MPD1/YOR288C Summary Help

Standard Name MPD1
Systematic Name YOR288C
Feature Type ORF, Verified
Description Member of the protein disulfide isomerase (PDI) family; interacts with and inhibits the chaperone activity of Cne1p; MPD1 overexpression in a pdi1 null mutant suppresses defects in Pdi1p functions such as carboxypeptidase Y maturation (1, 2, 3)
Chromosomal Location
ChrXV:853077 to 852121 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology Annotations All MPD1 GO evidence and references
  View Computational GO annotations for MPD1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Large-scale survey
null
overexpression
Resources
31 total interaction(s) for 24 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 1
  • Protein-RNA: 1
  • Reconstituted Complex: 3
  • Two-hybrid: 3

Genetic Interactions
  • Dosage Rescue: 2
  • Negative Genetic: 8
  • Phenotypic Enhancement: 3
  • Phenotypic Suppression: 3
  • Positive Genetic: 2
  • Synthetic Rescue: 1

Resources
Expression Summary
histogram
Resources
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXV:853077 to 852121 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
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..957 853077..852121 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 | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005814
References cited on this page View Complete Literature Guide for MPD1
1) Tachikawa H, et al.  (1995) Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett 369(2-3):212-6
2) Norgaard P, et al.  (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62
3) Kimura T, et al.  (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41