From Wikipedia, the free encyclopedia
Diphthamide biosynthesis protein 1 is a protein that in humans is encoded by the DPH1 gene .[5] [6] [7] posttranslational modification of histidine -715[8] 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 [ ]
^ a b c GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl , May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl , May 2017^ "Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ "Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .^ 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)
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. Bibcode :2002PNAS...9916899M . 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. Bibcode :2005Natur.437.1173R . doi :10.1038/nature04209 . PMID 16189514 . S2CID 4427026 .
Categories :
Genes on human chromosome 17 Post-translational modification Protein stubs
