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Details on Person UniProt:P13807 GYS1
| Class:Id | ReferenceGeneProduct:56096 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Fri February 6 2015;chain:2-737 added on Fri February 6 2015 |
| _displayName | UniProt:P13807 GYS1 |
| _timestamp | 2025-02-21 18:47:21 |
| chain | chain:1-737 |
| checksum | 0E321BBFDEB0BD7F |
| comment | FUNCTION Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.CATALYTIC ACTIVITY [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + UDP + H(+)ACTIVITY REGULATION Allosteric activation by glucose-6-phosphate (PubMed:35690592, PubMed:35835870). Phosphorylation reduces enzyme activity by constraining a tense conformation of the tetramer through inter-subunit interaction (PubMed:35690592, PubMed:35835870). Phosphorylation reduces the activity towards UDP-glucose (By similarity). When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (By similarity).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.INTERACTION Expressed in skeletal muscle and most other cell types where glycogen is present.PTM Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641 by DYRK2, leading to inactivation (By similarity). Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (PubMed:35835870).DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the glycosyltransferase 3 family. |
| description | recommendedName: fullName evidence="11"Glycogen [starch] synthase, muscle ecNumber evidence="1 13"2.4.1.11 alternativeName: fullName evidence="14"Glycogen synthase 1 |
| geneName | GYS1 GYS |
| identifier | P13807 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Allosteric enzyme Alternative splicing Diabetes mellitus Disease variant Glycogen biosynthesis Glycosyltransferase 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 |
| name | GYS1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9004140] ENSEMBL:ENSG00000104812 GYS1 [Homo sapiens] |
| secondaryIdentifier | GYS1_HUMAN Q9BTT9 |
| sequenceLength | 737 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:8964810] UniProt:P13807-1 GYS1 [Homo sapiens] [ReferenceIsoform:8964811] UniProt:P13807-2 GYS1 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:71565] GYS1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:71570] p-S-GYS1 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:3828056] GYS1 R462* [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:71569] O-phospho-L-serine at unknown position [NonsenseMutation:9827813] Nonsense mutation at L-arginine 462 |
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No pathways have been reviewed or authored by UniProt:P13807 GYS1 (56096)
