O09106 (HDAC1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 1
Short name=HD1
EC=3.5.1.98

Gene names

Name:

Hdac1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 By similarity. 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 By similarity. 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 By similarity. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2 By similarity. Interacts with DDIT3/CHOP. 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.27 Ref.30 Ref.31 Ref.32 Ref.33
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 histone H3 deacetylation Inferred from electronic annotation. Source: GOC histone H4 deacetylation Inferred from electronic annotation. Source: GOC negative regulation of apoptotic process Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL negative regulation of canonical Wnt receptor signaling pathway Inferred from genetic interaction PubMed 19503085. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction PubMed 21093383. Source: BHF-UCL 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	NuRD 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 neuronal cell body Inferred from direct assay PubMed 18651664. Source: MGI nuclear chromatin Inferred from direct assay PubMed 21093383. Source: BHF-UCL transcription factor complex Inferred from direct assay Ref.24. Source: UniProtKB
Molecular_function	DNA binding Inferred from direct assay PubMed 14593184PubMed 15608638. Source: MGI NAD-dependent histone deacetylase activity (H3-K14 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K18 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H3-K9 specific) Inferred from electronic annotation. Source: EC NAD-dependent histone deacetylase activity (H4-K16 specific) Inferred from electronic annotation. Source: EC 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dnmt1	P13864	3	EBI-301912,EBI-301927
Nfkb1	P25799	2	EBI-301912,EBI-643958
Rela	Q04207	2	EBI-301912,EBI-644400
Zbtb7a	O88939	2	EBI-301912,EBI-595063

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Histone deacetylase 1		PRO_0000114688
Regions
	Region	9 – 321	313	Histone deacetylase
Sites
	Active site	141	1	By similarity
Amino acid modifications
	Modified residue	74	1	N6-acetyllysine By similarity
	Modified residue	220	1	N6-acetyllysine By similarity
	Modified residue	393	1	Phosphoserine Ref.26 Ref.28 Ref.29
	Modified residue	421	1	Phosphoserine Ref.26 Ref.28 Ref.29
	Modified residue	423	1	Phosphoserine Ref.26 Ref.28 Ref.29
	Modified residue	432	1	N6-methylated lysine; by EHMT2 By similarity
	Cross-link	444		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	476		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O09106 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 7F64D3C17F5E4844	FASTA	482	55,075
	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

References

	« Hide 'large scale' referencesShow 'large scale' 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]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Melanoma.
[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]	"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-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Macrophage.
[29]	"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-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98207 mRNA. Translation: CAA66870.1. U80780 mRNA. Translation: AAB68398.1.
IPI	IPI00114232.
RefSeq	NP_032254.1. NM_008228.2.
UniGene	Mm.202504. Mm.391033.
3D structure databases
ProteinModelPortal	O09106.
SMR	O09106. Positions 8-373.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31499N.
IntAct	O09106. 20 interactions.
MINT	MINT-2568222.
PTM databases
PhosphoSite	O09106.
Proteomic databases
PaxDb	O09106.
PRIDE	O09106.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
GeneID	433759.
KEGG	mmu:433759.
Organism-specific databases
CTD	3065.
MGI	MGI:108086. Hdac1.
Phylogenomic databases
eggNOG	COG0123.
HOGENOM	HOG000225180.
HOVERGEN	HBG057112.
InParanoid	O09106.
KO	K06067.
OMA	RISCDEE.
OrthoDB	EOG4868CH.
Gene expression databases
ArrayExpress	O09106.
Bgee	O09106.
CleanEx	MM_HDAC1.
Genevestigator	O09106.
GermOnline	ENSMUSG00000061062. Mus musculus.
Family and domain databases
Gene3D	3.40.800.20. 1 hit.
InterPro	IPR000286. His_deacetylse. IPR003084. His_deacetylse_1. IPR023801. His_deacetylse_dom. [Graphical view]
PANTHER	PTHR10625. PTHR10625. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PIRSF	PIRSF037913. His_deacetylse_1. 1 hit.
PRINTS	PR01270. HDASUPER. PR01271. HISDACETLASE.
ProtoNet	Search...
Other
BindingDB	O09106.
ChEMBL	CHEMBL4001.
NextBio	408961.
SOURCE	Search...

Entry information

Entry name

HDAC1_MOUSE

Accession

Primary (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 3, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program