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Database: UniProt/SWISS-PROT
Entry: GYS2_MOUSE
LinkDB: GYS2_MOUSE
Original site: GYS2_MOUSE 
ID   GYS2_MOUSE              Reviewed;         704 AA.
AC   Q8VCB3; Q3UTY0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-FEB-2019, entry version 110.
DE   RecName: Full=Glycogen [starch] synthase, liver;
DE            EC=2.4.1.11;
GN   Name=Gys2;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, and Liver;
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).
RN   [6]
RP   INDUCTION.
RX   PubMed=20430893; DOI=10.1074/jbc.M110.110361;
RA   Doi R., Oishi K., Ishida N.;
RT   "CLOCK regulates circadian rhythms of hepatic glycogen synthesis
RT   through transcriptional activation of Gys2.";
RL   J. Biol. Chem. 285:22114-22121(2010).
RN   [7]
RP   BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, INTERACTION WITH
RP   GYG1, AND MUTAGENESIS OF SER-8; TRP-135; GLY-141; TYR-239; CYS-243 AND
RP   GLU-510.
RX   PubMed=24982189; DOI=10.1073/pnas.1402926111;
RA   Zeqiraj E., Tang X., Hunter R.W., Garcia-Rocha M., Judd A., Deak M.,
RA   von Wilamowitz-Moellendorff A., Kurinov I., Guinovart J.J., Tyers M.,
RA   Sakamoto K., Sicheri F.;
RT   "Structural basis for the recruitment of glycogen synthase by
RT   glycogenin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:E2831-2840(2014).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan.
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         Evidence={ECO:0000269|PubMed:24982189};
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).
CC       {ECO:0000250|UniProtKB:P13834}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.48 mM for UDP-glucose (at 30 degrees Celsius)
CC         {ECO:0000269|PubMed:24982189};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1 (via C-terminus); required for GYS2-
CC       mediated glycogen synthesis. {ECO:0000269|PubMed:24982189}.
CC   -!- INDUCTION: Expression in the liver oscillates in a circadian
CC       manner with peak levels during the night.
CC       {ECO:0000269|PubMed:20430893}.
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 (By similarity). Dephosphorylation at Ser-641
CC       and Ser-645 by PP1 activates the enzyme (By similarity).
CC       Phosphorylation at Ser-8 is not required for interaction with GYG1
CC       (PubMed:24982189). Interaction with GYG1 does not regulate the
CC       phosphorylation at Ser-8 and Ser-641 (PubMed:24982189).
CC       {ECO:0000250|UniProtKB:P13807, ECO:0000250|UniProtKB:P13834,
CC       ECO:0000269|PubMed:24982189}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; AK138992; BAE23850.1; -; mRNA.
DR   EMBL; BC021322; AAH21322.1; -; mRNA.
DR   EMBL; BC158081; AAI58082.1; -; mRNA.
DR   CCDS; CCDS20683.1; -.
DR   RefSeq; NP_663547.2; NM_145572.2.
DR   UniGene; Mm.275975; -.
DR   ProteinModelPortal; Q8VCB3; -.
DR   SMR; Q8VCB3; -.
DR   IntAct; Q8VCB3; 2.
DR   MINT; Q8VCB3; -.
DR   STRING; 10090.ENSMUSP00000032371; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   iPTMnet; Q8VCB3; -.
DR   PhosphoSitePlus; Q8VCB3; -.
DR   SwissPalm; Q8VCB3; -.
DR   jPOST; Q8VCB3; -.
DR   MaxQB; Q8VCB3; -.
DR   PaxDb; Q8VCB3; -.
DR   PeptideAtlas; Q8VCB3; -.
DR   PRIDE; Q8VCB3; -.
DR   Ensembl; ENSMUST00000032371; ENSMUSP00000032371; ENSMUSG00000030244.
DR   GeneID; 232493; -.
DR   KEGG; mmu:232493; -.
DR   UCSC; uc009epi.2; mouse.
DR   CTD; 2998; -.
DR   MGI; MGI:2385254; Gys2.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; Q8VCB3; -.
DR   KO; K00693; -.
DR   OMA; TADEWGD; -.
DR   OrthoDB; 264593at2759; -.
DR   TreeFam; TF300306; -.
DR   Reactome; R-MMU-3322077; Glycogen synthesis.
DR   UniPathway; UPA00164; -.
DR   PRO; PR:Q8VCB3; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   Bgee; ENSMUSG00000030244; Expressed in 51 organ(s), highest expression level in liver.
DR   ExpressionAtlas; Q8VCB3; baseline and differential.
DR   Genevisible; Q8VCB3; MM.
DR   GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043265; C:ectoplasm; ISS:UniProtKB.
DR   GO; GO:0005536; F:glucose binding; ISO:MGI.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0005977; P:glycogen metabolic process; ISO:MGI.
DR   GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
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    704       Glycogen [starch] synthase, liver.
FT                                /FTId=PRO_0000274489.
FT   BINDING      40     40       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000250|UniProtKB:P17625}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     627    627       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P54840}.
FT   MOD_RES     641    641       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     645    645       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     649    649       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     653    653       Phosphoserine; by GSK3-alpha and GSK3-
FT                                beta. {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     657    657       Phosphoserine; by CK2.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     684    684       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355}.
FT   MUTAGEN       8      8       S->A: Abolishes phosphorylation. No
FT                                effect on the interaction with GYG1. Does
FT                                not affect the result of other mutations;
FT                                when associated with A-135; R-135; R-141;
FT                                A-239; A-243; or R-243.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     135    135       W->A: No effect on the interaction with
FT                                GYG1. No effect on the interaction with
FT                                GYG1; when associated with A-8.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     135    135       W->R: Loss of interaction with GYG1. Loss
FT                                of interaction with GYG1; when associated
FT                                with A-8. {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     141    141       G->R: Loss of interaction with GYG1. Loss
FT                                of function. Loss of interaction with
FT                                GYG1; when associated with A-8.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     239    239       Y->A: Loss of interaction with GYG1. Loss
FT                                of function. Loss of interaction with
FT                                GYG1; when associated with A-8.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     243    243       C->A: No effect on the interaction with
FT                                GYG1. Loss of interaction with GYG1; when
FT                                associated with A-8.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     243    243       C->R: Loss of interaction with GYG1. Loss
FT                                of function. Loss of interaction with
FT                                GYG1; when associated with A-8.
FT                                {ECO:0000269|PubMed:24982189}.
FT   MUTAGEN     510    510       E->A: Loss of catalytic activity.
FT                                {ECO:0000269|PubMed:24982189}.
FT   CONFLICT    630    630       T -> M (in Ref. 2; AAH21322).
FT                                {ECO:0000305}.
FT   CONFLICT    656    656       C -> S (in Ref. 2; AAH21322).
FT                                {ECO:0000305}.
SQ   SEQUENCE   704 AA;  80871 MW;  C4B87195B5FC41FE CRC64;
     MLRGRSLSVT SLGGLPVWEA ERLPVEDLLL FEVSWEVTNK VGGICTVIQT KAKTTADEWG
     ENYFLIGPYF EHNMKTQVEQ CEPTNDAVRK AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI
     SSSAWNLDRW KGDFWEACGV GIPHHDREAN DMLIFGSLTA WFLKEVTDHA DGKHVIAQFH
     EWQAGTGLIL SRARKLPIAT VFTTHATLLG RYLCAANIDF YNQLDKFDID KEAGERQIYH
     RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY
     KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSNV
     TVVVFFIMPA KTNNFNVETL KGQAVRKQLW DTVHCLKEKF GKKLYDGLLR GEIPDMNSIL
     DRDDLTIMKR AIFSTQRQSL PPVTTHNMID DSTDPILSTI RRIGLFNNRA DRVKVILHPE
     FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFVQE
     HVADPTAYGI YIVDRRFRSP DDSCNQLTQF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY
     LGRYYQHARH LTLSRAFPDK FHLEPTSPPT TDGFKYPRPS SVPPSPSGSQ ASSPQCSDAE
     DEEDEDERYD EEEEAERDRL NIKSPFSLNH FPKGKKKLHG EYKN
//
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