| 释义 |
- References
- Further reading
{{Infobox_gene}}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. References1. ^{{cite journal | vauthors = Phillips NJ, Zeigler MR, Deaven LL | title = A cDNA from the ovarian cancer critical region of deletion on chromosome 17p13.3 | journal = Cancer Lett | volume = 102 | issue = 1-2 | pages = 85–90 |date=May 1996 | pmid = 8603384 | pmc = | doi =10.1016/0304-3835(96)04169-9 }}
2. ^{{cite journal | vauthors = Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH | title = Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2 | journal = Mol Cell Biol | volume = 24 | issue = 21 | pages = 9487–97 |date=Oct 2004 | pmid = 15485916 | pmc = 522255 | doi = 10.1128/MCB.24.21.9487-9497.2004 }}
3. ^{{cite web | title = Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1801| accessdate = }}
4. ^{{cite journal | vauthors = Webb TR, Cross SH, McKie L, Edgar R, Vizor L, Harrison J, Peters J, Jackson IJ | title = Diphthamide modification of eEF2 requires a J-domain protein and is essential for normal development | journal = J. Cell Sci. | volume = 121 | issue = Pt 19 | pages = 3140–5 | year = 2008 | pmid = 18765564 | pmc = 2592597 | doi = 10.1242/jcs.035550 | quote = 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{{refbegin | 2}}- {{cite journal | vauthors=Schultz DC, Vanderveer L, Berman DB |title=Identification of two candidate tumor suppressor genes on chromosome 17p13.3. |journal=Cancer Res. |volume=56 |issue= 9 |pages= 1997–2002 |year= 1996 |pmid= 8616839 |doi= |display-authors=etal}}
- {{cite journal | vauthors=Bruening W, Prowse AH, Schultz DC |title=Expression of OVCA1, a candidate tumor suppressor, is reduced in tumors and inhibits growth of ovarian cancer cells. |journal=Cancer Res. |volume=59 |issue= 19 |pages= 4973–83 |year= 1999 |pmid= 10519411 |doi= |display-authors=etal}}
- {{cite journal | vauthors=Salicioni AM, Xi M, Vanderveer LA |title=Identification and structural analysis of human RBM8A and RBM8B: two highly conserved RNA-binding motif proteins that interact with OVCA1, a candidate tumor suppressor. |journal=Genomics |volume=69 |issue= 1 |pages= 54–62 |year= 2001 |pmid= 11013075 |doi= 10.1006/geno.2000.6315 |display-authors=etal}}
- {{cite journal | vauthors=Chen CM, Behringer RR |title=Cloning, structure, and expression of the mouse Ovca1 gene. |journal=Biochem. Biophys. Res. Commun. |volume=286 |issue= 5 |pages= 1019–26 |year= 2001 |pmid= 11527402 |doi= 10.1006/bbrc.2001.5488 }}
- {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
- {{cite journal | vauthors=Cardoso C, Leventer RJ, Ward HL |title=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. |journal=Am. J. Hum. Genet. |volume=72 |issue= 4 |pages= 918–30 |year= 2003 |pmid= 12621583 |doi=10.1086/374320 | pmc=1180354 |display-authors=etal}}
- {{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
- {{cite journal | vauthors=Rual JF, Venkatesan K, Hao T |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |display-authors=etal}}
{{refend}}{{protein-stub}} 1 : Posttranslational modification |