Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

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  + dolichyl β-D-glucosyl phosphate

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  = α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

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  + dolichyl phosphate

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  + H⁺

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  • See the description of this molecule in ChEBI.

  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
    Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
    Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.
  EC:2.4.1.267
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.5

    "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
    Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
    Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

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  zoom

  +

  dolichyl β-D-glucosyl phosphate

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  zoom

  =

  α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol

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  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  dolichyl phosphate

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  • Search chemical reactions in Rhea for this molecule.

  zoom

  +

  H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity Source: SGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases."
    Burda P., Jakob C.A., Beinhauer J., Hegemann J.H., Aebi M.
    Glycobiology 9:617-625(1999) [PubMed] [Europe PMC] [Abstract]
• transferase activity, transferring hexosyl groups Source: SGDInferred from mutant phenotypeⁱ
  • Ref.5

    "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
    Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
    Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.

GO - Biological processⁱ

• aerobic respiration Source: SGDInferred from mutant phenotypeⁱ
  • "A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast."
    Mendelsohn R.D., Helmerhorst E.J., Cipollo J.F., Kukuruzinska M.A.
    Biochim Biophys Acta 1723:33-44(2005) [PubMed] [Europe PMC] [Abstract]
• dolichol-linked oligosaccharide biosynthetic process Source: InterPro
• oligosaccharide-lipid intermediate biosynthetic process Source: SGDInferred from mutant phenotypeⁱ
  • "Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases."
    Burda P., Jakob C.A., Beinhauer J., Hegemann J.H., Aebi M.
    Glycobiology 9:617-625(1999) [PubMed] [Europe PMC] [Abstract]
• protein glycosylation Source: SGDInferred from mutant phenotypeⁱ
  • Ref.5

    "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway."
    Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.
    Glycobiology 6:493-498(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, CHARACTERIZATION.
• protein N-linked glycosylation Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Topology

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MAIGKRLLVN KPAEESFYAS PMYDFLYPFR PVGNQWLPEY IIFVCAVILR 
        60         70         80         90        100
CTIGLGPYSG KGSPPLYGDF EAQRHWMEIT QHLPLSKWYW YDLQYWGLDY 
       110        120        130        140        150
PPLTAFHSYL LGLIGSFFNP SWFALEKSRG FESPDNGLKT YMRSTVIISD 
       160        170        180        190        200
ILFYFPAVIY FTKWLGRYRN QSPIGQSIAA SAILFQPSLM LIDHGHFQYN 
       210        220        230        240        250
SVMLGLTAYA INNLLDEYYA MAAVCFVLSI CFKQMALYYA PIFFAYLLSR 
       260        270        280        290        300
SLLFPKFNIA RLTVIAFATL ATFAIIFAPL YFLGGGLKNI HQCIHRIFPF 
       310        320        330        340        350
ARGIFEDKVA NFWCVTNVFV KYKERFTIQQ LQLYSLIATV IGFLPAMIMT 
       360        370        380        390        400
LLHPKKHLLP YVLIACSMSF FLFSFQVHEK TILIPLLPIT LLYSSTDWNV 
       410        420        430        440        450
LSLVSWINNV ALFTLWPLLK KDGLHLQYAV SFLLSNWLIG NFSFITPRFL 
       460        470        480        490        500
PKSLTPGPSI SSINSDYRRR SLLPYNVVWK SFIIGTYIAM GFYHFLDQFV 
       510        520        530        540 
APPSKYPDLW VLLNCAVGFI CFSIFWLWSY YKIFTSGSKS MKDL       

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. Yeast
   Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
2. Yeast chromosome XV
   Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
3. PATHWAY comments
   Index of metabolic and biosynthesis pathways
4. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
5. SIMILARITY comments
   Index of protein domains and families