ALG8: Difference between revisions

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{{Infobox_gene}}
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'''Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''ALG8'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)
| HGNCid = 23161
| Symbol = ALG8
| AltSymbols =; MGC2840
| OMIM = 608103
| ECnumber = 
| Homologene = 6931
| MGIid = 2141959
| GeneAtlas_image1 = PBB_GE_ALG8_203545_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| 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}}
| Process = {{GNF_GO|id=GO:0006487 |text = protein amino acid N-linked glycosylation}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 79053
    | Hs_Ensembl = ENSG00000159063
    | Hs_RefseqProtein = NP_001007028
    | Hs_RefseqmRNA = NM_001007027
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 77489636
    | Hs_GenLoc_end = 77528343
    | Hs_Uniprot = Q9BVK2
    | Mm_EntrezGene = 381903
    | Mm_Ensembl = ENSMUSG00000035704
    | Mm_RefseqmRNA = NM_199035
    | Mm_RefseqProtein = NP_950200
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 97246820
    | Mm_GenLoc_end = 97267358
    | Mm_Uniprot = Q3TKP5
  }}
}}
'''Asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)''', also known as '''ALG8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ih). Alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=79053| accessdate = }}</ref>
| summary_text = This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ih). Alternatively spliced 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=Jaeken J |title=Congenital disorders of glycosylation (CDG): update and new developments. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 3 |pages= 423-6 |year= 2005 |pmid= 15272470 |doi=  }}
*{{cite journal  | author=Jaeken J |title=Congenital disorders of glycosylation (CDG): update and new developments. |journal=J. Inherit. Metab. Dis. |volume=27 |issue= 3 |pages= 423–6 |year= 2005 |pmid= 15272470 |doi=10.1023/B:BOLI.0000031221.44647.9e }}
*{{cite journal  | author=Jaeken J, Carchon H |title=Congenital disorders of glycosylation: a booming chapter of pediatrics. |journal=Curr. Opin. Pediatr. |volume=16 |issue= 4 |pages= 434-9 |year= 2004 |pmid= 15273506 |doi=  }}
*{{cite journal  | vauthors=Jaeken J, Carchon H |title=Congenital disorders of glycosylation: a booming chapter of pediatrics. |journal=Curr. Opin. Pediatr. |volume=16 |issue= 4 |pages= 434–9 |year= 2004 |pmid= 15273506 |doi=10.1097/01.mop.0000133636.56790.4a }}
*{{cite journal  | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal  | vauthors=Adams MD, Kerlavage AR, Fleischmann RD |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3–174 |year= 1995 |pmid= 7566098 |doi=<!-- none available --> |url=http://www.columbia.edu/itc/biology/pollack/w4065/client_edit/readings/nature377_3.pdf | format=PDF  |display-authors=etal}}
*{{cite journal  | author=Stanchi F, Bertocco E, Toppo S, ''et al.'' |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69-80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H }}
*{{cite journal  | vauthors=Stanchi F, Bertocco E, Toppo S |title=Characterization of 16 novel human genes showing high similarity to yeast sequences. |journal=Yeast |volume=18 |issue= 1 |pages= 69–80 |year= 2001 |pmid= 11124703 |doi= 10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H |display-authors=etal}}
*{{cite journal  | author=Oriol R, Martinez-Duncker I, Chantret I, ''et al.'' |title=Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate. |journal=Mol. Biol. Evol. |volume=19 |issue= 9 |pages= 1451-63 |year= 2003 |pmid= 12200473 |doi=  }}
*{{cite journal  | vauthors=Oriol R, Martinez-Duncker I, Chantret I |title=Common origin and evolution of glycosyltransferases using Dol-P-monosaccharides as donor substrate. |journal=Mol. Biol. Evol. |volume=19 |issue= 9 |pages= 1451–63 |year= 2003 |pmid= 12200473 |doi=  10.1093/oxfordjournals.molbev.a004208|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=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=Chantret I, Dancourt J, Dupré T, ''et al.'' |title=A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9962-71 |year= 2003 |pmid= 12480927 |doi= 10.1074/jbc.M211950200 }}
*{{cite journal  | vauthors=Chantret I, Dancourt J, Dupré T |title=A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9962–71 |year= 2003 |pmid= 12480927 |doi= 10.1074/jbc.M211950200 |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=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=Schollen E, Frank CG, Keldermans L, ''et al.'' |title=Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). |journal=J. Med. Genet. |volume=41 |issue= 7 |pages= 550-6 |year= 2004 |pmid= 15235028 |doi=  }}
*{{cite journal  | vauthors=Schollen E, Frank CG, Keldermans L |title=Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency). |journal=J. Med. Genet. |volume=41 |issue= 7 |pages= 550–6 |year= 2004 |pmid= 15235028 |doi=10.1136/jmg.2003.016923 | pmc=1735831  |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 }}
*{{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=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117-26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal  | vauthors=Otsuki T, Ota T, Nishikawa T |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 |display-authors=etal}}
*{{cite journal  | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal  | vauthors=Kimura K, Wakamatsu A, Suzuki Y |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* [https://www.ncbi.nlm.nih.gov/books/NBK1332/  GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
* {{UCSC gene info|ALG8}}
 
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{{Glycosyltransferases}}
 
 
{{gene-11-stub}}

Latest revision as of 17:58, 29 August 2017

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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

Probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase is an enzyme that in humans is encoded by the ALG8 gene.[1]

This gene encodes a member of the ALG6/ALG8 glucosyltransferase family. The encoded protein catalyzes the addition of the second glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation of proteins. Mutations in this gene have been associated with congenital disorder of glycosylation type Ih (CDG-Ih). Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: ALG8 asparagine-linked glycosylation 8 homolog (S. cerevisiae, alpha-1,3-glucosyltransferase)".

Further reading

External links



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