• Official Full Name
  • WD repeat domain 45
  • Background
  • This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This gene has a pseudogene at chromosome 4q31.3. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity and full-length nature of some variants have not been determined.
  • Synonyms
  • WDR45; WD repeat domain 45; WD repeat domain, X linked 1 , WDRX1; WD repeat domain phosphoinositide-interacting protein 4; JM5; WIPI4; WD repeat containing protein 45; WD repeat domain phosphoinositide interacting protein 4; WD repeat domain, X linked 1; WD45 repeat protein interacting with phosphoinositides 4; WDRX1; WDRXI4; WIPI 4; WD repeat domain, X-linked 1; WD repeat-containing protein 45; WIPI-4
Source (Host):E. coliSpecies:Human
Product nameRecombinant Human WDR45, GST-tagged
Source (Host):Mammalian CellsSpecies:Mouse
Product nameRecombinant Mouse WDR45 Protein
Source (Host):Mammalian CellsSpecies:Rat
Product nameRecombinant Rat WDR45 Protein
Source (Host):Mammalian CellsSpecies:Rhesus Macaque
Product nameRecombinant Rhesus monkey WDR45 Protein, His-tagged
Source (Host):Mammalian CellsSpecies:Zebrafish
Product nameRecombinant Zebrafish WDR45
Source (Host):Species:Human
Product nameRecombinant Human WDR45 293 Cell Lysate

WDR45 Related Articles

Saitsu, H; Nishimura, T; et al. De novo mutations in the autophagy gene WDR45 cause static encephalopathy of childhood with neurodegeneration in adulthood. NATURE GENETICS 45:445-449(2013).
Guderian, G; Peter, C; et al. RioK1, a New Interactor of Protein Arginine Methyltransferase 5 (PRMT5), Competes with pICln for Binding and Modulates PRMT5 Complex Composition and Substrate Specificity. JOURNAL OF BIOLOGICAL CHEMISTRY 286:1976-1986(2011).