YDL176W Summary Help

Systematic Name YDL176W
Feature Type ORF, Verified
Description Protein of unknown function; predicted by computational methods to be involved in fructose-1,6-bisphosphatase (Fbp1p) degradation; interacts with components of the GID complex; YDL176W is not an essential gene (1, 2, 3)
Chromosomal Location
ChrIV:142097 to 144223 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All YDL176W GO evidence and references
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 4 genes
Resources
Large-scale survey
null
Resources
17 total interaction(s) for 16 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Affinity Capture-RNA: 1

Genetic Interactions
  • Negative Genetic: 7
  • Positive Genetic: 4

Resources
Expression Summary
histogram
Resources
Length (a.a.) 708
Molecular Weight (Da) 81,464
Isoelectric Point (pI) 6.65
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIV:142097 to 144223 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2127 142097..144223 2011-02-03 1996-07-31
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 SGDIDS000002335
References cited on this page View Complete Literature Guide for YDL176W
1) Pitre S, et al.  (2006) PIPE: a protein-protein interaction prediction engine based on the re-occurring short polypeptide sequences between known interacting protein pairs. BMC Bioinformatics 7():365
2) Fisk DG, et al.  (2006) Saccharomyces cerevisiae S288C genome annotation: a working hypothesis. Yeast 23(12):857-65
3) Ulitsky I, et al.  (2008) From E-MAPs to module maps: dissecting quantitative genetic interactions using physical interactions. Mol Syst Biol 4:209