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Q941D6 (HDA14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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 14

EC=3.5.1.98
Gene names
Name:HDA14
Ordered Locus Names:At4g33470
ORF Names:F17M5.230
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.5

Catalytic activity

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

Subcellular location

Nucleus By similarity.

Miscellaneous

HDA14 is not required for the cellular patterning in the root epidermis.

Sequence similarities

Belongs to the histone deacetylase family.

Sequence caution

The sequence CAB38805.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80064.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

tubulin deacetylation

Inferred from direct assay PubMed 22404109. Source: TAIR

   Cellular_componentchloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

cytosol

Inferred from direct assay PubMed 22404109. Source: TAIR

nucleus

Inferred from direct assay PubMed 22404109. Source: TAIR

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

alpha-tubulin binding

Inferred from direct assay PubMed 22404109. Source: TAIR

beta-tubulin binding

Inferred from direct assay PubMed 22404109. Source: TAIR

protein phosphatase 2A binding

Inferred from direct assay PubMed 22404109. Source: TAIR

protein self-association

Inferred from physical interaction PubMed 22404109. Source: TAIR

tubulin deacetylase activity

Inferred from direct assay PubMed 22404109. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 423422Histone deacetylase 14
PRO_0000280090

Regions

Region62 – 392331Histone deacetylase

Sites

Active site2021 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q941D6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: EA56909AFC9672E0

FASTA42345,577
        10         20         30         40         50         60 
MSMALIVRPF FVPGSAGISG SRNICKKNQW RKYLLKPSGS SINCSFSTEK NPLLPSIQQL 

        70         80         90        100        110        120 
ADARLIYSVS AALGHNKESH PECSARVPAI VNALEMNELT PKFRGSQILE LANFKTATVE 

       130        140        150        160        170        180 
DIANVHDKAY VFGLEKAMDE ASDSGLIFIE GSGPTYATST TFQDSLIAAG AGMALVDSVI 

       190        200        210        220        230        240 
AASRNSVDPP IGFALIRPPG HHAVPKGPMG FCVFGNVAIA ARHAQRTHGL KRIFIIDFDV 

       250        260        270        280        290        300 
HHGNGTNDAF TEDPDIFFLS THQDGSYPGT GKISDIGKGK GEGTTLNLPL PGGSGDIAMR 

       310        320        330        340        350        360 
TVFEEIIVPC AQRFKPDIIL VSAGYDAHVL DPLANLQFTT ATYYSLAKDI KRLAKEVCGG 

       370        380        390        400        410        420 
RCVFFLEGGY NLESLSSSVA DSFRALLGED SLASEFDNPA YLYDEPMRKV RDAIQRAKSI 


HCL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [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. 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.
[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]"Histone acetylation affects expression of cellular patterning genes in the Arabidopsis root epidermis."
Xu C.-R., Liu C., Wang Y.-L., Li L.-C., Chen W.-Q., Xu Z.-H., Bai S.-N.
Proc. Natl. Acad. Sci. U.S.A. 102:14469-14474(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL035678 Genomic DNA. Translation: CAB38805.1. Sequence problems.
AL161583 Genomic DNA. Translation: CAB80064.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86231.1.
AY052234 mRNA. Translation: AAK97704.1.
AY113069 mRNA. Translation: AAM47377.1.
PIRT05998.
RefSeqNP_567921.1. NM_119501.3.
UniGeneAt.26427.

3D structure databases

ProteinModelPortalQ941D6.
SMRQ941D6. Positions 61-422.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14768. 2 interactions.
STRING3702.AT4G33470.1-P.

Proteomic databases

PaxDbQ941D6.
PRIDEQ941D6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G33470.1; AT4G33470.1; AT4G33470.
GeneID829484.
KEGGath:AT4G33470.

Organism-specific databases

TAIRAT4G33470.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225183.
InParanoidQ941D6.
OMALELANFK.
PhylomeDBQ941D6.
ProtClustDBCLSN2689736.

Enzyme and pathway databases

BioCycARA:AT4G33470-MONOMER.

Gene expression databases

GenevestigatorQ941D6.

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 nameHDA14_ARATH
AccessionPrimary (citable) accession number: Q941D6
Secondary accession number(s): Q9SZC4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 76 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