DPH1

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
Orthologs
SpeciesHumanMouse
Entrez

1801

116905

Ensembl

ENSG00000108963

ENSMUSG00000078789

UniProt

Q9BZG8

Q5NCQ5

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

  1. GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl, 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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