DPH1

DPH1
Identifikatori
Aliasi	DPH1
Vanjski ID-jevi	OMIM: 603527 MGI: 2151233 HomoloGene: 1059 GeneCards: DPH1
Lokacija gena (čovjek)
Hrom.	Hromosom 17 (čovjek)
Kraj	2,043,898 bp
Lokacija gena (miš)
Hrom.	Hromosom 11 (miš)
Kraj	75,082,067 bp
Ontologija gena
Molekularna funkcija	• GO:0001948, GO:0016582 vezivanje za proteine; • aktivnost sa transferazom;
Ćelijska komponenta	• citoplazma; • citosol; • jedro; • nukleoplazma; • međućelijske veze;
Biološki proces	• Ćelijska proliferacija; • peptidyl-diphthamide biosynthetic process from peptidyl-histidine;
	Izvori:Amigo / QuickGO
Ortolozi
	1801
	116905
	ENSG00000108963
	ENSMUSG00000078789
	Q9BZG8
	Q5NCQ5
	NM_001346574; NM_001346575; NM_001346576; NM_001383
	NM_144491
	NP_001333503; NP_001333504; NP_001333505; NP_001374
	NP_652762
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein 1 biosinteze diftamida je protein koji je kod ljudi kodiran genom DPH1.^[5]^[6]^[7] Kodira protein koji obavlja posttranslacijsku modifikaciju histidina-715^[8] na eukariotskom faktoru 2 elongacije tokom tanslacije u diftamid. Čini se da je ova modifikacija važna u translaciji ciklina D u ćelijama jajnika. DPH1 mutira u 90% završne faze karcinoma jajnika, obično uz gubitak heterozigotnosti.

Dužina polipeptidnog lanca je 443 aminokiseline, sa molekulskom težinom od 48.805.^[9]

Aminokiselinska sekvenca

Simboli

C: Cistein
D: Asparaginska kiselina
E: Glutaminska kiselina
F: Fenilalanin
G: Glicin
H: Histidin
I: Izoleucin
K: Lizin
L: Leucin
M: Metionin
N: Asparagin
P: Prolin
Q: Glutamin
R: Arginin
S: Serin
T: Treonin
V: Valin
W: Triptofan
Y: Tirozin

10	20	30	40	50
MRRQVMAALV	VSGAAEQGGR	DGPGRGRAPR	GRVANQIPPE	ILKNPQLQAA
IRVLPSNYNF	EIPKTIWRIQ	QAQAKKVALQ	MPEGLLLFAC	TIVDILERFT
EAEVMVMGDV	TYGACCVDDF	TARALGADFL	VHYGHSCLIP	MDTSAQDFRV
LYVFVDIRID	TTHLLDSLRL	TFPPATALAL	VSTIQFVSTL	QAAAQELKAE
YRVSVPQCKP	LSPGEILGCT	SPRLSKEVEA	VVYLGDGRFH	LESVMIANPN
VPAYRYDPYS	KVLSREHYDH	QRMQAARQEA	IATARSAKSW	GLILGTLGRQ
GSPKILEHLE	SRLRALGLSF	VRLLLSEIFP	SKLSLLPEVD	VWVQVACPRL
SIDWGTAFPK	PLLTPYEAAV	ALRDISWQQP	YPMDFYAGSS	LGPWTVNHGQ
DRRPHAPGRP	ARGKVQEGSA	RPPSAVACED	CSCRDEKVAP	LAP

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Phillips NJ, Zeigler MR, Deaven LL (maj 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.
^ 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.
^ "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".
^ 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)
^ "UniProt, Q9BZG8". Pristupljeno 12. 9. 2017.

Dopunska literatura

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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000108963 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000078789 - Ensembl, maj 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.

[pmid8603384-5] Phillips NJ, Zeigler MR, Deaven LL (maj 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.

[pmid15485916-6] 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.

[entrez-7] "Entrez Gene: DPH1 DPH1 homolog (S. cerevisiae)".

[pmid18765564-8] 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)

[UniProt-9] "UniProt, Q9BZG8". Pristupljeno 12. 9. 2017.

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