P47011 · GLG2_YEAST

Function

function

Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase (PubMed:15479227, PubMed:8524228, PubMed:8900126).
Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives (PubMed:8900126).

Miscellaneous

Present with 981 molecules/cell in log phase SD medium.

Catalytic activity

Cofactor

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site10UDP (UniProtKB | ChEBI)
Binding site10UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site16UDP (UniProtKB | ChEBI)
Binding site16UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site95UDP (UniProtKB | ChEBI)
Binding site95UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site104UDP-alpha-D-glucose (UniProtKB | ChEBI)
Site104Important for catalytic activity
Binding site120Mn2+ (UniProtKB | ChEBI)
Binding site120UDP (UniProtKB | ChEBI)
Binding site120UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site121UDP (UniProtKB | ChEBI)
Binding site121UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site122Mn2+ (UniProtKB | ChEBI)
Binding site122UDP (UniProtKB | ChEBI)
Binding site122UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site158UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site159UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site185UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site188UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site189UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site249Mn2+ (UniProtKB | ChEBI)
Binding site249UDP (UniProtKB | ChEBI)
Binding site252UDP (UniProtKB | ChEBI)
Binding site252UDP-alpha-D-glucose (UniProtKB | ChEBI)
Binding site255UDP (UniProtKB | ChEBI)
Binding site255UDP-alpha-D-glucose (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentvacuole
Molecular Functionglycogenin glucosyltransferase activity
Molecular Functionglycosyltransferase activity
Molecular Functionmetal ion binding
Biological Processglycogen biosynthetic process

Keywords

Enzyme and pathway databases

Protein family/group databases

    • GT8Glycosyltransferase Family 8

Names & Taxonomy

Protein names

  • Recommended name
    Glycogenin-2
  • EC number
  • Alternative names
    • Glycogen synthesis initiator protein 2
    • Glycogenin glucosyltransferase 2

Gene names

    • Name
      GLG2
    • ORF names
      J0663
    • Ordered locus names
      YJL137C

Organism names

Accessions

  • Primary accession
    P47011
  • Secondary accessions
    • D6VW47

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Vacuole
Note: Localizes to glycogen granules (glycosomes) in the cytoplasm. Localizes to the vacuole during nitrogen starvation-induced glycophagy (autophagy of glycosomes).

Keywords

Phenotypes & Variants

Disruption phenotype

Simultaneous knockout of GLG1 abolishes glycogen biosynthesis.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis230Eliminates glycogen accumulation; when associated with F-232 and F-367.
Mutagenesis232Eliminates glycogen accumulation; when associated with F-230 and F-367.
Mutagenesis367Eliminates glycogen accumulation; when associated with F-230 and F-232.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00002151821-380Glycogenin-2
Glycosylation230O-linked (Glc...) tyrosine
Glycosylation232O-linked (Glc...) tyrosine
Glycosylation367O-linked (Glc...) tyrosine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with glycogen synthase GSY2.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region331-355Disordered
Compositional bias338-352Basic and acidic residues

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    380
  • Mass (Da)
    44,546
  • Last updated
    1996-02-01 v1
  • Checksum
    36BDF556DEF397C0
MAKKVAICTLLYSRDYLPGALTLAYQLQKLLKHAVVEDEITLCLLIEKKLFGDEFKPQEIALIRSLFKEIIIIEPLKDQEKSIEKNKANLELLKRPELSHTLLKARLWELVQFDQVLFLDADTLPLNKEFFEILRLYPEQTRFQIAAVPDIGWPDMFNTGVLLLIPDLDMATSLQDFLIKTVSIDGADQGIFNQFFNPICNYSKEVLHKVSPLMEWIRLPFTYNVTMPNYGYQSSPAMNFFQQHIRLIHFIGTFKPWSRNTTDYDDHYYQLWRSTQRELYSECHLSNYFTHLQLGNIETETNFYHEPPCLQDLLNHGKRENQKHVDLDITSVDRNASQKSTAEKHDIEKPTSKPQSAFKFDWESTDYLDRVQRAFPKPDT

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict241in Ref. 5; AA sequence
Compositional bias338-352Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U25436
EMBL· GenBank· DDBJ
AAA91644.1
EMBL· GenBank· DDBJ
Genomic DNA
X87371
EMBL· GenBank· DDBJ
CAA60818.1
EMBL· GenBank· DDBJ
Genomic DNA
Z49412
EMBL· GenBank· DDBJ
CAA89432.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006943
EMBL· GenBank· DDBJ
DAA08663.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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