DPH1

DPH1
Identifiers
Aliases	DPH1 , DPH2L, DPH2L1, OVCA1, DEDSSH, diphthamide biosynthesis 1
External IDs	OMIM: 603527; MGI: 2151233; HomoloGene: 1059; GeneCards: DPH1; OMA:DPH1 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17p13.3 Start 2,030,137 bp [1] End 2,043,898 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 B5|11 45.76 cM Start 75,068,469 bp [2] End 75,082,067 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pituitary gland right hemisphere of cerebellum anterior pituitary right uterine tube body of pancreas right frontal lobe left ovary prostate right ovary left uterine tube Top expressed in proximal tubule adrenal gland epiblast liver spermatocyte striatum of neuraxis right kidney dentate gyrus of hippocampal formation granule cell urinary bladder embryo More reference expression data BioGPS n/a
Gene ontology Molecular function protein binding transferase activity Cellular component cytoplasm cytosol nucleus nucleoplasm cell junction Biological process cell population proliferation peptidyl-diphthamide biosynthetic process from peptidyl-histidine Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 11: 75.07 – 75.08 Mb PubMed search [3] [4]
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. 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

• 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. Bibcode:2001BBRC..286.1019C. 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.