Q9C9L0 · CUL3B_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 CUL3A.

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 Functionubiquitin protein ligase binding
Biological Processprotein ubiquitination
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cullin-3B
  • Short names
    AtCUL3b

Gene names

    • Name
      CUL3B
    • ORF names
      T6C23.13
    • Ordered locus names
      At1g69670

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
    Q9C9L0
  • Secondary accessions
    • Q711G4

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

No visible phenotype. Cul3a and cul3b double mutant is embryonic lethal (PubMed:16045478).

Variants

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The viewer provides 49 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.

Type
IDPosition(s)Description
ChainPRO_00003968501-732Cullin-3B
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

Expression

Developmental stage

Expressed in developing and mature reproductive organs and during embryogenesis.

Gene expression databases

Interaction

Subunit

Interacts with BTB/POZ-MATH proteins BPM1 and BPM3.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q9C9L0BPM1 Q8L7653EBI-541687, EBI-540891
BINARY Q9C9L0RBX1A Q940X73EBI-541687, EBI-532404

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain662-724Cullin neddylation

Sequence similarities

Belongs to the cullin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    732
  • Mass (Da)
    85,610
  • Last updated
    2001-06-01 v1
  • Checksum
    83B667E9CE3C7C7D
MSNQKKRNFQIEAFKQRVVVDPKYADKTWKILEHAIHEIYNHNASGLSFEELYRNAYNMVLHKYGDKLYTGLVTTMTFHLKEICKSIEEAQGGAFLELLNRKWNDHNKALQMIRDILMYMDRTYVSTTKKTHVHELGLHLWRDNVVYSSKIQTRLLNTLLDLVHKERTGEVIDRVLMRNVIKMFMDLGESVYQDDFEKPFLEASAEFYKVESMEFIESCDCGEYLKKAEKPLVEEVERVVNYLDAKSEAKITSVVEREMIANHVQRLVHMENSGLVNMLLNDKYEDMGRMYSLFRRVANGLVTVRDVMTLHLREMGKQLVTDPEKSKDPVEFVQRLLDERDKYDRIINMAFNNDKTFQNALNSSFEYFVNLNTRSPEFISLFVDDKLRKGLKGVGEEDVDLILDKVMMLFRYLQEKDVFEKYYKQHLAKRLLSGKTVSDDAERNLIVKLKTECGYQFTSKLEGMFTDMKTSHDTLLGFYNSHPELSEGPTLVVQVLTTGSWPTQPTIQCNLPAEVSVLCEKFRSYYLGTHTGRRLSWQTNMGTADIKAVFGKGQKHELNVSTFQMCVLMLFNNSDRLSYKEIEQATEIPTPDLKRCLQSMACVKGKNVLRKEPMSKEIAEEDWFVVNDRFASKFYKVKIGTVVAQKETEPEKQETRQRVEEDRKPQIEAAIVRIMKSRRVLDHNNIIAEVTKQLQTRFLANPTEIKKRIESLIERDFLERDNTDRKLYRYLA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC013289
EMBL· GenBank· DDBJ
AAG52544.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
AEE34961.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002684
EMBL· GenBank· DDBJ
ANM60547.1
EMBL· GenBank· DDBJ
Genomic DNA
AJ344541
EMBL· GenBank· DDBJ
CAC87839.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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