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Protein

Elongator complex protein 3

Gene

HAG3

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

Functioni

Histone acetyltransferase component of the large multiprotein complex Elongator that is involved in the regulation of transcription initiation and elongation. May also have a methyltransferase activity. Promotes organs development by modulating cell division rate. Required for auxin distribution or signaling. Involved in tRNA wobble uridine modification. Mediates the establishment of leaf polarity independently of AS2 and the ta-siRNA-related pathway.3 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi117 – 1171Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi127 – 1271Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi130 – 1301Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

GO - Biological processi

  • auxin-activated signaling pathway Source: UniProtKB-KW
  • cell proliferation Source: TAIR
  • DNA mediated transformation Source: TAIR
  • histone acetylation Source: GO_Central
  • organ growth Source: TAIR
  • regulation of auxin mediated signaling pathway Source: UniProtKB
  • regulation of leaf formation Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • specification of organ axis polarity Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: GO_Central
  • tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Auxin signaling pathway, Transcription, Transcription regulation, tRNA processing

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciARA:AT5G50320-MONOMER.
BRENDAi2.3.1.48. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongator complex protein 3 (EC:2.3.1.48)
Short name:
AtELP3
Alternative name(s):
Elongator component 3
Protein ELONGATA 3
Protein ENHANCER-OF-ASYMMETRIC-LEAVES-TWO1
Gene namesi
Name:HAG3
Synonyms:EAST1, ELO3, ELP3
Ordered Locus Names:At5g50320
ORF Names:MXI22.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G50320.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: TAIR
  • Elongator holoenzyme complex Source: UniProtKB
  • histone acetyltransferase complex Source: GO_Central
  • nuclear euchromatin Source: UniProtKB
  • nucleus Source: TAIR
  • transcription elongation factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Slow growing rate associated with pale-green and downwardly curled narrow leaves and reduced root growth that results from a decreased cell division rate and a reduced apical dominance. Defect in tRNA wobble uridine modification. Filamentous leaves with abaxialized epidermis in AS2 defective plants.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi200 – 2001R → W in east1-1; slow growth associated with pale-green and downwardly curled leaves. 1 Publication
Mutagenesisi331 – 3311D → N in elo3-1; reduced cell proliferation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 565565Elongator complex protein 3PRO_0000232128Add
BLAST

Proteomic databases

PaxDbiQ93ZR1.
PRIDEiQ93ZR1.

Expressioni

Tissue specificityi

Expressed in meristematic tissues of in roots, leaves, seedlings, cotyledons, floral buds and shoot apices.2 Publications

Interactioni

Subunit structurei

Component of the RNA polymerase II elongator complex (Elongator) made of at least six subunits, ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6.1 Publication

Protein-protein interaction databases

BioGridi20344. 1 interaction.
IntActiQ93ZR1. 1 interaction.
STRINGi3702.AT5G50320.1.

Structurei

3D structure databases

ProteinModelPortaliQ93ZR1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini414 – 565152N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ELP3 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1243.
HOGENOMiHOG000227514.
InParanoidiQ93ZR1.
KOiK07739.
OMAiGYKVVSH.
PhylomeDBiQ93ZR1.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93ZR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATAVVMNGE LKKQPRPGKG GYQGRGLTEE EARVRAISEI VSTMIERSHR
60 70 80 90 100
NENVDLNAIK TAACRKYGLA RAPKLVEMIA ALPDSERETL LPKLRAKPVR
110 120 130 140 150
TASGIAVVAV MSKPHRCPHI ATTGNICVYC PGGPDSDFEY STQSYTGYEP
160 170 180 190 200
TSMRAIRARY NPYVQARSRI DQLKRLGHSV DKVEFILMGG TFMSLPAEYR
210 220 230 240 250
DFFIRNLHDA LSGHTSANVE EAVAYSEHSA TKCIGMTIET RPDYCLGPHL
260 270 280 290 300
RQMLIYGCTR LEIGVQSTYE DVARDTNRGH TVAAVADCFC LAKDAGFKVV
310 320 330 340 350
AHMMPDLPNV GVERDMESFK EFFESPSFRA DGLKIYPTLV IRGTGLYELW
360 370 380 390 400
KTGRYRNYPP EQLVDIVARI LSMVPPWTRV YRVQRDIPMP LVTSGVEKGN
410 420 430 440 450
LRELALARMD DLGLKCRDVR TREAGIQDIH HKIKPEQVEL VRRDYTANEG
460 470 480 490 500
WETFLSYEDT RQDILVGLLR LRKCGKNVTC PELMGKCSVV RELHVYGTAV
510 520 530 540 550
PVHGRDADKL QHQGYGTLLM EEAERIARRE HRSNKIGVIS GVGTRHYYRK
560
LGYELEGPYM VKHLL
Length:565
Mass (Da):63,694
Last modified:December 1, 2001 - v1
Checksum:i8F993E4D41CF4B05
GO

Sequence cautioni

The sequence AAL06951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ964958 mRNA. Translation: CAI79647.1.
AB012248 Genomic DNA. Translation: BAB09451.1.
CP002688 Genomic DNA. Translation: AED95925.1.
AY054293 mRNA. Translation: AAL06951.1. Different initiation.
AY056323 mRNA. Translation: AAL07172.1.
AY133528 mRNA. Translation: AAM91358.1.
RefSeqiNP_568725.1. NM_124412.2.
UniGeneiAt.20657.

Genome annotation databases

EnsemblPlantsiAT5G50320.1; AT5G50320.1; AT5G50320.
GeneIDi835098.
KEGGiath:AT5G50320.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ964958 mRNA. Translation: CAI79647.1.
AB012248 Genomic DNA. Translation: BAB09451.1.
CP002688 Genomic DNA. Translation: AED95925.1.
AY054293 mRNA. Translation: AAL06951.1. Different initiation.
AY056323 mRNA. Translation: AAL07172.1.
AY133528 mRNA. Translation: AAM91358.1.
RefSeqiNP_568725.1. NM_124412.2.
UniGeneiAt.20657.

3D structure databases

ProteinModelPortaliQ93ZR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi20344. 1 interaction.
IntActiQ93ZR1. 1 interaction.
STRINGi3702.AT5G50320.1.

Proteomic databases

PaxDbiQ93ZR1.
PRIDEiQ93ZR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G50320.1; AT5G50320.1; AT5G50320.
GeneIDi835098.
KEGGiath:AT5G50320.

Organism-specific databases

TAIRiAT5G50320.

Phylogenomic databases

eggNOGiCOG1243.
HOGENOMiHOG000227514.
InParanoidiQ93ZR1.
KOiK07739.
OMAiGYKVVSH.
PhylomeDBiQ93ZR1.

Enzyme and pathway databases

BioCyciARA:AT5G50320-MONOMER.
BRENDAi2.3.1.48. 399.

Miscellaneous databases

PROiQ93ZR1.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The elongata mutants identify a functional Elongator complex in plants with a role in cell proliferation during organ growth."
    Nelissen H., Fleury D., Bruno L., Robles P., de Veylder L., Traas J., Micol J., Van Montagu M., Inze D., Van Lijsebettens M.
    Proc. Natl. Acad. Sci. U.S.A. 102:7754-7759(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-331, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
    Strain: cv. Landsberg erecta.
    Tissue: Seedling.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
    Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
    DNA Res. 5:203-216(1998) [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.
    , 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.
  5. "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: NOMENCLATURE.
  6. "Elongator function in tRNA wobble uridine modification is conserved between yeast and plants."
    Mehlgarten C., Jablonowski D., Wrackmeyer U., Tschitschmann S., Sondermann D., Jaeger G., Gong Z., Bystroem A.S., Schaffrath R., Breunig K.D.
    Mol. Microbiol. 76:1082-1094(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  8. "Asymmetric leaves2 and Elongator, a histone acetyltransferase complex, mediate the establishment of polarity in leaves of Arabidopsis thaliana."
    Kojima S., Iwasaki M., Takahashi H., Imai T., Matsumura Y., Fleury D., Van Lijsebettens M., Machida Y., Machida C.
    Plant Cell Physiol. 52:1259-1273(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-200, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiELP3_ARATH
AccessioniPrimary (citable) accession number: Q93ZR1
Secondary accession number(s): Q9FK40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 100 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.