O49500 · MBR2_ARATH

Function

function

E3 ubiquitin-protein ligase that functions as a regulator of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent way. Proteasome-dependent degradation of MED25 seems to activate its function as positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT and consequently to promote flowering. May function downstream of HAL3 and be required for HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth.

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
Biological Processflower development
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein ubiquitination
Biological Processvegetative to reproductive phase transition of meristem

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase MBR2
  • EC number
  • Alternative names
    • HAL3-interacting protein 1 homolog (AtHIP1)
    • MED25-binding RING-H2 protein 2
    • RING-H2 finger MBR2
    • RING-type E3 ubiquitin transferase MBR2

Gene names

    • Name
      MBR2
    • Synonyms
      HIP1
    • Ordered locus names
      At4g34040

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
    O49500

Proteomes

Organism-specific databases

Genome annotation databases

Phenotypes & Variants

Disruption phenotype

No visible phenotype under normal growth conditions, but the double mutant plants mbr1-1 and mbr2-1 show delayed flowering.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis639Unable to promote MED25 degradation; when associated with A-642.
Mutagenesis642Unable to promote MED25 degradation; when associated with A-639.

Variants

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

The viewer provides 62 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004294171-666E3 ubiquitin-protein ligase MBR2

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with MED25 and UBC11.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Region1-58Disordered
Compositional bias73-93Polar residues
Region73-95Disordered
Compositional bias155-175Polar residues
Region155-179Disordered
Compositional bias221-241Polar residues
Region221-329Disordered
Compositional bias257-272Polar residues
Compositional bias282-305Polar residues
Region400-433Disordered
Compositional bias418-433Polar residues
Region457-491Disordered
Compositional bias464-483Polar residues
Zinc finger619-660RING-type; atypical

Domain

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

Sequence similarities

Belongs to the RING-type zinc finger family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    666
  • Mass (Da)
    71,539
  • Last updated
    1998-06-01 v1
  • Checksum
    6A6794EC7275BFBB
MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTGSSSSGDGQPSMIHLPALTRNIHQFAWSASSSSRANSMPEEGLSPWDAPRINSEQPVFTTPANETRNPVQDQFCWSFTRGNPSTSGDSPFVPRAGSSSGIHGLQPNPTWVTPHNQSRISEVAPWSLFPSIESESATHGASLPLLPTGPSVSSNEAAAPSGSSSRSHRSRQRRSGLLLERQNDHLHLRHLGRSLAADNDGRNRLISEIRQVLSAMRRGENLRFEDYMVFDPLIYQGMAEMHDRHRDMRLDVDNMSYEELLALGERIGDVSTGLSEEVILKVMKQHKHTSSAAGSHQDMEPCCVCQEEYAEGDDLGTLGCGHEFHTACVKQWLMLKNLCPICKTVALST

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias73-93Polar residues
Compositional bias155-175Polar residues
Compositional bias221-241Polar residues
Compositional bias257-272Polar residues
Compositional bias282-305Polar residues
Compositional bias418-433Polar residues
Compositional bias464-483Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL021961
EMBL· GenBank· DDBJ
CAA17568.1
EMBL· GenBank· DDBJ
Genomic DNA
AL161584
EMBL· GenBank· DDBJ
CAB80121.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE86313.1
EMBL· GenBank· DDBJ
Genomic DNA
BT015366
EMBL· GenBank· DDBJ
AAU05489.1
EMBL· GenBank· DDBJ
mRNA
BT020341
EMBL· GenBank· DDBJ
AAV85696.1
EMBL· GenBank· DDBJ
mRNA
AK229265
EMBL· GenBank· DDBJ
BAF01129.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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