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P17625 (GYS2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen [starch] synthase, liver

EC=2.4.1.11
Gene names
Name:Gys2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length704 AA.
Sequence statusComplete.
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.

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.

Post-translational modification

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.

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 704704Glycogen [starch] synthase, liver
PRO_0000194769

Sites

Binding site401UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by PKA By similarity
Modified residue6411Phosphoserine; by GSK3-alpha and GSK3-beta 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 residue6841Phosphoserine By similarity

Experimental info

Sequence conflict821E → R in AAA41255. Ref.1
Sequence conflict2681H → D in AAA41255. Ref.1
Sequence conflict555 – 5573RRF → SV in AAA41255. Ref.1
Sequence conflict6221H → Y in AAA41255. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17625 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 926BD3057470A1D4

FASTA70480,734
        10         20         30         40         50         60 
MLRGRSLSVT SLGGLPAWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQS KAKTTANEWG 

        70         80         90        100        110        120 
ENYFLIGPYF EHNVKTQVEP CEPANDAVRK AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI 

       130        140        150        160        170        180 
SSSVWNLDRW KGDFWEACGV GIPHDDREAN DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH 

       190        200        210        220        230        240 
EWQAGTGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNQLDKFNID KEAGERQIYH 

       250        260        270        280        290        300 
RYCMERASVH CAHVFTTVSE ITAIEADHML KRKPDVVTPN GLNVKKFSAV HEFQNLHATY 

       310        320        330        340        350        360 
KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSNV 

       370        380        390        400        410        420 
TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCMKEKF GKKLYDGLLR GEIPDMNSIL 

       430        440        450        460        470        480 
DRDDLTIMKR AIFSTQRHSL PPVTTHNMID DSTDPILSTI RRIGLFNNRT DRVKVILHPE 

       490        500        510        520        530        540 
FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE 

       550        560        570        580        590        600 
HVADPTAYGI YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY 

       610        620        630        640        650        660 
LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ TSSPQSSDVE 

       670        680        690        700 
NEGDEDERYD EEEEAERDRL NIKSPFSLNH IPKGKKKLHG EYKN 

« Hide

References

[1]"The primary structure of rat liver glycogen synthase deduced by cDNA cloning. Absence of phosphorylation sites 1a and 1b."
Bai G., Zhang Z., Werner R., Nuttall F.Q., Tan A.W.H., Lee E.Y.C.
J. Biol. Chem. 265:7843-7848(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Glucose-regulated localization of liver glycogen synthase at the hepatocyte periphery."
Ferrer J.C., Baque S., Guinovart J.J.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05446 mRNA. Translation: AAA41255.1.
AF346902 mRNA. Translation: AAK16592.1.
PIRA35362.
RefSeqNP_037221.1. NM_013089.1.
UniGeneRn.2906.

3D structure databases

ProteinModelPortalP17625.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17625. 1 interaction.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteP17625.

Proteomic databases

PRIDEP17625.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25623.
KEGGrno:25623.
UCSCRGD:2773. rat.

Organism-specific databases

CTD2998.
RGD2773. Gys2.

Phylogenomic databases

HOVERGENHBG001960.
KOK00693.
PhylomeDBP17625.

Enzyme and pathway databases

UniPathwayUPA00164.

Gene expression databases

GenevestigatorP17625.

Family and domain databases

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

Other

NextBio607401.
PROP17625.

Entry information

Entry nameGYS2_RAT
AccessionPrimary (citable) accession number: P17625
Secondary accession number(s): Q99MF8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 96 of the entry and version 2 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