Histone deacetylase 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q13547 (HDAC1_HUMAN)

Last modified February 9, 2010. Version 124. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	HDAC1
Synonyms:	RPD3L1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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. Ref.19 Ref.32
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, AOF2/LSD1, 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, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541. Interacts with the non-histone region of H2AFY. Interacts with HDAC9. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with BANP, CBFA2T3 and KDM5B. Interacts with SAP30L. Interacts with E4F1. Interacts with KFL1 By similarity. Interacts with SV40 large T antigen. Interacts with CHFR, PRDM16, SP1, SP3 and SMAD3. Interacts with RB1 and SMARCA4/BRG1. Interacts with TRAF6. Ref.19 Ref.32 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.20 Ref.22 Ref.23 Ref.24 Ref.26 Ref.28 Ref.29 Ref.33 Ref.35 Ref.36 Ref.46 Ref.48
Subcellular location	Nucleus.
Tissue specificity	Ubiquitous, with higher levels in heart, pancreas and testis, and lower levels in kidney and brain.
Post-translational modification	Sumoylated on Lys-444 and Lys-476; which promotes enzymatic activity. Desumoylated by SENP1. Ref.15 Ref.16 Ref.25 Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity and interactions with NuRD and SIN3 complexes. Ubiquitinated by CHFR, leading to its degradation by the proteasome By similarity. Ref.48
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.

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Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: ProtInc chromatin remodeling Inferred by curator. Source: UniProtKB histone deacetylation Ref.48 Inferred from mutant phenotype. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from Experiment. Source: Reactome negative regulation of gene-specific transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB positive regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB positive regulation of receptor biosynthetic process Inferred from mutant phenotype. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuRD complex Inferred from direct assay. Source: UniProtKB Sin3 complex Inferred from direct assay. Source: UniProtKB cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	histone deacetylase activity Ref.48 Inferred from mutant phenotype. Source: UniProtKB histone deacetylase binding Inferred from physical interaction. Source: UniProtKB identical protein binding Inferred from physical interaction. Source: IntAct transcription activator activity Inferred from direct assay. Source: UniProtKB transcription factor activity Ref.2 Traceable author statement. Source: ProtInc transcription factor binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-301834,EBI-301834
BRMS1	Q9HCU9	2	EBI-301834,EBI-714781
DAXX	Q9UER7	1	EBI-301834,EBI-77321
DNMT3L	Q9UJW3	2	EBI-301834,EBI-740967
HCFC1	P51610	1	EBI-301834,EBI-396176
HDAC2	Q92769	2	EBI-301834,EBI-301821
HIST1H4A	P62805	1	EBI-301834,EBI-302023
MBD1	Q9UIS9	2	EBI-301834,EBI-867196
MORF4L2	Q15014	1	EBI-301834,EBI-399257
NCOR2	Q9Y618	1	EBI-301834,EBI-80830
NFKB1	P19838	2	EBI-301834,EBI-300010
Nrip1	Q8CBD1	1	EBI-301834,EBI-1771626	From a different organism.
RB1	P06400	1	EBI-301834,EBI-491274
RBBP4	Q09028	1	EBI-301834,EBI-620823
RBBP7	Q16576	1	EBI-301834,EBI-352227
RELA	Q04206	2	EBI-301834,EBI-73886
Rere	Q80TZ9	1	EBI-301834,EBI-904076	From a different organism.
RFX1	P22670	1	EBI-301834,EBI-716037
SAP18	O00422	2	EBI-301834,EBI-1044156
SUV39H1	O43463	2	EBI-301834,EBI-349968
TP53	P04637	1	EBI-301834,EBI-366083

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

Histone deacetylase 1

PRO_0000114687

Regions

Region

9 – 321

313

Histone deacetylase

Sites

Active site

141

Amino acid modifications

Modified residue

N6-acetyllysine Ref.50

Modified residue

220

N6-acetyllysine Ref.50

Modified residue

221

Phosphotyrosine Ref.30

Modified residue

393

Phosphoserine Ref.31 Ref.34 Ref.40 Ref.42 Ref.45 Ref.49

Modified residue

406

Phosphoserine Ref.38

Modified residue

421

Phosphoserine; by CK2 Ref.31 Ref.42 Ref.45 Ref.49 Ref.10 Ref.37 Ref.43

Modified residue

423

Phosphoserine; by CK2 Ref.31 Ref.42 Ref.45 Ref.49 Ref.10 Ref.37 Ref.43

Cross-link

444

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16

Cross-link

476

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.16

Experimental info

Mutagenesis

141

H → A: Abolishes histone deacetylase activity. Ref.48

Mutagenesis

287

F → Y: Abolishes interaction with CHFR; when associated with I-297. Ref.48

Mutagenesis

297

M → I: Abolishes interaction with CHFR; when associated with Y-287. Ref.48

Mutagenesis

391 – 482

Missing: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.

Mutagenesis

421

S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. Ref.10

Mutagenesis

421

S → D or E: Slightly decreases deacetylase activity. Ref.10

Mutagenesis

423

S → A: Strongly decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes. Ref.10

Mutagenesis

423

S → D or E: Decreases deacetylase activity. Ref.10

Mutagenesis

424

E → A: Slightly decreases deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.

Mutagenesis

425

E → A: No effect on deacetylase activity, no effect on interaction with NuRD and SIN3 complexes.

Mutagenesis

426

E → A: Decreases deacetylase activity, and disrupts interaction with NuRD and SIN3 complexes.

Sequence conflict

312

W → R in BAA08909. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13547-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 4D35B7C1ED7838D6
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FASTA

482

55,103

        10         20         30         40         50         60 
MAQTQGTRRK 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 EESGDEDEDD PDKRISICSS DKRIACEEEF 

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


LA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p." Taunton J., Hassig C.A., Schreiber S.L. Science 272:408-411(1996) [PubMed: 8602529] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell.
[2]	"Isolation and mapping of a human gene (RPD3L1) that is homologous to RPD3, a transcription factor in Saccharomyces cerevisiae." Furukawa Y., Kawakami T., Sudo K., Inazawa J., Matsumine A., Akiyama T., Nakamura Y. Cytogenet. Cell Genet. 73:130-133(1996) [PubMed: 8646880] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal lung.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[4]	"MEF-2 function is modified by a novel co-repressor, MITR." Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S., Towers N., Spohr G., Kouzarides T., Mohun T.J. EMBO J. 18:5085-5098(1999) [PubMed: 10487760] [Abstract] Cited for: INTERACTION WITH HDAC9.
[5]	"BCoR, a novel corepressor involved in BCL-6 repression." Huynh K.D., Fischle W., Verdin E., Bardwell V.J. Genes Dev. 14:1810-1823(2000) [PubMed: 10898795] [Abstract] Cited for: INTERACTION WITH BCOR.
[6]	"HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins." Cai R.L., Yan-Neale Y., Cueto M.A., Xu H., Cohen D. J. Biol. Chem. 275:27909-27916(2000) [PubMed: 10846170] [Abstract] Cited for: INTERACTION WITH THE 9-1-1 COMPLEX AND HUS1.
[7]	"Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing." Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M. J. Biol. Chem. 275:40782-40787(2000) [PubMed: 11006275] [Abstract] Cited for: INTERACTION WITH NRIP1.
[8]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed: 10669754] [Abstract] Cited for: INTERACTION WITH DAXX.
[9]	"Identification of a transcriptional repressor related to the noncatalytic domain of histone deacetylases 4 and 5." Zhou X., Richon V.M., Rifkind R.A., Marks P.A. Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000) [PubMed: 10655483] [Abstract] Cited for: INTERACTION WITH HDAC9.
[10]	"Histone deacetylase 1 phosphorylation promotes enzymatic activity and complex formation." Pflum M.K.H., Tong J.K., Lane W.S., Schreiber S.L. J. Biol. Chem. 276:47733-47741(2001) [PubMed: 11602581] [Abstract] Cited for: PHOSPHORYLATION AT SER-421 AND SER-423, MUTAGENESIS OF SER-421 AND SER-423, MASS SPECTROMETRY.
[11]	"Sharp, an inducible cofactor that integrates nuclear receptor repression and activation." Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M. Genes Dev. 15:1140-1151(2001) [PubMed: 11331609] [Abstract] Cited for: INTERACTION WITH MINT.
[12]	"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1." Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H. J. Biol. Chem. 276:6817-6824(2001) [PubMed: 11102443] [Abstract] Cited for: INTERACTION WITH MBD2 AND MBD3.
[13]	"TGIF2 interacts with histone deacetylase 1 and represses transcription." Melhuish T.A., Gallo C.M., Wotton D. J. Biol. Chem. 276:32109-32114(2001) [PubMed: 11427533] [Abstract] Cited for: INTERACTION WITH TGIF2.
[14]	"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: 11533236] [Abstract] Cited for: INTERACTION WITH CBFA2T3.
[15]	"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase." Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E., Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A. EMBO J. 21:2682-2691(2002) [PubMed: 12032081] [Abstract] Cited for: SUMOYLATION.
[16]	"SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities." David G., Neptune M.A., DePinho R.A. J. Biol. Chem. 277:23658-23663(2002) [PubMed: 11960997] [Abstract] Cited for: SUMOYLATION AT LYS-444 AND LYS-476.
[17]	"Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1." Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W. Genes Dev. 17:896-911(2003) [PubMed: 12670868] [Abstract] Cited for: INTERACTION WITH HCFC1.
[18]	"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed: 12493763] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC2; HMG20B; AOF2; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[19]	"Acetylated SP3 is a transcriptional activator." Ammanamanchi S., Freeman J.W., Brattain M.G. J. Biol. Chem. 278:35775-35780(2003) [PubMed: 12837748] [Abstract] Cited for: INTERACTION WITH SP3, FUNCTION.
[20]	"Human MI-ER1 alpha and beta function as transcriptional repressors by recruitment of histone deacetylase 1 to their conserved ELM2 domain." Ding Z., Gillespie L.L., Paterno G.D. Mol. Cell. Biol. 23:250-258(2003) [PubMed: 12482978] [Abstract] Cited for: INTERACTION WITH MIER1.
[21]	"Identification and characterization of three new components of the mSin3A corepressor complex." Fleischer T.C., Yun U.J., Ayer D.E. Mol. Cell. Biol. 23:3456-3467(2003) [PubMed: 12724404] [Abstract] Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[22]	"Modulation of p120E4F transcriptional activity by the Gam1 adenoviral early protein." Colombo R., Draetta G.F., Chiocca S. Oncogene 22:2541-2547(2003) [PubMed: 12730668] [Abstract] Cited for: INTERACTION WITH E4F1.
[23]	"Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex." Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W. Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed: 15451426] [Abstract] Cited for: INTERACTION WITH BRMS1L.
[24]	"Site-specific acetylation of the fetal globin activator NF-E4 prevents its ubiquitination and regulates its interaction with the histone deacetylase, HDAC1." Zhao Q., Cumming H., Cerruti L., Cunningham J.M., Jane S.M. J. Biol. Chem. 279:41477-41486(2004) [PubMed: 15273251] [Abstract] Cited for: INTERACTION WITH NFE4.
[25]	"SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1." Cheng J., Wang D., Wang Z., Yeh E.T.H. Mol. Cell. Biol. 24:6021-6028(2004) [PubMed: 15199155] [Abstract] Cited for: DESUMOYLATION BY SENP1.
[26]	"ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain." Unoki M., Nishidate T., Nakamura Y. Oncogene 23:7601-7610(2004) [PubMed: 15361834] [Abstract] Cited for: INTERACTION WITH UHRF1 AND UHRF2.
[27]	"NuRD and SIN3 histone deacetylase complexes in development." Ahringer J. Trends Genet. 16:351-356(2000) [PubMed: 10904264] [Abstract] Cited for: REVIEW ON DEACETYLASE COMPLEXES.
[28]	"Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein." Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F. J. Biol. Chem. 280:28507-28518(2005) [PubMed: 15927959] [Abstract] Cited for: INTERACTION WITH KDM4A.
[29]	"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: 16166625] [Abstract] Cited for: INTERACTION WITH BANP.
[30]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, MASS SPECTROMETRY.
[31]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Epithelium.
[32]	"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription." Hung J.J., Wang Y.T., Chang W.C. Mol. Cell. Biol. 26:1770-1785(2006) [PubMed: 16478997] [Abstract] Cited for: INTERACTION WITH SP1, FUNCTION.
[33]	"SAP30L interacts with members of the Sin3A corepressor complex and targets Sin3A to the nucleolus." Viiri K.M., Korkeamaeki H., Kukkonen M.K., Nieminen L.K., Lindfors K., Peterson P., Maeki M., Kainulainen H., Lohi O. Nucleic Acids Res. 34:3288-3298(2006) [PubMed: 16820529] [Abstract] Cited for: INTERACTION WITH SAP30L.
[34]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
[35]	"Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases." Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J. Int. J. Cancer 121:265-275(2007) [PubMed: 17373667] [Abstract] Cited for: INTERACTION WITH KDM5B.
[36]	"Involvement of chromatin and histone deacetylation in SV40 T antigen transcription regulation." Valls E., Blanco-Garcia N., Aquizu N., Piedra D., Estaras C., de la Cruz X., Martinez-Balbas M.A. Nucleic Acids Res. 35:1958-1968(2007) [PubMed: 17341466] [Abstract] Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN.
[37]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, MASS SPECTROMETRY.
[38]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, MASS SPECTROMETRY.
[39]	"Nuclear tumor necrosis factor receptor-associated factor 6 in lymphoid cells negatively regulates c-Myb-mediated transactivation through small ubiquitin-related modifier-1 modification." Pham L.V., Zhou H.J., Lin-Lee Y.C., Tamayo A.T., Yoshimura L.C., Fu L., Darnay B.G., Ford R.J. J. Biol. Chem. 283:5081-5089(2008) [PubMed: 18093978] [Abstract] Cited for: INTERACTION WITH TRAF6.
[40]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
[41]	"A calcium-dependent switch in a CREST-BRG1 complex regulates activity-dependent gene expression." Qiu Z., Ghosh A. Neuron 60:775-787(2008) [PubMed: 19081374] [Abstract] Cited for: FUNCTION, INTERACTION WITH RB1 AND SMARCA4/BRG1.
[42]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY.
[43]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: Liver.
[44]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[45]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY.
[46]	"SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells." Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T. J. Biol. Chem. 284:3334-3344(2009) [PubMed: 19049980] [Abstract] Cited for: INTERACTION WITH PRDM16 AND SMAD3.
[47]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, MASS SPECTROMETRY.
[48]	"Chfr is linked to tumour metastasis through the downregulation of HDAC1." Oh Y.M., Kwon Y.E., Kim J.M., Bae S.J., Lee B.K., Yoo S.J., Chung C.H., Deshaies R.J., Seol J.H. Nat. Cell Biol. 11:295-302(2009) [PubMed: 19182791] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH CHFR, MUTAGENESIS OF HIS-141; PHE-287 AND MET-297.
[49]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND SER-423, MASS SPECTROMETRY. Tissue: T-cell.
[50]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-220, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U50079 mRNA. Translation: AAC50475.1.
D50405 mRNA. Translation: BAA08909.1.
BC000301 mRNA. Translation: AAH00301.1.

IPI

IPI00013774.

RefSeq

NP_004955.2.

UniGene

Hs.88556

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TYI	model	-	A	1-482	[»]

SMR

Q13547. Positions 12-373.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24184N.

IntAct

Q13547. 40 interactions.

STRING

Q13547.

PTM databases

PhosphoSite

Q13547.

Proteomic databases

PeptideAtlas

Q13547.

PRIDE

Q13547.

Genome annotation databases

Ensembl

ENST00000373548; ENSP00000362649; ENSG00000116478; Homo sapiens. [Genome view]

GeneID

3065.

KEGG

hsa:3065.

UCSC

uc001bvb.1. human.

Organism-specific databases

CTD

3065.

GeneCards

GC01P032525.

H-InvDB

HIX0000369.
HIX0077545.

HGNC

HGNC:4852. HDAC1.

HPA

CAB005017.

MIM

601241. gene.

PharmGKB

PA29226.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14610.

HOGENOM

HBG396919.

HOVERGEN

Q13547.

InParanoid

Q13547.

OMA

IFKPVIS.

OrthoDB

EOG94XN2W.

PhylomeDB

Q13547.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
ps1pathway. Presenilin action in Notch and Wnt signaling.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_11061. Signalling by NGF.

Gene expression databases

ArrayExpress

Q13547.

Bgee

Q13547.

CleanEx

HS_HDAC1.

Genevestigator

Q13547.

GermOnline

ENSG00000116478. Homo sapiens.

Family and domain databases

InterPro

IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
[Graphical view]

Gene3D

G3DSA:3.40.800.20. His_deacetylse. 1 hit.

PANTHER

PTHR10625. His_deacetylse. 1 hit.
PTHR10625:SF28. His_deacetylse_1. 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 Resources

DrugBank

DB02546. Vorinostat.

NextBio

12125.

SOURCE

Search...

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Entry information

Entry name

HDAC1_HUMAN

Accession

Primary (citable) accession number: Q13547
Secondary accession number(s): Q92534

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	February 9, 2010
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents