P47011 · GLG2_YEAST
- ProteinGlycogenin-2
- GeneGLG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids380 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + UDP + H+
Cofactor
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 10 | UDP (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 10 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 16 | UDP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 16 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 95 | UDP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 95 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 104 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 104 | Important for catalytic activity | ||||
Sequence: K | ||||||
Binding site | 120 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 120 | UDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 120 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 121 | UDP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 121 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 122 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | UDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 122 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 158 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 159 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 185 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 188 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 189 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 249 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 249 | UDP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 252 | UDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 252 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 255 | UDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 255 | UDP-alpha-D-glucose (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | vacuole | |
Molecular Function | glycogenin glucosyltransferase activity | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | glycogen biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycogenin-2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP47011
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Simultaneous knockout of GLG1 abolishes glycogen biosynthesis.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 230 | Eliminates glycogen accumulation; when associated with F-232 and F-367. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 232 | Eliminates glycogen accumulation; when associated with F-230 and F-367. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 367 | Eliminates glycogen accumulation; when associated with F-230 and F-232. | ||||
Sequence: Y → F |
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.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215182 | 1-380 | Glycogenin-2 | |||
Sequence: MAKKVAICTLLYSRDYLPGALTLAYQLQKLLKHAVVEDEITLCLLIEKKLFGDEFKPQEIALIRSLFKEIIIIEPLKDQEKSIEKNKANLELLKRPELSHTLLKARLWELVQFDQVLFLDADTLPLNKEFFEILRLYPEQTRFQIAAVPDIGWPDMFNTGVLLLIPDLDMATSLQDFLIKTVSIDGADQGIFNQFFNPICNYSKEVLHKVSPLMEWIRLPFTYNVTMPNYGYQSSPAMNFFQQHIRLIHFIGTFKPWSRNTTDYDDHYYQLWRSTQRELYSECHLSNYFTHLQLGNIETETNFYHEPPCLQDLLNHGKRENQKHVDLDITSVDRNASQKSTAEKHDIEKPTSKPQSAFKFDWESTDYLDRVQRAFPKPDT | ||||||
Glycosylation | 230 | O-linked (Glc...) tyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 232 | O-linked (Glc...) tyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 367 | O-linked (Glc...) tyrosine | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 331-355 | Disordered | ||||
Sequence: SVDRNASQKSTAEKHDIEKPTSKPQ | ||||||
Compositional bias | 338-352 | Basic and acidic residues | ||||
Sequence: QKSTAEKHDIEKPTS |
Sequence similarities
Belongs to the glycosyltransferase 8 family. Glycogenin subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length380
- Mass (Da)44,546
- Last updated1996-02-01 v1
- Checksum36BDF556DEF397C0
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 241 | in Ref. 5; AA sequence | ||||
Sequence: Missing | ||||||
Compositional bias | 338-352 | Basic and acidic residues | ||||
Sequence: QKSTAEKHDIEKPTS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |