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P70288

- HDAC2_MOUSE

UniProt

P70288 - HDAC2_MOUSE

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Protein

Histone deacetylase 2

Gene

Hdac2

Organism
Mus musculus (Mouse)
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 (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. deacetylase activity Source: UniProtKB
  4. enzyme binding Source: UniProtKB
  5. histone deacetylase activity Source: UniProtKB
  6. Krueppel-associated box domain binding Source: UniProtKB
  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: Ensembl
  12. protein deacetylase activity Source: BHF-UCL
  13. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  14. RNA polymerase II distal enhancer 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. ATP-dependent chromatin remodeling Source: Ensembl
  2. cardiac muscle cell development Source: MGI
  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. 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_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.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_257106. HDACs deacetylate histones.

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
Complete GO annotation...

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

BgeeiP70288.
CleanExiMM_HDAC2.
ExpressionAtlasiP70288. baseline and differential.
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. Interacts with SIX3.By similarity14 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200260. 47 interactions.
DIPiDIP-32854N.
IntActiP70288. 27 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.
InParanoidiP70288.
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

        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 GHAKCVEVAK 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 SGEKTDPKGA KSEQLSNP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 27 interactions.
MINTi MINT-146936.

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 P70288.
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.
REACT_235780. RNA Polymerase I Transcription Initiation.
REACT_257106. HDACs deacetylate histones.

Miscellaneous databases

ChiTaRSi Hdac2. mouse.
NextBioi 287693.
PROi P70288.
SOURCEi Search...

Gene expression databases

Bgeei P70288.
CleanExi MM_HDAC2.
ExpressionAtlasi P70288. baseline and differential.
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

« 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].
    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. Cited for: INTERACTION WITH SIX3.
  15. "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.
  16. "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].
  17. "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.
  18. "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.
  19. "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.
  20. Cited for: S-NITROSYLATION BY GAPDH.
  21. "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.
  22. "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.
  23. "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: November 26, 2014
This is version 148 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