Gys2
entrez
232493
canonical
uniprot
Q8VCB3
canonical
ensembl
ENSMUSG00000030244
resolver
ensp
ENSMUSP00000032371
resolver
enst
ENSMUST00000032371
resolver
genesymbol
Gys2
resolver
uniprot
Q3UTY0
resolver
uniprot_entry
GYS2_MOUSE
resolver
uniprot_sec
Q3UTY0
resolver
activity_regulation
ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate. Phosphorylation reduces the activity towards UDP-glucose. When in the non-phosphorylated state, glycogen synthase does not require glucose-6-phosphate as an allosteric activator; when phosphorylated it does (By similarity). {ECO:0000250|UniProtKB:P13834, ECO:0000250|UniProtKB:P54840}.
uniprot
proteins
amino_acid_sequence
MLRGRSLSVTSLGGLPVWEAERLPVEDLLLFEVSWEVTNKVGGICTVIQTKAKTTADEWGENYFLIGPYFEHNMKTQVEQCEPTNDAVRKAVDAMNKHGCQVHFGRWLIEGSPYVVLFDISSSAWNLDRWKGDFWEACGVGIPHHDREANDMLIFGSLTAWFLKEVTDHADGKHVIAQFHEWQAGTGLILSRARKLPIATVFTTHATLLGRYLCAANIDFYNQLDKFDIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMYKARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSNVTVVVFFIMPAKTNNFNVETLKGQAVRKQLWDTVHCLKEKFGKKLYDGLLRGEIPDMNSILDRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRADRVKVILHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFVQEHVADPTAYGIYIVDRRFRSPDDSCNQLTQFLYGFCKQSRRQRIIQRNRTERLSDLLDWRYLGRYYQHARHLTLSRAFPDKFHLEPTSPPTTDGFKYPRPSSVPPSPSGSQASSPQCSDAEDEEDEDERYDEEEEAERDRLNIKSPFSLNHFPKGKKKLHGEYKN
uniprot
proteins
ec_number
2.4.1.11
uniprot
proteins
function
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. {ECO:0000269|PubMed:24982189}.
uniprot
proteins
mass_dalton
80871
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="S->A: Abolishes phosphorylation. No effect on the interaction with GYG1. Does not affect the result of other mutations; when associated with A-135; R-135; R-141; A-239; A-243; or R-243."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 135; /note="W->A: No effect on the interaction with GYG1. No effect on the interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 135; /note="W->R: Loss of interaction with GYG1. Loss of interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 141; /note="G->R: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 239; /note="Y->A: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 243; /note="C->A: No effect on the interaction with GYG1. Loss of interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 243; /note="C->R: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 510; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:24982189
uniprot
proteins
pathway_participation
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:24982189}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation reduces the activity towards UDP-alpha-D-glucose (By similarity). 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). 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 (PubMed:24982189). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (PubMed:24982189). {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834, ECO:0000250|UniProtKB:P17625, ECO:0000250|UniProtKB:P54840, ECO:0000269|PubMed:24982189}.
uniprot
proteins
protein_family
Glycosyltransferase 3 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
20430893
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24982189
uniprot
proteins
sequence_length
704
uniprot
proteins