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

Q92769 (HDAC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 2

Short name=HD2
EC=3.5.1.98
Gene names
Name:HDAC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 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. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Ref.31

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, 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 RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with SNW1, HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Part of a complex containing the core histones H2A, H2B, H3 and H4, DEK and unphosphorylated DAXX. Part of a complex containing ATR and CHD4. Forms a heterologous complex at least with YY1. Interacts with ATR, CBFA2T3, DNMT1, MINT, HDAC10, HCFC1, NRIP1, KDM4A and PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3, ARID4B, HDAC1 and HDAC2. Interacts with CHFR and SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts with TSHZ3 (via its N-terminus). Interacts with APEX1; the interaction is not dependent on the acetylated status of APEX1. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with FAM64A. Interacts with BCL6 (non-acetylated form). Part of a complex containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2. Interacts with CRY1, INSM1 and ZNF431. Ref.6 Ref.7 Ref.8 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.24 Ref.26 Ref.27 Ref.29 Ref.31 Ref.32 Ref.36

Subcellular location

Nucleus.

Tissue specificity

Widely expressed; lower levels in brain and lung.

Post-translational modification

S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching By similarity.

Sequence similarities

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

Sequence caution

The sequence AAH31055.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG59420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   Molecular functionChromatin regulator
Hydrolase
Repressor
   PTMAcetylation
Phosphoprotein
S-nitrosylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP-dependent chromatin remodeling

Inferred from direct assay PubMed 16217013. Source: UniProt

blood coagulation

Traceable author statement. Source: Reactome

cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

chromatin remodeling

Inferred by curator PubMed 17827154. Source: BHF-UCL

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic digit morphogenesis

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

epidermal cell differentiation

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

eyelid development in camera-type eye

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

fungiform papilla formation

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

hair follicle placode formation

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

hippocampus development

Inferred from electronic annotation. Source: Ensembl

histone H3 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone deacetylation

Inferred from mutant phenotype PubMed 19372552. Source: BHF-UCL

maintenance of chromatin silencing

Inferred from mutant phenotype PubMed 19372552. Source: BHF-UCL

negative regulation of MHC class II biosynthetic process

Inferred by curator PubMed 19041327. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell cycle

Traceable author statement. Source: Reactome

negative regulation of intrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron projection development

Inferred from sequence or structural similarity PubMed 18754010. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from mutant phenotype PubMed 19041327. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19041327PubMed 19276356. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19276356. Source: BHF-UCL

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

odontogenesis of dentin-containing tooth

Inferred from sequence or structural similarity PubMed 21093383. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 18347167. Source: BHF-UCL

positive regulation of collagen biosynthetic process

Inferred by curator PubMed 19041327. Source: BHF-UCL

positive regulation of oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from mutant phenotype PubMed 19041327. Source: BHF-UCL

positive regulation of receptor biosynthetic process

Inferred from mutant phenotype PubMed 18316616. Source: BHF-UCL

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19041327PubMed 19372552. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred by curator PubMed 19041327. Source: BHF-UCL

regulation of protein deacetylation

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of sarcomere organization

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from direct assay PubMed 20075857. Source: UniProtKB

NuRD complex

Inferred from direct assay PubMed 19644445. Source: UniProtKB

Sin3 complex

Inferred from direct assay PubMed 14966270. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 12711221. Source: UniProtKB

heterochromatin

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay PubMed 16217013. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18347167. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 16217013. Source: UniProt

replication fork

Inferred from electronic annotation. Source: Ensembl

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionNAD-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 22926524. Source: BHF-UCL

chromatin DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter binding

Inferred from electronic annotation. Source: Ensembl

deacetylase activity

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 11062478PubMed 11641274. Source: UniProtKB

histone deacetylase activity

Inferred from direct assay PubMed 16642021. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11062478PubMed 11259576PubMed 11641274Ref.13Ref.17PubMed 14752048PubMed 17984088Ref.32Ref.31PubMed 19505873Ref.36. Source: UniProtKB

protein deacetylase activity

Inferred from mutant phenotype PubMed 19041327. Source: BHF-UCL

sequence-specific DNA binding

Inferred from direct assay PubMed 19276356. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction PubMed 17827154. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Histone deacetylase 2
PRO_0000114693

Regions

Region9 – 322314Histone deacetylase
Compositional bias300 – 3034Poly-Gly

Sites

Active site1421 By similarity

Amino acid modifications

Modified residue2621S-nitrosocysteine By similarity
Modified residue2741S-nitrosocysteine By similarity
Modified residue3941Phosphoserine Ref.23 Ref.25 Ref.33 Ref.34 Ref.37
Modified residue4221Phosphoserine Ref.23 Ref.33 Ref.34 Ref.37
Modified residue4241Phosphoserine Ref.23 Ref.33 Ref.34 Ref.37

Natural variations

Natural variant2301R → C. Ref.1
Corresponds to variant rs1042903 [ dbSNP | Ensembl ].
VAR_025311
Natural variant3151Y → H. Ref.5
Corresponds to variant rs17852888 [ dbSNP | Ensembl ].
VAR_025312

Experimental info

Sequence conflict93 – 942QR → HI in AAC50814. Ref.1
Sequence conflict1031V → A in AAC50814. Ref.1
Sequence conflict1461S → Y in AAC50814. Ref.1
Sequence conflict2481K → M in BAG59420. Ref.2
Sequence conflict2811G → D in BAG59420. Ref.2

Secondary structure

............................................................ 488
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92769 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 775419CCCDAE07FA

FASTA48855,364
        10         20         30         40         50         60 
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA 

        70         80         90        100        110        120 
TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA 

       130        140        150        160        170        180 
GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH 

       190        200        210        220        230        240 
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ 

       250        260        270        280        290        300 
IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG 

       310        320        330        340        350        360 
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM 

       370        380        390        400        410        420 
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE 

       430        440        450        460        470        480 
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDTKGT 


KSEQLSNP 

« Hide

References

« Hide 'large scale' references
[1]"Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3."
Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.
Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CYS-230.
Tissue: Mammary gland.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-315.
Tissue: Testis.
[6]"Molecular association between ATR and two components of the nucleosome remodeling and deacetylating complex, HDAC2 and CHD4."
Schmidt D.R., Schreiber S.L.
Biochemistry 38:14711-14717(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATR, IDENTIFICATION IN A COMPLEX CONTAINING ATR AND CHD4.
[7]"A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.
J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNW1.
[8]"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."
Rountree M.R., Bachman K.E., Baylin S.B.
Nat. Genet. 25:269-277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNMT1 AND DMAP1.
[9]"NuRD and SIN3 histone deacetylase complexes in development."
Ahringer J.
Trends Genet. 16:351-356(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON DEACETYLASE COMPLEXES.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINT.
[11]"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.
[12]"Isolation and characterization of a novel class II histone deacetylase, HDAC10."
Fischer D.D., Cai R., Bhatia U., Asselbergs F.A.M., Song C., Terry R., Trogani N., Widmer R., Atadja P., Cohen D.
J. Biol. Chem. 277:6656-6666(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HDAC10.
[13]"The transcriptional repressor Sp3 is associated with CK2-phosphorylated histone deacetylase 2."
Sun J.M., Chen H.Y., Moniwa M., Litchfield D.W., Seto E., Davie J.R.
J. Biol. Chem. 277:35783-35786(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SP3.
[14]"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek."
Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G.
J. Cell Sci. 115:3319-3330(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAXX AND DEK.
[15]"Acetylation inactivates the transcriptional repressor BCL6."
Bereshchenko O.R., Gu W., Dalla-Favera R.
Nat. Genet. 32:606-613(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL6.
[16]"Role of acetylated human AP-endonuclease (APE1/Ref-1) in regulation of the parathyroid hormone gene."
Bhakat K.K., Izumi T., Yang S.H., Hazra T.K., Mitra S.
EMBO J. 22:6299-6309(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH PHF21A; HDAC1; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[19]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
[20]"The transcriptional corepressor, PELP1, recruits HDAC2 and masks histones using two separate domains."
Choi Y.B., Ko J.K., Shin J.
J. Biol. Chem. 279:50930-50941(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[21]"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.
[22]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JMJD2A.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SAP30L.
[25]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CDYL; MIER1; MIER2 AND HDAC1.
[27]"CtBP is an essential corepressor for BCL6 autoregulation."
Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A., Ye B.H.
Mol. Cell. Biol. 28:2175-2186(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL6.
[28]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"RCS1, a substrate of APC/C, controls the metaphase to anaphase transition."
Zhao W.M., Coppinger J.A., Seki A., Cheng X.L., Yates J.R. III, Fang G.
Proc. Natl. Acad. Sci. U.S.A. 105:13415-13420(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAM64A.
[30]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"FE65 binds Teashirt, inhibiting expression of the primate-specific caspase-4."
Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J., Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.
PLoS ONE 4:E5071-E5071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TSHZ3.
[32]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHFR.
[33]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[34]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SMARCAD1.
[37]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND SER-424, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"Exploration of the HDAC2 foot pocket: Synthesis and SAR of substituted N-(2-aminophenyl)benzamides."
Bressi J.C., Jennings A.J., Skene R., Wu Y., Melkus R., De Jong R., O'Connell S., Grimshaw C.E., Navre M., Gangloff A.R.
Bioorg. Med. Chem. Lett. 20:3142-3145(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 9-374 IN COMPLEX WITH SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDE INHIBITORS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31814 mRNA. Translation: AAC50814.1.
AK296856 mRNA. Translation: BAG59420.1. Different initiation.
AL590398 Genomic DNA. No translation available.
FO393415 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW48254.1.
CH471051 Genomic DNA. Translation: EAW48255.1.
BC031055 mRNA. Translation: AAH31055.2. Different initiation.
CCDSCCDS43493.2.
RefSeqNP_001518.3. NM_001527.3.
UniGeneHs.3352.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3MAXX-ray2.05A/B/C9-374[»]
4LXZX-ray1.85A/B/C8-376[»]
4LY1X-ray1.57A/B/C8-376[»]
ProteinModelPortalQ92769.
SMRQ92769. Positions 9-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109316. 358 interactions.
DIPDIP-24220N.
IntActQ92769. 105 interactions.
MINTMINT-90593.
STRING9606.ENSP00000381331.

Chemistry

BindingDBQ92769.
ChEMBLCHEMBL2093865.
DrugBankDB02546. Vorinostat.
GuidetoPHARMACOLOGY2616.

PTM databases

PhosphoSiteQ92769.

Polymorphism databases

DMDM68068066.

Proteomic databases

MaxQBQ92769.
PRIDEQ92769.

Protocols and materials databases

DNASU3066.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000519065; ENSP00000430432; ENSG00000196591.
GeneID3066.
KEGGhsa:3066.
UCSCuc003pwc.2. human.

Organism-specific databases

CTD3066.
GeneCardsGC06M114254.
HGNCHGNC:4853. HDAC2.
HPACAB005054.
HPA011727.
MIM605164. gene.
neXtProtNX_Q92769.
PharmGKBPA29227.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000225180.
HOVERGENHBG057112.
InParanoidQ92769.
KOK06067.
PhylomeDBQ92769.
TreeFamTF106171.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_71. Gene Expression.
SABIO-RKQ92769.

Gene expression databases

ArrayExpressQ92769.
BgeeQ92769.
CleanExHS_HDAC2.
GenevestigatorQ92769.

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

EvolutionaryTraceQ92769.
GeneWikiHistone_deacetylase_2.
GenomeRNAi3066.
NextBio12129.
PROQ92769.
SOURCESearch...

Entry information

Entry nameHDAC2_HUMAN
AccessionPrimary (citable) accession number: Q92769
Secondary accession number(s): B4DL58 expand/collapse secondary AC list , E1P561, Q5SRI8, Q5SZ86, Q8NEH4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 21, 2005
Last modified: July 9, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM