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Protein

Glycogen [starch] synthase, liver

Gene

Gys2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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).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 (By similarity).By similarity

Kineticsi

  1. KM=0.48 mM for UDP-glucose (at 30 degrees Celsius)1 Publication

    Pathwayi

    Sites

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

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Glycogen biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_292921. Glycogen synthesis.
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 6

    Organism-specific databases

    MGIiMGI:2385254. Gys2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81S → A: Abolishes phosphorylation. No effect on the interaction with GYG1. Does not affect the result of other mutations; when associated with A-135; R-135; R-141; A-239; A-243; or R-243. 1 Publication
    Mutagenesisi135 – 1351W → A: No effect on the interaction with GYG1. No effect on the interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi135 – 1351W → R: Loss of interaction with GYG1. Loss of interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi141 – 1411G → R: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi239 – 2391Y → A: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi243 – 2431C → A: No effect on the interaction with GYG1. Loss of interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi243 – 2431C → R: Loss of interaction with GYG1. Loss of function. Loss of interaction with GYG1; when associated with A-8. 1 Publication
    Mutagenesisi510 – 5101E → A: Loss of catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 704704Glycogen [starch] synthase, liverPRO_0000274489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Phosphoserine; by AMPK and 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 – 6841Phosphoserine1 Publication

    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 (By similarity). 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 (PubMed:24982189). Interaction with GYG1 does not regulate the phosphorylation at Ser-8 and Ser-641 (PubMed:24982189).By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8VCB3.
    PaxDbiQ8VCB3.
    PRIDEiQ8VCB3.

    PTM databases

    PhosphoSiteiQ8VCB3.

    Expressioni

    Inductioni

    Expression in the liver oscillates in a circadian manner with peak levels during the night.1 Publication

    Gene expression databases

    BgeeiQ8VCB3.
    CleanExiMM_GYS2.
    GenevestigatoriQ8VCB3.

    Interactioni

    Subunit structurei

    Interacts with GYG1 (via C-terminus); required for GYS2-mediated glycogen synthesis.1 Publication

    Protein-protein interaction databases

    IntActiQ8VCB3. 2 interactions.
    MINTiMINT-4119490.
    STRINGi10090.ENSMUSP00000032371.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8VCB3.
    SMRiQ8VCB3. Positions 26-619.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 3 family.Curated

    Phylogenomic databases

    eggNOGiCOG0438.
    GeneTreeiENSGT00390000018612.
    HOGENOMiHOG000160890.
    HOVERGENiHBG001960.
    InParanoidiQ8VCB3.
    KOiK00693.
    OMAiIMKRAIY.
    OrthoDBiEOG741Z1N.
    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.

    Q8VCB3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLRGRSLSVT SLGGLPVWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQT
    60 70 80 90 100
    KAKTTADEWG ENYFLIGPYF EHNMKTQVEQ CEPTNDAVRK AVDAMNKHGC
    110 120 130 140 150
    QVHFGRWLIE GSPYVVLFDI SSSAWNLDRW KGDFWEACGV GIPHHDREAN
    160 170 180 190 200
    DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH EWQAGTGLIL SRARKLPIAT
    210 220 230 240 250
    VFTTHATLLG RYLCAANIDF YNQLDKFDID KEAGERQIYH RYCMERASVH
    260 270 280 290 300
    CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY
    310 320 330 340 350
    KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN
    360 370 380 390 400
    FLLRMHKSNV TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCLKEKF
    410 420 430 440 450
    GKKLYDGLLR GEIPDMNSIL DRDDLTIMKR AIFSTQRQSL PPVTTHNMID
    460 470 480 490 500
    DSTDPILSTI RRIGLFNNRA DRVKVILHPE FLSSTSPLLP MDYEEFVRGC
    510 520 530 540 550
    HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFVQE 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
    ASSPQCSDAE DEEDEDERYD EEEEAERDRL NIKSPFSLNH FPKGKKKLHG

    EYKN
    Length:704
    Mass (Da):80,871
    Last modified:July 27, 2011 - v2
    Checksum:iC4B87195B5FC41FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti630 – 6301T → M in AAH21322 (PubMed:15489334).Curated
    Sequence conflicti656 – 6561C → S in AAH21322 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK138992 mRNA. Translation: BAE23850.1.
    BC021322 mRNA. Translation: AAH21322.1.
    BC158081 mRNA. Translation: AAI58082.1.
    CCDSiCCDS20683.1.
    RefSeqiNP_663547.2. NM_145572.2.
    UniGeneiMm.275975.

    Genome annotation databases

    EnsembliENSMUST00000032371; ENSMUSP00000032371; ENSMUSG00000030244.
    GeneIDi232493.
    KEGGimmu:232493.
    UCSCiuc009epi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK138992 mRNA. Translation: BAE23850.1.
    BC021322 mRNA. Translation: AAH21322.1.
    BC158081 mRNA. Translation: AAI58082.1.
    CCDSiCCDS20683.1.
    RefSeqiNP_663547.2. NM_145572.2.
    UniGeneiMm.275975.

    3D structure databases

    ProteinModelPortaliQ8VCB3.
    SMRiQ8VCB3. Positions 26-619.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ8VCB3. 2 interactions.
    MINTiMINT-4119490.
    STRINGi10090.ENSMUSP00000032371.

    Protein family/group databases

    CAZyiGT3. Glycosyltransferase Family 3.

    PTM databases

    PhosphoSiteiQ8VCB3.

    Proteomic databases

    MaxQBiQ8VCB3.
    PaxDbiQ8VCB3.
    PRIDEiQ8VCB3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000032371; ENSMUSP00000032371; ENSMUSG00000030244.
    GeneIDi232493.
    KEGGimmu:232493.
    UCSCiuc009epi.2. mouse.

    Organism-specific databases

    CTDi2998.
    MGIiMGI:2385254. Gys2.

    Phylogenomic databases

    eggNOGiCOG0438.
    GeneTreeiENSGT00390000018612.
    HOGENOMiHOG000160890.
    HOVERGENiHBG001960.
    InParanoidiQ8VCB3.
    KOiK00693.
    OMAiIMKRAIY.
    OrthoDBiEOG741Z1N.
    TreeFamiTF300306.

    Enzyme and pathway databases

    UniPathwayiUPA00164.
    ReactomeiREACT_292921. Glycogen synthesis.

    Miscellaneous databases

    NextBioi381135.
    PROiQ8VCB3.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8VCB3.
    CleanExiMM_GYS2.
    GenevestigatoriQ8VCB3.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "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.
      Tissue: Aorta and Vein.
    2. "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: FVB/N.
      Tissue: Liver.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    4. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "CLOCK regulates circadian rhythms of hepatic glycogen synthesis through transcriptional activation of Gys2."
      Doi R., Oishi K., Ishida N.
      J. Biol. Chem. 285:22114-22121(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    6. Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, INTERACTION WITH GYG1, MUTAGENESIS OF SER-8; TRP-135; GLY-141; TYR-239; CYS-243 AND GLU-510.

    Entry informationi

    Entry nameiGYS2_MOUSE
    AccessioniPrimary (citable) accession number: Q8VCB3
    Secondary accession number(s): Q3UTY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: July 27, 2011
    Last modified: May 27, 2015
    This is version 85 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

    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.