DPH1

Diphthamide biosynthesis 1
Identifiers
Symbols	DPH1 ; DPH2L; DPH2L1; OVCA1
External IDs	OMIM: 603527 HomoloGene: 1059 GeneCards: DPH1 Gene
Gene ontology Molecular function • protein binding Cellular component • nucleus • cytosol Biological process • cell proliferation • peptidyl-diphthamide biosynthetic process from peptidyl-histidine • post-translational protein modification • cellular protein metabolic process Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1801	116905
Ensembl	ENSG00000108963	ENSMUSG00000078789
UniProt	Q9BZG8	Q5NCQ5
RefSeq (mRNA)	NM_001383	NM_144491
RefSeq (protein)	NP_001374	NP_652762
Location (UCSC)	Chr 17: 2.03 – 2.04 Mb	Chr 11: 75.18 – 75.19 Mb
PubMed search

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.

References

1. Phillips NJ, Zeigler MR, Deaven LL (May 1996). "A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3". Cancer Lett 102 (1-2): 85–90. doi:10.1016/0304-3835(96)04169-9. PMID 8603384.
2. Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH (Oct 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. doi:10.1128/MCB.24.21.9487-9497.2004. PMC 522255. PMID 15485916.
3. "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".
4. Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ (2008). "Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development". J. Cell. Sci. 121 (Pt 19): 3140–5. doi:10.1242/jcs.035550. PMC 2592597. PMID 18765564. 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)

Further reading

• Schultz DC, Vanderveer L, Berman DB; et al. (1996). "Identification of two candidate tumor suppressor genes on chromosome 17p13.3.". Cancer Res. 56 (9): 1997–2002. PMID 8616839.
• Bruening W, Prowse AH, Schultz DC; et al. (1999). "Expression of OVCA1, a candidate tumor suppressor, is reduced in tumors and inhibits growth of ovarian cancer cells.". Cancer Res. 59 (19): 4973–83. PMID 10519411.
• Salicioni AM, Xi M, Vanderveer LA; et al. (2001). "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. doi:10.1006/geno.2000.6315. PMID 11013075.
• Chen CM, Behringer RR (2001). "Cloning, structure, and expression of the mouse Ovca1 gene.". Biochem. Biophys. Res. Commun. 286 (5): 1019–26. doi:10.1006/bbrc.2001.5488. PMID 11527402.
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cardoso C, Leventer RJ, Ward HL; et al. (2003). "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. doi:10.1086/374320. PMC 1180354. PMID 12621583.
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Rual JF, Venkatesan K, Hao T; et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.