P40492 · FYV10_YEAST

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).

Miscellaneous

Present with 784 molecules/cell in log phase SD medium.

Caution

It is not certain that this protein has E3 ubiquitin-protein ligase activity by itself. Lacks a detectable RING-type zinc finger domain; the sequence in this region is highly divergent and lacks most of the expected Cys residues. Still, Cys-434 in this highly divergent region is required for ubiquitination of FBP1, suggesting a direct role in catalyzing ubiquitination.

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.

Features

Showing features for site.

TypeIDPosition(s)Description
Site434Essential for ubiquitin ligase activity

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular ComponentGID complex
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Biological Processnegative regulation of apoptotic process
Biological Processnegative regulation of gluconeogenesis
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein FYV10
  • EC number
  • Alternative names
    • Function required for yeast viability protein 10
    • Glucose-induced degradation protein 9
    • Probable E3 ubiquitin-protein ligase GID9

Gene names

    • Name
      FYV10
    • Synonyms
      GID9
    • Ordered locus names
      YIL097W

Organism names

Accessions

  • Primary accession
    P40492
  • Secondary accessions
    • D6VVJ0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis434Abolishes FBP1 ubiquitination and degradation.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002029701-516Protein FYV10

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P40492RMD5 Q125082EBI-25137, EBI-38868
View interactors in UniProtKB
View CPX-301 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, zinc finger.

TypeIDPosition(s)Description
Domain187-245CTLH
Zinc finger434-501RING-Gid-type

Sequence similarities

Belongs to the FYV10 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    516
  • Mass (Da)
    59,894
  • Last updated
    1995-02-01 v1
  • Checksum
    2EACCF8C6C314D56
MAEKSIFNEPDVDFHLKLNQQLFHIPYELLSKRIKHTQAVINKETKSLHEHTAALNQIFEHNDVEHDELALAKITEMIRKVDHIERFLNTQIKSYCQILNRIKKRLEFFHELKDIKSQNSGTSHNGNNEGTRTKLIQWYQSYTNILIGDYLTRNNPIKYNSETKDHWNSGVVFLKQSQLDDLIDYDVLLEANRISTSLLHERNLLPLISWINENKKTLTKKSSILEFQARLQEYIELLKVDNYTDAIVCFQRFLLPFVKSNFTDLKLASGLLIFIKYCNDQKPTSSTSSGFDTEEIKSQSLPMKKDRIFQHFFHKSLPRITSKPAVNTTDYDKSSLINLQSGDFERYLNLLDDQRWSVLNDLFLSDFYSMYGISQNDPLLIYLSLGISSLKTRDCLHPSDDENGNQETETATTAEKEVEDLQLFTLHSLKRKNCPVCSETFKPITQALPFAHHIQSQLFENPILLPNGNVYDSKKLKKLAKTLKKQNLISLNPGQIMDPVDMKIFCESDSIKMYPT

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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