P27472 · GYS2_YEAST
- ProteinGlycogen [starch] synthase isoform 2
- GeneGSY2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids705 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan. Is believed to regulate the synthesis of glycogen.
Miscellaneous
Present with 14600 molecules/cell in log phase SD medium.
Catalytic activity
- [(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H+ + UDPThis reaction proceeds in the forward direction.
[(1→4)-α-D-glucosyl](n) RHEA-COMP:9584 + CHEBI:58885 = [(1→4)-α-D-glucosyl](n+1) RHEA-COMP:9587 + CHEBI:15378 + CHEBI:58223
Activity regulation
Allosteric activation by glucose-6-phosphate, and phosphorylation by a cAMP-dependent kinase.
Pathway
Glycan biosynthesis; glycogen biosynthesis.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | glycogen (starch) synthase activity | |
Molecular Function | identical protein binding | |
Molecular Function | molecular function inhibitor activity | |
Biological Process | glycogen biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycogen [starch] synthase isoform 2
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP27472
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000194774 | 1-705 | Glycogen [starch] synthase isoform 2 | |||
Sequence: MSRDLQNHLLFETATEVANRVGGIYSVLKSKAPITVAQYKDHYHLIGPLNKATYQNEVDILDWKKPEAFSDEMRPVQHALQTMESRGVHFVYGRWLIEGAPKVILFDLDSVRGYSNEWKGDLWSLVGIPSPENDFETNDAILLGYTVAWFLGEVAHLDSQHAIVAHFHEWLAGVALPLCRKRRIDVVTIFTTHATLLGRYLCASGSFDFYNCLESVDVDHEAGRFGIYHRYCIERAAAHSADVFTTVSQITAFEAEHLLKRKPDGILPNGLNVIKFQAFHEFQNLHALKKEKINDFVRGHFHGCFDFDLDNTLYFFIAGRYEYKNKGADMFIEALARLNYRLKVSGSKKTVVAFIVMPAKNNSFTVEALKGQAEVRALENTVHEVTTSIGKRIFDHAIRYPHNGLTTELPTDLGELLKSSDKVMLKRRILALRRPEGQLPPIVTHNMVDDANDLILNKIRQVQLFNSPSDRVKMIFHPEFLNANNPILGLDYDEFVRGCHLGVFPSYYEPWGYTPAECTVMGVPSITTNVSGFGAYMEDLIETNQAKDYGIYIVDRRFKAPDESVEQLVDYMEEFVKKTRRQRINQRNRTERLSDLLDWKRMGLEYVKARQLALRRGYPDQFRELVGEELNDSNMDALAGGKKLKVARPLSVPGSPRDLRSNSTVYMTPGDLGTLQEVNNADDYFSLGVNPAADDDDDGPYADDS | ||||||
Modified residue | 159 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 363 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 467 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 651 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 655 | Phosphoserine; by PHO85 | ||||
Sequence: S | ||||||
Modified residue | 661 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 663 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 668 | Phosphothreonine; by PHO85 | ||||
Sequence: T |
Post-translational modification
Phosphorylated by the cyclin-CDK PCL10-PHO85. Phosphorylation causes inactivation of enzyme.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with PCL10.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P27472 | GLG1 P36143 | 3 | EBI-8036, EBI-2064417 | |
BINARY | P27472 | GSY1 P23337 | 4 | EBI-8036, EBI-8031 | |
BINARY | P27472 | GSY2 P27472 | 3 | EBI-8036, EBI-8036 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 686-705 | Disordered | ||||
Sequence: SLGVNPAADDDDDGPYADDS |
Sequence similarities
Belongs to the glycosyltransferase 3 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length705
- Mass (Da)80,079
- Last updated2007-01-23 v3
- Checksum4670D8328CEDB0D2
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 248 | in Ref. 4; AA sequence | ||||
Sequence: S → P | ||||||
Sequence conflict | 535 | in Ref. 1; AAA88716 | ||||
Sequence: A → S | ||||||
Sequence conflict | 622 | in Ref. 4; AA sequence | ||||
Sequence: F → FF |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M65206 EMBL· GenBank· DDBJ | AAA88716.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U17244 EMBL· GenBank· DDBJ | AAB67378.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09571.1 EMBL· GenBank· DDBJ | Genomic DNA |