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Q5R9H0 (GYS1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glycogen [starch] synthase, muscle

EC=2.4.1.11
Gene names
Name:GYS1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Glycan biosynthesis; glycogen biosynthesis.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 737736Glycogen [starch] synthase, muscle
PRO_0000366919

Sites

Binding site391UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by AMPK and PKA By similarity
Modified residue111Phosphoserine By similarity
Modified residue6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK By similarity
Modified residue6451Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6491Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6531Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6571Phosphoserine; by CK2 By similarity
Modified residue6981Phosphoserine By similarity
Modified residue7271Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R9H0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 21F7CF6CB0D40A35

FASTA73783,798
        10         20         30         40         50         60 
MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGA 

        70         80         90        100        110        120 
NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 

       130        140        150        160        170        180 
ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKLHVVAHFH 

       190        200        210        220        230        240 
EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH 

       250        260        270        280        290        300 
RYCMERAAAH CAHVFTTVSQ ITAIEAQYLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 

       310        320        330        340        350        360 
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ 

       370        380        390        400        410        420 
TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML 

       430        440        450        460        470        480 
DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE 

       490        500        510        520        530        540 
FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE 

       550        560        570        580        590        600 
HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 

       610        620        630        640        650        660 
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 

       670        680        690        700        710        720 
EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS 

       730 
TPSEPLSPTS SLGEERN 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859418 mRNA. Translation: CAH91590.1.
RefSeqNP_001125937.1. NM_001132465.1.

3D structure databases

ProteinModelPortalQ5R9H0.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172871.
KEGGpon:100172871.

Organism-specific databases

CTD2997.

Phylogenomic databases

HOGENOMHOG000160890.
HOVERGENHBG001960.
InParanoidQ5R9H0.
KOK00693.

Enzyme and pathway databases

UniPathwayUPA00164.

Family and domain databases

InterProIPR008631. Glycogen_synth.
[Graphical view]
PANTHERPTHR10176. PTHR10176. 1 hit.
PfamPF05693. Glycogen_syn. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGYS1_PONAB
AccessionPrimary (citable) accession number: Q5R9H0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 21, 2004
Last modified: May 29, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways