Q9M9Y4 · DRIP1_ARATH
- ProteinE3 ubiquitin protein ligase DRIP1
- GeneDRIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids421 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that acts as a negative regulator of the response to water stress. Mediates ubiquitination and subsequent proteasomal degradation of the drought-induced transcriptional activator DREB2A. Functionally redundant with DRIP2.
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 | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | protein autoubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | response to water deprivation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin protein ligase DRIP1
- 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 accessionQ9M9Y4
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype. Drip1 and drip2 double mutant shows delayed growth and development, but increased tolerance to drought stress, compared to wild-type.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 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_0000397042 | 1-421 | E3 ubiquitin protein ligase DRIP1 | |||
Sequence: MMIKVKKETMRACLSCSICDNILRDATTISECLHTFCRKCIYEKITEDEIETCPVCNIDLGSTPLEKLRPDHNLQDLRAKIFALKRRKVKAPGIVSLPGKRKERSISSLVVSTPMVSAQAGTTRRRTKAPTRKELRNGSLAERTVKKEESSGDELLESTSSPDTLNKFTQNKRQSKKSCKESISNKENKDGDEPWDSKMDWKPLNFLVEVANGTKPLKSSASQGSGSKSEHANVSRNQFQGSKTKTKNKKRKCKREDDKSNNGDPTTSETVTPKRMRTTQRKRSATTLGDSRNLPQPDESSAKQERRNGPVWFSLVASNDQEGGTSLPQIPANFLRIRDGNTTVSFIQKYLMRKLDLESENEIEIKCMGEAVIPTLTLYNLVDLWLQKSSNHQRFAALVGSSAKDFTMVLVYARKLPECNM |
Post-translational modification
Autoubiquitinated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with DREB2A.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9M9Y4 | DREB2A O82132 | 4 | EBI-1786858, EBI-1786840 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for zinc finger, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 16-57 | RING-type | ||||
Sequence: CSICDNILRDATTISECLHTFCRKCIYEKITEDEIETCPVCN | ||||||
Compositional bias | 106-125 | Polar residues | ||||
Sequence: ISSLVVSTPMVSAQAGTTRR | ||||||
Region | 106-198 | Disordered | ||||
Sequence: ISSLVVSTPMVSAQAGTTRRRTKAPTRKELRNGSLAERTVKKEESSGDELLESTSSPDTLNKFTQNKRQSKKSCKESISNKENKDGDEPWDSK | ||||||
Compositional bias | 132-154 | Basic and acidic residues | ||||
Sequence: RKELRNGSLAERTVKKEESSGDE | ||||||
Compositional bias | 155-172 | Polar residues | ||||
Sequence: LLESTSSPDTLNKFTQNK | ||||||
Compositional bias | 174-198 | Basic and acidic residues | ||||
Sequence: QSKKSCKESISNKENKDGDEPWDSK | ||||||
Compositional bias | 216-242 | Polar residues | ||||
Sequence: PLKSSASQGSGSKSEHANVSRNQFQGS | ||||||
Region | 216-307 | Disordered | ||||
Sequence: PLKSSASQGSGSKSEHANVSRNQFQGSKTKTKNKKRKCKREDDKSNNGDPTTSETVTPKRMRTTQRKRSATTLGDSRNLPQPDESSAKQERR | ||||||
Compositional bias | 282-298 | Polar residues | ||||
Sequence: KRSATTLGDSRNLPQPD |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9M9Y4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length421
- Mass (Da)47,328
- Last updated2010-08-10 v2
- Checksum56F7D797DE944567
Q9M9Y4-2
- Name2
- Differences from canonical
- 1-114: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8ARB2 | A0A1P8ARB2_ARATH | DRIP1 | 399 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039633 | 1-114 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 106-125 | Polar residues | ||||
Sequence: ISSLVVSTPMVSAQAGTTRR | ||||||
Compositional bias | 132-154 | Basic and acidic residues | ||||
Sequence: RKELRNGSLAERTVKKEESSGDE | ||||||
Compositional bias | 155-172 | Polar residues | ||||
Sequence: LLESTSSPDTLNKFTQNK | ||||||
Compositional bias | 174-198 | Basic and acidic residues | ||||
Sequence: QSKKSCKESISNKENKDGDEPWDSK | ||||||
Compositional bias | 216-242 | Polar residues | ||||
Sequence: PLKSSASQGSGSKSEHANVSRNQFQGS | ||||||
Compositional bias | 282-298 | Polar residues | ||||
Sequence: KRSATTLGDSRNLPQPD |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC011001 EMBL· GenBank· DDBJ | AAF63142.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE28033.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE28034.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX815334 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BT033132 EMBL· GenBank· DDBJ | ACF28393.1 EMBL· GenBank· DDBJ | mRNA |