁱ	11 – 14	Combined sources	4
Helixⁱ	27 – 38	Combined sources	12
Helixⁱ	41 – 44	Combined sources	4
Beta strandⁱ	45 – 48	Combined sources	4
Helixⁱ	55 – 58	Combined sources	4
Turnⁱ	59 – 61	Combined sources	3
Helixⁱ	64 – 72	Combined sources	9
Turnⁱ	75 – 77	Combined sources	3
Helixⁱ	78 – 81	Combined sources	4
Helixⁱ	82 – 88	Combined sources	7
Beta strandⁱ	91 – 94	Combined sources	4
Helixⁱ	100 – 119	Combined sources	20
Beta strandⁱ	124 – 128	Combined sources	5
Beta strandⁱ	145 – 147	Combined sources	3
Helixⁱ	149 – 157	Combined sources	9
Turnⁱ	158 – 160	Combined sources	3
Beta strandⁱ	164 – 168	Combined sources	5
Beta strandⁱ	170 – 172	Combined sources	3
Helixⁱ	175 – 180	Combined sources	6
Turnⁱ	181 – 183	Combined sources	3
Beta strandⁱ	185 – 194	Combined sources	10
Helixⁱ	212 – 214	Combined sources	3
Beta strandⁱ	217 – 223	Combined sources	7
Helixⁱ	229 – 247	Combined sources	19
Beta strandⁱ	250 – 255	Combined sources	6
Helixⁱ	258 – 260	Combined sources	3
Helixⁱ	273 – 284	Combined sources	12
Beta strandⁱ	290 – 293	Combined sources	4
Helixⁱ	300 – 314	Combined sources	15
Helixⁱ	329 – 332	Combined sources	4
Turnⁱ	333 – 335	Combined sources	3
Beta strandⁱ	337 – 339	Combined sources	3
Helixⁱ	352 – 367	Combined sources	16

Show more details

3D structure databases

ProteinModelPortalⁱ	O15379
SMRⁱ	O15379
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	3 – 316	Histone deacetylaseAdd BLAST		314

Sequence similaritiesⁱ

Belongs to the histone deacetylase family. HD type 1 subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1342 Eukaryota COG0123 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000144047
HOGENOMⁱ	HOG000225180
HOVERGENⁱ	HBG057112
InParanoidⁱ	O15379
KEGG Orthology (KO) More...KOⁱ	K11404
OMAⁱ	PRAWTHL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G067J
PhylomeDBⁱ	O15379
TreeFamⁱ	TF352182

Family and domain databases

Gene3Dⁱ	3.40.800.20, 1 hit
InterProⁱ	View protein in InterPro IPR000286 His_deacetylse IPR003084 His_deacetylse_1 IPR023801 His_deacetylse_dom IPR037138 His_deacetylse_dom_sf IPR023696 Ureohydrolase_dom_sf
PANTHERⁱ	PTHR10625 PTHR10625, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00850 Hist_deacetyl, 1 hit
PIRSFⁱ	PIRSF037913 His_deacetylse_1, 1 hit
PRINTSⁱ	PR01270 HDASUPER PR01271 HISDACETLASE
SUPFAMⁱ	SSF52768 SSF52768, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O15379-1) [UniParc]FASTA Add to basket

Also known as: RPD3-2B

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP 
        60         70         80         90        100
YQASQHDMCR FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL 
       110        120        130        140        150
FEFCSRYTGA SLQGATQLNN KICDIAINWA GGLHHAKKFE ASGFCYVNDI 
       160        170        180        190        200
VIGILELLKY HPRVLYIDID IHHGDGVQEA FYLTDRVMTV SFHKYGNYFF 
       210        220        230        240        250
PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI NQVVDFYQPT 
       260        270        280        290        300
CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV 
       310        320        330        340        350
RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN 
       360        370        380        390        400
SRQYLDQIRQ TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP 
       410        420 
EENYSRPEAP NEFYDGDHDN DKESDVEI

Length:428

Mass (Da):48,848

Last modified:July 15, 1998 - v2

Checksum:ⁱ94485C1EBDCF5AD0

GO

Isoform 2 (identifier: O15379-2) [UniParc]FASTA Add to basket

Also known as: RPD3-2A

The sequence of this isoform differs from the canonical sequence as follows:
1-15: MAKTVAYFYDPDVGN → MIVFKPYQASQHDMCR

« Hide

        10         20         30         40         50
MIVFKPYQAS QHDMCRFHYG AGHPMKPHRL ALTHSLVLHY GLYKKMIVFK 
        60         70         80         90        100
PYQASQHDMC RFHSEDYIDF LQRVSPTNMQ GFTKSLNAFN VGDDCPVFPG 
       110        120        130        140        150
LFEFCSRYTG ASLQGATQLN NKICDIAINW AGGLHHAKKF EASGFCYVND 
       160        170        180        190        200
IVIGILELLK YHPRVLYIDI DIHHGDGVQE AFYLTDRVMT VSFHKYGNYF 
       210        220        230        240        250
FPGTGDMYEV GAESGRYYCL NVPLRDGIDD QSYKHLFQPV INQVVDFYQP 
       260        270        280        290        300
TCIVLQCGAD SLGCDRLGCF NLSIRGHGEC VEYVKSFNIP LLVLGGGGYT 
       310        320        330        340        350
VRNVARCWTY ETSLLVEEAI SEELPYSEYF EYFAPDFTLH PDVSTRIENQ 
       360        370        380        390        400
NSRQYLDQIR QTIFENLKML NHAPSVQIHD VPADLLTYDR TDEADAEERG 
       410        420 
PEENYSRPEA PNEFYDGDHD NDKESDVEI

Show »

Length:429

Mass (Da):49,111

Checksum:ⁱ0B654598513D284B

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

E7ESJ6	E7ESJ6_HUMAN	Histone deacetylase 3 Histone deacetylase 3	HDAC3	218	Annotation score:
E7EW19	E7EW19_HUMAN	Histone deacetylase 3 Histone deacetylase 3	HDAC3	53	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	359	R → L in AAC52038 (PubMed:9464271).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_033988	411	N → S. Corresponds to variant dbSNP:rs34901743Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_002079	1 – 15	MAKTV…PDVGN → MIVFKPYQASQHDMCR in isoform 2. 1 PublicationAdd BLAST		15

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U66914 mRNA Translation: AAC52038.1 U75697 mRNA Translation: AAB88241.1 U75696 mRNA Translation: AAB88240.1 AF005482 mRNA Translation: AAB87752.1 AF039703 mRNA Translation: AAC98927.1 AF059650 Genomic DNA Translation: AAC26509.1 CH471062 Genomic DNA Translation: EAW61915.1 CH471062 Genomic DNA Translation: EAW61916.1 BC000614 mRNA Translation: AAH00614.1 AF053138, AF053137 Genomic DNA Translation: AAC08351.1 AF053139 Genomic DNA Translation: AAC08352.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS4264.1 [O15379-1]
PIRⁱ	JC5834
NCBI Reference Sequences More...RefSeqⁱ	NP_003874.2, NM_003883.3 [O15379-1]
UniGeneⁱ	Hs.519632

Genome annotation databases

Ensemblⁱ	ENST00000305264; ENSP00000302967; ENSG00000171720 [O15379-1]
GeneIDⁱ	8841
KEGGⁱ	hsa:8841
UCSC genome browser More...UCSCⁱ	uc003llf.3 human [O15379-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O15379	Histone deacetylase 3 (Fragment)		wild yak		445	UniRef100_O15379
Histone deacetylase		CALJA		428
Histone deacetylase		PANTR		428
Histone deacetylase		MACMU		428
Histone deacetylase		PONAB		428
+37

Protein	Similar proteins		Species	Score	Length	Source
O15379	Histone deacetylase 3		XENLA		428	UniRef90_O15379
Histone deacetylase 3		XENTR		428
Histone deacetylase 3		PONAB		428
Histone deacetylase 3		CHICK		428
Histone deacetylase 3		MOUSE		424
+157

Protein	Similar proteins		Species	Score	Length	Source
O15379	Histone deacetylase 3		PONAB		428	UniRef50_O15379
Histone deacetylase 3		CHICK		428
Histone deacetylase 3		XENLA		428
Histone deacetylase 3		XENTR		428
Histone deacetylase 3		MOUSE		424
+302

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U66914 mRNA Translation: AAC52038.1 U75697 mRNA Translation: AAB88241.1 U75696 mRNA Translation: AAB88240.1 AF005482 mRNA Translation: AAB87752.1 AF039703 mRNA Translation: AAC98927.1 AF059650 Genomic DNA Translation: AAC26509.1 CH471062 Genomic DNA Translation: EAW61915.1 CH471062 Genomic DNA Translation: EAW61916.1 BC000614 mRNA Translation: AAH00614.1 AF053138, AF053137 Genomic DNA Translation: AAC08351.1 AF053139 Genomic DNA Translation: AAC08352.1
CCDSⁱ	CCDS4264.1 [O15379-1]
PIRⁱ	JC5834
RefSeqⁱ	NP_003874.2, NM_003883.3 [O15379-1]
UniGeneⁱ	Hs.519632

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4A69	X-ray	2.06	A/B	1-376	[»]
ProteinModelPortalⁱ	O15379
SMRⁱ	O15379
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114368, 222 interactors
CORUMⁱ	O15379
DIPⁱ	DIP-24253N
IntActⁱ	O15379, 83 interactors
MINTⁱ	O15379
STRINGⁱ	9606.ENSP00000302967

Chemistry databases

BindingDBⁱ	O15379
ChEMBLⁱ	CHEMBL1829
DrugBankⁱ	DB05015 Belinostat DB05651 MGCD-0103 DB06603 Panobinostat DB05223 SB939 DB02546 Vorinostat
GuidetoPHARMACOLOGYⁱ	2617

PTM databases

iPTMnetⁱ	O15379
PhosphoSitePlusⁱ	O15379

Polymorphism and mutation databases

BioMutaⁱ	HDAC3

BioMutaⁱ

HDAC3

Proteomic databases

EPDⁱ	O15379
MaxQBⁱ	O15379
PaxDbⁱ	O15379
PeptideAtlasⁱ	O15379
PRIDEⁱ	O15379
ProteomicsDBⁱ	48618 48619 [O15379-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	8841
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000305264; ENSP00000302967; ENSG00000171720 [O15379-1]
GeneIDⁱ	8841
KEGGⁱ	hsa:8841
UCSCⁱ	uc003llf.3 human [O15379-1]

Organism-specific databases

CTDⁱ	8841
DisGeNETⁱ	8841
EuPathDBⁱ	HostDB:ENSG00000171720.9
GeneCardsⁱ	HDAC3
HGNCⁱ	HGNC:4854 HDAC3
HPAⁱ	CAB005583 HPA052052
MIMⁱ	605166 gene
neXtProtⁱ	NX_O15379
OpenTargetsⁱ	ENSG00000171720
PharmGKBⁱ	PA29228
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1342 Eukaryota COG0123 LUCA
GeneTreeⁱ	ENSGT00910000144047
HOGENOMⁱ	HOG000225180
HOVERGENⁱ	HBG057112
InParanoidⁱ	O15379
KOⁱ	K11404
OMAⁱ	PRAWTHL
OrthoDBⁱ	EOG091G067J
PhylomeDBⁱ	O15379
TreeFamⁱ	TF352182

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1368071 NR1D1 (REV-ERBA) represses gene expression R-HSA-193670 p75NTR negatively regulates cell cycle via SC1 R-HSA-1989781 PPARA activates gene expression R-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis 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-381340 Transcriptional regulation of white adipocyte differentiation R-HSA-390471 Association of TriC/CCT with target proteins during biosynthesis R-HSA-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) R-HSA-400253 Circadian Clock R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis R-HSA-8940973 RUNX2 regulates osteoblast differentiation R-HSA-8943724 Regulation of PTEN gene transcription
SABIO-RKⁱ	O15379
SignaLinkⁱ	O15379
SIGNORⁱ	O15379

Miscellaneous databases

ChiTaRSⁱ	HDAC3 human
GeneWikiⁱ	HDAC3
GenomeRNAiⁱ	8841
PMAP-CutDBⁱ	O15379
Protein Ontology More...PROⁱ	PR:O15379
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000171720 Expressed in 225 organ(s), highest expression level in right hemisphere of cerebellum
CleanExⁱ	HS_HDAC3
ExpressionAtlasⁱ	O15379 baseline and differential
Genevisibleⁱ	O15379 HS

Family and domain databases

Gene3Dⁱ	3.40.800.20, 1 hit
InterProⁱ	View protein in InterPro IPR000286 His_deacetylse IPR003084 His_deacetylse_1 IPR023801 His_deacetylse_dom IPR037138 His_deacetylse_dom_sf IPR023696 Ureohydrolase_dom_sf
PANTHERⁱ	PTHR10625 PTHR10625, 1 hit
Pfamⁱ	View protein in Pfam PF00850 Hist_deacetyl, 1 hit
PIRSFⁱ	PIRSF037913 His_deacetylse_1, 1 hit
PRINTSⁱ	PR01270 HDASUPER PR01271 HISDACETLASE
SUPFAMⁱ	SSF52768 SSF52768, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	HDAC3_HUMAN
Accessionⁱ	O15379Primary (citable) accession number: O15379 Secondary accession number(s): D3DQE1 , O43268, Q9UEI5, Q9UEV0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	July 15, 1998
	Last modified:	November 7, 2018
	This is version 201 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 5
Human chromosome 5: entries, gene names and cross-references to MIM

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UniProtKB - O15379 (HDAC3_HUMAN)

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Histone deacetylase 3

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ