GYS2
entrez
2998
canonical
uniprot
P54840
canonical
ensembl
ENSG00000111713
resolver
ensp
ENSP00000261195
resolver
ensp
ENSP00000667728
resolver
ensp
ENSP00000667739
resolver
enst
ENST00000261195
resolver
genesymbol
GYS2
resolver
hgnc
HGNC:4707
resolver
uniprot
A0AVD8
resolver
uniprot_entry
GYS2_HUMAN
resolver
uniprot_sec
A0AVD8
resolver
activity_regulation
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). {ECO:0000269|PubMed:1731614}.
uniprot
proteins
amino_acid_sequence
MLRGRSLSVTSLGGLPQWEVEELPVEELLLFEVAWEVTNKVGGIYTVIQTKAKTTADEWGENYFLIGPYFEHNMKTQVEQCEPVNDAVRRAVDAMNKHGCQVHFGRWLIEGSPYVVLFDIGYSAWNLDRWKGDLWEACSVGIPYHDREANDMLIFGSLTAWFLKEVTDHADGKYVVAQFHEWQAGIGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNHLDKFNIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMYKARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSDITVMVFFIMPAKTNNFNVETLKGQAVRKQLWDVAHSVKEKFGKKLYDALLRGEIPDLNDILDRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRTDRVKVILHPEFLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMQEHVADPTAYGIYIVDRRFRSPDDSCNQLTKFLYGFCKQSRRQRIIQRNRTERLSDLLDWRYLGRYYQHARHLTLSRAFPDKFHVELTSPPTTEGFKYPRPSSVPPSPSGSQASSPQSSDVEDEVEDERYDEEEEAERDRLNIKSPFSLSHVPHGKKKLHGEYKN
uniprot
proteins
disease_involvement
DISEASE: Glycogen storage disease 0 (GSD0) [MIM:240600]: A metabolic disorder characterized by fasting hypoglycemia presenting in infancy or early childhood, high blood ketones and low alanine and lactate concentrations. Although feeding relieves symptoms, it often results in postprandial hyperglycemia and hyperlactatemia. {ECO:0000269|PubMed:9691087}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:1731614, ECO:0000269|PubMed:9691087}.
uniprot
proteins
mass_dalton
80989
uniprot
proteins
pathway_participation
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:1731614, ECO:0000269|PubMed:9691087}.
uniprot
proteins
post_translational_modification
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). {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834, ECO:0000250|UniProtKB:Q8VCB3}.
uniprot
proteins
protein_family
Glycosyltransferase 3 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
1731614
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8203908
uniprot
proteins
pubmed
9691087
uniprot
proteins
sequence_length
703
uniprot
proteins