A0A2K1ICR0 · A0A2K1ICR0_PHYPA

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)

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 Componentcytoplasm
Cellular Componentubiquitin ligase complex
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
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
      PHYPA_030542

Organism names

Accessions

  • Primary accession
    A0A2K1ICR0

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-29Disordered
Compositional bias9-29Acidic residues
Domain131-345RING-type
Domain135-183RING-type
Region594-638Disordered

Sequence similarities

Belongs to the RBR family. Ariadne subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    758
  • Mass (Da)
    84,938
  • Last updated
    2018-03-28 v1
  • Checksum
    97545AD8D95A8FA3
MGDDGIDYGNDHEDTESEEDYVGDDGACAGYDDYVGDDEEVLTNQEPADTSHKVITRESLLAAQKDDIRKVVEVLALRPRQARTLLIHYRWNLENLFGAIAEKGYGPVFLEAGLPPPETEVVVPVADDASVSVRCGTCLEDVPTTTATRMDCGHAFCNECWTQYFIIKIKDGQSRRVTCMEHNCGAICDEDKVRDLVGLQDPESVQRYERFLLESYIEDNAKVKWCPSTPHCGNAIRLEGEPFCEIECKCGQQFCFNCMAEPHSPCSCNMWTLWDKKCKDESETVNWLTVHTKPCPKCHKPVEKNGGCNLVSCICGQAFCWLCGAATGREHNWNSIEGHSCGRFQDEKEKEAARAQRDLKRYIHYHSRWKGHLDSLKLEQKQEETVKEKITTLEASHCQVKDYSWLTIGLQRLFRARRALSYSFAFAYFMFGNDLFKDDISEEQNAINQNLFEDQQQKLEETVERLSKLVKVVETPLEENTDDSYMQDIRLQVINFTTLTDGLCRRMYEVIENDLLGSLQLATHHIAPYKTGGAERASEIAAEPERFHIDRTQDIKSESRSKTDCLSIANVAAEHADGDIGGKQVKLEVEVSGDVDMSETPSADRVHKRPNLYPSSPRSCKRFGKEPSVSGPSVVREPGKTFGSISEIVINSDAALDSVPSSSYSTTLWEGIALGSKDVSGQQRLNPAEKLHWENATLSASPTGETDGQDELLQQQSDSTEWQFGALNAQPAVSTCSSDFDSQGGIIQMNINRPWNDG

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7I4CUL2A0A7I4CUL2_PHYPA625

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-29Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ABEU02000026
EMBL· GenBank· DDBJ
PNR27061.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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