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O09106

- HDAC1_MOUSE

UniProt

O09106 - HDAC1_MOUSE

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Protein

Histone deacetylase 1

Gene

Hdac1

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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression 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. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation.5 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 sitei141 – 1411By similarity

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. core promoter binding Source: UniProtKB
  3. deacetylase activity Source: UniProtKB
  4. DNA binding Source: MGI
  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. RNA polymerase II repressing transcription factor binding Source: MGI
  12. sequence-specific DNA binding transcription factor activity Source: MGI
  13. transcription corepressor activity Source: MGI
  14. transcription factor binding Source: UniProtKB
  15. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. circadian regulation of gene expression Source: UniProtKB
  3. circadian rhythm Source: UniProtKB
  4. embryonic digit morphogenesis Source: BHF-UCL
  5. endoderm development Source: MGI
  6. epidermal cell differentiation Source: BHF-UCL
  7. eyelid development in camera-type eye Source: BHF-UCL
  8. fungiform papilla formation Source: BHF-UCL
  9. hair follicle placode formation Source: BHF-UCL
  10. hippocampus development Source: MGI
  11. histone H3 deacetylation Source: UniProtKB
  12. histone H4 deacetylation Source: UniProtKB
  13. negative regulation of apoptotic process Source: BHF-UCL
  14. negative regulation of canonical Wnt signaling pathway Source: MGI
  15. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  16. negative regulation of intrinsic apoptotic signaling pathway Source: MGI
  17. negative regulation of transcription, DNA-templated Source: UniProtKB
  18. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  19. neuron differentiation Source: MGI
  20. odontogenesis of dentin-containing tooth Source: BHF-UCL
  21. positive regulation of cell proliferation Source: BHF-UCL
  22. positive regulation of oligodendrocyte differentiation Source: MGI
  23. 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_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199110. G0 and Early G1.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SABIO-RKO09106.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 1 (EC:3.5.1.98)
Short name:
HD1
Gene namesi
Name:Hdac1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:108086. Hdac1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. heterochromatin Source: MGI
  3. histone deacetylase complex Source: UniProtKB
  4. neuronal cell body Source: MGI
  5. nuclear chromatin Source: BHF-UCL
  6. nucleus Source: MGI
  7. NuRD complex Source: MGI
  8. protein complex Source: MGI
  9. transcriptional repressor complex Source: MGI
  10. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482Histone deacetylase 1PRO_0000114688Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei220 – 2201N6-acetyllysineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Modified residuei423 – 4231PhosphoserineBy similarity
Modified residuei432 – 4321N6-methylated lysine; by EHMT2By similarity
Cross-linki444 – 444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki476 – 476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1.By similarity
Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.By similarity
Ubiquitinated by CHFR and KCTD11, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO09106.
PaxDbiO09106.
PRIDEiO09106.

PTM databases

PhosphoSiteiO09106.

Expressioni

Tissue specificityi

Widely expressed with higher levels in thymus and testis and lower levels in liver. Present in muscle (at protein level).1 Publication

Inductioni

By interleukin-2.

Gene expression databases

BgeeiO09106.
CleanExiMM_HDAC1.
ExpressionAtlasiO09106. baseline and differential.
GenevestigatoriO09106.

Interactioni

Subunit structurei

Part of the core histone deacetylase (HDAC) complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex associates with MTA2, MBD2, 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 BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Component of a RCOR/GFI/KDM1A/HDAC complex. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with the non-histone region of H2AFY. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with SP1; the interaction deacetylates SP1 and regulates its transcriptional activity. Interacts with SP3; the interaction deacetylates SP3 and regulates its transcriptional activity. In vitro, C(18) ceramides increase this interaction and the subsequent SP3 deacetylation and SP3-mediated repression of the TERT promoter. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with C10orf90/FATS (via its N-terminal); the interaction prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to CDK5R1 (p25). Interacts directly with GFI1 and GFI1B. Interacts with NR1D2 (via C-terminus). Interacts with TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG promoter and thus inhibits MYOD1 transcriptional activity. Interacts with BAZ2A/TIP5, BANP, BCL6, BCOR, BHLHE40/DEC1, BRMS1, BRMS1L, CBFA2T3, CHFR, CIART, CRY1, DAXX, DDIT3/CHOP, DDX5, DNMT1, E4F1, EP300, HCFC1, HDAC9, INSM1, NFE4, NR4A2/NURR1, MIER1, KDM4A, KDM5B, KLF1, MINT, NRIP1, PCAF, PHB2, PRDM6, PRDM16, RB1, RERE, SAMSN1, SAP30L, SETDB1, SMAD3, SMARCA4/BRG1, SMYD2, SUV39H1, TGIF, TGIF2, TRAF6, UHRF1, UHRF2, ZMYND15, ZNF431 and ZNF541. Interacts with KDM5A.35 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dnmt1P138643EBI-301912,EBI-301927
GscQ025912EBI-301912,EBI-7457485
Nfkb1P257992EBI-301912,EBI-643958
RelaQ042072EBI-301912,EBI-644400
Zbtb7aO889392EBI-301912,EBI-595063
Znf431E9QAG83EBI-301912,EBI-9549639

Protein-protein interaction databases

BioGridi241423. 89 interactions.
DIPiDIP-31499N.
IntActiO09106. 31 interactions.
MINTiMINT-2568222.

Structurei

3D structure databases

ProteinModelPortaliO09106.
SMRiO09106. Positions 8-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 321313Histone deacetylaseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000225180.
HOVERGENiHBG057112.
InParanoidiO09106.
KOiK06067.
OMAiLTQGTKR.
OrthoDBiEOG7DNNTW.
PhylomeDBiO09106.
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.

O09106-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK
60 70 80 90 100
MEIYRPHKAN AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC
110 120 130 140 150
PVFDGLFEFC QLSTGGSVAS AVKLNKQQTD IAVNWAGGLH HAKKSEASGF
160 170 180 190 200
CYVNDIVLAI LELLKYHQRV LYIDIDIHHG DGVEEAFYTT DRVMTVSFHK
210 220 230 240 250
YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI FKPVMSKVME
260 270 280 290 300
MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
310 320 330 340 350
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM
360 370 380 390 400
TNQNTNEYLE KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED
410 420 430 440 450
PDKRISICSS DKRIACEEEF SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE
460 470 480
KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK LA
Length:482
Mass (Da):55,075
Last modified:July 1, 1997 - v1
Checksum:i7F64D3C17F5E4844
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98207 mRNA. Translation: CAA66870.1.
U80780 mRNA. Translation: AAB68398.1.
CCDSiCCDS18696.1.
RefSeqiNP_032254.1. NM_008228.2.
UniGeneiMm.202504.
Mm.391033.

Genome annotation databases

EnsembliENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
GeneIDi433759.
KEGGimmu:433759.
UCSCiuc008uxg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X98207 mRNA. Translation: CAA66870.1 .
U80780 mRNA. Translation: AAB68398.1 .
CCDSi CCDS18696.1.
RefSeqi NP_032254.1. NM_008228.2.
UniGenei Mm.202504.
Mm.391033.

3D structure databases

ProteinModelPortali O09106.
SMRi O09106. Positions 8-376.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 241423. 89 interactions.
DIPi DIP-31499N.
IntActi O09106. 31 interactions.
MINTi MINT-2568222.

Chemistry

BindingDBi O09106.
ChEMBLi CHEMBL4001.

PTM databases

PhosphoSitei O09106.

Proteomic databases

MaxQBi O09106.
PaxDbi O09106.
PRIDEi O09106.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102597 ; ENSMUSP00000099657 ; ENSMUSG00000028800 .
GeneIDi 433759.
KEGGi mmu:433759.
UCSCi uc008uxg.1. mouse.

Organism-specific databases

CTDi 3065.
MGIi MGI:108086. Hdac1.

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000225180.
HOVERGENi HBG057112.
InParanoidi O09106.
KOi K06067.
OMAi LTQGTKR.
OrthoDBi EOG7DNNTW.
PhylomeDBi O09106.
TreeFami TF106171.

Enzyme and pathway databases

Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199110. G0 and Early G1.
REACT_200667. NoRC negatively regulates rRNA expression.
REACT_202086. p75NTR negatively regulates cell cycle via SC1.
REACT_214440. NoRC negatively regulates rRNA expression.
REACT_216539. formation of the beta-catenin:TCF transactivating complex.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
SABIO-RK O09106.

Miscellaneous databases

NextBioi 408961.
PROi O09106.
SOURCEi Search...

Gene expression databases

Bgeei O09106.
CleanExi MM_HDAC1.
ExpressionAtlasi O09106. baseline and differential.
Genevestigatori O09106.

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. "Identification of mouse histone deacetylase 1 as a growth factor-inducible gene."
    Bartl S., Taplick J., Lagger G., Khier H., Kuchler K., Seiser C.
    Mol. Cell. Biol. 17:5033-5043(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  2. Johnson C.A.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
  4. "DNA methyltransferase Dnmt1 associates with histone deacetylase activity."
    Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.
    Nat. Genet. 24:88-91(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMT1.
  5. Cited for: INTERACTION WITH HDAC7.
  6. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
    Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
    J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9.
  7. "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.
  8. "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene promoter and represses RNA polymerase I transcription."
    Zhou Y., Santoro R., Grummt I.
    EMBO J. 21:4632-4640(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ2A.
  9. "Identification of mammalian Sds3 as an integral component of the Sin3/histone deacetylase corepressor complex."
    Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C., Hou H. Jr., Chen K., DePinho R.A.
    Mol. Cell. Biol. 22:2743-2750(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIN3B.
  10. "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.
  11. "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.
  12. "Biochemical fractionation reveals association of DNA methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a histone H3 methyltransferase and Hdac1."
    Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.
    J. Cell. Biochem. 88:855-864(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DNMT3A.
  13. "Atrophin 2 recruits histone deacetylase and is required for the function of multiple signaling centers during mouse embryogenesis."
    Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.
    Development 131:3-14(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RERE.
  14. "Transcriptional regulation by the repressor of estrogen receptor activity via recruitment of histone deacetylases."
    Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.
    J. Biol. Chem. 279:24834-24843(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHB2.
  15. "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.
  16. "Stage-specific repression by the EKLF transcriptional activator."
    Chen X., Bieker J.J.
    Mol. Cell. Biol. 24:10416-10424(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLF1, FUNCTION.
  17. "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.
  18. "The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing."
    Zhou Y., Grummt I.
    Curr. Biol. 15:1434-1438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAZ2A.
  19. Cited for: INTERACTION WITH H2AFY.
  20. "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex."
    Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.
    Mol. Cell. Biol. 25:8415-8429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BANP.
  21. "Histone deacetylase 9 couples neuronal activity to muscle chromatin acetylation and gene expression."
    Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N., Schaeffer L.
    Nat. Neurosci. 8:313-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC9, TISSUE SPECIFICITY.
  22. "Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex."
    Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.
    Mol. Cancer 5:26-26(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMYD2.
  23. "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.
  24. Cited for: INTERACTION WITH HDAC9.
  25. "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.
  26. "A novel germ cell-specific protein, SHIP1, forms a complex with chromatin remodeling activity during spermatogenesis."
    Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y., Eddy E.M., Cho C.
    J. Biol. Chem. 283:35283-35294(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF541.
  27. "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation through release of SMRT-mediated repression."
    Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P., Smidt M.P.
    Development 136:531-540(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR4A2.
  28. Cited for: INTERACTION WITH SAMSN1.
  29. "Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit myogenic differentiation and mediate anti-myogenic effects of glucocorticoids."
    Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G., Donato R., Riccardi C.
    J. Biol. Chem. 285:10385-10396(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSC22D3.
    Strain: DBA/2.
    Tissue: Myoblast.
  30. "Zmynd15 encodes a histone deacetylase-dependent transcriptional repressor essential for spermiogenesis and male fertility."
    Yan W., Si Y., Slaymaker S., Li J., Zheng H., Young D.L., Aslanian A., Saunders L., Verdin E., Charo I.F.
    J. Biol. Chem. 285:31418-31426(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZMYND15.
  31. "An HDAC1-binding domain within FATS bridges p21 turnover to radiation-induced tumorigenesis."
    Li Z., Zhang Q., Mao J.H., Weise A., Mrasek K., Fan X., Zhang X., Liehr T., Lu K.H., Balmain A., Cai W.W.
    Oncogene 29:2659-2671(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C10ORF90/FATS AND CDKN1A/P21.
  32. "Stress-induced C/EBP homology protein (CHOP) represses MyoD transcription to delay myoblast differentiation."
    Alter J., Bengal E.
    PLoS ONE 6:E29498-E29498(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDIT3.
  33. "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.
  34. "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock."
    DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J., Panda S.
    Science 333:1881-1885(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KDM5A.
  35. "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.
  36. "Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
    Duong H.A., Weitz C.J.
    Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A LARGE PER COMPLEX.
  37. Cited for: FUNCTION, INTERACTION WITH CIART.

Entry informationi

Entry nameiHDAC1_MOUSE
AccessioniPrimary (citable) accession number: O09106
Secondary accession number(s): P97476
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 153 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