Gyg1
entrez
27357
canonical
uniprot
Q9R062
canonical
ensembl
ENSMUSG00000019528
resolver
ensp
ENSMUSP00000136035
resolver
ensp
ENSMUSP00000138949
resolver
ensp
ENSMUSP00000180710
resolver
enst
ENSMUST00000178328
resolver
genesymbol
Gyg1
resolver
genesymbol_syn
Gyg
resolver
uniprot
Q3TWR9
resolver
uniprot_entry
GLYG_MOUSE
resolver
uniprot_sec
Q3TWR9
resolver
amino_acid_sequence
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRMVVLTSPQVSDSMRKVLETVFDDVIMVDVLDSGDSAHLTLMKRPELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSGWATTDITKHLPFVYNLSSISIYSYLPAFKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVNCDSQDPTVSHPEFLNLWWDTFTTNVLPLLQHHGLVKDASSYLMMEHVSGALSDLSFGEAPAAPQPSMSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
uniprot
proteins
ec_number
2.4.1.186
uniprot
proteins
function
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. {ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:P46976}.
uniprot
proteins
mass_dalton
37402
uniprot
proteins
mutagenesis
MUTAGEN 305; /note="K->A: No loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 308; /note="W->A: No loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 315; /note="Y->A: Severe loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 321; /note="F->A: Severe loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 324; /note="I->A: Severe loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 328; /note="L->A: Severe loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189"; MUTAGEN 332; /note="L->A: No loss of interaction with GYS2."; /evidence="ECO:0000269|PubMed:24982189
uniprot
proteins
pathway_participation
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000250|UniProtKB:P46976}.
uniprot
proteins
post_translational_modification
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. {ECO:0000250|UniProtKB:P13280}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
uniprot
proteins
protein_family
Glycogenin subfamily
uniprot
proteins
protein_family
Glycosyltransferase 8 family
uniprot
proteins
pubmed
10542328
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24982189
uniprot
proteins
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13280}. Nucleus {ECO:0000250|UniProtKB:P13280}. Note=Localizes to glycogen granules (glycosomes) in the cytoplasm (By similarity). Cytosolic localization is dependent on the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:C4R941, ECO:0000250|UniProtKB:P13280}.
uniprot
proteins