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Protein

Glycogen [starch] synthase, liver

Gene

Gys2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.

Catalytic activityi

UDP-alpha-D-glucose + ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).

Enzyme regulationi

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).By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401UDP-glucoseBy similarity

GO - Molecular functioni

  1. glucose binding Source: RGD
  2. glycogen (starch) synthase activity Source: UniProtKB

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB
  2. glycogen metabolic process Source: RGD
  3. response to glucose Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase, liver (EC:2.4.1.11)
Gene namesi
Name:Gys2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2773. Gys2.

Subcellular locationi

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. cortical actin cytoskeleton Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytoskeleton Source: UniProtKB
  5. cytosol Source: UniProtKB
  6. ectoplasm Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704Glycogen [starch] synthase, liverPRO_0000194769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by PKABy similarity
Modified residuei627 – 6271PhosphoserineBy similarity
Modified residuei641 – 6411Phosphoserine; by GSK3-alpha and GSK3-betaBy similarity
Modified residuei645 – 6451Phosphoserine; by GSK3-alpha and GSK3-betaBy similarity
Modified residuei649 – 6491Phosphoserine; by GSK3-alpha and GSK3-betaBy similarity
Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-betaBy similarity
Modified residuei657 – 6571Phosphoserine; by CK2By similarity
Modified residuei684 – 6841PhosphoserineBy similarity

Post-translational modificationi

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). Phosphorylation at Ser-8 is not required for interaction with GYG1 (By similarity). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP17625.

PTM databases

PhosphoSiteiP17625.

Expressioni

Gene expression databases

GenevestigatoriP17625.

Interactioni

Subunit structurei

Interacts with GYG1 (via C-terminus); required for GYS2-mediated glycogen synthesis.By similarity

Protein-protein interaction databases

IntActiP17625. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP17625.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 3 family.Curated

Phylogenomic databases

HOVERGENiHBG001960.
InParanoidiP17625.
KOiK00693.
PhylomeDBiP17625.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17625-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRGRSLSVT SLGGLPAWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQS
60 70 80 90 100
KAKTTANEWG ENYFLIGPYF EHNVKTQVEP CEPANDAVRK AVDAMNKHGC
110 120 130 140 150
QVHFGRWLIE GSPYVVLFDI SSSVWNLDRW KGDFWEACGV GIPHDDREAN
160 170 180 190 200
DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH EWQAGTGLIL SRARKLPIAT
210 220 230 240 250
IFTTHATLLG RYLCAANIDF YNQLDKFNID KEAGERQIYH RYCMERASVH
260 270 280 290 300
CAHVFTTVSE ITAIEADHML KRKPDVVTPN GLNVKKFSAV HEFQNLHATY
310 320 330 340 350
KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN
360 370 380 390 400
FLLRMHKSNV TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCMKEKF
410 420 430 440 450
GKKLYDGLLR GEIPDMNSIL DRDDLTIMKR AIFSTQRHSL PPVTTHNMID
460 470 480 490 500
DSTDPILSTI RRIGLFNNRT DRVKVILHPE FLSSTSPLLP MDYEEFVRGC
510 520 530 540 550
HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE HVADPTAYGI
560 570 580 590 600
YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY
610 620 630 640 650
LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ
660 670 680 690 700
TSSPQSSDVE NEGDEDERYD EEEEAERDRL NIKSPFSLNH IPKGKKKLHG

EYKN
Length:704
Mass (Da):80,734
Last modified:December 16, 2008 - v2
Checksum:i926BD3057470A1D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821E → R in AAA41255 (PubMed:2110561).Curated
Sequence conflicti268 – 2681H → D in AAA41255 (PubMed:2110561).Curated
Sequence conflicti555 – 5573RRF → SV in AAA41255 (PubMed:2110561).Curated
Sequence conflicti622 – 6221H → Y in AAA41255 (PubMed:2110561).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05446 mRNA. Translation: AAA41255.1.
AF346902 mRNA. Translation: AAK16592.1.
PIRiA35362.
UniGeneiRn.2906.

Genome annotation databases

KEGGirno:25623.
UCSCiRGD:2773. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05446 mRNA. Translation: AAA41255.1.
AF346902 mRNA. Translation: AAK16592.1.
PIRiA35362.
UniGeneiRn.2906.

3D structure databases

ProteinModelPortaliP17625.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP17625. 1 interaction.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteiP17625.

Proteomic databases

PRIDEiP17625.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGirno:25623.
UCSCiRGD:2773. rat.

Organism-specific databases

CTDi2998.
RGDi2773. Gys2.

Phylogenomic databases

HOVERGENiHBG001960.
InParanoidiP17625.
KOiK00693.
PhylomeDBiP17625.

Enzyme and pathway databases

UniPathwayiUPA00164.

Miscellaneous databases

NextBioi607401.
PROiP17625.

Gene expression databases

GenevestigatoriP17625.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGYS2_RAT
AccessioniPrimary (citable) accession number: P17625
Secondary accession number(s): Q99MF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 16, 2008
Last modified: April 1, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.