O49500 · MBR2_ARATH
- ProteinE3 ubiquitin-protein ligase MBR2
- GeneMBR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids666 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Pathway
Protein modification; protein ubiquitination.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | flower development | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein ubiquitination | |
Biological Process | vegetative to reproductive phase transition of meristem |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase MBR2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO49500
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 639 | Unable to promote MED25 degradation; when associated with A-642. | ||||
Sequence: H → A | ||||||
Mutagenesis | 642 | Unable to promote MED25 degradation; when associated with A-639. | ||||
Sequence: H → A |
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.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000429417 | 1-666 | E3 ubiquitin-protein ligase MBR2 | |||
Sequence: MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSSSHVVQNHNWWSFGESSSRLGPSDHLNSNGSKTDRQLLSDGYGFEEGQSGMLLPGESFLRGSSSSHMLSHVNLGKDMDIGSGLQTSGVVIRHNNCETSLGSSSQTAEERSSGPGSSLGGLGSSCKRKALEGAPSHSFPGESHGCFFQTENGAWNEGLAQYDASSSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTGSSSSGDGQPSMIHLPALTRNIHQFAWSASSSSRANSMPEEGLSPWDAPRINSEQPVFTTPANETRNPVQDQFCWSFTRGNPSTSGDSPFVPRAGSSSGIHGLQPNPTWVTPHNQSRISEVAPWSLFPSIESESATHGASLPLLPTGPSVSSNEAAAPSGSSSRSHRSRQRRSGLLLERQNDHLHLRHLGRSLAADNDGRNRLISEIRQVLSAMRRGENLRFEDYMVFDPLIYQGMAEMHDRHRDMRLDVDNMSYEELLALGERIGDVSTGLSEEVILKVMKQHKHTSSAAGSHQDMEPCCVCQEEYAEGDDLGTLGCGHEFHTACVKQWLMLKNLCPICKTVALST |
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-58 | Disordered | ||||
Sequence: MQGPRSTGDSSTGINYADGEPICSTNSETTSNNILNPVDVQFPNNTTGSGRPTYASSS | ||||||
Compositional bias | 73-93 | Polar residues | ||||
Sequence: SSSRLGPSDHLNSNGSKTDRQ | ||||||
Region | 73-95 | Disordered | ||||
Sequence: SSSRLGPSDHLNSNGSKTDRQLL | ||||||
Compositional bias | 155-175 | Polar residues | ||||
Sequence: SLGSSSQTAEERSSGPGSSLG | ||||||
Region | 155-179 | Disordered | ||||
Sequence: SLGSSSQTAEERSSGPGSSLGGLGS | ||||||
Compositional bias | 221-241 | Polar residues | ||||
Sequence: SSLSLSMPSQNSPNVNNQSGL | ||||||
Region | 221-329 | Disordered | ||||
Sequence: SSLSLSMPSQNSPNVNNQSGLPEPRFGLGGGRAVTASAFPSTRSTETISRPGRRLNPGQPPESVAFSFTQSGSSVRQQQQLPATSPFVDPLDARAIPVTGSSSSGDGQP | ||||||
Compositional bias | 257-272 | Polar residues | ||||
Sequence: SAFPSTRSTETISRPG | ||||||
Compositional bias | 282-305 | Polar residues | ||||
Sequence: ESVAFSFTQSGSSVRQQQQLPATS | ||||||
Region | 400-433 | Disordered | ||||
Sequence: NPSTSGDSPFVPRAGSSSGIHGLQPNPTWVTPHN | ||||||
Compositional bias | 418-433 | Polar residues | ||||
Sequence: GIHGLQPNPTWVTPHN | ||||||
Region | 457-491 | Disordered | ||||
Sequence: GASLPLLPTGPSVSSNEAAAPSGSSSRSHRSRQRR | ||||||
Compositional bias | 464-483 | Polar residues | ||||
Sequence: PTGPSVSSNEAAAPSGSSSR | ||||||
Zinc finger | 619-660 | RING-type; atypical | ||||
Sequence: CCVCQEEYAEGDDLGTLGCGHEFHTACVKQWLMLKNLCPICK |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length666
- Mass (Da)71,539
- Last updated1998-06-01 v1
- Checksum6A6794EC7275BFBB
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 73-93 | Polar residues | ||||
Sequence: SSSRLGPSDHLNSNGSKTDRQ | ||||||
Compositional bias | 155-175 | Polar residues | ||||
Sequence: SLGSSSQTAEERSSGPGSSLG | ||||||
Compositional bias | 221-241 | Polar residues | ||||
Sequence: SSLSLSMPSQNSPNVNNQSGL | ||||||
Compositional bias | 257-272 | Polar residues | ||||
Sequence: SAFPSTRSTETISRPG | ||||||
Compositional bias | 282-305 | Polar residues | ||||
Sequence: ESVAFSFTQSGSSVRQQQQLPATS | ||||||
Compositional bias | 418-433 | Polar residues | ||||
Sequence: GIHGLQPNPTWVTPHN | ||||||
Compositional bias | 464-483 | Polar residues | ||||
Sequence: PTGPSVSSNEAAAPSGSSSR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |