A0A5P1EML2 · A0A5P1EML2_ASPOF

Function

function

Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.

Catalytic activity

  • [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine.
    EC:2.3.2.31 (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 Componentcytoplasm
Cellular Componentubiquitin ligase complex
Molecular Functionnucleic acid binding
Molecular FunctionRNA-DNA hybrid ribonuclease activity
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processprotein polyubiquitination
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RBR-type E3 ubiquitin transferase
  • EC number

Gene names

    • ORF names
      A4U43_C06F1010

Organism names

  • Taxonomic identifier
  • Strain
    • cv. DH0086
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Asparagaceae > Asparagoideae > Asparagus

Accessions

  • Primary accession
    A0A5P1EML2

Proteomes

Genome annotation databases

Subcellular Location

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-60Disordered
Compositional bias12-56Acidic residues
Domain203-422RING-type
Domain207-255RING-type

Sequence similarities

Belongs to the RBR family. Ariadne subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    526
  • Mass (Da)
    59,101
  • Last updated
    2020-02-26 v1
  • Checksum
    50B44DF8899575A5
MGSHHDDVEEEFRSCCEDEEWQDTEECLAELLSSDEEVEEDADDDDDDDGASSGESEDEDGVSLRVFFKGVSVSEGGGGLGAKASGIGVVMETSGGDSVFKVQKKLDFFVDVLVAEHLALLDGLIEAQRNGVQRIVALTDNEEVYHQIAEAVPHEDQLLVALGYRILELSNDFEAFVLKLVCRSELVRPLKLAREAVGILDASINQCLVCCCEEKQQSQIIKLKCSHSFCLNCMIVHVEGKLQALQVPIKCPQVRCKYHISKNAFKSFLPISCYQSLERATMEAKVLNLDRVYCPFPDCSVLFSPGQHSASRASSSNQYEINCVECQECCRLLCSSCGVPWHSSMSCEEYQSLSVEERDAGDANLLRLAQNNNWRRCQQCRRMVELTQGCFRVTCWCGHEFCYSCSAGYHSGTQTCQCTFWGDEQESSEPSTPSNHEADQWRWEPFDPLPSITDNYSEQERAQLALIQRFLAGGFGINDDHHHNQIQSPPRCSDSYLDAIKDLNQLPWLERFVSVISDSYHEDYIQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias12-56Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM007386
EMBL· GenBank· DDBJ
ONK65791.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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