Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone deacetylase 9

Gene

HDA9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371By similarity

GO - Molecular functioni

GO - Biological processi

  • negative regulation of seed germination Source: TAIR
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciARA:AT3G44680-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase 9 (EC:3.5.1.98)
Gene namesi
Name:HDA9
Ordered Locus Names:At3g44680
ORF Names:T18B22.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G44680.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Histone deacetylase 9PRO_0000280088Add
BLAST

Proteomic databases

PRIDEiQ8H0W2.

Expressioni

Gene expression databases

GenevestigatoriQ8H0W2.

Interactioni

Subunit structurei

Interacts with AHL22.1 Publication

Protein-protein interaction databases

BioGridi8914. 5 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8H0W2.
SMRiQ8H0W2. Positions 6-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni6 – 318313Histone deacetylaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi296 – 2994Poly-Gly
Compositional biasi384 – 42441Asp-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000225180.
InParanoidiQ8H0W2.
KOiK06067.
OMAiDERMDQH.
PhylomeDBiQ8H0W2.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.

Sequencei

Sequence statusi: Complete.

Q8H0W2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSKDKISYF YDGDVGSVYF GPNHPMKPHR LCMTHHLILA YGLHSKMEVY
60 70 80 90 100
RPHKAYPIEM AQFHSPDYVE FLQRINPENQ NLFPNEMARY NLGEDCPVFE
110 120 130 140 150
DLFEFCQLYA GGTIDAARRL NNKLCDIAIN WAGGLHHAKK CDASGFCYIN
160 170 180 190 200
DLVLGILELL KHHPRVLYID IDVHHGDGVE EAFYFTDRVM TVSFHKFGDK
210 220 230 240 250
FFPGTGDVKE IGEREGKFYA INVPLKDGID DSSFNRLFRT IISKVVEIYQ
260 270 280 290 300
PGAIVLQCGA DSLARDRLGC FNLSIDGHAE CVKFVKKFNL PLLVTGGGGY
310 320 330 340 350
TKENVARCWT VETGILLDTE LPNEIPENDY IKYFAPDFSL KIPGGHIENL
360 370 380 390 400
NTKSYISSIK VQILENLRYI QHAPSVQMQE VPPDFYIPDF DEDEQNPDVR
410 420
ADQRSRDKQI QRDDEYFDGD NDNDAS
Length:426
Mass (Da):48,688
Last modified:March 1, 2003 - v1
Checksum:iB7B4B9D7432C6DBD
GO

Sequence cautioni

The sequence CAB72470.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138652 Genomic DNA. Translation: CAB72470.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE77930.1.
BT002003 mRNA. Translation: AAN72014.1.
BT006576 mRNA. Translation: AAP31920.1.
PIRiT47443.
RefSeqiNP_190054.2. NM_114336.3.
UniGeneiAt.36124.

Genome annotation databases

EnsemblPlantsiAT3G44680.1; AT3G44680.1; AT3G44680.
GeneIDi823594.
KEGGiath:AT3G44680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138652 Genomic DNA. Translation: CAB72470.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE77930.1.
BT002003 mRNA. Translation: AAN72014.1.
BT006576 mRNA. Translation: AAP31920.1.
PIRiT47443.
RefSeqiNP_190054.2. NM_114336.3.
UniGeneiAt.36124.

3D structure databases

ProteinModelPortaliQ8H0W2.
SMRiQ8H0W2. Positions 6-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi8914. 5 interactions.

Proteomic databases

PRIDEiQ8H0W2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G44680.1; AT3G44680.1; AT3G44680.
GeneIDi823594.
KEGGiath:AT3G44680.

Organism-specific databases

TAIRiAT3G44680.

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000225180.
InParanoidiQ8H0W2.
KOiK06067.
OMAiDERMDQH.
PhylomeDBiQ8H0W2.

Enzyme and pathway databases

BioCyciARA:AT3G44680-MONOMER.

Miscellaneous databases

PROiQ8H0W2.

Gene expression databases

GenevestigatoriQ8H0W2.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSiPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "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: GENE FAMILY, NOMENCLATURE.
  5. "The AT-hook motif-containing protein AHL22 regulates flowering initiation by modifying FLOWERING LOCUS T chromatin in Arabidopsis."
    Yun J., Kim Y.S., Jung J.H., Seo P.J., Park C.M.
    J. Biol. Chem. 287:15307-15316(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AHL22.

Entry informationi

Entry nameiHDA9_ARATH
AccessioniPrimary (citable) accession number: Q8H0W2
Secondary accession number(s): Q9M1N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 1, 2003
Last modified: May 27, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.