P46976 · GLYG_HUMAN
- ProteinGlycogenin-1
- GeneGYG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids350 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
Catalytic activity
- L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H+ + UDPThis reaction proceeds in the forward direction.
Cofactor
Note: Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.
Activity regulation
Inhibited by palladium ions.
Pathway
Glycan biosynthesis; glycogen biosynthesis.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9-15 | substrate | ||||
Sequence: LTTNDAY | ||||||
Binding site | 77 | substrate | ||||
Sequence: R | ||||||
Site | 86 | Important for catalytic activity | ||||
Sequence: K | ||||||
Binding site | 102 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102-104 | substrate | ||||
Sequence: DAD | ||||||
Binding site | 104 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 133-135 | substrate | ||||
Sequence: NSG | ||||||
Binding site | 160-164 | substrate | ||||
Sequence: DGGDQ | ||||||
Binding site | 212 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 212-218 | substrate | ||||
Sequence: HFLGRVK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | ficolin-1-rich granule lumen | |
Cellular Component | lysosomal lumen | |
Cellular Component | membrane | |
Cellular Component | secretory granule lumen | |
Molecular Function | glycogenin glucosyltransferase activity | |
Molecular Function | glycosyltransferase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity | |
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-1
- EC number
- Short namesGN-1; GN1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP46976
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Glycogen storage disease 15 (GSD15)
- Note
- DescriptionA metabolic disorder resulting in muscle weakness, associated with the glycogen depletion in skeletal muscle, and cardiac arrhythmia, associated with the accumulation of abnormal storage material in the heart. The skeletal muscle shows a marked predominance of slow-twitch, oxidative muscle fibers and mitochondrial proliferation.
- See alsoMIM:613507
Natural variants in GSD15
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_063768 | 83 | T>M | in GSD15; loss of autoglucosylation; dbSNP:rs267606858 |
Polyglucosan body myopathy 2 (PGBM2)
- Note
- DescriptionA glycogen storage disease characterized by polyglucosan accumulation in muscle, and skeletal myopathy without cardiac involvement. Most patients manifest slowly progressive, hip girdle, shoulder girdle, and/or hand and leg muscle weakness. Polyglucosan contains abnormally long and poorly branched glucosyl chains and is variably resistant to digestion by alpha-amylase.
- See alsoMIM:616199
Natural variants in PGBM2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_072706 | 16 | A>P | in PGBM2; dbSNP:rs200947378 | |
VAR_072707 | 102 | D>H | in PGBM2; dbSNP:rs143137713 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_072706 | 16 | in PGBM2; dbSNP:rs200947378 | |||
Sequence: A → P | ||||||
Natural variant | VAR_063768 | 83 | in GSD15; loss of autoglucosylation; dbSNP:rs267606858 | |||
Sequence: T → M | ||||||
Natural variant | VAR_072707 | 102 | in PGBM2; dbSNP:rs143137713 | |||
Sequence: D → H | ||||||
Mutagenesis | 195 | Loss of glucosylation. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 447 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000215176 | 2-350 | UniProt | Glycogenin-1 | |||
Sequence: TDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIRKHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ | |||||||
Modified residue | 44 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 46 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 195 | UniProt | O-linked (Glc...) tyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195.
Phosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in skeletal muscle and heart, with lower levels in brain, lung, kidney and pancreas.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Part of the GYS1-GYG1 complex, a heterooctamer composed of a tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may dissociate from GYG1 dimers to continue glycogen polymerization on its own (PubMed:17055998, PubMed:22160680, PubMed:35690592, PubMed:35835870).
May also form a heterooctamer complex with GYS2 (via GYG1 C-terminus) (By similarity).
May also form a heterooctamer complex with GYS2 (via GYG1 C-terminus) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P46976 | GYS1 P13807 | 9 | EBI-740533, EBI-740553 | |
BINARY | P46976-2 | GYS1 P13807 | 3 | EBI-12017394, EBI-740553 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 301-333 | Interaction with GYS1 | ||||
Sequence: SHLSLGEIPAMAQPFVSSEERKERWEQGQADYM |
Sequence similarities
Belongs to the glycosyltransferase 8 family. Glycogenin subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P46976-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameGN-1L
- Length350
- Mass (Da)39,384
- Last updated2007-01-23 v4
- ChecksumABAEEB7160DEC4DF
P46976-2
- NameGN-1
- Differences from canonical
- 277-293: Missing
P46976-3
- NameGN-1S
- Differences from canonical
- 204-350: FGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ → KMSQEPYHICPLGRSQLWHSRLYPRKNGRNDGNRARLIIWEQIPLTTSRGNLTLTSSRNTAFFCEHIHFTSLVSDT
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_001768 | 204-350 | in isoform GN-1S | |||
Sequence: FGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ → KMSQEPYHICPLGRSQLWHSRLYPRKNGRNDGNRARLIIWEQIPLTTSRGNLTLTSSRNTAFFCEHIHFTSLVSDT | ||||||
Alternative sequence | VSP_001769 | 277-293 | in isoform GN-1 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U44131 EMBL· GenBank· DDBJ | AAB00114.1 EMBL· GenBank· DDBJ | mRNA | ||
U31525 EMBL· GenBank· DDBJ | AAB09752.1 EMBL· GenBank· DDBJ | mRNA | ||
X79537 EMBL· GenBank· DDBJ | CAA56073.1 EMBL· GenBank· DDBJ | mRNA | ||
AF065481 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF065476 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF065477 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF065478 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF065479 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF065480 EMBL· GenBank· DDBJ | AAD31084.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF087942 EMBL· GenBank· DDBJ | AAD52093.1 EMBL· GenBank· DDBJ | mRNA | ||
CR536547 EMBL· GenBank· DDBJ | CAG38784.1 EMBL· GenBank· DDBJ | mRNA | ||
AC021059 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471052 EMBL· GenBank· DDBJ | EAW78894.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78895.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78896.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78898.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78900.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471052 EMBL· GenBank· DDBJ | EAW78901.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000033 EMBL· GenBank· DDBJ | AAH00033.1 EMBL· GenBank· DDBJ | mRNA |