F4JP52 · PQT3_ARATH
- ProteinE3 ubiquitin ligase PARAQUAT TOLERANCE 3
- GenePQT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids826 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-like protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to paraquat | |
Biological Process | negative regulation of response to oxidative stress | |
Biological Process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | |
Biological Process | positive regulation of response to oxidative stress | |
Biological Process | protein ubiquitination | |
Biological Process | response to cadmium ion | |
Biological Process | response to hydrogen peroxide | |
Biological Process | response to mannitol | |
Biological Process | response to oxidative stress | |
Biological Process | response to paraquat | |
Biological Process | response to salt stress | |
Biological Process | response to water deprivation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin ligase PARAQUAT TOLERANCE 3
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionF4JP52
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438583 | 1-826 | E3 ubiquitin ligase PARAQUAT TOLERANCE 3 | |||
Sequence: MAIYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVPGRPRIRIITREEPRVEDKVENVQADMNNVITADASPVEDEFDEFGNDLYSIPDAPAVHSNNLCHDSAPADDEETKLKALIDTPALDWHQQGADSFGPGRGYGRGMAGRMGGRGFGMERTTPPPGYVCHRCNVSGHFIQHCSTNGNPNFDVKRVKPPTGIPKSMLMATPNGSYSLPSGAVAVLKPNEDAFEKEMEGLTSTTRSVGEFPPELKCPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVCGATHVLADDLLPNKTLRDTINRILESGNSSAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLKPSIEIAEITSAWASAEIVKVEKPVDASANIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDYMMPMGPGPGNQYFNGFQPGFNGVQHGFNGVQPGFNGFHHGFNGFPGPFPGAMPPFVGYGFGGVIHPDPFAAQGFGFPNIPPPYRDLAEMGNRMNLQHPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA | ||||||
Modified residue | 278 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 397 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 800 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for domain, zinc finger, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-76 | DWNN | ||||
Sequence: IYYKFKSARDYDTISMDGPFITVGLLKEKIYETKHLGSGKDLDIVISNAQTNEEYLDEAMLIPKNTSVLIRRVP | ||||||
Zinc finger | 203-216 | CCHC-type | ||||
Sequence: CHRCNVSGHFIQHC | ||||||
Zinc finger | 288-326 | RING-type; degenerate | ||||
Sequence: CPLCKEVMRDAALASKCCLKSYCDKCIRDHIIAKSMCVC | ||||||
Region | 356-406 | Disordered | ||||
Sequence: SAENAGSMCQVQDMESVRCPPPKALSPTTSAASGGEKKPAPSNNNETSTLK | ||||||
Compositional bias | 381-406 | Polar residues | ||||
Sequence: SPTTSAASGGEKKPAPSNNNETSTLK | ||||||
Compositional bias | 435-459 | Polar residues | ||||
Sequence: NIQGSSNGKEAAVSQLNTQPPKEEM | ||||||
Region | 435-488 | Disordered | ||||
Sequence: NIQGSSNGKEAAVSQLNTQPPKEEMPQQVASGEQGKRKKKKPRMSGTDLAGPDY | ||||||
Region | 585-826 | Disordered | ||||
Sequence: HPIMGREEFEAKKTEMKRKRENEIRRSEGGNVVRDSEKSRIMNNSAVTSSPVKPKSRQGPPPPISSDYDRRRRSDRSSPERQSSRRFTSPPRSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTVEIDDNNKSNVFTRISFPEESSGKQRKTSKSSPAPPESSVAPVSSGRRHHSRREREMVEYDSSDDEDRHFKRKPSRYKRSPSVAPSDAGDEHFRHSKRSKGERARA | ||||||
Compositional bias | 587-619 | Basic and acidic residues | ||||
Sequence: IMGREEFEAKKTEMKRKRENEIRRSEGGNVVRD | ||||||
Compositional bias | 621-638 | Polar residues | ||||
Sequence: EKSRIMNNSAVTSSPVKP | ||||||
Compositional bias | 650-666 | Basic and acidic residues | ||||
Sequence: SDYDRRRRSDRSSPERQ | ||||||
Motif | 668-675 | Nuclear localization signal 1 | ||||
Sequence: SRRFTSPP | ||||||
Compositional bias | 676-721 | Basic and acidic residues | ||||
Sequence: RSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTV | ||||||
Motif | 695-702 | Nuclear localization signal 2 | ||||
Sequence: DRRRDRPR | ||||||
Compositional bias | 722-739 | Polar residues | ||||
Sequence: EIDDNNKSNVFTRISFPE | ||||||
Compositional bias | 767-792 | Basic and acidic residues | ||||
Sequence: RRHHSRREREMVEYDSSDDEDRHFKR | ||||||
Compositional bias | 808-826 | Basic and acidic residues | ||||
Sequence: AGDEHFRHSKRSKGERARA |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- Name1
- Length826
- Mass (Da)91,306
- Last updated2011-06-28 v1
- Checksum8561CAD8B8AD0C14
F4JP52-2
- Name2
- Differences from canonical
- 468-468: Q → QA
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8B518 | A0A1P8B518_ARATH | PQT3 | 708 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 381-406 | Polar residues | ||||
Sequence: SPTTSAASGGEKKPAPSNNNETSTLK | ||||||
Compositional bias | 435-459 | Polar residues | ||||
Sequence: NIQGSSNGKEAAVSQLNTQPPKEEM | ||||||
Alternative sequence | VSP_058683 | 468 | in isoform 2 | |||
Sequence: Q → QA | ||||||
Compositional bias | 587-619 | Basic and acidic residues | ||||
Sequence: IMGREEFEAKKTEMKRKRENEIRRSEGGNVVRD | ||||||
Compositional bias | 621-638 | Polar residues | ||||
Sequence: EKSRIMNNSAVTSSPVKP | ||||||
Compositional bias | 650-666 | Basic and acidic residues | ||||
Sequence: SDYDRRRRSDRSSPERQ | ||||||
Compositional bias | 676-721 | Basic and acidic residues | ||||
Sequence: RSSSRKSERDRHHDLDSEHDRRRDRPRETDRKHRKRSEKSSSDPTV | ||||||
Compositional bias | 722-739 | Polar residues | ||||
Sequence: EIDDNNKSNVFTRISFPE | ||||||
Compositional bias | 767-792 | Basic and acidic residues | ||||
Sequence: RRHHSRREREMVEYDSSDDEDRHFKR | ||||||
Sequence conflict | 776 | in Ref. 4; BAE99012 | ||||
Sequence: E → G | ||||||
Compositional bias | 808-826 | Basic and acidic residues | ||||
Sequence: AGDEHFRHSKRSKGERARA |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |