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Database: UniProt/SWISS-PROT
Entry: GYS1_MACMU
LinkDB: GYS1_MACMU
Original site: GYS1_MACMU 
ID   GYS1_MACMU              Reviewed;         737 AA.
AC   Q8MJ26;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   23-MAY-2018, entry version 79.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=GYS1; Synonyms=GYS;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Ortmeyer H.K., Marciani K.R., Hansen B.C.;
RT   "Monkey skeletal muscle glycogen synthase sequence.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC   -!- ENZYME 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: Phosphorylation at Ser-8 by AMPK inactivates the enzyme
CC       activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1
CC       and 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). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000305}.
DR   EMBL; AF529178; AAM93267.1; -; mRNA.
DR   RefSeq; NP_001028058.1; NM_001032886.1.
DR   UniGene; Mmu.3861; -.
DR   ProteinModelPortal; Q8MJ26; -.
DR   SMR; Q8MJ26; -.
DR   STRING; 9544.ENSMMUP00000005219; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   PRIDE; Q8MJ26; -.
DR   GeneID; 574233; -.
DR   KEGG; mcc:574233; -.
DR   CTD; 2997; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; Q8MJ26; -.
DR   KO; K00693; -.
DR   BRENDA; 2.4.1.11; 3126.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; 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   2: Evidence at transcript level;
KW   Allosteric enzyme; Complete proteome; Glycogen biosynthesis;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN         1    737       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000194764.
FT   BINDING      39     39       UDP-glucose. {ECO:0000250}.
FT   MOD_RES       8      8       Phosphoserine; by AMPK and PKA.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     412    412       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
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; 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     652    652       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:A2RRU1}.
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     672    672       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     698    698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     700    700       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     710    710       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     721    721       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     727    727       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
SQ   SEQUENCE   737 AA;  83787 MW;  B8B0B3114C58F56C CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EAPTPALKKT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     EWLAGIGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVALFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALSKAFPEH FTYEPSEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EDPRNGPLEE DSERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
     TPSEPLSPTS SLGEERN
//
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