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Database: UniProt/SWISS-PROT
Entry: GYS1_BOVIN
LinkDB: GYS1_BOVIN
Original site: GYS1_BOVIN 
ID   GYS1_BOVIN              Reviewed;         736 AA.
AC   A7MB78;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   05-DEC-2018, entry version 72.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=GYS1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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:
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: 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; BC151381; AAI51382.1; -; mRNA.
DR   RefSeq; NP_001094769.1; NM_001101299.1.
DR   UniGene; Bt.102939; -.
DR   UniGene; Bt.37378; -.
DR   ProteinModelPortal; A7MB78; -.
DR   SMR; A7MB78; -.
DR   STRING; 9913.ENSBTAP00000007423; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   PaxDb; A7MB78; -.
DR   PRIDE; A7MB78; -.
DR   Ensembl; ENSBTAT00000007423; ENSBTAP00000007423; ENSBTAG00000039958.
DR   GeneID; 786335; -.
DR   KEGG; bta:786335; -.
DR   CTD; 2997; -.
DR   VGNC; VGNC:29730; GYS1.
DR   eggNOG; KOG3742; Eukaryota.
DR   eggNOG; COG0438; LUCA.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HOG000160890; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; A7MB78; -.
DR   KO; K00693; -.
DR   OMA; GHFYGHM; -.
DR   OrthoDB; EOG091G0304; -.
DR   TreeFam; TF300306; -.
DR   Reactome; R-BTA-3322077; Glycogen synthesis.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000039958; Expressed in 9 organ(s), highest expression level in skeletal muscle tissue.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
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    736       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000358311.
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     698    698       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13834}.
FT   MOD_RES     700    700       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     709    709       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
FT   MOD_RES     720    720       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Z1E4}.
FT   MOD_RES     726    726       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P13807}.
SQ   SEQUENCE   736 AA;  83814 MW;  22300D8723EF94BD CRC64;
     MPLNRTLSMS SLPGLEDWED EFDLENTVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH
     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 VMGIPSVSTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPEY FTYEPHEADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPRDLPPDE DDERYDEDEE AAKDRRNIRA PEWPRRASCT SSTGSKRGSV DTAPSSSVST
     PSEPLSPASS LGEERN
//
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