Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O09106 (HDAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 1

Short name=HD1
EC=3.5.1.98
Gene names
Name:Hdac1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. 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. Ref.15 Ref.24

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

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. Associates with the 9-1-1 complex; interacts with HUS1. Found in a complex with DNMT3A and HDAC7. Interacts with BAZ2A/TIP5, BCOR, BRMS1L, DAXX, DNMT1, EP300, HCFC1, NFE4, PCAF, PHB2, MIER1, KDM4A, MINT, NRIP1, PRDM6, RERE, SETDB1, SMYD2, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with KDM5B and BRMS1. Interacts with TRIM28; the interaction recruits HDAC1 to E2F1 and inhibits its acetylation. Interacts with BANP and CBFA2T3. Interacts with SAP30L and KLF1. Interacts with E4F1. Interacts with CHFR, PRDM16, SP1, SP3, and SMAD3. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6. Interacts with TSHZ3 (via N-terminus); the interaction is direct. Found in a trimeric complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3. Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Interacts with NR4A2/NURR1. Interacts with SAMSN1. 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; the interaction is prevented by binding of C10orf90/FATS facilitating acetylation and stabilization of CDKN1A/p21. Binds to CDK5 complexed to CDK5R1 (p25). Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with ZMYND15. Interacts with DDX5. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with BCL6 and DDIT3/CHOP. Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with NR1D2 (via C-terminus). Interacts with ZNF431. Interacts with INSM1. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32

Subcellular location

Nucleus.

Tissue specificity

Widely expressed with higher levels in thymus and testis and lower levels in liver. Present in muscle (at protein level). Ref.20

Induction

By interleukin-2.

Post-translational modification

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.

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Traceable author statement PubMed 12711221. Source: UniProtKB

embryonic digit morphogenesis

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

endoderm development

Inferred from direct assay PubMed 15060137. Source: MGI

epidermal cell differentiation

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

eyelid development in camera-type eye

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

fungiform papilla formation

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

hair follicle placode formation

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

hippocampus development

Inferred from genetic interaction PubMed 19380719. Source: MGI

negative regulation of apoptotic process

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

negative regulation of canonical Wnt signaling pathway

Inferred from genetic interaction PubMed 19503085. Source: MGI

negative regulation of intrinsic apoptotic signaling pathway

Inferred from genetic interaction PubMed 21093383. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: MGI

neuron differentiation

Inferred from genetic interaction PubMed 19380719. Source: MGI

odontogenesis of dentin-containing tooth

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL

positive regulation of oligodendrocyte differentiation

Inferred from genetic interaction PubMed 19503085. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentNuRD complex

Inferred from direct assay PubMed 11836251PubMed 22075476. Source: MGI

cytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

heterochromatin

Inferred from direct assay PubMed 14519686PubMed 14643676. Source: MGI

histone deacetylase complex

Traceable author statement PubMed 12711221. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 18651664. Source: MGI

nuclear chromatin

Inferred from direct assay PubMed 21093383. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 20720167PubMed 21874024. Source: MGI

protein complex

Inferred from direct assay PubMed 19796622. Source: MGI

transcription factor complex

Inferred from direct assay Ref.24. Source: UniProtKB

transcriptional repressor complex

Inferred from physical interaction PubMed 17182846. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 14593184PubMed 15608638. Source: MGI

Krueppel-associated box domain binding

Inferred from physical interaction Ref.31. Source: UniProtKB

NAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 19235719. Source: MGI

chromatin binding

Inferred from direct assay PubMed 16109736PubMed 16678101PubMed 17905753. Source: MGI

histone deacetylase activity

Inferred from direct assay Ref.4. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17392792. Source: MGI

transcription corepressor activity

Inferred from direct assay PubMed 15509593PubMed 8917507. Source: MGI

transcription factor binding

Traceable author statement PubMed 12711221. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Histone deacetylase 1
PRO_0000114688

Regions

Region9 – 321313Histone deacetylase

Sites

Active site1411 By similarity

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2201N6-acetyllysine By similarity
Modified residue3931Phosphoserine By similarity
Modified residue4211Phosphoserine By similarity
Modified residue4231Phosphoserine By similarity
Modified residue4321N6-methylated lysine; by EHMT2 By similarity
Cross-link444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link476Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
O09106 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 7F64D3C17F5E4844

FASTA48255,075
        10         20         30         40         50         60 
MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN 

        70         80         90        100        110        120 
AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS 

       130        140        150        160        170        180 
AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG 

       190        200        210        220        230        240 
DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI 

       250        260        270        280        290        300 
FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG 

       310        320        330        340        350        360 
GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE 

       370        380        390        400        410        420 
KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF 

       430        440        450        460        470        480 
SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK 


LA 

« Hide

References

[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]"Identification of a nuclear domain with deacetylase activity."
Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.
Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000) [PubMed] [Europe PMC] [Abstract]
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]"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.
[16]"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.
[17]"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.
[18]"Structural characterization of the histone variant macroH2A."
Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R., Khochbin S., Luger K.
Mol. Cell. Biol. 25:7616-7624(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH H2AFY.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"Neuroprotection by histone deacetylase-related protein."
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R., Olson E.N., D'Mello S.R.
Mol. Cell. Biol. 26:3550-3564(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC9.
[24]"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.
[25]"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.
[26]"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.
[27]"SLy2 targets the nuclear SAP30/HDAC1 complex."
Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A., Schmitz I., Beer-Hammer S.
Int. J. Biochem. Cell Biol. 42:1472-1481(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAMSN1.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98207 mRNA. Translation: CAA66870.1.
U80780 mRNA. Translation: AAB68398.1.
RefSeqNP_032254.1. NM_008228.2.
UniGeneMm.202504.
Mm.391033.

3D structure databases

ProteinModelPortalO09106.
SMRO09106. Positions 8-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid241423. 89 interactions.
DIPDIP-31499N.
IntActO09106. 30 interactions.
MINTMINT-2568222.

Chemistry

BindingDBO09106.
ChEMBLCHEMBL4001.

PTM databases

PhosphoSiteO09106.

Proteomic databases

PaxDbO09106.
PRIDEO09106.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
GeneID433759.
KEGGmmu:433759.
UCSCuc008uxg.1. mouse.

Organism-specific databases

CTD3065.
MGIMGI:108086. Hdac1.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidO09106.
KOK06067.
OMALTQGTKR.
OrthoDBEOG7DNNTW.
PhylomeDBO09106.
TreeFamTF106171.

Gene expression databases

BgeeO09106.
CleanExMM_HDAC1.
GenevestigatorO09106.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

NextBio408961.
PROO09106.
SOURCESearch...

Entry information

Entry nameHDAC1_MOUSE
AccessionPrimary (citable) accession number: O09106
Secondary accession number(s): P97476
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot