DPH1 explained
Diphthamide biosynthesis protein 1 is a protein that in humans is encoded by the DPH1 gene.[1] [2] [3] It encodes a protein that performs posttranslational modification of histidine-715[4] on eukaryotic translation elongation factor 2 to diphthamide. This modification appears to be important in the translation of Cyclin D in ovarian cells. DPH1 is mutated in 90% of ovarian cancers end stage, usually by loss of heterozygosity.
Further reading
- Schultz DC, Vanderveer L, Berman DB . Identification of two candidate tumor suppressor genes on chromosome 17p13.3. . Cancer Res. . 56 . 9 . 1997–2002 . 1996 . 8616839 . etal.
- Bruening W, Prowse AH, Schultz DC . Expression of OVCA1, a candidate tumor suppressor, is reduced in tumors and inhibits growth of ovarian cancer cells. . Cancer Res. . 59 . 19 . 4973–83 . 1999 . 10519411 . etal.
- Salicioni AM, Xi M, Vanderveer LA . Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif proteins that interact with OVCA1, a candidate tumor suppressor. . Genomics . 69 . 1 . 54–62 . 2001 . 11013075 . 10.1006/geno.2000.6315 . etal.
- Chen CM, Behringer RR . Cloning, structure, and expression of the mouse Ovca1 gene. . Biochem. Biophys. Res. Commun. . 286 . 5 . 1019–26 . 2001 . 11527402 . 10.1006/bbrc.2001.5488 .
- Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . etal . 2002PNAS...9916899M. free .
- Cardoso C, Leventer RJ, Ward HL . Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3. . Am. J. Hum. Genet. . 72 . 4 . 918–30 . 2003 . 12621583 . 10.1086/374320 . 1180354 . etal.
- Ota T, Suzuki Y, Nishikawa T . Complete sequencing and characterization of 21,243 full-length human cDNAs. . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . etal. free .
- Rual JF, Venkatesan K, Hao T . Towards a proteome-scale map of the human protein-protein interaction network. . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . etal. 2005Natur.437.1173R . 4427026 .
Notes and References
- Phillips NJ, Zeigler MR, Deaven LL . A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3 . Cancer Lett . 102 . 1–2 . 85–90 . May 1996 . 8603384 . 10.1016/0304-3835(96)04169-9 .
- Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH . 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 . Oct 2004 . 15485916 . 522255 . 10.1128/MCB.24.21.9487-9497.2004 .
- Web site: Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae).
- Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ . Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development . J. Cell Sci. . 121 . Pt 19 . 3140–5 . 2008 . 18765564 . 2592597 . 10.1242/jcs.035550 . Diphthamide modification is present in all eukaryotic organisms, in which it is restricted to a histidine residue of translation elongation factor 2 (eEF2, also known as EFT1; position 715 in mammals and 699 in yeast) .
