A7MB78 (GYS1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 40.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glycogen [starch] synthase, muscle EC=2.4.1.11 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 736 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan By similarity. |
| Catalytic activity | UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1). |
| Enzyme 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. |
| Pathway | |
| Subunit structure | Interacts with GYG1 By similarity. |
| Post-translational modification | 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. Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme By similarity. |
| Sequence similarities | Belongs to the glycosyltransferase 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycogen biosynthesis |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Phosphoprotein |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycogen biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB heart developmentInferred from electronic annotation. Source: Compara |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: Compara inclusion bodyInferred from electronic annotation. Source: Compara |
| Molecular_function | glycogen (starch) synthase activity Inferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 736 | 735 | Glycogen [starch] synthase, muscle | PRO_0000358311 | |||||
Sites | |||||||||
| Binding site | 39 | 1 | UDP-glucose By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 8 | 1 | Phosphoserine; by AMPK and PKA By similarity | ||||||
| Modified residue | 11 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 641 | 1 | Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK By similarity | ||||||
| Modified residue | 645 | 1 | Phosphoserine; by GSK3-alpha and GSK3-beta By similarity | ||||||
| Modified residue | 649 | 1 | Phosphoserine; by GSK3-alpha and GSK3-beta By similarity | ||||||
| Modified residue | 653 | 1 | Phosphoserine; by GSK3-alpha and GSK3-beta By similarity | ||||||
| Modified residue | 657 | 1 | Phosphoserine; by CK2 By similarity | ||||||
| Modified residue | 698 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 726 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal muscle. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC151381 mRNA. Translation: AAI51382.1. |
| IPI | IPI00823588. |
| RefSeq | NP_001094769.1. NM_001101299.1. |
| UniGene | Bt.102939. |
3D structure databases | |
| ProteinModelPortal | A7MB78. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000007423. |
Protein family/group databases | |
| CAZy | GT3. Glycosyltransferase Family 3. |
Proteomic databases | |
| PRIDE | A7MB78. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000007423; ENSBTAP00000007423; ENSBTAG00000039958. |
| GeneID | 786335. |
| KEGG | bta:786335. |
Organism-specific databases | |
| CTD | 2997. |
Phylogenomic databases | |
| eggNOG | COG0438. |
| GeneTree | ENSGT00390000018612. |
| HOGENOM | HOG000160890. |
| HOVERGEN | HBG001960. |
| InParanoid | A7MB78. |
| KO | K00693. |
| OMA | HEWLAGL. |
| OrthoDB | EOG4C2H91. |
Enzyme and pathway databases | |
| UniPathway | UPA00164. |
Family and domain databases | |
| InterPro | IPR008631. Glycogen_synth. [Graphical view] |
| PANTHER | PTHR10176. PTHR10176. 1 hit. |
| Pfam | PF05693. Glycogen_syn. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20927821. |
Entry information
| Entry name | GYS1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: A7MB78 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
