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 03-AUG-2022, entry version 162.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 synthase
RT kinase in skeletal muscle and is responsive to glucose 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 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 = [(1->4)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:58223, 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 the
CC non-phosphorylated state, glycogen synthase does not require glucose-6-
CC phosphate as an allosteric activator; when phosphorylated it does (By
CC 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 CSNK2A2
CC is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-
CC 645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an
CC GSK3B. Phosphorylated at Ser-641 by PASK, leading to inactivation;
CC phosphorylation by PASK is inhibited by glycogen. Phosphorylated at
CC Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641
CC and Ser-645 by PP1 activates the enzyme (By similarity).
CC Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity.
CC {ECO:0000250, ECO:0000269|PubMed:15561936}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 3 family. {ECO:0000305}.
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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 AlphaFoldDB; Q9Z1E4; -.
DR SMR; Q9Z1E4; -.
DR BioGRID; 200132; 18.
DR IntAct; Q9Z1E4; 4.
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 ProteomicsDB; 271352; -.
DR Antibodypedia; 3582; 416 antibodies from 39 providers.
DR DNASU; 14936; -.
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 VEuPathDB; HostDB:ENSMUSG00000003865; -.
DR eggNOG; KOG3742; Eukaryota.
DR GeneTree; ENSGT00390000018612; -.
DR InParanoid; Q9Z1E4; -.
DR OMA; YFFTSGR; -.
DR OrthoDB; 264593at2759; -.
DR PhylomeDB; Q9Z1E4; -.
DR TreeFam; TF300306; -.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 14936; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Gys1; mouse.
DR PRO; PR:Q9Z1E4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z1E4; protein.
DR Bgee; ENSMUSG00000003865; Expressed in plantaris and 259 other tissues.
DR ExpressionAtlas; Q9Z1E4; baseline and differential.
DR Genevisible; Q9Z1E4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; 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; IDA:MGI.
DR GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
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; Glycogen biosynthesis; Glycosyltransferase;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..738
FT /note="Glycogen [starch] synthase, muscle"
FT /id="PRO_0000194765"
FT REGION 632..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine; by AMPK and PKA"
FT /evidence="ECO:0000269|PubMed:15561936"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and
FT PASK"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2RRU1"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13834"
FT MOD_RES 709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13807"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 3
FT /note="L -> R (in Ref. 1; CAA64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> V (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> M (in Ref. 3; BAE42275)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..112
FT /note="GP -> D (in Ref. 1; CAA64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="G -> A (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> G (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..155
FT /note="FG -> YS (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="C -> S (in Ref. 1; CAA64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="L -> V (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="N -> I (in Ref. 2; AAD09457)"
FT /evidence="ECO:0000305"
FT CONFLICT 581..582
FT /note="QR -> HG (in Ref. 1; CAA64322)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="A -> V (in Ref. 2; AAD09457)"
FT /evidence="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
