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Database: UniProt/SWISS-PROT
Entry: GYS1_MOUSE
LinkDB: GYS1_MOUSE
Original site: GYS1_MOUSE 
ID   GYS1_MOUSE              Reviewed;         738 AA.
AC   Q9Z1E4; P54859; Q3TBN4; Q8BQG4; Q8VEB0;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   16-JAN-2019, entry version 145.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=Gys1; Synonyms=Gys, Gys3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss albino; TISSUE=Astrocyte;
RX   PubMed=8793107; DOI=10.1016/0169-328X(95)00305-C;
RA   Pellegri G., Rossier C., Magistretti P.J., Martin J.-L.;
RT   "Cloning, localization and induction of mouse brain glycogen
RT   synthase.";
RL   Brain Res. Mol. Brain Res. 38:191-199(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seldin M.F., Xue Z., Rochelle J.M., DeBry R., Surwit R.;
RT   "Mouse glycogen synthase gene.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION AT SER-8.
RX   PubMed=15561936; DOI=10.2337/diabetes.53.12.3074;
RA   Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B.,
RA   Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F.,
RA   Richter E.A., Wojtaszewski J.F.;
RT   "The alpha2-5'AMP-activated protein kinase is a site 2 glycogen
RT   synthase kinase in skeletal muscle and is responsive to glucose
RT   loading.";
RL   Diabetes 53:3074-3081(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-645; SER-649;
RP   SER-653; SER-657; SER-672; SER-709; THR-722; THR-724 AND SER-728, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Pancreas;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose =
CC         [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP;
CC         Xref=Rhea:RHEA:18549, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:58885; EC=2.4.1.11;
CC   -!- ACTIVITY REGULATION: Allosteric activation by glucose-6-phosphate.
CC       Phosphorylation reduces the activity towards UDP-glucose. When in
CC       the non-phosphorylated state, glycogen synthase does not require
CC       glucose-6-phosphate as an allosteric activator; when
CC       phosphorylated it does (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1. {ECO:0000250}.
CC   -!- PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and
CC       CSNK2A2 is required for inhibitory phosphorylation at Ser-641
CC       (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site
CC       4) by GSK3A an GSK3B. Phosphorylated at Ser-641 by PASK, leading
CC       to inactivation; phosphorylation by PASK is inhibited by glycogen.
CC       Phosphorylated at Ser-641 by DYRK2, leading to inactivation.
CC       Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the
CC       enzyme (By similarity). Phosphorylation at Ser-8 by AMPK
CC       inactivates the enzyme activity. {ECO:0000250,
CC       ECO:0000269|PubMed:15561936}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; X94616; CAA64322.1; -; mRNA.
DR   EMBL; U53218; AAD09457.1; -; mRNA.
DR   EMBL; AK050813; BAC34420.1; -; mRNA.
DR   EMBL; AK171148; BAE42275.1; -; mRNA.
DR   EMBL; CH466603; EDL22855.1; -; Genomic_DNA.
DR   EMBL; BC019389; AAH19389.1; -; mRNA.
DR   EMBL; BC131687; AAI31688.1; -; mRNA.
DR   EMBL; BC131688; AAI31689.1; -; mRNA.
DR   EMBL; BC152550; AAI52551.1; -; mRNA.
DR   CCDS; CCDS21244.1; -.
DR   RefSeq; NP_109603.2; NM_030678.3.
DR   UniGene; Mm.275654; -.
DR   ProteinModelPortal; Q9Z1E4; -.
DR   SMR; Q9Z1E4; -.
DR   BioGrid; 200132; 1.
DR   IntAct; Q9Z1E4; 5.
DR   MINT; Q9Z1E4; -.
DR   STRING; 10090.ENSMUSP00000003964; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; Q9Z1E4; -.
DR   PhosphoSitePlus; Q9Z1E4; -.
DR   SwissPalm; Q9Z1E4; -.
DR   EPD; Q9Z1E4; -.
DR   jPOST; Q9Z1E4; -.
DR   MaxQB; Q9Z1E4; -.
DR   PaxDb; Q9Z1E4; -.
DR   PeptideAtlas; Q9Z1E4; -.
DR   PRIDE; Q9Z1E4; -.
DR   Ensembl; ENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
DR   GeneID; 14936; -.
DR   KEGG; mmu:14936; -.
DR   UCSC; uc009gve.1; mouse.
DR   CTD; 2997; -.
DR   MGI; MGI:101805; Gys1.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; Q9Z1E4; -.
DR   KO; K00693; -.
DR   OMA; GHFYGHM; -.
DR   OrthoDB; 264593at2759; -.
DR   PhylomeDB; Q9Z1E4; -.
DR   TreeFam; TF300306; -.
DR   Reactome; R-MMU-3322077; Glycogen synthesis.
DR   UniPathway; UPA00164; -.
DR   PRO; PR:Q9Z1E4; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000003865; Expressed in 305 organ(s), highest expression level in soleus muscle.
DR   ExpressionAtlas; Q9Z1E4; baseline and differential.
DR   Genevisible; Q9Z1E4; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016234; C:inclusion body; IDA:MGI.
DR   GO; GO:0005536; F:glucose binding; ISO:MGI.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IMP:MGI.
DR   GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Complete proteome; Glycogen biosynthesis;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    738       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000194765.
FT   BINDING      39     39       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000269|PubMed:15561936}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     641    641       Phosphoserine; by DYRK2, GSK3-alpha,
FT                                GSK3-beta and PASK.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     645    645       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     649    649       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     652    652       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2RRU1}.
FT   MOD_RES     653    653       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     657    657       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     672    672       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     698    698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     709    709       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     711    711       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     722    722       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     724    724       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     728    728       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CONFLICT      3      3       L -> R (in Ref. 1; CAA64322).
FT                                {ECO:0000305}.
FT   CONFLICT     70     70       E -> V (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT     80     80       L -> M (in Ref. 3; BAE42275).
FT                                {ECO:0000305}.
FT   CONFLICT    111    112       GP -> D (in Ref. 1; CAA64322).
FT                                {ECO:0000305}.
FT   CONFLICT    120    120       G -> A (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT    148    148       A -> G (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT    154    155       FG -> YS (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT    191    191       C -> S (in Ref. 1; CAA64322).
FT                                {ECO:0000305}.
FT   CONFLICT    208    208       L -> V (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT    228    228       N -> I (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
FT   CONFLICT    581    582       QR -> HG (in Ref. 1; CAA64322).
FT                                {ECO:0000305}.
FT   CONFLICT    640    640       A -> V (in Ref. 2; AAD09457).
FT                                {ECO:0000305}.
SQ   SEQUENCE   738 AA;  83927 MW;  D1F9252CA908FF69 CRC64;
     MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH
     EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS SSTGGSKRSN SVDTGPSSSL
     STPTEPLSPT SSLGEERN
//
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