Reviewed, UniProtKB/Swiss-Prot Q94EJ2 (HDA8_ARATH)

Names and origin

Protein names

Recommended name:
    Histone deacetylase 8
    EC=3.5.1.98

Gene names

Name:	HDA8
Ordered Locus Names:	At1g08460
ORF Names:	T27G7_7, T27G7.14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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.
Catalytic activity	Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the histone deacetylase family.
Sequence caution	The sequence AAF22892.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Hydrolase Repressor
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Histone deacetylase 8		PRO_0000280087
Regions
	Region	5 – 336	332	Histone deacetylase
Sites
	Active site	145	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q94EJ2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 538E741343EC8CF3	FASTA	377	41,263
	10 20 30 40 50 60 MVTNRVDVFW HEGMLRHDAV EGVFDTGYDP GFLDVLEKHP ENADRVRNML SILRRGPIAP 70 80 90 100 110 120 HVNWFTGLPA IVSELLMFHT SEYIEKLVEA DKSGERCEIA AGTFMSPGSW EAALLAAGTT 130 140 150 160 170 180 LSAMQHILDC HGKIAYALVR PPGHHSQPTQ ADGYCFLNNA ALAVKLALNS GSCSRVAVID 190 200 210 220 230 240 IDVHYGNGTA EGFYTSDKVL TVSLHMNHGS WGSSHPQKGS IDELGEDVGL GYNLNVPLPN 250 260 270 280 290 300 GTGDRGYEYA MNELVVPAVR RFGPDMVVLV VGQDSSAFDP NGRQSLTMNG YRRIGQIMRG 310 320 330 340 350 360 VAEEHSHGRL LMVQEGGYHV TYAAYCLHAM LEGVLKIPEP HLSDPIAYYP EEEANAVAAV 370 ESIKTYHTEF VPFLRGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes." Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A. Nucleic Acids Res. 30:5036-5055(2002) [PubMed: 12466527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF510167 mRNA. Translation: AAM49769.1. AC006932 Genomic DNA. Translation: AAF22892.1. Sequence problems. AF410272 mRNA. Translation: AAK95258.1. AF428369 mRNA. Translation: AAL16299.1. Different initiation. AY097371 mRNA. Translation: AAM19887.1.
IPI	IPI00548930.
PIR	G86217.
RefSeq	NP_563817.1.
UniGene	At.26246
3D structure databases
HSSP	HSSP built from PDB template 1C3P based on UniProtKB O67135.
ModBase	Search...
Proteomic databases
PRIDE	Q94EJ2.
Genome annotation databases
GeneID	837366.
GenomeReviews	Gene locus AT1G08460 in contig CT485782_GR.
KEGG	ath:AT1G08460.
NMPDR	fig|3702.1.peg.1054.
Organism-specific databases
TAIR	At1g08460.
Phylogenomic databases
OMA	GRRTTEN.
Gene expression databases
Genevestigator	Q94EJ2.
Family and domain databases
InterPro	IPR000286. His_deacetylse. [Graphical view]
Gene3D	G3DSA:3.40.800.20. His_deacetylse. 1 hit.
PANTHER	PTHR10625. His_deacetylse. 1 hit.
Pfam	PF00850. Hist_deacetyl. 1 hit. [Graphical view]
PRINTS	PR01270. HDASUPER.
ProtoNet	Search...

Entry information

Entry name

HDA8_ARATH

Accession

Primary (citable) accession number: Q94EJ2
Secondary accession number(s): Q944J5, Q9SJE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2007
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)