DPH1/YIL103W Summary Help

Standard Name DPH1 1
Systematic Name YIL103W
Feature Type ORF, Verified
Description Protein required for synthesis of diphthamide; required along with Dph2p, Kti11p, Jjj3p, and Dph5p; diphthamide is a modified histidine residue of translation elongation factor 2 (Eft1p or Eft2p); may act in a complex with Dph2p and Kti11p (2, 3)
Name Description DiPHthamide biosynthesis 3
Chromosomal Location
ChrIX:171751 to 173028 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All DPH1 GO evidence and references
  View Computational GO annotations for DPH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 1 genes
Resources
Pathways
Classical genetics
null
unspecified
Large-scale survey
null
Resources
48 total interaction(s) for 37 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 24
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 2
  • Biochemical Activity: 1
  • Two-hybrid: 2

Genetic Interactions
  • Negative Genetic: 12
  • Synthetic Growth Defect: 4
  • Synthetic Rescue: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 425
Molecular Weight (Da) 48,310
Isoelectric Point (pI) 8.33
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIX:171751 to 173028 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1994-12-10
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1278 171751..173028 2011-02-03 1994-12-10
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
Retired NameKIF48
Primary SGDIDS000001365
References cited on this page View Complete Literature Guide for DPH1
1) Chen JY, et al.  (1985) Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae. Mol Cell Biol 5(12):3357-60
2) Fichtner L, et al.  (2003) Elongator's toxin-target (TOT) function is nuclear localization sequence dependent and suppressed by post-translational modification. Mol Microbiol 49(5):1297-307
3) Liu S, et al.  (2004) Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol 24(21):9487-97