Reviewed, UniProtKB/Swiss-Prot Q92769 (HDAC2_HUMAN)

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.
Sequence processing	The displayed sequence is not processed.
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 By similarity. 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.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subunit structure	Interacts with the non-histone region of H2AFY 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/BRAF35, AOF2/LSD1, RCOR1/CoREST and PHF21A/BHC80. 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, DNMT1, MINT, HDAC7, HDAC10, HCFC1, NRIP1, MJD2A/JHDM3A, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts with the non-histone region of H2AFY. Interacts with PELP1. Component of a mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with CBFA2T3. Interacts with SAP30L.
Subcellular location	Nucleus.
Tissue specificity	Widely expressed; lower levels in brain and lung.
Sequence similarities	Belongs to the histone deacetylase family. Type 1 subfamily.
Sequence caution	The sequence CAI14206.1 differs from that shown. Reason: Miscellaneous discrepancy. Intron retention.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Chromatin regulator Hydrolase Repressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Ref.1 Traceable author statement. Source: ProtInc transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB histone deacetylase complex Traceable author statement. Source: UniProtKB
Molecular function	enzyme binding Inferred from physical interaction. Source: UniProtKB histone deacetylase activity Traceable author statement. Source: UniProtKB transcription factor activity Ref.1 Traceable author statement. Source: ProtInc transcription factor binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRMS1	Q9HCU9	2	EBI-301821,EBI-714781
DAXX	Q9UER7	1	EBI-301821,EBI-77321
HCFC1	P51610	1	EBI-301821,EBI-396176
HDAC1	Q13547	2	EBI-301821,EBI-301834
HDAC10	Q969S8	1	EBI-301821,EBI-301762
MBD1	Q9UIS9	2	EBI-301821,EBI-867196
RFX5	P48382	1	EBI-301821,EBI-923266
SIN3A	Q96ST3	2	EBI-301821,EBI-347218
SUV39H1	O43463	2	EBI-301821,EBI-349968

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92769-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q92769-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRSPPCGLLR...SPVAAVAGEP

Note: No experimental confirmation available.

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	394	1	Phosphoserine Ref.18 Ref.20 Ref.22 Ref.23
	Modified residue	407	1	Phosphoserine Ref.23 Ref.21
	Modified residue	422	1	Phosphoserine Ref.18 Ref.23 Ref.21
	Modified residue	424	1	Phosphoserine Ref.18 Ref.23 Ref.21
Natural variations
	Alternative sequence	1	1	M → MRSPPCGLLRWFGGPLLASW CRCHLRFRAFGTSAGWYRAF PAPPPLLPPACPSPRDYRPH VSLSPFLSRPSRGGSSSSSS SRRRSPVAAVAGEP in isoform 2.		VSP_037162
	Natural variant	230	1	R → C: dbSNP rs1042903. Ref.1		VAR_025311
	Natural variant	315	1	Y → H: dbSNP rs17852888. Ref.4		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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2. Checksum: 55C8D6F0CA2B3580	FASTA	581	65,407
	10 20 30 40 50 60 MRSPPCGLLR WFGGPLLASW CRCHLRFRAF GTSAGWYRAF PAPPPLLPPA CPSPRDYRPH 70 80 90 100 110 120 VSLSPFLSRP SRGGSSSSSS SRRRSPVAAV AGEPAYSQGG GKKKVCYYYD GDIGNYYYGQ 130 140 150 160 170 180 GHPMKPHRIR MTHNLLLNYG LYRKMEIYRP HKATAEEMTK YHSDEYIKFL RSIRPDNMSE 190 200 210 220 230 240 YSKQMQRFNV GEDCPVFDGL FEFCQLSTGG SVAGAVKLNR QQTDMAVNWA GGLHHAKKSE 250 260 270 280 290 300 ASGFCYVNDI VLAILELLKY HQRVLYIDID IHHGDGVEEA FYTTDRVMTV SFHKYGEYFP 310 320 330 340 350 360 GTGDLRDIGA GKGKYYAVNF PMRDGIDDES YGQIFKPIIS KVMEMYQPSA VVLQCGADSL 370 380 390 400 410 420 SGDRLGCFNL TVKGHAKCVE VVKTFNLPLL MLGGGGYTIR NVARCWTYET AVALDCEIPN 430 440 450 460 470 480 ELPYNDYFEY FGPDFKLHIS PSNMTNQNTP EYMEKIKQRL FENLRMLPHA PGVQMQAIPE 490 500 510 520 530 540 DAVHEDSGDE DGEDPDKRIS IRASDKRIAC DEEFSDSEDE GEGGRRNVAD HKKGAKKARI 550 560 570 580 EEDKKETEDK KTDVKEEDKS KDNSGEKTDT KGTKSEQLSN P

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] (ISOFORM 1), 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] (ISOFORM 2). 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]	"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] (ISOFORM 1), VARIANT HIS-315. Tissue: Testis.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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; AOF2; RCOR1; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[14]	"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.
[15]	"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.
[16]	"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition." Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V. Nucleic Acids Res. 32:1957-1966(2004) [PubMed: 15060175] [Abstract] Cited for: INTERACTION WITH NRIP1.
[17]	"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.
[18]	"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: Epithelium.
[19]	"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.
[20]	"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: Epithelium.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U31814 mRNA. Translation: AAC50814.1. AK296856 mRNA. Translation: BAG59420.1. AL590398 Genomic DNA. Translation: CAI14206.1. AL590398, AL671967 Genomic DNA. Translation: CAI14207.1. AL671967, AL590398 Genomic DNA. Translation: CAI15363.1. BC031055 mRNA. Translation: AAH31055.2.
IPI	IPI00289601.
RefSeq	NP_001518.2.
UniGene	Hs.3352
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:24220N.
IntAct	Q92769. 27 interactions.
PTM databases
PhosphoSite	Q92769.
Proteomic databases
PRIDE	Q92769.
Genome annotation databases
Ensembl	ENSG00000196591. Homo sapiens. [Contig view]
GeneID	3066.
KEGG	hsa:3066.
Organism-specific databases
GeneCards	GC06M114368.
HGNC	HGNC:4853. HDAC2.
HPA	CAB005054. HPA011727.
MIM	605164. gene.
PharmGKB	PA29227.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q92769.
HOVERGEN	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_11061. Signalling by NGF. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q92769.
Bgee	Q92769.
CleanEx	HS_HDAC2.
GermOnline	ENSG00000196591. 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	12129.
SOURCE	Search...

Entry information

Entry name

HDAC2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 21, 2005
Last modified:	June 16, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)