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{{technical|date=October 2009}}
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{{Infobox_gene}}
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'''UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase''' is an [[enzyme]] that in [[humans]] is encoded by the ''DPAGT1'' [[gene]].<ref name="pmid8244387">{{Cite journal| vauthors = Smith MW, Clark SP, Hutchinson JS, Wei YH, Churukian AC, Daniels LB, Diggle KL, Gen MW, Romo AJ, Lin Y | title = A sequence-tagged site map of human chromosome 11 | journal = Genomics | volume = 17 | issue = 3 | pages = 699–725 |date=Dec 1993 | pmid = 8244387 | pmc = | doi =10.1006/geno.1993.1392  |display-authors=etal}}</ref><ref name="entrez">{{Cite web| title = Entrez Gene: DPAGT1 dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1798| accessdate = }}</ref>
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Mutations in '''DPAGT1''' cause {{SWL|type=genetic_defect_results_in_disease|target=muscle weakness|label=myasthenia}}.{{Cite journal
{{GNF_Protein_box
  | pmid = 24759841
| image =
| year = 2014
| image_source =
| author1 = Selcen
| PDB =  
| first1 = D
  | Name = Dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)
| title = DPAGT1 myasthenia and myopathy: Genetic, phenotypic, and expression studies
| HGNCid = 2995
| journal = Neurology
| Symbol = DPAGT1
| last2 = Shen
| AltSymbols =; ALG7; CDG-Ij; D11S366; DGPT; DPAGT; DPAGT2; G1PT; GPT; UAGT; UGAT
| first2 = X. M.
| OMIM = 191350
| last3 = Brengman
| ECnumber =
| first3 = J
| Homologene = 1058
| last4 = Li
| MGIid = 1196396
| first4 = Y
| GeneAtlas_image1 = PBB_GE_DPAGT1_209509_s_at_tn.png
| last5 = Stans
| GeneAtlas_image2 = PBB_GE_DPAGT1_212525_s_at_tn.png
| first5 = A. A.
| Function = {{GNF_GO|id=GO:0003975 |text = UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| last6 = Wieben
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| first6 = E
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}}
| last7 = Engel
| Orthologs = {{GNF_Ortholog_box
| first7 = A. G.
    | Hs_EntrezGene = 1798
| doi = 10.1212/WNL.0000000000000435
    | Hs_Ensembl = ENSG00000172269
| volume=82
    | Hs_RefseqProtein = NP_001373
| issue=20
    | Hs_RefseqmRNA = NM_001382
  | pages=1822–30
    | Hs_GenLoc_db =
| pmc = 4035711
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 118472427
    | Hs_GenLoc_end = 118484251
    | Hs_Uniprot = Q9H3H5
    | Mm_EntrezGene = 13478
    | Mm_Ensembl = ENSMUSG00000032123
    | Mm_RefseqmRNA = NM_007875
    | Mm_RefseqProtein = NP_031901
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 44077840
    | Mm_GenLoc_end = 44084595
    | Mm_Uniprot = Q9CPT1
  }}
}}
}}
'''Dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)''', also known as '''DPAGT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DPAGT1 dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1798| accessdate = }}</ref>


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{{PBB_Summary
{{PBB Summary
| section_title =  
| section_title =
| summary_text = The protein encoded by this gene is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4. This protein is an integral membrane protein of the endoplasmic reticulum. The congenital disorder of glycosylation type Ij is caused by mutation in the gene encoding this enzyme. Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: DPAGT1 dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1798| accessdate = }}</ref>
| summary_text = The [[protein]] encoded by this gene is an enzyme that [[catalyzes]] the first step in the [[dolichol]]-linked [[oligosaccharide]] [[Metabolic pathway|pathway]] (also see [[Genetic pathway]]) for [[glycoprotein]] [[biosynthesis]]. This enzyme belongs to the [[glycosyltransferase]] family 4. This protein is an integral [[membrane protein]] of the [[endoplasmic reticulum]]. The [[congenital disorder of glycosylation]] type Ij is caused by [[mutation]] in the gene encoding this enzyme. Alternatively spliced [[Transcription (genetics)|transcript]] variants encoding different isoforms have been identified.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{Refbegin| 2}}
{{PBB_Further_reading
{{PBB_Further reading
| citations =  
| citations =
*{{cite journal | author=Freeze HH |title=Update and perspectives on congenital disorders of glycosylation. |journal=Glycobiology |volume=11 |issue= 12 |pages= 129R-143R |year= 2002 |pmid= 11805072 |doi=  }}
* {{Cite journal| author=Freeze HH |title=Update and perspectives on congenital disorders of glycosylation |journal=Glycobiology |volume=11 |issue= 12 |pages= 129R–143R |year= 2002 |pmid= 11805072 |doi=10.1093/glycob/11.12.129R }}
*{{cite journal | author=Freeze HH |title=Human disorders in N-glycosylation and animal models. |journal=Biochim. Biophys. Acta |volume=1573 |issue= 3 |pages= 388-93 |year= 2003 |pmid= 12417423 |doi=  }}
* {{Cite journal| author=Freeze HH |title=Human disorders in N-glycosylation and animal models |journal=Biochim. Biophys. Acta |volume=1573 |issue= 3 |pages= 388–93 |year= 2003 |pmid= 12417423 |doi=  10.1016/S0304-4165(02)00408-7}}
*{{cite journal | author=Miller BS, Freeze HH |title=New disorders in carbohydrate metabolism: congenital disorders of glycosylation and their impact on the endocrine system. |journal=Reviews in endocrine & metabolic disorders |volume=4 |issue= 1 |pages= 103-13 |year= 2003 |pmid= 12618564 |doi=  }}
* {{Cite journal| vauthors=Miller BS, Freeze HH |title=New disorders in carbohydrate metabolism: congenital disorders of glycosylation and their impact on the endocrine system |journal=Reviews in endocrine & metabolic disorders |volume=4 |issue= 1 |pages= 103–13 |year= 2003 |pmid= 12618564 |doi=10.1023/A:1021883605280 }}
*{{cite journal | author=Volpe JJ, Sakakihara Y, Ishii S |title=Dolichol-linked glycoprotein synthesis in developing mammalian brain: maturational changes of the N-acetylglucosaminylphosphotransferase. |journal=Brain Res. |volume=430 |issue= 2 |pages= 277-84 |year= 1987 |pmid= 3038274 |doi= }}
* {{Cite journal| vauthors=Volpe JJ, Sakakihara Y, Ishii S |title=Dolichol-linked glycoprotein synthesis in developing mammalian brain: maturational changes of the N-acetylglucosaminylphosphotransferase |journal=Brain Res. |volume=430 |issue= 2 |pages= 277–84 |year= 1987 |pmid= 3038274 |doi= 10.1016/0165-3806(87)90160-x }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{Cite journal| vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Smith MW, Clark SP, Hutchinson JS, ''et al.'' |title=A sequence-tagged site map of human chromosome 11. |journal=Genomics |volume=17 |issue= 3 |pages= 699-725 |year= 1993 |pmid= 8244387 |doi= }}
* {{Cite journal| vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
* {{Cite journal| vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
* {{Cite journal| vauthors=Eckert V, Blank M, Mazhari-Tabrizi R |title=Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae |journal=Glycobiology |volume=8 |issue= 1 |pages= 77–85 |year= 1998 |pmid= 9451016 |doi=10.1093/glycob/8.1.77 |display-authors=etal}}
*{{cite journal | author=Eckert V, Blank M, Mazhari-Tabrizi R, ''et al.'' |title=Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae. |journal=Glycobiology |volume=8 |issue= 1 |pages= 77-85 |year= 1998 |pmid= 9451016 |doi=  }}
* {{Cite journal| vauthors=Meissner JD, Naumann A, Mueller WH, Scheibe RJ |title=Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells |journal=Biochem. J. |volume=338 |issue=  2|pages= 561–8 |year= 1999 |pmid= 10024536 |doi=10.1042/0264-6021:3380561  | pmc=1220086 }}
*{{cite journal | author=Meissner JD, Naumann A, Mueller WH, Scheibe RJ |title=Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells. |journal=Biochem. J. |volume=338 ( Pt 2) |issue=  |pages= 561-8 |year= 1999 |pmid= 10024536 |doi=  }}
* {{Cite journal| vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{Cite journal| vauthors=Regis S, Dagnino F, Caroli F, Filocamo M |title=Genomic structure of the human UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase gene |journal=DNA Seq. |volume=13 |issue= 5 |pages= 245–50 |year= 2003 |pmid= 12592703 |doi=  10.1080/1042517021000017126}}
*{{cite journal | author=Regis S, Dagnino F, Caroli F, Filocamo M |title=Genomic structure of the human UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase gene. |journal=DNA Seq. |volume=13 |issue= 5 |pages= 245-50 |year= 2003 |pmid= 12592703 |doi=  }}
* {{Cite journal| vauthors=Newell JW, Seo NS, Enns GM |title=Congenital disorder of glycosylation Ic in patients of Indian origin |journal=Mol. Genet. Metab. |volume=79 |issue= 3 |pages= 221–8 |year= 2004 |pmid= 12855228 |doi=10.1016/S1096-7192(03)00089-1 |display-authors=etal}}
*{{cite journal | author=Newell JW, Seo NS, Enns GM, ''et al.'' |title=Congenital disorder of glycosylation Ic in patients of Indian origin. |journal=Mol. Genet. Metab. |volume=79 |issue= 3 |pages= 221-8 |year= 2004 |pmid= 12855228 |doi=  }}
* {{Cite journal| vauthors=Wu X, Rush JS, Karaoglu D |title=Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij |journal=Hum. Mutat. |volume=22 |issue= 2 |pages= 144–50 |year= 2004 |pmid= 12872255 |doi= 10.1002/humu.10239 |display-authors=etal}}
*{{cite journal | author=Wu X, Rush JS, Karaoglu D, ''et al.'' |title=Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij. |journal=Hum. Mutat. |volume=22 |issue= 2 |pages= 144-50 |year= 2004 |pmid= 12872255 |doi= 10.1002/humu.10239 }}
* {{Cite journal| vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
* {{Cite journal| vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
}}
{{refend}}
{{Refend}}
 
==External links==
* [https://www.ncbi.nlm.nih.gov/books/NBK1332/  GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
 
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Latest revision as of 22:50, 15 May 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene.[1][2]

Mutations in DPAGT1 cause myasthenia .Selcen, D; Shen, X. M.; Brengman, J; Li, Y; Stans, A. A.; Wieben, E; Engel, A. G. (2014). "DPAGT1 myasthenia and myopathy: Genetic, phenotypic, and expression studies". Neurology. 82 (20): 1822–30. doi:10.1212/WNL.0000000000000435. PMC 4035711. PMID 24759841.

The protein encoded by this gene is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway (also see Genetic pathway) for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4. This protein is an integral membrane protein of the endoplasmic reticulum. The congenital disorder of glycosylation type Ij is caused by mutation in the gene encoding this enzyme. Alternatively spliced transcript variants encoding different isoforms have been identified.[2]

References

  1. ↑ Smith MW, Clark SP, Hutchinson JS, Wei YH, Churukian AC, Daniels LB, Diggle KL, Gen MW, Romo AJ, Lin Y, et al. (Dec 1993). "A sequence-tagged site map of human chromosome 11". Genomics. 17 (3): 699–725. doi:10.1006/geno.1993.1392. PMID 8244387.
  2. ↑ 2.0 2.1 "Entrez Gene: DPAGT1 dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P transferase)".

Further reading

External links



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