Query author contributions in Reactome
Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.
If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.
Details on Person UniProt:P46976 GYG1
| Class:Id | ReferenceGeneProduct:55746 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 6 2015;chain:2-350 added on Fri February 6 2015;initiator methionine:1 for 55746 removed on Fri Nov 03 2023;initiator methionine: for 55746 added on Fri Nov 03 2023;initiator methionine: for 55746 removed on Fri Aug 15 2025;initiator methionine:1 for 55746 added on Fri Aug 15 2025 |
| _displayName | UniProt:P46976 GYG1 |
| _timestamp | 2025-08-15 21:22:52 |
| chain | initiator methionine:1 chain:2-350 |
| checksum | ABAEEB7160DEC4DF |
| comment | FUNCTION Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. 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.CATALYTIC ACTIVITY L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + UDP + H(+)CATALYTIC ACTIVITY [1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + UDP + H(+)COFACTOR Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.ACTIVITY REGULATION Inhibited by palladium ions.PATHWAY Glycan biosynthesis; glycogen biosynthesis.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).INTERACTION Localizes to glycogen granules (glycosomes) in the cytoplasm (By similarity). Cytosolic localization is dependent on the actin cytoskeleton (By similarity).ALTERNATIVE PRODUCTS Highly expressed in skeletal muscle and heart, with lower levels in brain, lung, kidney and pancreas.PTM 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.PTM Phosphorylated.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyltransferase 8 family. Glycogenin subfamily. |
| description | recommendedName: fullName evidence="17"Glycogenin-1 shortName: GN-1 shortName: GN1 ecNumber evidence="6 8"2.4.1.186 |
| geneName | GYG1 GYG |
| identifier | P46976 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing Cytoplasm Disease variant Glycogen biosynthesis Glycogen storage disease Glycoprotein Manganese Metal-binding Nucleus Phosphoprotein Proteomics identification Reference proteome Transferase |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | GYG1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8991290] ENSEMBL:ENSG00000163754 GYG1 [Homo sapiens] |
| secondaryIdentifier | GLYG_HUMAN D3DNH0 D3DNH1 D3DNH2 Q6FHZ1 Q9UNV0 |
| sequenceLength | 350 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:148068] UniProt:P46976-2 GYG1 [Homo sapiens] [ReferenceIsoform:148069] UniProt:P46976-3 GYG1 [Homo sapiens] [ReferenceIsoform:404105] UniProt:P46976-1 GYG1 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:70174] glycogen-GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:70179] limit dextrin-glycogenin-1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:70186] poly((1,4)-alpha-glucosyl)GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:70190] GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:70292] oligo((1,4)-alpha-glucosyl) GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:70298] ((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl)GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:3777092] polysaccharide-P-GYG1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:3814832] GYG1 T83M [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5357542] ((1,6)-alpha-glucosyl)poly((1,4)-alpha-glucosyl)GYG1 [lysosomal lumen] [Homo sapiens] [EntityWithAccessionedSequence:5357545] poly((1,4)-alpha-glucosyl)GYG1 [lysosomal lumen] [Homo sapiens] |
| (referenceSequence) | [GroupModifiedResidue:70173] O4'-glucosyl-L-tyrosine (glycogen group) at 195 [GroupModifiedResidue:70178] O4'-glucosyl-L-tyrosine ((1,4-alpha-D-glucosyl)(n)-L-tyrosyl residue) at 194 [GroupModifiedResidue:70185] O4'-glucosyl-L-tyrosine ((1,4-alpha-D-glucosyl)(n)-L-tyrosyl residue) at 195 [GroupModifiedResidue:70291] O4'-glucosyl-L-tyrosine (alpha-D-glucosyl {alpha-D-glucosyl-(1->4)}n-alpha-D-glucopyranoside) at 195 [GroupModifiedResidue:70297] O4'-glucosyl-L-tyrosine (glycogen (amylose chain)n-[(1->6)-amylose chain]4) at 194 [GroupModifiedResidue:3777098] O4'-glucosyl-L-tyrosine (polysaccharide phosphate group) at 195 [ReplacedResidue:3814834] L-threonine 83 replaced with L-methionine |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:P46976 GYG1 (55746)
