Q9ZVH4 · CUL3A_ARATH

Function

function

Component of the cullin-RING ubiquitin ligases (CRL), or CUL3-RBX1-BTB protein E3 ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the CRL complex depends on the BTB domain-containing protein as the substrate recognition component. Involved in embryo pattern formation and endosperm development. Required for the normal division and organization of the root stem cells and columella root cap cells. Regulates primary root growth by an unknown pathway, but in an ethylene-dependent manner. Functions in distal root patterning, by an ethylene-independent mechanism. Functionally redundant with CUL3B.

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 Functionubiquitin protein ligase binding
Biological Processpositive regulation of flower development
Biological Processresponse to red or far red light
Biological Processubiquitin-dependent protein catabolic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Cullin-3A
  • Short names
    AtCUL3a

Gene names

    • Name
      CUL3A
    • Synonyms
      CUL3
    • ORF names
      T24P13.25
      , T2P11.2
    • Ordered locus names
      At1g26830

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
    Q9ZVH4
  • Secondary accessions
    • Q0WL17
    • Q7Y1Y8

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth condition. Reduced sensitivity of the inhibition of hypocotyl growth in far-red light. Cul3a and cul3b double mutant is embryonic lethal (PubMed:16045478).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis48-49Abolishes the interaction with AT1G21780 protein.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, cross-link.

TypeIDPosition(s)Description
ChainPRO_00003968491-732Cullin-3A
Cross-link676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

Post-translational modification

Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

Expressed during flower development in floral meristem, sepals, petals, developing carpels, growing integuments and tetrads of megaspores. In mature ovules, expressed in the cells of the embryo sac. Expressed in the sporogenous cells, tetrads of microspores and mature pollen in stamens After fertilization, expressed in the embryo and endosperm at the globular and heart stages. The progressively decreases during ovule development and is not observed in the developing seed coat.

Gene expression databases

Interaction

Subunit

Interacts with CSN2 and RBX1A. Interacts with BTB/POZ domain-containing proteins BPM1, BPM2, BPM3, BPM6, BT1, BT2, BT3, BT5, AT1G01640, AT1G21780 and AT5G48510 (PubMed:12615944, PubMed:15618422, PubMed:15659098, PubMed:15749712, PubMed:15772280).
Interacts with SR1IP1 (PubMed:24528504).
Interacts with NPR3 and NPR4 (PubMed:22699612).
Binds to NPR1; this interaction requires NPR3 and NPR4 (PubMed:22699612, PubMed:35545668).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the cullin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    85,313
  • Last updated
    1999-05-01 v1
  • Checksum
    40F58A46BB5572ED
MSNQKKRNFQIEAFKHRVVVDPKYADKTWQILERAIHQIYNQDASGLSFEELYRNAYNMVLHKFGEKLYTGFIATMTSHLKEKSKLIEAAQGGSFLEELNKKWNEHNKALEMIRDILMYMDRTYIESTKKTHVHPMGLNLWRDNVVHFTKIHTRLLNTLLDLVQKERIGEVIDRGLMRNVIKMFMDLGESVYQEDFEKPFLDASSEFYKVESQEFIESCDCGDYLKKSEKRLTEEIERVAHYLDAKSEEKITSVVEKEMIANHMQRLVHMENSGLVNMLLNDKYEDLGRMYNLFRRVTNGLVTVRDVMTSHLREMGKQLVTDPEKSKDPVEFVQRLLDERDKYDKIINTAFGNDKTFQNALNSSFEYFINLNARSPEFISLFVDDKLRKGLKGITDVDVEVILDKVMMLFRYLQEKDVFEKYYKQHLAKRLLSGKTVSDDAERSLIVKLKTECGYQFTSKLEGMFTDMKTSEDTMRGFYGSHPELSEGPTLIVQVLTTGSWPTQPAVPCNLPAEVSVLCEKFRSYYLGTHTGRRLSWQTNMGTADIKAIFGKGQKHELNVSTFQMCVLMLFNNSDRLSYKEIEQATEIPAADLKRCLQSLACVKGKNVIKKEPMSKDIGEEDLFVVNDKFTSKFYKVKIGTVVAQKETEPEKQETRQRVEEDRKPQIEAAIVRIMKSRKILDHNNIIAEVTKQLQPRFLANPTEIKKRIESLIERDFLERDSTDRKLYRYLA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict458in Ref. 4; BAF02190

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ319540
EMBL· GenBank· DDBJ
CAC85344.1
EMBL· GenBank· DDBJ
mRNA
AJ344252
EMBL· GenBank· DDBJ
CAC87120.1
EMBL· GenBank· DDBJ
mRNA
AC005508
EMBL· GenBank· DDBJ
AAD14503.1
EMBL· GenBank· DDBJ
Genomic DNA
AC006535
EMBL· GenBank· DDBJ
AAF87034.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE30747.1
EMBL· GenBank· DDBJ
Genomic DNA
AK230392
EMBL· GenBank· DDBJ
BAF02190.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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