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P13834

- GYS1_RABIT

UniProt

P13834 - GYS1_RABIT

Protein

Glycogen [starch] synthase, muscle

Gene

GYS1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      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.1 Publication

    Catalytic activityi

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

    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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391UDP-glucoseBy similarity

    GO - Molecular functioni

    1. glycogen (starch) synthase activity Source: UniProtKB

    GO - Biological processi

    1. glycogen biosynthetic process 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, muscle (EC:2.4.1.11)
    Gene namesi
    Name:GYS1
    Synonyms:GYS
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi641 – 6411S → A: Loss of an inhibitory phosphorylation site. Abolishes phosphorylation by DYRK2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 735734Glycogen [starch] synthase, musclePRO_0000194767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine; by AMPK and PKA2 Publications
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei641 – 6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK4 Publications
    Modified residuei645 – 6451Phosphoserine; by GSK3-alpha and GSK3-beta3 Publications
    Modified residuei649 – 6491Phosphoserine; by GSK3-alpha and GSK3-beta3 Publications
    Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-beta2 Publications
    Modified residuei657 – 6571Phosphoserine; by CK22 Publications
    Modified residuei698 – 6981Phosphoserine2 Publications
    Modified residuei725 – 7251PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-8 is required for modification of Ser-11 by casein kinase I.2 Publications
    Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme By similarity. Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity By similarity. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. 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 and GSK3B.By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with GYG1.By similarity

    Protein-protein interaction databases

    IntActiP13834. 4 interactions.
    MINTiMINT-8146730.

    Structurei

    3D structure databases

    ProteinModelPortaliP13834.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0438.
    HOGENOMiHOG000160890.
    HOVERGENiHBG001960.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P13834-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLSRTLSVS SLPGLEDWED EFDLENSVLF EVAWEVANKV GGIYTVLQTK    50
    AKVTGDEWGD NYFLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK 100
    VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND 150
    AVLFGFLTTW FLGEFLAQNE EKPHVVAHFH EWLAGIGLCL CRARRLPVAT 200
    IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH RYCMERAAAH 250
    CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 300
    KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN 350
    YLLRVNGSEQ TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF 400
    GRKLYESLLV GSLPDMNKML DKEDFTMMKR AIFATQRQSF PPVCTHNMLD 450
    DSSDPILTTI RRIGLFNSSA DRVKVIFHPE FLSSTSPLLP VDYEEFVRGC 500
    HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE HIADPSAYGI 550
    YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 600
    LGRYYMSARH MALAKAFPDH FTYEPHEADA TQGYRYPRPA SVPPSPSLSR 650
    HSSPHQSEDE EEPRDGLPEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT 700
    SSSGGSKRSN SVDTSSLSTP SEPLSPASSL GEERN 735
    Length:735
    Mass (Da):83,601
    Last modified:January 23, 2007 - v4
    Checksum:i53ABE9DBE769ADBC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti692 – 6921E → Q AA sequence (PubMed:3087361)Curated
    Sequence conflicti726 – 7261P → S AA sequence (PubMed:3087361)Curated
    Sequence conflicti726 – 7261P → S AA sequence (PubMed:2842154)Curated
    Sequence conflicti728 – 7281S → P AA sequence (PubMed:3087361)Curated
    Sequence conflicti728 – 7281S → P AA sequence (PubMed:2842154)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017114 mRNA. Translation: AAB69872.1.
    PIRiA33369.
    RefSeqiNP_001075492.1. NM_001082023.1.
    UniGeneiOcu.2171.

    Genome annotation databases

    GeneIDi100008660.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017114 mRNA. Translation: AAB69872.1 .
    PIRi A33369.
    RefSeqi NP_001075492.1. NM_001082023.1.
    UniGenei Ocu.2171.

    3D structure databases

    ProteinModelPortali P13834.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13834. 4 interactions.
    MINTi MINT-8146730.

    Protein family/group databases

    CAZyi GT3. Glycosyltransferase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100008660.

    Organism-specific databases

    CTDi 2997.

    Phylogenomic databases

    eggNOGi COG0438.
    HOGENOMi HOG000160890.
    HOVERGENi HBG001960.

    Enzyme and pathway databases

    UniPathwayi UPA00164 .

    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. "Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones."
      Zhang W.M., Browner M.F., Fletterick R.J., DePaoli-Roach A.A., Roach P.J.
      FASEB J. 3:2532-2536(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Skeletal muscle.
    2. "Identification of the C-terminus of rabbit skeletal muscle glycogen synthase."
      Cohen P., Holmes C.F.B.
      Biochem. Biophys. Res. Commun. 137:542-545(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30 AND 612-735.
    3. "Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase."
      Rylatt D.B., Aitken A., Bilham T., Condon G.D., Embi N., Cohen P.
      Eur. J. Biochem. 107:529-537(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-30, PHOSPHORYLATION AT SER-8; SER-641; SER-645 AND SER-649.
    4. "Effect of proteases on the structure and activity of rabbit skeletal muscle glycogen synthetase."
      Huang T.S., Krebs E.G.
      FEBS Lett. 98:66-70(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
    5. "Analysis of the in vivo phosphorylation state of rabbit skeletal muscle glycogen synthase by fast-atom-bombardment mass spectrometry."
      Poulter L., Ang S.G., Gibson B.W., Williams D.H., Holmes C.F., Caudwell F.B., Pitcher J., Cohen P.
      Eur. J. Biochem. 175:497-510(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15; 639-662 AND 694-735, PHOSPHORYLATION AT SER-8; SER-11; SER-641; SER-645; SER-649; SER-653; SER-657 AND SER-698.
    6. "Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit."
      Mahrenholz A.M., Wang Y.H., Roach P.J.
      J. Biol. Chem. 263:10561-10567(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 6-21; 31-44 AND 286-300.
    7. "Phosphate groups as substrate determinants for casein kinase I action."
      Flotow H., Graves P.R., Wang A.Q., Fiol C.J., Roeske R.W., Roach P.J.
      J. Biol. Chem. 265:14264-14269(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 665-683.
    8. "Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Identification of the sites phosphorylated by casein kinase-I."
      Kuret J., Woodgett J.R., Cohen P.
      Eur. J. Biochem. 151:39-48(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    9. "Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40."
      Mahrenholz A.M., Votaw P., Roach P.J., Depaoli-Roach A.A., Zioncheck T.F., Harrison M.L., Geahlen R.L.
      Biochem. Biophys. Res. Commun. 155:52-58(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 665-683.
    10. "Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3."
      Fiol C.J., Mahrenholz A.M., Wang Y., Roeske R.W., Roach P.J.
      J. Biol. Chem. 262:14042-14048(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-641; SER-645; SER-649; SER-653 AND SER-657.
    11. "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases."
      Skurat A.V., Dietrich A.D.
      J. Biol. Chem. 279:2490-2498(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-641, ENZYME REGULATION, MUTAGENESIS OF SER-641.

    Entry informationi

    Entry nameiGYS1_RABIT
    AccessioniPrimary (citable) accession number: P13834
    Secondary accession number(s): O18817
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 102 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, 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