F4JP52 · PQT3_ARATH

Function

function

E3 ubiquitin ligase acting as a negative regulator of oxidative stress tolerance, probably by mediating 26S proteasome-mediated degradation of PRMT13/PRMT4B, thus preventing APX1 and GPX1 accumulation via the reduction of histone H3 methylation (H3R17me2a). Confers sensitivity to cadmium CdCl2 and salt NaCl stresses.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-like protein ligase activity
Molecular Functionzinc ion binding
Biological Processcellular response to paraquat
Biological Processnegative regulation of response to oxidative stress
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processpositive regulation of response to oxidative stress
Biological Processprotein ubiquitination
Biological Processresponse to cadmium ion
Biological Processresponse to hydrogen peroxide
Biological Processresponse to mannitol
Biological Processresponse to oxidative stress
Biological Processresponse to paraquat
Biological Processresponse to salt stress
Biological Processresponse to water deprivation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin ligase PARAQUAT TOLERANCE 3
  • EC number

Gene names

    • Name
      PQT3
    • ORF names
      dl4740w
      , FCAALL.426
    • Ordered locus names
      At4g17410

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    F4JP52
  • Secondary accessions
    • F4JP50
    • O23583
    • O23584
    • Q0WV36

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Nucleus

Keywords

Phenotypes & Variants

Disruption phenotype

Increased tolerance to paraquat-triggered oxidative stress associated with PRMT13/PRMT4B, APX1 and GPX1 accumulation due to increased histone H3 methylation (H3R17me2a).

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 170 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00004385831-826E3 ubiquitin ligase PARAQUAT TOLERANCE 3
Modified residue278Phosphoserine
Modified residue397Phosphoserine
Modified residue800Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed constitutively in both shoot and root tissues.

Induction

Repressed rapidly by oxidative stress such as paraquat, hydrogen peroxide H2O2, mannitol, drought and cadmium ion CdCl2.

Gene expression databases

Interaction

Subunit

Interacts with PRMT13/PRMT4B in the nucleus.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, zinc finger, region, compositional bias, motif.

TypeIDPosition(s)Description
Domain3-76DWNN
Zinc finger203-216CCHC-type
Zinc finger288-326RING-type; degenerate
Region356-406Disordered
Compositional bias381-406Polar residues
Compositional bias435-459Polar residues
Region435-488Disordered
Region585-826Disordered
Compositional bias587-619Basic and acidic residues
Compositional bias621-638Polar residues
Compositional bias650-666Basic and acidic residues
Motif668-675Nuclear localization signal 1
Compositional bias676-721Basic and acidic residues
Motif695-702Nuclear localization signal 2
Compositional bias722-739Polar residues
Compositional bias767-792Basic and acidic residues
Compositional bias808-826Basic and acidic residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

F4JP52-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    826
  • Mass (Da)
    91,306
  • Last updated
    2011-06-28 v1
  • Checksum
    8561CAD8B8AD0C14
MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA

F4JP52-2

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1P8B518A0A1P8B518_ARATHPQT3708

Sequence caution

The sequence CAB10521.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB10522.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB78743.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB78744.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias381-406Polar residues
Compositional bias435-459Polar residues
Alternative sequenceVSP_058683468in isoform 2
Compositional bias587-619Basic and acidic residues
Compositional bias621-638Polar residues
Compositional bias650-666Basic and acidic residues
Compositional bias676-721Basic and acidic residues
Compositional bias722-739Polar residues
Compositional bias767-792Basic and acidic residues
Sequence conflict776in Ref. 4; BAE99012
Compositional bias808-826Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z97343
EMBL· GenBank· DDBJ
CAB10521.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
Z97343
EMBL· GenBank· DDBJ
CAB10522.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161546
EMBL· GenBank· DDBJ
CAB78743.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161546
EMBL· GenBank· DDBJ
CAB78744.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002687
EMBL· GenBank· DDBJ
AEE83884.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE83885.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE83886.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
ANM66691.1
EMBL· GenBank· DDBJ
Genomic DNA
AK226942
EMBL· GenBank· DDBJ
BAE99012.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp