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P70288

- HDAC2_MOUSE

UniProt

P70288 - HDAC2_MOUSE

Protein

Histone deacetylase 2

Gene

Hdac2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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 By similarity. 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.By similarity3 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: MGI
    3. core promoter binding Source: Ensembl
    4. deacetylase activity Source: UniProtKB
    5. enzyme binding Source: UniProtKB
    6. histone deacetylase activity Source: UniProtKB
    7. Krueppel-associated box domain binding Source: UniProtKB
    8. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    9. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    10. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    11. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    12. protein binding Source: UniProtKB
    13. protein deacetylase activity Source: BHF-UCL
    14. sequence-specific DNA binding Source: Ensembl
    15. sequence-specific DNA binding transcription factor activity Source: MGI
    16. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. cardiac muscle cell development Source: MGI
    2. cellular response to heat Source: Ensembl
    3. chromatin modification Source: UniProtKB
    4. circadian regulation of gene expression Source: UniProtKB
    5. dendrite development Source: UniProtKB
    6. embryonic digit morphogenesis Source: BHF-UCL
    7. epidermal cell differentiation Source: BHF-UCL
    8. eyelid development in camera-type eye Source: BHF-UCL
    9. fungiform papilla formation Source: BHF-UCL
    10. hair follicle placode formation Source: BHF-UCL
    11. hippocampus development Source: MGI
    12. histone deacetylation Source: MGI
    13. histone H3 deacetylation Source: UniProtKB
    14. histone H4 deacetylation Source: UniProtKB
    15. maintenance of chromatin silencing Source: Ensembl
    16. negative regulation of apoptotic process Source: BHF-UCL
    17. negative regulation of canonical Wnt signaling pathway Source: MGI
    18. negative regulation of cardiac muscle cell proliferation Source: MGI
    19. negative regulation of intrinsic apoptotic signaling pathway Source: MGI
    20. negative regulation of neuron projection development Source: BHF-UCL
    21. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    22. negative regulation of transcription, DNA-templated Source: BHF-UCL
    23. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    24. neuron differentiation Source: MGI
    25. odontogenesis of dentin-containing tooth Source: BHF-UCL
    26. positive regulation of cell proliferation Source: BHF-UCL
    27. positive regulation of oligodendrocyte differentiation Source: MGI
    28. positive regulation of proteolysis Source: Ensembl
    29. positive regulation of receptor biosynthetic process Source: Ensembl
    30. positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
    31. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    32. protein deacetylation Source: BHF-UCL
    33. regulation of protein deacetylation Source: MGI
    34. regulation of protein kinase B signaling Source: MGI
    35. regulation of sarcomere organization Source: MGI
    36. response to cocaine Source: Ensembl
    37. response to drug Source: Ensembl
    38. 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_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_202086. p75NTR negatively regulates cell cycle via SC1.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 2 (EC:3.5.1.98)
    Short name:
    HD2
    Alternative name(s):
    YY1 transcription factor-binding protein
    Gene namesi
    Name:Hdac2
    Synonyms:Yy1bp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1097691. Hdac2.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. ESC/E(Z) complex Source: UniProtKB
    3. heterochromatin Source: MGI
    4. histone deacetylase complex Source: UniProtKB
    5. nuclear chromatin Source: BHF-UCL
    6. nucleus Source: MGI
    7. NuRD complex Source: Ensembl
    8. replication fork Source: MGI
    9. Sin3 complex Source: Ensembl
    10. transcriptional repressor complex Source: MGI
    11. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi152 – 1521C → A: Does not affect S-nitrosylation. 1 Publication
    Mutagenesisi262 – 2621C → A: Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with A-274. 1 Publication
    Mutagenesisi274 – 2741C → A: Impairs S-nitrosylation. Abolishes S-nitrosylation; when associated with A-262. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 488488Histone deacetylase 2PRO_0000114694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei262 – 2621S-nitrosocysteine1 Publication
    Modified residuei274 – 2741S-nitrosocysteine1 Publication
    Modified residuei394 – 3941Phosphoserine3 Publications
    Modified residuei422 – 4221Phosphoserine2 Publications
    Modified residuei424 – 4241Phosphoserine2 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 MTA1.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP70288.
    PaxDbiP70288.
    PRIDEiP70288.

    PTM databases

    PhosphoSiteiP70288.

    Expressioni

    Gene expression databases

    ArrayExpressiP70288.
    BgeeiP70288.
    CleanExiMM_HDAC2.
    GenevestigatoriP70288.

    Interactioni

    Subunit structurei

    Interacts with SNW1, PELP1, ATR, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A, CHFR and SAP30L. 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. 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. 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. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CBFA2T3, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. 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 By similarity. Interacts with MTA1, with a preference for sumoylated MTA1.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Znf431E9QAG83EBI-302251,EBI-9549639

    Protein-protein interaction databases

    BioGridi200260. 47 interactions.
    DIPiDIP-32854N.
    IntActiP70288. 26 interactions.
    MINTiMINT-146936.

    Structurei

    3D structure databases

    ProteinModelPortaliP70288.
    SMRiP70288. Positions 9-376.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062889.
    HOGENOMiHOG000225180.
    HOVERGENiHBG057112.
    InParanoidiB2RRP3.
    KOiK06067.
    OrthoDBiEOG7DNNTW.
    PhylomeDBiP70288.
    TreeFamiTF106171.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P70288-1 [UniParc]FASTAAdd to Basket

    « 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 GHAKCVEVAK TFNLPLLMLG 300
    GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN 350
    MTNQNTPEYM EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE 400
    DPDKRISIRA SDKRIACDEE FSDSEDEGEG GRRNVADHKK GAKKARIEED 450
    KKETEDKKTD VKEEDKSKDN SGEKTDPKGA KSEQLSNP 488
    Length:488
    Mass (Da):55,302
    Last modified:February 1, 1997 - v1
    Checksum:iB9843D24A775157C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti289 – 2891A → V in EDL04897. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31758 mRNA. Translation: AAC52889.1.
    CH466540 Genomic DNA. Translation: EDL04897.1.
    BC138517 mRNA. Translation: AAI38518.1.
    CCDSiCCDS23783.1.
    RefSeqiNP_032255.2. NM_008229.2.
    UniGeneiMm.19806.

    Genome annotation databases

    EnsembliENSMUST00000019911; ENSMUSP00000019911; ENSMUSG00000019777.
    GeneIDi15182.
    KEGGimmu:15182.
    UCSCiuc007evf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U31758 mRNA. Translation: AAC52889.1 .
    CH466540 Genomic DNA. Translation: EDL04897.1 .
    BC138517 mRNA. Translation: AAI38518.1 .
    CCDSi CCDS23783.1.
    RefSeqi NP_032255.2. NM_008229.2.
    UniGenei Mm.19806.

    3D structure databases

    ProteinModelPortali P70288.
    SMRi P70288. Positions 9-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200260. 47 interactions.
    DIPi DIP-32854N.
    IntActi P70288. 26 interactions.
    MINTi MINT-146936.

    Chemistry

    BindingDBi P70288.

    PTM databases

    PhosphoSitei P70288.

    Proteomic databases

    MaxQBi P70288.
    PaxDbi P70288.
    PRIDEi P70288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000019911 ; ENSMUSP00000019911 ; ENSMUSG00000019777 .
    GeneIDi 15182.
    KEGGi mmu:15182.
    UCSCi uc007evf.1. mouse.

    Organism-specific databases

    CTDi 3066.
    MGIi MGI:1097691. Hdac2.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062889.
    HOGENOMi HOG000225180.
    HOVERGENi HBG057112.
    InParanoidi B2RRP3.
    KOi K06067.
    OrthoDBi EOG7DNNTW.
    PhylomeDBi P70288.
    TreeFami TF106171.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_202086. p75NTR negatively regulates cell cycle via SC1.
    REACT_214440. NoRC negatively regulates rRNA expression.

    Miscellaneous databases

    NextBioi 287693.
    PROi P70288.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70288.
    Bgeei P70288.
    CleanExi MM_HDAC2.
    Genevestigatori P70288.

    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].
      Tissue: Lymphoma.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Brain.
    4. "SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors."
      Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C., Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K., Rosenfeld M.G., Ayer D.E., Eisenman R.N.
      Mol. Cell 2:33-42(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAP30.
    5. Cited for: INTERACTION WITH HDAC7.
    6. "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.
    7. "Functional and physical interaction between the histone methyl transferase Suv39H1 and histone deacetylases."
      Vaute O., Nicolas E., Vandel L., Trouche D.
      Nucleic Acids Res. 30:475-481(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUV39H1.
    8. "An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B."
      Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L., Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.
      Biochem. J. 369:651-657(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1.
    9. "Circadian and light-induced transcription of clock gene Per1 depends on histone acetylation and deacetylation."
      Naruse Y., Oh-hashi K., Iijima N., Naruse M., Yoshioka H., Tanaka M.
      Mol. Cell. Biol. 24:6278-6287(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK, INTERACTION WITH CRY1.
    10. Cited for: INTERACTION WITH H2AFY.
    11. "PRISM/PRDM6, a transcriptional repressor that promotes the proliferative gene program in smooth muscle cells."
      Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G., Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.
      Mol. Cell. Biol. 26:2626-2636(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRDM6.
    12. "Epigenetic regulation of hematopoietic differentiation by Gfi-1 and Gfi-1b is mediated by the cofactors CoREST and LSD1."
      Saleque S., Kim J., Rooke H.M., Orkin S.H.
      Mol. Cell 27:562-572(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY AS A COMPONENT OF A GFI-RCOR-KDM1A-HDAC COMPLEX, INTERACTION WITH GFI1 AND GFI1B, FUNCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons."
      Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A.
      Nature 455:411-415(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION AT CYS-262 AND CYS-274, MUTAGENESIS OF CYS-152; CYS-262 AND CYS-274.
    15. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(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: Embryonic fibroblast.
    17. "Revelation of p53-independent function of MTA1 in DNA damage response via modulation of the p21 WAF1-proliferating cell nuclear antigen pathway."
      Li D.Q., Pakala S.B., Reddy S.D., Ohshiro K., Peng S.H., Lian Y., Fu S.W., Kumar R.
      J. Biol. Chem. 285:10044-10052(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Regulation of NF-kappaB circuitry by a component of the nucleosome remodeling and deacetylase complex controls inflammatory response homeostasis."
      Pakala S.B., Bui-Nguyen T.M., Reddy S.D., Li D.Q., Peng S., Rayala S.K., Behringer R.R., Kumar R.
      J. Biol. Chem. 285:23590-23597(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION, INTERACTION WITH MTA1.
    19. Cited for: S-NITROSYLATION BY GAPDH.
    20. "A novel KRAB domain-containing zinc finger transcription factor ZNF431 directly represses Patched1 transcription."
      He Z., Cai J., Lim J.W., Kroll K., Ma L.
      J. Biol. Chem. 286:7279-7289(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF431.
    21. "ZFP932 suppresses cellular Hedgehog response and Patched1 transcription."
      Huang G.J., He Z., Ma L.
      Vitam. Horm. 88:309-332(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF431.
    22. "Insm1 controls development of pituitary endocrine cells and requires a SNAG domain for function and for recruitment of histone-modifying factors."
      Welcker J.E., Hernandez-Miranda L.R., Paul F.E., Jia S., Ivanov A., Selbach M., Birchmeier C.
      Development 140:4947-4958(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INSM1.

    Entry informationi

    Entry nameiHDAC2_MOUSE
    AccessioniPrimary (citable) accession number: P70288
    Secondary accession number(s): B2RRP3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3