A0A1P8AXV0 · A0A1P8AXV0_ARATH

Function

function

Functions as an E3 ubiquitin ligase.

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

1787100200300400500600700
TypeIDPosition(s)Description
Binding site455ATP (UniProtKB | ChEBI)

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
Molecular FunctionATP binding
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionubiquitin-protein transferase activity
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      F27F23.21
      , F27F23_21
    • Ordered locus names
      At2g19410

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
    A0A1P8AXV0

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Proteomic databases

Expression

Gene expression databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region191-295Disordered
Compositional bias193-208Polar residues
Compositional bias224-240Polar residues
Compositional bias256-272Polar residues
Compositional bias273-295Basic and acidic residues
Domain428-691Protein kinase
Domain710-783U-box

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    787
  • Mass (Da)
    89,225
  • Last updated
    2017-04-12 v1
  • Checksum
    7106F1A8833122D1
MVVMLTQEMSGGGGPKAEEGQLFVAVAVKGLIGDKLGGAGSRRAVRWAVDNLLPKADKFVMIHVIPTITSIPTPTGDRLPVEEVEESVVEMYVRDVKKEYETVFVPFLKMCKSTRSTKRYFRSRRTKGTGVPLTVLRYAPETCEVYIVCKDRITTKSMDPLINREPCTSPHAAATAHDFLRDWAASFHTLRSPTLPDPRQSTEAGTRRSASARELRFEALSLTCNKPKTPQSSKASSATTPEIFRRRRGSDIPQLNYSDFDKTCTKPQSNVENIVSEHRDSDRSPPETSRKSKKVEIEEEVERLKNELQSTVFKYKQACEELFSTQNKVKMLSTEYLNESKRVNNAVEKEELQRNTAALEKERYMKAVKEVETAKALLAREFCQRQIAEVNALRTYLEKKKVIDQLLGTDHRYRKYTIEEIVTATEGFSPEKVIGEGGYGKVYQCSLDSTPAAVKVVRLDTPEKKQEFLKEVEVLSQLRHPHVVLLLGACPENGCLVYEYLENGSLEEYIFHRKNKPPLPWFIRFRVIFEVACGLAFLHSSKPEPIVHRDLKPGNILLNRNYVSKIADVGLAKLVTDVAPDNVTMYRNSVLAGTLHYIDPEYHRTGTIRPKSDLYAFGIIILQLLTARNPSGIVPAVENAVKKGTLTEMLDKSVTDWPLAETEELARIGLKCAEFRCRDRPDLKSEVIPVLKRLVETANSKVKKEGSNLRAPSHYFCPILREIMEEPEIAADGFTYERKAILAWLEKHNISPVTRQKLDHFKLTPNHTLRSAIRDWKSRVRFSNVVV

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q8S8S7PUB34_ARATHPUB34801
A0A1P8AY00A0A1P8AY00_ARATHAt2g19410822

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias193-208Polar residues
Compositional bias224-240Polar residues
Compositional bias256-272Polar residues
Compositional bias273-295Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002685
EMBL· GenBank· DDBJ
ANM61488.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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