Q92769 (HDAC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone deacetylase 2
Short name=HD2
EC=3.5.1.98

Gene names

Name:

HDAC2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	488 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. 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. Ref.30
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with HDAC7, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the H2AFY (via the non-histone region) By similarity. 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 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. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22 Ref.30 Ref.31
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. The sequence CAI14206.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Acetylation Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome chromatin remodeling Inferred by curator. Source: BHF-UCL dendrite development Inferred from sequence or structural similarity. Source: UniProtKB embryonic digit morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL epidermal cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL eyelid development in camera-type eye Inferred from sequence or structural similarity. Source: BHF-UCL fungiform papilla formation Inferred from sequence or structural similarity. Source: BHF-UCL hair follicle placode formation Inferred from sequence or structural similarity. Source: BHF-UCL maintenance of chromatin silencing Inferred from mutant phenotype. Source: BHF-UCL negative regulation of MHC class II biosynthetic process Inferred by curator. Source: BHF-UCL negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of cell cycle Traceable author statement. Source: Reactome negative regulation of neuron projection development Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome odontogenesis of dentin-containing tooth Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cell proliferation Inferred from mutant phenotype. Source: BHF-UCL positive regulation of collagen biosynthetic process Inferred by curator. Source: BHF-UCL positive regulation of proteolysis Inferred from mutant phenotype. Source: BHF-UCL positive regulation of receptor biosynthetic process Inferred from mutant phenotype. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	ESC/E(Z) complex Inferred from direct assay. Source: UniProtKB NuRD complex Inferred from direct assay. Source: UniProtKB Sin3 complex Inferred from direct assay. Source: UniProtKB cytoplasm Traceable author statement. Source: UniProtKB
Molecular function	NAD-dependent histone deacetylase activity (H3-K14 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 sequence or structural similarity. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB histone deacetylase activity (H3-K16 specific) Inferred from electronic annotation. Source: EC sequence-specific DNA binding Inferred from direct assay. Source: BHF-UCL transcription factor binding Inferred from physical interaction. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRMS1	Q9HCU9	3	EBI-301821,EBI-714781
DAXX	Q9UER7	2	EBI-301821,EBI-77321
HCFC1	P51610	2	EBI-301821,EBI-396176
HDAC1	Q13547	5	EBI-301821,EBI-301834
MBD1	Q9UIS9	2	EBI-301821,EBI-867196
MYC	P01106	2	EBI-301821,EBI-447544
RFX5	P48382	4	EBI-301821,EBI-923266
SIN3A	Q96ST3	3	EBI-301821,EBI-347218
SUV39H1	O43463	3	EBI-301821,EBI-349968

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 488

488

Histone deacetylase 2

PRO_0000114693

Regions

Region

9 – 322

314

Histone deacetylase

Compositional bias

300 – 303

4

Poly-Gly

Sites

Active site

142

1

By similarity

Amino acid modifications

Modified residue

75

1

N6-acetyllysine Ref.33

Modified residue

90

1

N6-acetyllysine Ref.33

Modified residue

262

1

S-nitrosocysteine By similarity

Modified residue

274

1

S-nitrosocysteine By similarity

Modified residue

394

1

Phosphoserine Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.32

Modified residue

407

1

Phosphoserine Ref.24 Ref.27

Modified residue

422

1

Phosphoserine Ref.21 Ref.24 Ref.27 Ref.28 Ref.32

Modified residue

424

1

Phosphoserine Ref.21 Ref.24 Ref.27 Ref.28 Ref.32

Natural variations

Natural variant

230

1

R → C. Ref.1
Corresponds to variant rs1042903 [ dbSNP | Ensembl ].

VAR_025311

Natural variant

315

1

Y → H. Ref.5
Corresponds to variant rs17852888 [ dbSNP | Ensembl ].

VAR_025312

Experimental info

Sequence conflict

93 – 94

2

QR → HI in AAC50814. Ref.1

Sequence conflict

103

1

V → A in AAC50814. Ref.1

Sequence conflict

146

1

S → Y in AAC50814. Ref.1

Sequence conflict

248

1

K → M in BAG59420. Ref.2

Sequence conflict

281

1

G → D in BAG59420. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

488

Helix Strand Turn

Details...

Beta strand

12 – 15

4

Helix

34 – 45

12

Helix

49 – 51

3

Beta strand

52 – 55

4

Helix

62 – 65

4

Turn

66 – 68

3

Helix

71 – 79

9

Helix

82 – 87

6

Helix

89 – 94

6

Helix

108 – 114

7

Helix

123 – 126

4

Beta strand

131 – 134

4

Helix

156 – 164

9

Turn

165 – 167

3

Beta strand

171 – 175

5

Turn

185 – 190

6

Beta strand

192 – 201

10

Beta strand

224 – 229

6

Turn

235 – 238

4

Helix

242 – 253

12

Beta strand

256 – 261

6

Helix

283 – 290

8

Beta strand

296 – 299

4

Helix

306 – 320

15

Helix

335 – 337

3

Beta strand

343 – 345

3

Helix

357 – 371

15

Sequences

	Sequence		Length	Mass (Da)
	Q92769 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: 775419CCCDAE07FA	FASTA	488	55,364
	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

References

	« Hide 'large scale' referencesShow '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: 8917507] [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. , 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: 14702039] [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. , 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: 14574404] [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. , 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: 15489334] [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: 10545197] [Abstract] Cited for: INTERACTION WITH ATR, IDENTIFICATION IN A COMPLEX CONTAINING ATR AND CHD4.
[7]	"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: 10888872] [Abstract] Cited for: INTERACTION WITH DNMT1 AND DMAP1.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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: 11739383] [Abstract] Cited for: INTERACTION WITH HDAC10.
[12]	"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: 12176973] [Abstract] Cited for: INTERACTION WITH SP3.
[13]	"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: 12140263] [Abstract] Cited for: INTERACTION WITH DAXX AND DEK.
[14]	"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: 14633989] [Abstract] Cited for: INTERACTION WITH APEX1.
[15]	"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.
[16]	"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; HDAC1; HMG20B; KDM1A; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[17]	"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.
[18]	"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: 15456770] [Abstract] Cited for: INTERACTION WITH PELP1.
[19]	"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: 15060175] [Abstract] Cited for: INTERACTION WITH NRIP1.
[20]	"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 JMJD2A.
[21]	"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-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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.
[23]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[24]	"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-407; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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-394, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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-394, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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-394; SER-407; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[28]	"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-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[29]	"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-394, MASS SPECTROMETRY.
[30]	"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: 19343227] [Abstract] Cited for: FUNCTION, INTERACTION WITH TSHZ3.
[31]	"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: INTERACTION WITH CHFR.
[32]	"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-394; SER-422 AND SER-424, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[33]	"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-75 AND LYS-90, MASS SPECTROMETRY.
[34]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]	"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: 20392638] [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. Translation: CAI14206.1. Sequence problems.
AL590398, AL671967 Genomic DNA. Translation: CAI14207.1.
AL671967, AL590398 Genomic DNA. Translation: CAI15363.1.
CH471051 Genomic DNA. Translation: EAW48254.1.
CH471051 Genomic DNA. Translation: EAW48255.1.
BC031055 mRNA. Translation: AAH31055.2. Different initiation.

IPI

IPI00289601.

RefSeq

NP_001518.3. NM_001527.3.

UniGene

Hs.3352.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3MAX	X-ray	2.05	A/B/C	9-374	[»]

ProteinModelPortal

Q92769.

SMR

Q92769. Positions 9-374.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24220N.

IntAct

Q92769. 68 interactions.

MINT

MINT-90593.

STRING

Q92769.

PTM databases

PhosphoSite

Q92769.

Polymorphism databases

DMDM

68068066.

Proteomic databases

PRIDE

Q92769.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368632; ENSP00000357621; ENSG00000196591.
ENST00000398283; ENSP00000381331; ENSG00000196591.

GeneID

3066.

KEGG

hsa:3066.

UCSC

uc003pwc.1. human.

Organism-specific databases

CTD

3066.

GeneCards

GC06M114307.

H-InvDB

HIX0006155.

HGNC

HGNC:4853. HDAC2.

HPA

CAB005054.
HPA011727.

MIM

605164. gene.

neXtProt

NX_Q92769.

PharmGKB

PA29227.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15575.

GeneTree

ENSGT00530000062889.

HOGENOM

HBG396919.

HOVERGEN

HBG057112.

InParanoid

Q92769.

OrthoDB

EOG4868CH.

PhylomeDB

Q92769.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
telomerasepathway. Regulation of Telomerase.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q92769.

Bgee

Q92769.

CleanEx

HS_HDAC2.

Genevestigator

Q92769.

GermOnline

ENSG00000196591. Homo sapiens.

Family and domain databases

InterPro

IPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]

Gene3D

G3DSA:3.40.800.20. His_deacetylse. 1 hit.

KO

K06067.

PANTHER

PTHR10625. His_deacetylse. 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

DrugBank

DB02546. Vorinostat.

NextBio

12129.

SOURCE

Search...

Entry information

Entry name

HDAC2_HUMAN

Accession

Primary (citable) accession number: Q92769
Secondary accession number(s): B4DL58 , E1P561, Q5SRI8, Q5SZ86, Q8NEH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 21, 2005
Last modified:	January 25, 2012
This is version 133 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.