A0A397Y6R8 · A0A397Y6R8_BRACM

Function

function

E3 ubiquitin-protein ligase.

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)

Pathway

Protein modification; protein ubiquitination.

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 Componentendoplasmic reticulum membrane
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase RMA
  • EC number
  • Alternative names
    • Protein RING membrane-anchor
    • RING-type E3 ubiquitin transferase RMA

Gene names

    • ORF names
      BRARA_I04008

Organism names

  • Taxonomic identifier
  • Strain
    • cv. B-3
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica

Accessions

  • Primary accession
    A0A397Y6R8

Proteomes

Subcellular Location

Endomembrane system
Endoplasmic reticulum membrane
; Single-pass type IV membrane protein

Keywords

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region107-127Disordered
Domain139-179RING-type
Region405-437Disordered
Compositional bias415-437Basic and acidic residues

Domain

The RING-type zinc finger domain is responsible for E3 ligase activity.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    437
  • Mass (Da)
    48,681
  • Last updated
    2018-12-05 v1
  • Checksum
    7359130ED925D59F
MGEELSDTMNLDLNLGPGPESDLQLVSNETVNLADWTNNNPSERSSEAVTRIRTRHRTRFRQLNLPIPVLSETHAMDIELNQLMGSGAALQTGEGSERGNEDLKMCENNGGEAVGDGVSEKKGDVEKTSGGGDGNFFDCNICLDLSKEPVLTCCGHLYCWPCLFQWLNISDAKECPVCKGEVTAKTVTPIYGRGNHKREVEESLDTKIPMRPHAKRIESLRNTIQRSPFTIPMEEMIRRIQSRFERDSTPVPDFSNREASERVNDRANSILNRLMTSRGVRSEQNQASAVAATASENINLNPNIAAADLEGETTTRFHPLLIRRQLQSHRVARISNFTSALSSAERLVDAYFRTHPLGRNHNHQELNHHSPVVVDDRDSFSSIAAVINSESQVDTAVEIDSMVTLSTSSSRRRNENGSRVSDVDSADSRPPRRRRFT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias415-437Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM010636
EMBL· GenBank· DDBJ
RID47414.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
Help