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Q94EJ2 (HDA8_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histone deacetylase 8

EC=3.5.1.98
Gene names
Name:HDA8
Ordered Locus Names:At1g08460
ORF Names:T27G7.14, T27G7_7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

The sequence AAL16299.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Histone deacetylase 8
PRO_0000280087

Regions

Region5 – 336332Histone deacetylase

Sites

Active site1451 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q94EJ2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 538E741343EC8CF3

FASTA37741,263
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF510167 mRNA. Translation: AAM49769.1.
AC006932 Genomic DNA. Translation: AAF22892.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28294.1.
AF410272 mRNA. Translation: AAK95258.1.
AF428369 mRNA. Translation: AAL16299.1. Different initiation.
AY097371 mRNA. Translation: AAM19887.1.
PIRG86217.
RefSeqNP_563817.1. NM_100719.3.
UniGeneAt.26246.

3D structure databases

ProteinModelPortalQ94EJ2.
SMRQ94EJ2. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G08460.1-P.

Proteomic databases

PaxDbQ94EJ2.
PRIDEQ94EJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08460.1; AT1G08460.1; AT1G08460.
GeneID837366.
KEGGath:AT1G08460.

Organism-specific databases

TAIRAT1G08460.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225183.
InParanoidQ94EJ2.
OMASAMQHIL.
PhylomeDBQ94EJ2.
ProtClustDBCLSN2687728.

Enzyme and pathway databases

BioCycARA:AT1G08460-MONOMER.

Gene expression databases

GenevestigatorQ94EJ2.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Entry information

Entry nameHDA8_ARATH
AccessionPrimary (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: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names