VID30/YGL227W Summary Help

Standard Name VID30 1
Systematic Name YGL227W
Alias GID1 2 , 3
Feature Type ORF, Verified
Description Central component of GID Complex, involved in FBPase degradation; interacts strongly with Gid8p to serve as a scaffold for other GID Complex subunits; contains SPRY domain and 3 domains that are also found in Gid8p - LisH, CTLH, and CRA; required for association of Vid vesicles and actin patches in vacuole import and degradation pathway; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm (3, 4, 5, 6, 7, 8)
Name Description Vacuolar Import and Degradation 1
Chromosomal Location
ChrVII:69671 to 72547 | ORF Map | GBrowse
Gene Ontology Annotations All VID30 GO evidence and references
  View Computational GO annotations for VID30
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 10 genes
Classical genetics
Large-scale survey
106 total interaction(s) for 63 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 34
  • Affinity Capture-Western: 11
  • Co-fractionation: 1
  • Protein-peptide: 7

Genetic Interactions
  • Negative Genetic: 35
  • Phenotypic Enhancement: 3
  • Positive Genetic: 11
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 958
Molecular Weight (Da) 108,178
Isoelectric Point (pI) 4.32
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:69671 to 72547 | ORF Map | GBrowse
Last Update Coordinates: 2004-07-15 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..2877 69671..72547 2004-07-15 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003196
References cited on this page View Complete Literature Guide for VID30
1) McCann, J., et al.  (2000) A novel membrane-associated protein Vid30p regulates import of fructose-1,6-bisphosphatase into Vid vesicles
2) Hammerle M, et al.  (1998) Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. J Biol Chem 273(39):25000-5
3) 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
4) van Der Merwe GK, et al.  (2001) Ammonia regulates VID30 expression and Vid30p function shifts nitrogen metabolism toward glutamate formation especially when Saccharomyces cerevisiae is grown in low concentrations of ammonia. J Biol Chem 276(31):28659-66
5) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
6) 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
7) Alibhoy AA, et al.  (2012) Vid30 is required for the association of Vid vesicles and actin patches in the vacuole import and degradation pathway. Autophagy 8(1):29-46
8) 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