B6TI40 · B6TI40_MAIZE

  • Protein
    E3 ubiquitin-protein ligase RMA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea

Accessions

  • Primary accession
    B6TI40

Subcellular Location

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

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane227-246Helical

Keywords

Expression

Gene expression databases

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-42Disordered
Domain49-90RING-type
Region103-145Disordered
Compositional bias125-139Polar residues

Domain

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    247
  • Mass (Da)
    26,083
  • Last updated
    2008-12-16 v1
  • Checksum
    EB8E20839276A45D
MSGGNAWSPLPSHGFESDSGGMGSRAGEPVARTNSGGGSSSKDSGSFECNICLDLAQDPVVTLCGHLFCWPCLYEWLHVHAHSQECPVCKAVVEEGKLVPLYGRGGNSTSPRARSVAGVEIPSRPTGQRPSTAPQPDHSNHYPPQNPWFMGAGAPPVAGGRWGNYTFSAAIGGLFPLLSFQVHVFPQVSAYGPAAGFPYGYGHSFHGWHGHGYGFPRQAPQGQQVDAYLKVLLLVVGVLVIASLIAF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias125-139Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU964655
EMBL· GenBank· DDBJ
ACG36773.1
EMBL· GenBank· DDBJ
mRNA

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