Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9LXN8 (HDA17_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase 17

EC=3.5.1.98
Gene names
Name:HDA17
Ordered Locus Names:At3g44490
ORF Names:F14L2.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length158 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158Histone deacetylase 17
PRO_0000280092

Regions

Region3 – 5048Histone deacetylase
Compositional bias28 – 314Poly-Gly
Compositional bias116 – 15641Asp-rich

Experimental info

Sequence conflict581S → P in BT014712. Ref.3
Sequence conflict941Q → R in BT014712. Ref.3
Sequence conflict1331V → A in BT014712. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9LXN8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B4C29ACF84F232E0

FASTA15818,116
        10         20         30         40         50         60 
MAFSMLFTGH AECVKFVKKF NLPLLVTGGG GYTKENVARC WTVETGILLD TELPNEISEN 

        70         80         90        100        110        120 
DYIKYFAPDF SLKIPGGHIE NLNTKSYISS IKVQILENLR YIQHAPSVQM QEVPPDFYIP 

       130        140        150 
DFDEDEQNPD VRVDQRSRDK QIQRDDEYFD GDNDNDAS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Center for eukaryotic structural genomics (CESG)
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-158.
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL353818 Genomic DNA. Translation: CAB88531.1.
CP002686 Genomic DNA. Translation: AEE77907.1.
BT014712 mRNA. No translation available.
PIRT48929.
RefSeqNP_190035.1. NM_114317.2.
UniGeneAt.66492.

3D structure databases

ProteinModelPortalQ9LXN8.
SMRQ9LXN8. Positions 3-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G44490.1-P.

Proteomic databases

PaxDbQ9LXN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G44490.1; AT3G44490.1; AT3G44490.
GeneID823574.
KEGGath:AT3G44490.

Organism-specific databases

TAIRAT3G44490.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000112868.
InParanoidQ9LXN8.
KOK06067.
OMADNEGESH.
PhylomeDBQ9LXN8.
ProtClustDBCLSN2684485.

Enzyme and pathway databases

BioCycARA:AT3G44490-MONOMER.

Gene expression databases

GenevestigatorQ9LXN8.

Family and domain databases

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

Entry information

Entry nameHDA17_ARATH
AccessionPrimary (citable) accession number: Q9LXN8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 81 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