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Details on Person UniProt:P54840 GYS2
| Class:Id | ReferenceGeneProduct:56098 |
|---|---|
| _chainChangeLog | chain:1-703 added on Fri February 6 2015 |
| _displayName | UniProt:P54840 GYS2 |
| _timestamp | 2025-02-21 19:18:14 |
| chain | chain:1-703 |
| checksum | 718F000D6D00CA4A |
| 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:1731614). Phosphorylation reduces the activity towards UDP-glucose (PubMed:1731614). When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (PubMed:1731614).BIOPHYSICOCHEMICAL PROPERTIES Optimum pH is 7.5-8.5 (at 25 degrees Celsius) (non-phosphorylated state). Optimum pH is 8.5 (at 25 degrees Celsius) (most phosphorylated state).PATHWAY Glycan biosynthesis; glycogen biosynthesis.SUBUNIT Part of the glycogen synthase (GS)-glycogenin complex, a heterooctamer composed of a tetramer of GS and 2 dimers of glycogenin, where each GS protomer binds to one glycogenin subunit (via glycogenin C-terminus); the GS tetramer may dissociate from glycogenin dimers to continue glycogen polymerization on its own (By similarity). May also form a heterooctamer complex with GYG1 (via GYG1 C-terminus) (By similarity).TISSUE SPECIFICITY Specifically expressed in liver (at protein level).PTM 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. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8 is not required for interaction with GYG1 (By similarity). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (By similarity).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="13"Glycogen [starch] synthase, liver ecNumber evidence="7 9"2.4.1.11 alternativeName: fullName evidence="14"Glycogen synthase 2 |
| geneName | GYS2 |
| identifier | P54840 |
| isSequenceChanged | FALSE |
| keyword | Allosteric enzyme Disease variant Glycogen biosynthesis Glycogen storage disease 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 | GYS2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8988420] ENSEMBL:ENSG00000111713 GYS2 [Homo sapiens] |
| secondaryIdentifier | GYS2_HUMAN A0AVD8 |
| sequenceLength | 703 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:71599] GYS2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:71604] p-S-GYS2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:3858519] GYS2 H446D [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:3858521] GYS2 N39S [cytosol] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:71603] O-phospho-L-serine at unknown position [ReplacedResidue:3858511] L-asparagine 39 replaced with L-serine [ReplacedResidue:3858515] L-histidine 446 replaced with L-aspartic acid |
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No pathways have been reviewed or authored by UniProt:P54840 GYS2 (56098)
