DPH1

DPH1
Identifiers
Aliases	DPH1, DPH2L, DPH2L1, OVCA1, DEDSSH, diphthamide biosynthesis 1
External IDs	MGI: 2151233 HomoloGene: 1059 GeneCards: DPH1
Gene location (Human)
Chr.	Chromosome 17 (human)[1]
End	2,043,430 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	75,191,241 bp[2]
Gene ontology
Molecular function	• protein binding; • transferase activity;
Cellular component	• cytoplasm; • cytosol; • cell nucleus; • nucleoplasm; • cell junction;
Biological process	• cell proliferation; • peptidyl-diphthamide biosynthetic process from peptidyl-histidine;
	Sources:Amigo / QuickGO
Orthologs
	1801
	116905
	ENSG00000108963
	ENSMUSG00000078789
	Q9BZG8
	Q5NCQ5
	NM_001346574; NM_001346575; NM_001346576; NM_001383
	NM_144491
	NP_001333503; NP_001333504; NP_001333505; NP_001374
	NP_652762
	Wikidata
View/Edit Human	View/Edit Mouse

Diphthamide biosynthesis protein 1 is a protein that in humans is encoded by the DPH1 gene.^[5]^[6]^[7] It encodes a protein that performs posttranslational modification of histidine-715^[8] 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 2 3 GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ 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.
↑ "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".
↑ 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)

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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid8603384-5] 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.

[pmid15485916-6] 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.

[entrez-7] "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".

[pmid18765564-8] 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)

DPH1

References

Further reading