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.

DPH1
Identifiers
AliasesDPH1, DPH2L, DPH2L1, OVCA1, DEDSSH, diphthamide biosynthesis 1
External IDsOMIM: 603527; MGI: 2151233; HomoloGene: 1059; GeneCards: DPH1; OMA:DPH1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001346574
NM_001346575
NM_001346576
NM_001383

NM_144491

RefSeq (protein)

NP_001333503
NP_001333504
NP_001333505
NP_001374

NP_652762

Location (UCSC)Chr 17: 2.03 – 2.04 MbChr 11: 75.07 – 75.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108963Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078789Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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.
  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.
  7. ^ "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".
  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)

Further reading

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