DPH1

Protein-coding gene in the species Homo sapiens
DPH1
Identifiers
AliasesDPH1, DPH2L, DPH2L1, OVCA1, DEDSSH, diphthamide biosynthesis 1
External IDsOMIM: 603527; MGI: 2151233; HomoloGene: 1059; GeneCards: DPH1; OMA:DPH1 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for DPH1
Genomic location for DPH1
Band17p13.3Start2,030,137 bp[1]
End2,043,898 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for DPH1
Genomic location for DPH1
Band11 B5|11 45.76 cMStart75,068,469 bp[2]
End75,082,067 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000108963 – Ensembl, May 2017
  2. ^ a b c 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. 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.


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