Q8VY10 · UBC24_ARATH
- ProteinProbable ubiquitin-conjugating enzyme E2 24
- GeneUBC24
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids907 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E2 ubiquitin-protein ligase that mediates E1-dependent protein ubiquitination (PubMed:24474629).
Mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability (PubMed:22634761).
Negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions by facilitating the degradation of PHT1 proteins at the endomembrane (PubMed:22634761, PubMed:24122829).
Functions cooperatively with NLA to regulate the abundance of the inorganic phosphate (Pi) transporters PHT1-1, PHT1-2 and PHT1-3 in different subcellular compartments (PubMed:24122828).
Regulates Pi homeostasis by mediating, cooperatively with NLA, polyubiquitination of PHT1-4 and its targeting for degradation (PubMed:24474629).
Mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability (PubMed:22634761).
Negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions by facilitating the degradation of PHT1 proteins at the endomembrane (PubMed:22634761, PubMed:24122829).
Functions cooperatively with NLA to regulate the abundance of the inorganic phosphate (Pi) transporters PHT1-1, PHT1-2 and PHT1-3 in different subcellular compartments (PubMed:24122828).
Regulates Pi homeostasis by mediating, cooperatively with NLA, polyubiquitination of PHT1-4 and its targeting for degradation (PubMed:24474629).
Miscellaneous
MicroRNA399 (miR399) can be sequestered by IPS1, a non-protein coding RNA containing a motif with sequence complementarity to miR399, but with a mismatched loop at the expected miRNA cleavage site. Thus IPS1 mimics the target of miR399 to block the cleavage of UBC24/PHO2 under Pi-deficient conditions.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 748 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | ATP binding | |
Molecular Function | ligase activity | |
Molecular Function | ubiquitin conjugating enzyme activity | |
Biological Process | cellular response to phosphate starvation | |
Biological Process | phosphate ion homeostasis | |
Biological Process | phosphate ion transport | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of phosphate transmembrane transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable ubiquitin-conjugating enzyme E2 24
- 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 accessionQ8VY10
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Plants are unable to regulate the amount of phosphate accumulated into shoots.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 748 | Loss of ubiquitin conjugase activity and loss of down-regulation of PHO1. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 95 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_0000344361 | 1-907 | Probable ubiquitin-conjugating enzyme E2 24 | |||
Sequence: MEMSLTDSDWDSSSDSGSSEHEEVEFSYGGRAQNIFSNLEETIGKIDEFLSFERGFMYGDIVRSATEPSGQSGRVINIDMFVNLESTHGKIMKEVDTKRLQKLRSISLSDYVINGPWVGRVDKIVERVSVTLDDGTNYEVLVDGQDKLVAIPPNLLEDSQYSYYPGQRVQVKLAHAPRSTTWLCGTWRGTQVMGTVCTVEAGLVYVDWVASIVMEGDRNLTAPQALQNPESLTLLPCVSHASWQLGDWCILPGSSHCDIAERQTPNVAAYNLNECHKTFQKGFNRNMQNSGLDELFVITKTKMKVAVMWQDGSCSLGVDSQQLLPVGAVNAHDFWPEQFVVEKETCNSKKWGVVKAVNAKEQTVKVQWTIQVEKEATGCVDEVMEEIVSAYELLEHPDFGFCFSDVVVKLLPEGKFDPNADTIVATEAKHLLTESDYSGAYFLSSIGVVTGFKNGSVKVKWANGSTSKVAPCEIWKMERSEYSNSSTVSSEGSVQDLSQKISQSDEASSNHQETGLVKLYSVGESCNENIPECSSFFLPKAAIGFITNLASSLFGYQGSTSVISSHSRCNDSEDQSDSEVLVQETAESYDNSETNSGEVDMTTTMVNIPIEGKGINKTLDSTLLENSRNQVRFRQFDMVNDCSDHHFLSSDKGLAQSQVTKSWVKKVQQEWSNLEANLPNTIYVRVCEERMDLLRAALVGAPGTPYHDGLFFFDIMLPPQYPHEPPMVHYHSGGMRLNPNLYESGRVCLSLLNTWSGSGTEVWNAGSSSILQLLLSFQALVLNEKPYFNEAGYDKQLGRAEGEKNSVSYNENAFLITCKSMISMLRKPPKHFEMLVKDHFTHRAQHVLAACKAYMEGVPVGSSANLQGNSTTNSTGFKIMLSKLYPKLLEAFSEIGVDCVQEIGPES |
Proteomic databases
Expression
Tissue specificity
Expressed in the vascular tissues of cotyledons, leaves, roots, sepals, filaments, anthers and junctions between the inflorescence stems and siliques.
Induction
Down-regulated by phosphate deprivation (PubMed:16679424).
Systemically regulated by microRNA399 (miR399) (PubMed:16679424, PubMed:18390805).
Systemically regulated by microRNA399 (miR399) (PubMed:16679424, PubMed:18390805).
Developmental stage
Up-regulated in senescing leaves and maturating seeds.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MEMSLTDSDWDSSSDSGSSEHEE | ||||||
Region | 485-509 | Disordered | ||||
Sequence: SSTVSSEGSVQDLSQKISQSDEASS | ||||||
Domain | 662-822 | UBC core | ||||
Sequence: SWVKKVQQEWSNLEANLPNTIYVRVCEERMDLLRAALVGAPGTPYHDGLFFFDIMLPPQYPHEPPMVHYHSGGMRLNPNLYESGRVCLSLLNTWSGSGTEVWNAGSSSILQLLLSFQALVLNEKPYFNEAGYDKQLGRAEGEKNSVSYNENAFLITCKSMI |
Sequence similarities
Belongs to the ubiquitin-conjugating enzyme family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q8VY10-1
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
- Length907
- Mass (Da)100,484
- Last updated2002-03-01 v1
- Checksum6C9CB1D8A3A95359
Q8VY10-2
- Name2
- Differences from canonical
- 1-476: Missing
Sequence caution
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034751 | 1-476 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ027037 EMBL· GenBank· DDBJ | AAY44863.1 EMBL· GenBank· DDBJ | mRNA | ||
U78721 EMBL· GenBank· DDBJ | AAC69130.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002685 EMBL· GenBank· DDBJ | AEC08882.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY074292 EMBL· GenBank· DDBJ | AAL66989.1 EMBL· GenBank· DDBJ | mRNA | ||
AY091326 EMBL· GenBank· DDBJ | AAM14265.1 EMBL· GenBank· DDBJ | mRNA | ||
AK229934 EMBL· GenBank· DDBJ | BAF01760.1 EMBL· GenBank· DDBJ | mRNA | ||
AK230162 EMBL· GenBank· DDBJ | BAF01971.1 EMBL· GenBank· DDBJ | mRNA |