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Q9Z1E4

- GYS1_MOUSE

UniProt

Q9Z1E4 - GYS1_MOUSE

Protein

Glycogen [starch] synthase, muscle

Gene

Gys1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (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.By similarity

    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 sitei39 – 391UDP-glucoseBy similarity

    GO - Molecular functioni

    1. glucose binding Source: Ensembl
    2. glycogen (starch) synthase activity Source: MGI
    3. protein binding Source: MGI

    GO - Biological processi

    1. glycogen biosynthetic process Source: MGI
    2. heart development Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Glycogen biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.
    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, Gys3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:101805. Gys1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. inclusion body Source: MGI

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 738737Glycogen [starch] synthase, musclePRO_0000194765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine; by AMPK and PKA1 Publication
    Modified residuei11 – 111PhosphoserineBy similarity
    Modified residuei641 – 6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASKBy 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 residuei698 – 6981PhosphoserineBy similarity
    Modified residuei728 – 7281PhosphoserineBy 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. 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. Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity.By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z1E4.
    PaxDbiQ9Z1E4.
    PRIDEiQ9Z1E4.

    PTM databases

    PhosphoSiteiQ9Z1E4.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z1E4.
    BgeeiQ9Z1E4.
    GenevestigatoriQ9Z1E4.

    Interactioni

    Subunit structurei

    Interacts with GYG1.By similarity

    Protein-protein interaction databases

    IntActiQ9Z1E4. 4 interactions.
    MINTiMINT-4097092.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z1E4.
    SMRiQ9Z1E4. Positions 23-621.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0438.
    GeneTreeiENSGT00390000018612.
    HOGENOMiHOG000160890.
    HOVERGENiHBG001960.
    InParanoidiQ8VEB0.
    KOiK00693.
    OMAiFAMKRHG.
    OrthoDBiEOG741Z1N.
    PhylomeDBiQ9Z1E4.
    TreeFamiTF300306.

    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.

    Q9Z1E4-1 [UniParc]FASTAAdd to Basket

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    MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK    50
    AKVTGDEWGD NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK 100
    VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND 150
    AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH EWLAGVGLCL 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 FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR 650
    HSSPHQSEDE EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS 700
    SSTGGSKRSN SVDTGPSSSL STPTEPLSPT SSLGEERN 738
    Length:738
    Mass (Da):83,927
    Last modified:December 16, 2008 - v2
    Checksum:iD1F9252CA908FF69
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31L → R in CAA64322. (PubMed:8793107)Curated
    Sequence conflicti70 – 701E → V in AAD09457. 1 PublicationCurated
    Sequence conflicti80 – 801L → M in BAE42275. (PubMed:16141072)Curated
    Sequence conflicti111 – 1122GP → D in CAA64322. (PubMed:8793107)Curated
    Sequence conflicti120 – 1201G → A in AAD09457. 1 PublicationCurated
    Sequence conflicti148 – 1481A → G in AAD09457. 1 PublicationCurated
    Sequence conflicti154 – 1552FG → YS in AAD09457. 1 PublicationCurated
    Sequence conflicti191 – 1911C → S in CAA64322. (PubMed:8793107)Curated
    Sequence conflicti208 – 2081L → V in AAD09457. 1 PublicationCurated
    Sequence conflicti228 – 2281N → I in AAD09457. 1 PublicationCurated
    Sequence conflicti581 – 5822QR → HG in CAA64322. (PubMed:8793107)Curated
    Sequence conflicti640 – 6401A → V in AAD09457. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94616 mRNA. Translation: CAA64322.1.
    U53218 mRNA. Translation: AAD09457.1.
    AK050813 mRNA. Translation: BAC34420.1.
    AK171148 mRNA. Translation: BAE42275.1.
    CH466603 Genomic DNA. Translation: EDL22855.1.
    BC019389 mRNA. Translation: AAH19389.1.
    BC131687 mRNA. Translation: AAI31688.1.
    BC131688 mRNA. Translation: AAI31689.1.
    BC152550 mRNA. Translation: AAI52551.1.
    CCDSiCCDS21244.1.
    RefSeqiNP_109603.2. NM_030678.3.
    UniGeneiMm.275654.

    Genome annotation databases

    EnsembliENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
    GeneIDi14936.
    KEGGimmu:14936.
    UCSCiuc009gve.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94616 mRNA. Translation: CAA64322.1 .
    U53218 mRNA. Translation: AAD09457.1 .
    AK050813 mRNA. Translation: BAC34420.1 .
    AK171148 mRNA. Translation: BAE42275.1 .
    CH466603 Genomic DNA. Translation: EDL22855.1 .
    BC019389 mRNA. Translation: AAH19389.1 .
    BC131687 mRNA. Translation: AAI31688.1 .
    BC131688 mRNA. Translation: AAI31689.1 .
    BC152550 mRNA. Translation: AAI52551.1 .
    CCDSi CCDS21244.1.
    RefSeqi NP_109603.2. NM_030678.3.
    UniGenei Mm.275654.

    3D structure databases

    ProteinModelPortali Q9Z1E4.
    SMRi Q9Z1E4. Positions 23-621.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z1E4. 4 interactions.
    MINTi MINT-4097092.

    Protein family/group databases

    CAZyi GT3. Glycosyltransferase Family 3.

    PTM databases

    PhosphoSitei Q9Z1E4.

    Proteomic databases

    MaxQBi Q9Z1E4.
    PaxDbi Q9Z1E4.
    PRIDEi Q9Z1E4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003964 ; ENSMUSP00000003964 ; ENSMUSG00000003865 .
    GeneIDi 14936.
    KEGGi mmu:14936.
    UCSCi uc009gve.1. mouse.

    Organism-specific databases

    CTDi 2997.
    MGIi MGI:101805. Gys1.

    Phylogenomic databases

    eggNOGi COG0438.
    GeneTreei ENSGT00390000018612.
    HOGENOMi HOG000160890.
    HOVERGENi HBG001960.
    InParanoidi Q8VEB0.
    KOi K00693.
    OMAi FAMKRHG.
    OrthoDBi EOG741Z1N.
    PhylomeDBi Q9Z1E4.
    TreeFami TF300306.

    Enzyme and pathway databases

    UniPathwayi UPA00164 .
    Reactomei REACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.

    Miscellaneous databases

    NextBioi 287255.
    PROi Q9Z1E4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z1E4.
    Bgeei Q9Z1E4.
    Genevestigatori Q9Z1E4.

    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. "Cloning, localization and induction of mouse brain glycogen synthase."
      Pellegri G., Rossier C., Magistretti P.J., Martin J.-L.
      Brain Res. Mol. Brain Res. 38:191-199(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss albino.
      Tissue: Astrocyte.
    2. "Mouse glycogen synthase gene."
      Seldin M.F., Xue Z., Rochelle J.M., DeBry R., Surwit R.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell and Embryo.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Czech II.
      Tissue: Mammary tumor.
    6. "The alpha2-5'AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading."
      Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F., Richter E.A., Wojtaszewski J.F.
      Diabetes 53:3074-3081(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-8.

    Entry informationi

    Entry nameiGYS1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z1E4
    Secondary accession number(s): P54859
    , Q3TBN4, Q8BQG4, Q8VEB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 113 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3