Q9LYW5 · LUL1_ARATH

Function

function

Acts 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 (in vitro).

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
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable E3 ubiquitin-protein ligase LUL1
  • EC number
  • Alternative names
    • Probable RING-type E3 ubiquitin transferase LUL1
    • Protein LOG2-LIKE UBIQUITIN LIGASE 1
    • RING finger protein 370

Gene names

    • Name
      LUL1
    • Synonyms
      RF370
    • ORF names
      F15A17_230, MOK16.11
    • Ordered locus names
      At5g03200

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
    Q9LYW5
  • Secondary accessions
    • Q8GZ27
    • Q8L8P7

Proteomes

Organism-specific databases

Genome annotation databases

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain.

TypeIDPosition(s)Description
Initiator methionine1Removed
Lipidation2N-myristoyl glycine
ChainPRO_00004199472-337Probable E3 ubiquitin-protein ligase LUL1

Post-translational modification

Myristoylated (in vitro).

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, zinc finger.

TypeIDPosition(s)Description
Region139-255DAR2 domain
Zinc finger285-324RING-type; atypical

Domain

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    337
  • Mass (Da)
    37,720
  • Last updated
    2000-10-01 v1
  • Checksum
    FF353C1900702147
MGNLISLIFCCGRRQRSNIPPAMETAPLELPPNRFVFAAVPPYLNPNPNYVDQYPGNCLPPPVTEPPMLPYNFNHLHHYPPNSYQLPHPLFHGGRYPILPPPTYVHQKAVTIRNDVNLKKKTLTLIPDPENPNRLLVSFTFDASMPGRITVVFFATEDAECNLRATKEDTLPPITFDFGEGLGQKFIQSSGTGIDLTAFKDSELFKEVDTDVFPLAVKAEATPAEEGKSGSTNVQITQVVYTKEKGEIKIEVVKQILWVNKRRYELLEIYGIENTVDGSDEGKECVVCLSEPRDTTVLPCRHMCMCSGCAKALRFQTNLCPVCRQPVEMLLEINKNG

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict29in Ref. 4; BAC41920
Sequence conflict40in Ref. 6; AAM67190
Sequence conflict106in Ref. 4; BAC41920

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB005240
EMBL· GenBank· DDBJ
BAB08380.1
EMBL· GenBank· DDBJ
Genomic DNA
AL163002
EMBL· GenBank· DDBJ
CAB86087.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002688
EMBL· GenBank· DDBJ
AED90569.1
EMBL· GenBank· DDBJ
Genomic DNA
AK117244
EMBL· GenBank· DDBJ
BAC41920.1
EMBL· GenBank· DDBJ
mRNA
BT025883
EMBL· GenBank· DDBJ
ABF85785.1
EMBL· GenBank· DDBJ
mRNA
AY088884
EMBL· GenBank· DDBJ
AAM67190.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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