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P17625

- GYS2_RAT

UniProt

P17625 - GYS2_RAT

Protein

Glycogen [starch] synthase, liver

Gene

Gys2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    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

    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: 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

    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 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.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP17625.

    PTM databases

    PhosphoSiteiP17625.

    Expressioni

    Gene expression databases

    GenevestigatoriP17625.

    Interactioni

    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.
    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

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    MLRGRSLSVT SLGGLPAWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQS    50
    KAKTTANEWG ENYFLIGPYF EHNVKTQVEP CEPANDAVRK AVDAMNKHGC 100
    QVHFGRWLIE GSPYVVLFDI SSSVWNLDRW KGDFWEACGV GIPHDDREAN 150
    DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH EWQAGTGLIL SRARKLPIAT 200
    IFTTHATLLG RYLCAANIDF YNQLDKFNID KEAGERQIYH RYCMERASVH 250
    CAHVFTTVSE ITAIEADHML KRKPDVVTPN GLNVKKFSAV HEFQNLHATY 300
    KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN 350
    FLLRMHKSNV TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCMKEKF 400
    GKKLYDGLLR GEIPDMNSIL DRDDLTIMKR AIFSTQRHSL PPVTTHNMID 450
    DSTDPILSTI RRIGLFNNRT DRVKVILHPE FLSSTSPLLP MDYEEFVRGC 500
    HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE HVADPTAYGI 550
    YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY 600
    LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ 650
    TSSPQSSDVE NEGDEDERYD EEEEAERDRL NIKSPFSLNH IPKGKKKLHG 700
    EYKN 704
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05446 mRNA. Translation: AAA41255.1.
    AF346902 mRNA. Translation: AAK16592.1.
    PIRiA35362.
    RefSeqiNP_037221.1. NM_013089.1.
    UniGeneiRn.2906.

    Genome annotation databases

    GeneIDi25623.
    KEGGirno:25623.
    UCSCiRGD:2773. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05446 mRNA. Translation: AAA41255.1 .
    AF346902 mRNA. Translation: AAK16592.1 .
    PIRi A35362.
    RefSeqi NP_037221.1. NM_013089.1.
    UniGenei Rn.2906.

    3D structure databases

    ProteinModelPortali P17625.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P17625. 1 interaction.

    Protein family/group databases

    CAZyi GT3. Glycosyltransferase Family 3.

    PTM databases

    PhosphoSitei P17625.

    Proteomic databases

    PRIDEi P17625.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25623.
    KEGGi rno:25623.
    UCSCi RGD:2773. rat.

    Organism-specific databases

    CTDi 2998.
    RGDi 2773. Gys2.

    Phylogenomic databases

    HOVERGENi HBG001960.
    KOi K00693.
    PhylomeDBi P17625.

    Enzyme and pathway databases

    UniPathwayi UPA00164 .

    Miscellaneous databases

    NextBioi 607401.
    PROi P17625.

    Gene expression databases

    Genevestigatori P17625.

    Family and domain databases

    InterProi IPR008631. Glycogen_synth.
    [Graphical view ]
    PANTHERi PTHR10176. PTHR10176. 1 hit.
    Pfami PF05693. Glycogen_syn. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 97 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