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Q92769

- HDAC2_HUMAN

UniProt

Q92769 - HDAC2_HUMAN

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Protein

Histone deacetylase 2

Gene

HDAC2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor 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. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A.2 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 sitei142 – 1421By similarity

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. chromatin DNA binding Source: Ensembl
  3. deacetylase activity Source: UniProtKB
  4. enzyme binding Source: UniProtKB
  5. histone deacetylase activity Source: BHF-UCL
  6. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  7. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  8. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  9. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  10. poly(A) RNA binding Source: UniProtKB
  11. protein deacetylase activity Source: BHF-UCL
  12. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  13. sequence-specific DNA binding Source: BHF-UCL
  14. sequence-specific DNA binding transcription factor activity Source: Ensembl
  15. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProt
  2. blood coagulation Source: Reactome
  3. cardiac muscle cell development Source: Ensembl
  4. chromatin remodeling Source: BHF-UCL
  5. circadian regulation of gene expression Source: UniProtKB
  6. dendrite development Source: UniProtKB
  7. embryonic digit morphogenesis Source: BHF-UCL
  8. epidermal cell differentiation Source: BHF-UCL
  9. eyelid development in camera-type eye Source: BHF-UCL
  10. fungiform papilla formation Source: BHF-UCL
  11. hair follicle placode formation Source: BHF-UCL
  12. hippocampus development Source: Ensembl
  13. histone deacetylation Source: BHF-UCL
  14. histone H3 deacetylation Source: UniProtKB
  15. histone H4 deacetylation Source: UniProtKB
  16. maintenance of chromatin silencing Source: BHF-UCL
  17. negative regulation of apoptotic process Source: BHF-UCL
  18. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  19. negative regulation of cardiac muscle cell proliferation Source: Ensembl
  20. negative regulation of cell cycle Source: Reactome
  21. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
  22. negative regulation of MHC class II biosynthetic process Source: BHF-UCL
  23. negative regulation of neuron projection development Source: BHF-UCL
  24. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  25. negative regulation of transcription, DNA-templated Source: BHF-UCL
  26. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  27. neurotrophin TRK receptor signaling pathway Source: Reactome
  28. odontogenesis of dentin-containing tooth Source: BHF-UCL
  29. positive regulation of cell proliferation Source: BHF-UCL
  30. positive regulation of collagen biosynthetic process Source: BHF-UCL
  31. positive regulation of oligodendrocyte differentiation Source: Ensembl
  32. positive regulation of proteolysis Source: BHF-UCL
  33. positive regulation of receptor biosynthetic process Source: BHF-UCL
  34. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  35. positive regulation of transcription, DNA-templated Source: BHF-UCL
  36. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  37. regulation of protein deacetylation Source: Ensembl
  38. regulation of protein kinase B signaling Source: Ensembl
  39. regulation of sarcomere organization Source: Ensembl
  40. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_228222. HDACs deacetylate histones.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_953. RNA Polymerase I Transcription Initiation.
SABIO-RKQ92769.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 2 (EC:3.5.1.98)
Short name:
HD2
Gene namesi
Name:HDAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:4853. HDAC2.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. ESC/E(Z) complex Source: UniProtKB
  3. heterochromatin Source: Ensembl
  4. nuclear chromatin Source: UniProt
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
  7. NuRD complex Source: UniProtKB
  8. protein complex Source: UniProt
  9. replication fork Source: Ensembl
  10. Sin3 complex Source: UniProtKB
  11. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29227.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Histone deacetylase 2PRO_0000114693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei262 – 2621S-nitrosocysteineBy similarity
Modified residuei274 – 2741S-nitrosocysteineBy similarity
Modified residuei394 – 3941Phosphoserine5 Publications
Modified residuei422 – 4221Phosphoserine4 Publications
Modified residuei424 – 4241Phosphoserine4 Publications

Post-translational modificationi

S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching. S-Nitrosylation interferes with its interaction with MTA1 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiQ92769.
PRIDEiQ92769.

PTM databases

PhosphoSiteiQ92769.

Expressioni

Tissue specificityi

Widely expressed; lower levels in brain and lung.

Gene expression databases

BgeeiQ92769.
CleanExiHS_HDAC2.
ExpressionAtlasiQ92769. baseline and differential.
GenevestigatoriQ92769.

Organism-specific databases

HPAiCAB005054.
HPA011727.

Interactioni

Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, 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 RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with FAM64A. Interacts with BCL6 (non-acetylated form). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Interacts with NACC2. Interacts with MTA1, with a preference for sumoylated MTA1. Interacts with SIX3 (By similarity).By similarity27 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL11BQ9C0K03EBI-301821,EBI-6597578
BRMS1Q9HCU94EBI-301821,EBI-714781
DAXXQ9UER72EBI-301821,EBI-77321
HCFC1P516102EBI-301821,EBI-396176
HDAC1Q1354710EBI-301821,EBI-301834
K8Q2HR827EBI-301821,EBI-9006943From a different organism.
MBD1Q9UIS92EBI-301821,EBI-867196
MTA1Q133304EBI-301821,EBI-714236
MYCP011062EBI-301821,EBI-447544
NPM1P067482EBI-301821,EBI-78579
RFX5P483824EBI-301821,EBI-923266
SIN3AQ96ST34EBI-301821,EBI-347218
SRA1Q9HD152EBI-301821,EBI-727136
SUV39H1O434633EBI-301821,EBI-349968

Protein-protein interaction databases

BioGridi109316. 363 interactions.
DIPiDIP-24220N.
IntActiQ92769. 110 interactions.
MINTiMINT-90593.
STRINGi9606.ENSP00000381331.

Structurei

Secondary structure

1
488
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Helixi20 – 223Combined sources
Helixi34 – 4512Combined sources
Helixi48 – 514Combined sources
Beta strandi52 – 554Combined sources
Helixi62 – 654Combined sources
Turni66 – 683Combined sources
Helixi71 – 799Combined sources
Turni82 – 843Combined sources
Helixi85 – 884Combined sources
Helixi89 – 957Combined sources
Beta strandi98 – 1014Combined sources
Helixi107 – 12620Combined sources
Beta strandi131 – 1355Combined sources
Helixi156 – 1649Combined sources
Turni165 – 1673Combined sources
Beta strandi171 – 1755Combined sources
Beta strandi177 – 1793Combined sources
Helixi182 – 1876Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 20110Combined sources
Helixi218 – 2203Combined sources
Beta strandi224 – 2296Combined sources
Helixi235 – 25319Combined sources
Beta strandi256 – 2616Combined sources
Helixi264 – 2663Combined sources
Helixi279 – 29113Combined sources
Beta strandi296 – 2994Combined sources
Helixi306 – 32015Combined sources
Helixi335 – 3384Combined sources
Turni339 – 3413Combined sources
Beta strandi343 – 3453Combined sources
Helixi357 – 37115Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MAXX-ray2.05A/B/C9-374[»]
4LXZX-ray1.85A/B/C8-376[»]
4LY1X-ray1.57A/B/C8-376[»]
ProteinModelPortaliQ92769.
SMRiQ92769. Positions 9-376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92769.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 322314Histone deacetylaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi300 – 3034Poly-Gly

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00530000062889.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiQ92769.
KOiK06067.
PhylomeDBiQ92769.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92769-1) [UniParc]FASTAAdd to Basket

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
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR
60 70 80 90 100
KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED
110 120 130 140 150
CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG
160 170 180 190 200
FCYVNDIVLA ILELLKYHQR VLYIDIDIHH GDGVEEAFYT TDRVMTVSFH
210 220 230 240 250
KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM
260 270 280 290 300
EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
310 320 330 340 350
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN
360 370 380 390 400
MTNQNTPEYM EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE
410 420 430 440 450
DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED
460 470 480
KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNP
Length:488
Mass (Da):55,364
Last modified:June 21, 2005 - v2
Checksum:i775419CCCDAE07FA
GO
Isoform 2 (identifier: Q92769-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Note: No experimental confirmation available.

Show »
Length:458
Mass (Da):51,998
Checksum:i73BF368ACAA58819
GO

Sequence cautioni

The sequence AAH31055.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG59420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 942QR → HI in AAC50814. (PubMed:8917507)Curated
Sequence conflicti103 – 1031V → A in AAC50814. (PubMed:8917507)Curated
Sequence conflicti146 – 1461S → Y in AAC50814. (PubMed:8917507)Curated
Sequence conflicti248 – 2481K → M in BAG59420. (PubMed:14702039)Curated
Sequence conflicti281 – 2811G → D in BAG59420. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti230 – 2301R → C.1 Publication
Corresponds to variant rs1042903 [ dbSNP | Ensembl ].
VAR_025311
Natural varianti315 – 3151Y → H.1 Publication
Corresponds to variant rs17852888 [ dbSNP | Ensembl ].
VAR_025312

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030Missing in isoform 2. 1 PublicationVSP_056175Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31814 mRNA. Translation: AAC50814.1.
AK092156 mRNA. Translation: BAG52487.1.
AK296856 mRNA. Translation: BAG59420.1. Different initiation.
AL590398 Genomic DNA. No translation available.
AL671967 Genomic DNA. No translation available.
FO393415 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48252.1.
CH471051 Genomic DNA. Translation: EAW48253.1.
CH471051 Genomic DNA. Translation: EAW48254.1.
CH471051 Genomic DNA. Translation: EAW48255.1.
BC031055 mRNA. Translation: AAH31055.2. Different initiation.
CCDSiCCDS43493.2. [Q92769-1]
RefSeqiNP_001518.3. NM_001527.3. [Q92769-1]
UniGeneiHs.3352.

Genome annotation databases

EnsembliENST00000368632; ENSP00000357621; ENSG00000196591. [Q92769-3]
ENST00000519065; ENSP00000430432; ENSG00000196591. [Q92769-1]
ENST00000519108; ENSP00000430008; ENSG00000196591. [Q92769-3]
GeneIDi3066.
KEGGihsa:3066.
UCSCiuc003pwc.2. human. [Q92769-1]

Polymorphism databases

DMDMi68068066.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31814 mRNA. Translation: AAC50814.1 .
AK092156 mRNA. Translation: BAG52487.1 .
AK296856 mRNA. Translation: BAG59420.1 . Different initiation.
AL590398 Genomic DNA. No translation available.
AL671967 Genomic DNA. No translation available.
FO393415 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48252.1 .
CH471051 Genomic DNA. Translation: EAW48253.1 .
CH471051 Genomic DNA. Translation: EAW48254.1 .
CH471051 Genomic DNA. Translation: EAW48255.1 .
BC031055 mRNA. Translation: AAH31055.2 . Different initiation.
CCDSi CCDS43493.2. [Q92769-1 ]
RefSeqi NP_001518.3. NM_001527.3. [Q92769-1 ]
UniGenei Hs.3352.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3MAX X-ray 2.05 A/B/C 9-374 [» ]
4LXZ X-ray 1.85 A/B/C 8-376 [» ]
4LY1 X-ray 1.57 A/B/C 8-376 [» ]
ProteinModelPortali Q92769.
SMRi Q92769. Positions 9-376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109316. 363 interactions.
DIPi DIP-24220N.
IntActi Q92769. 110 interactions.
MINTi MINT-90593.
STRINGi 9606.ENSP00000381331.

Chemistry

BindingDBi Q92769.
ChEMBLi CHEMBL2093865.
DrugBanki DB01223. Aminophylline.
DB00227. Lovastatin.
DB01303. Oxtriphylline.
DB00277. Theophylline.
DB00313. Valproic Acid.
DB02546. Vorinostat.
GuidetoPHARMACOLOGYi 2616.

PTM databases

PhosphoSitei Q92769.

Polymorphism databases

DMDMi 68068066.

Proteomic databases

MaxQBi Q92769.
PRIDEi Q92769.

Protocols and materials databases

DNASUi 3066.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368632 ; ENSP00000357621 ; ENSG00000196591 . [Q92769-3 ]
ENST00000519065 ; ENSP00000430432 ; ENSG00000196591 . [Q92769-1 ]
ENST00000519108 ; ENSP00000430008 ; ENSG00000196591 . [Q92769-3 ]
GeneIDi 3066.
KEGGi hsa:3066.
UCSCi uc003pwc.2. human. [Q92769-1 ]

Organism-specific databases

CTDi 3066.
GeneCardsi GC06M114254.
HGNCi HGNC:4853. HDAC2.
HPAi CAB005054.
HPA011727.
MIMi 605164. gene.
neXtProti NX_Q92769.
PharmGKBi PA29227.
GenAtlasi Search...

Phylogenomic databases

GeneTreei ENSGT00530000062889.
HOGENOMi HOG000225180.
HOVERGENi HBG057112.
InParanoidi Q92769.
KOi K06067.
PhylomeDBi Q92769.
TreeFami TF106171.

Enzyme and pathway databases

Reactomei REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_13695. p75NTR negatively regulates cell cycle via SC1.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_200856. NoRC negatively regulates rRNA expression.
REACT_228222. HDACs deacetylate histones.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_953. RNA Polymerase I Transcription Initiation.
SABIO-RK Q92769.

Miscellaneous databases

ChiTaRSi HDAC2. human.
EvolutionaryTracei Q92769.
GeneWikii Histone_deacetylase_2.
GenomeRNAii 3066.
NextBioi 12129.
PROi Q92769.
SOURCEi Search...

Gene expression databases

Bgeei Q92769.
CleanExi HS_HDAC2.
ExpressionAtlasi Q92769. baseline and differential.
Genevestigatori Q92769.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037913. His_deacetylse_1. 1 hit.
PRINTSi PR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3."
    Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.
    Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-230.
    Tissue: Mammary gland.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Tongue.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-315.
    Tissue: Testis.
  6. "Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4."
    Schmidt D.R., Schreiber S.L.
    Biochemistry 38:14711-14717(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATR, IDENTIFICATION IN A COMPLEX CONTAINING ATR AND CHD4.
  7. "A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
    Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.
    J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNW1.
  8. "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."
    Rountree M.R., Bachman K.E., Baylin S.B.
    Nat. Genet. 25:269-277(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMT1 AND DMAP1.
  9. "NuRD and SIN3 histone deacetylase complexes in development."
    Ahringer J.
    Trends Genet. 16:351-356(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON DEACETYLASE COMPLEXES.
  10. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
    Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
    Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MINT.
  11. "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with multiple histone deacetylases and binds mSin3A through its oligomerization domain."
    Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., Downing J.R., Meyers S., Hiebert S.W.
    Mol. Cell. Biol. 21:6470-6483(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  12. "Isolation and characterization of a novel class II histone deacetylase, HDAC10."
    Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., Trogani N., Widmer R., Atadja P., Cohen D.
    J. Biol. Chem. 277:6656-6666(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC10.
  13. "The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2."
    Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.
    J. Biol. Chem. 277:35783-35786(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SP3.
  14. "Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
    Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
    J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAXX AND DEK.
  15. "Acetylation inactivates the transcriptional repressor BCL6."
    Bereshchenko O.R., Gu W., Dalla-Favera R.
    Nat. Genet. 32:606-613(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL6.
  16. "Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene."
    Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.
    EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX1.
  17. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
    Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
    Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCFC1.
  18. "A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes."
    Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.
    J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC1; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
  19. "Identification and characterization of three new components of the mSin3A corepressor complex."
    Fleischer T.C., Yun U.J., Ayer D.E.
    Mol. Cell. Biol. 23:3456-3467(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
  20. "The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains."
    Choi Y.B., Ko J.K., Shin J.
    J. Biol. Chem. 279:50930-50941(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PELP1.
  21. "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
    Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
    Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRIP1.
  22. "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
    Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
    J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JMJD2A.
  23. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus."
    Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O.
    Nucleic Acids Res. 34:3288-3298(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAP30L.
  25. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
    Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
    Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC1.
  27. Cited for: INTERACTION WITH BCL6.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "RCS1, a substrate of APC/C, controls the metaphase to anaphase transition."
    Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.
    Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAM64A.
  30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. Cited for: FUNCTION, INTERACTION WITH TSHZ3.
  32. "Chfr is linked to tumour metastasis through the downregulation of HDAC1."
    Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H.
    Nat. Cell Biol. 11:295-302(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHFR.
  33. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MTA1.
  37. "Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
    Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
    Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMARCAD1.
  38. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "RBB, a novel transcription repressor, represses the transcription of HDM2 oncogene."
    Xuan C., Wang Q., Han X., Duan Y., Li L., Shi L., Wang Y., Shan L., Yao Z., Shang Y.
    Oncogene 32:3711-3721(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NACC2.
  40. "The subcellular distribution and function of MTA1 in cancer differentiation."
    Liu J., Xu D., Wang H., Zhang Y., Chang Y., Zhang J., Wang J., Li C., Liu H., Zhao M., Lin C., Zhan Q., Huang C., Qian H.
    Oncotarget 5:5153-5164(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MTA1.
  41. "Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides."
    Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R., O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R.
    Bioorg. Med. Chem. Lett. 20:3142-3145(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS.

Entry informationi

Entry nameiHDAC2_HUMAN
AccessioniPrimary (citable) accession number: Q92769
Secondary accession number(s): B3KRS5
, B4DL58, E1P561, Q5SRI8, Q5SZ86, Q8NEH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: November 26, 2014
This is version 166 of the entry and version 2 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3