P40492 · FYV10_YEAST
- ProteinProtein FYV10
- GeneFYV10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids516 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium (PubMed:12686616, PubMed:22044534).
Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616, PubMed:22044534).
May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin (PubMed:12663529).
Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616, PubMed:22044534).
May catalyze ubiquitination of target proteins in complex with RMD5 (Probable). Required for survival upon exposure to K1 killer toxin (PubMed:12663529).
Miscellaneous
Present with 784 molecules/cell in log phase SD medium.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 434 | Essential for ubiquitin ligase activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | GID complex | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of gluconeogenesis | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein FYV10
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP40492
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 434 | Abolishes FBP1 ubiquitination and degradation. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 12 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_0000202970 | 1-516 | Protein FYV10 | |||
Sequence: MAEKSIFNEPDVDFHLKLNQQLFHIPYELLSKRIKHTQAVINKETKSLHEHTAALNQIFEHNDVEHDELALAKITEMIRKVDHIERFLNTQIKSYCQILNRIKKRLEFFHELKDIKSQNSGTSHNGNNEGTRTKLIQWYQSYTNILIGDYLTRNNPIKYNSETKDHWNSGVVFLKQSQLDDLIDYDVLLEANRISTSLLHERNLLPLISWINENKKTLTKKSSILEFQARLQEYIELLKVDNYTDAIVCFQRFLLPFVKSNFTDLKLASGLLIFIKYCNDQKPTSSTSSGFDTEEIKSQSLPMKKDRIFQHFFHKSLPRITSKPAVNTTDYDKSSLINLQSGDFERYLNLLDDQRWSVLNDLFLSDFYSMYGISQNDPLLIYLSLGISSLKTRDCLHPSDDENGNQETETATTAEKEVEDLQLFTLHSLKRKNCPVCSETFKPITQALPFAHHIQSQLFENPILLPNGNVYDSKKLKKLAKTLKKQNLISLNPGQIMDPVDMKIFCESDSIKMYPT |
Proteomic databases
PTM databases
Interaction
Subunit
Identified in the GID complex. In the absence of glucose, the complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2, VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to glucose-containing medium, VID24/GID4 is induced and becomes part of the complex (PubMed:22645139).
Interacts with RMD5/GID2; the interaction is direct (PubMed:22044534).
Within the GID complex, interacts directly with VID28/GID5, GID8 and RMD5/GID2 (PubMed:22645139).
Interacts with RMD5/GID2; the interaction is direct (PubMed:22044534).
Within the GID complex, interacts directly with VID28/GID5, GID8 and RMD5/GID2 (PubMed:22645139).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P40492 | RMD5 Q12508 | 2 | EBI-25137, EBI-38868 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 187-245 | CTLH | ||||
Sequence: VLLEANRISTSLLHERNLLPLISWINENKKTLTKKSSILEFQARLQEYIELLKVDNYTD | ||||||
Zinc finger | 434-501 | RING-Gid-type | ||||
Sequence: CPVCSETFKPITQALPFAHHIQSQLFENPILLPNGNVYDSKKLKKLAKTLKKQNLISLNPGQIMDPVD |
Sequence similarities
Belongs to the FYV10 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length516
- Mass (Da)59,894
- Last updated1995-02-01 v1
- Checksum2EACCF8C6C314D56
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z38125 EMBL· GenBank· DDBJ | CAA86284.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692905 EMBL· GenBank· DDBJ | AAT92924.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006942 EMBL· GenBank· DDBJ | DAA08456.1 EMBL· GenBank· DDBJ | Genomic DNA |