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Q92769

- HDAC2_HUMAN

UniProt

Q92769 - HDAC2_HUMAN

Protein

Histone deacetylase 2

Gene

HDAC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    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. core promoter binding Source: Ensembl
    4. deacetylase activity Source: UniProtKB
    5. enzyme binding Source: UniProtKB
    6. histone deacetylase activity Source: BHF-UCL
    7. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    8. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    9. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    10. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    11. poly(A) RNA binding Source: UniProtKB
    12. protein binding Source: UniProtKB
    13. protein deacetylase activity Source: BHF-UCL
    14. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    15. sequence-specific DNA binding Source: BHF-UCL
    16. sequence-specific DNA binding transcription factor activity Source: Ensembl
    17. 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. cellular response to heat Source: Ensembl
    5. chromatin remodeling Source: BHF-UCL
    6. circadian regulation of gene expression Source: UniProtKB
    7. dendrite development Source: UniProtKB
    8. embryonic digit morphogenesis Source: BHF-UCL
    9. epidermal cell differentiation Source: BHF-UCL
    10. eyelid development in camera-type eye Source: BHF-UCL
    11. fungiform papilla formation Source: BHF-UCL
    12. hair follicle placode formation Source: BHF-UCL
    13. hippocampus development Source: Ensembl
    14. histone deacetylation Source: BHF-UCL
    15. histone H3 deacetylation Source: UniProtKB
    16. histone H4 deacetylation Source: UniProtKB
    17. maintenance of chromatin silencing Source: BHF-UCL
    18. negative regulation of apoptotic process Source: BHF-UCL
    19. negative regulation of canonical Wnt signaling pathway Source: Ensembl
    20. negative regulation of cardiac muscle cell proliferation Source: Ensembl
    21. negative regulation of cell cycle Source: Reactome
    22. negative regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    23. negative regulation of MHC class II biosynthetic process Source: BHF-UCL
    24. negative regulation of neuron projection development Source: BHF-UCL
    25. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    26. negative regulation of transcription, DNA-templated Source: BHF-UCL
    27. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    28. neurotrophin TRK receptor signaling pathway Source: Reactome
    29. odontogenesis of dentin-containing tooth Source: BHF-UCL
    30. positive regulation of cell proliferation Source: BHF-UCL
    31. positive regulation of collagen biosynthetic process Source: BHF-UCL
    32. positive regulation of oligodendrocyte differentiation Source: Ensembl
    33. positive regulation of proteolysis Source: BHF-UCL
    34. positive regulation of receptor biosynthetic process Source: BHF-UCL
    35. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    36. positive regulation of transcription, DNA-templated Source: BHF-UCL
    37. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    38. regulation of protein deacetylation Source: Ensembl
    39. regulation of protein kinase B signaling Source: Ensembl
    40. regulation of sarcomere organization Source: Ensembl
    41. response to cocaine Source: Ensembl
    42. response to drug Source: Ensembl
    43. transcription, DNA-templated Source: UniProtKB-KW

    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_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: BHF-UCL
    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

    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

    ArrayExpressiQ92769.
    BgeeiQ92769.
    CleanExiHS_HDAC2.
    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 MTA1.27 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. 360 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 – 154
    Helixi20 – 223
    Helixi34 – 4512
    Helixi48 – 514
    Beta strandi52 – 554
    Helixi62 – 654
    Turni66 – 683
    Helixi71 – 799
    Turni82 – 843
    Helixi85 – 884
    Helixi89 – 957
    Beta strandi98 – 1014
    Helixi107 – 12620
    Beta strandi131 – 1355
    Helixi156 – 1649
    Turni165 – 1673
    Beta strandi171 – 1755
    Beta strandi177 – 1793
    Helixi182 – 1876
    Turni188 – 1903
    Beta strandi192 – 20110
    Helixi218 – 2203
    Beta strandi224 – 2296
    Helixi235 – 25319
    Beta strandi256 – 2616
    Helixi264 – 2663
    Helixi279 – 29113
    Beta strandi296 – 2994
    Helixi306 – 32015
    Helixi335 – 3384
    Turni339 – 3413
    Beta strandi343 – 3453
    Helixi357 – 37115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    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

    MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR    50
    KMEIYRPHKA TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED 100
    CPVFDGLFEF CQLSTGGSVA GAVKLNRQQT DMAVNWAGGL HHAKKSEASG 150
    FCYVNDIVLA ILELLKYHQR VLYIDIDIHH GDGVEEAFYT TDRVMTVSFH 200
    KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ IFKPIISKVM 250
    EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG 300
    GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN 350
    MTNQNTPEYM EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE 400
    DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED 450
    KKETEDKKTD VKEEDKSKDN SGEKTDTKGT KSEQLSNP 488
    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.
    The sequence BAG59420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_001518.3. NM_001527.3.
    UniGeneiHs.3352.

    Genome annotation databases

    EnsembliENST00000368632; ENSP00000357621; ENSG00000196591.
    ENST00000519065; ENSP00000430432; ENSG00000196591.
    GeneIDi3066.
    KEGGihsa:3066.
    UCSCiuc003pwc.2. human.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqi NP_001518.3. NM_001527.3.
    UniGenei Hs.3352.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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. 360 interactions.
    DIPi DIP-24220N.
    IntActi Q92769. 110 interactions.
    MINTi MINT-90593.
    STRINGi 9606.ENSP00000381331.

    Chemistry

    BindingDBi Q92769.
    ChEMBLi CHEMBL2093865.
    DrugBanki 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 .
    ENST00000519065 ; ENSP00000430432 ; ENSG00000196591 .
    GeneIDi 3066.
    KEGGi hsa:3066.
    UCSCi uc003pwc.2. human.

    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

    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_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_953. RNA Polymerase I Transcription Initiation.
    SABIO-RK Q92769.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q92769.
    Bgeei Q92769.
    CleanExi HS_HDAC2.
    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

    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 0:0-0(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: October 1, 2014
    This is version 164 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