VID24/YBR105C Summary Help

Standard Name VID24 1
Systematic Name YBR105C
Alias GID4 2
Feature Type ORF, Verified
Description GID Complex regulatory subunit; binds GID Complex in response to glucose through interactions with complex member Vid28p; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase; peripheral membrane protein located at Vid (vacuole import and degradation) vesicles (1, 2, 3, 4)
Name Description Vacuolar Import and Degradation 1
Chromosomal Location
ChrII:451969 to 450881 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All VID24 GO evidence and references
  View Computational GO annotations for VID24
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 14 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
124 total interaction(s) for 87 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 22
  • Affinity Capture-RNA: 3
  • Affinity Capture-Western: 7
  • Co-purification: 1
  • PCA: 1
  • Protein-RNA: 1

Genetic Interactions
  • Negative Genetic: 84
  • Positive Genetic: 5

Resources
Expression Summary
histogram
Resources
Length (a.a.) 362
Molecular Weight (Da) 41,245
Isoelectric Point (pI) 6.74
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrII:451969 to 450881 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1089 451969..450881 2011-02-03 1997-01-28
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000309
References cited on this page View Complete Literature Guide for VID24
1) Chiang MC and Chiang HL  (1998) Vid24p, a novel protein localized to the fructose-1, 6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. J Cell Biol 140(6):1347-56
2) Regelmann J, et al.  (2003) Catabolite degradation of fructose-1,6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Mol Biol Cell 14(4):1652-63
3) Santt O, et al.  (2008) The Yeast GID Complex, a Novel Ubiquitin Ligase (E3) Involved in the Regulation of Carbohydrate Metabolism. Mol Biol Cell 19(8):3323-33
4) Menssen R, et al.  (2012) Exploring the topology of the Gid complex, the E3 ubiquitin ligase involved in catabolite-induced degradation of gluconeogenic enzymes. J Biol Chem 287(30):25602-14