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Glycogen [starch] synthase, muscle (EC 2.4.1.11)

 GYS1_HUMAN              Reviewed;         737 AA.
P13807; Q9BTT9;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Glycogen [starch] synthase, muscle;
EC=2.4.1.11;
Name=GYS1; Synonyms=GYS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=2493642; DOI=10.1073/pnas.86.5.1443;
Browner M.F., Nakano K., Bang A.G., Fletterick R.J.;
"Human muscle glycogen synthase cDNA sequence: a negatively charged
protein with an asymmetric charge distribution.";
Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT NIDDM SER-464.
PubMed=7657035; DOI=10.2337/diab.44.9.1099;
Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.;
"Isolation and characterization of the human muscle glycogen synthase
gene.";
Diabetes 44:1099-1105(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Endometrium;
PubMed=9010351; DOI=10.1016/S0960-0760(96)00138-0;
Su X., Schuler L., Shapiro S.S.;
"Cloning and characterization of a glycogen synthase cDNA from human
endometrium.";
J. Steroid Biochem. Mol. Biol. 59:459-465(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, Lymph, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION AT SER-641, AND MUTAGENESIS OF SER-641 AND SER-645.
PubMed=16275910; DOI=10.1073/pnas.0508481102;
Wilson W.A., Skurat A.V., Probst B., de Paoli-Roach A., Roach P.J.,
Rutter J.;
"Control of mammalian glycogen synthase by PAS kinase.";
Proc. Natl. Acad. Sci. U.S.A. 102:16596-16601(2005).
[8]
INTERACTION WITH GYG1.
PubMed=17055998; DOI=10.1016/j.abb.2006.09.024;
Skurat A.V., Dietrich A.D., Roach P.J.;
"Interaction between glycogenin and glycogen synthase.";
Arch. Biochem. Biophys. 456:93-97(2006).
[9]
INVOLVEMENT IN GSD0B.
PubMed=17928598; DOI=10.1056/NEJMoa066691;
Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G.,
Jotorp P., Oldfors A., Holme E.;
"Cardiomyopathy and exercise intolerance in muscle glycogen storage
disease 0.";
N. Engl. J. Med. 357:1507-1514(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND
SER-649, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
PubMed=21668450; DOI=10.1111/j.1471-4159.2011.07345.x;
Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.;
"R3F, a novel membrane-associated glycogen targeting subunit of
protein phosphatase 1 regulates glycogen synthase in astrocytoma cells
in response to glucose and extracellular signals.";
J. Neurochem. 118:596-610(2011).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-710 AND
SER-727, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND THR-700, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
reducing end of alpha-1,4-glucan.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + ((1->4)-alpha-D-
glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
-!- ENZYME REGULATION: Allosteric activation by glucose-6-phosphate.
Phosphorylation reduces the activity towards UDP-glucose. When in
the non-phosphorylated state, glycogen synthase does not require
glucose-6-phosphate as an allosteric activator; when
phosphorylated it does (By similarity). {ECO:0007001}.
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
-!- SUBUNIT: Interacts with GYG1. {ECO:0000269|PubMed:17055998}.
-!- INTERACTION:
Q13155:AIMP2; NbExp=3; IntAct=EBI-740553, EBI-745226;
Q8IYA8:CCDC36; NbExp=7; IntAct=EBI-740553, EBI-8638439;
P49841:GSK3B; NbExp=4; IntAct=EBI-740553, EBI-373586;
P46976:GYG1; NbExp=7; IntAct=EBI-740553, EBI-740533;
Q5BKZ1:ZNF326; NbExp=4; IntAct=EBI-740553, EBI-2560158;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13807-1; Sequence=Displayed;
Name=2;
IsoId=P13807-2; Sequence=VSP_042745;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation at Ser-8 by AMPK inactivates the enzyme
activity. Primed phosphorylation at Ser-657 (site 5) by CSNK2A1
and CSNK2A2 is required for inhibitory phosphorylation at Ser-641
(site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site
4) by GSK3A an GSK3B (By similarity). Phosphorylated at Ser-641 by
DYRK2, leading to inactivation (By similarity). Phosphorylated at
Ser-641 by PASK, leading to inactivation; phosphorylation by PASK
is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645
by PP1 activates the enzyme. {ECO:0000269|PubMed:16275910,
ECO:0007001}.
-!- DISEASE: Muscle glycogen storage disease 0 (GSD0b) [MIM:611556]:
Metabolic disorder characterized by fasting hypoglycemia
presenting in infancy or early childhood. The role of muscle
glycogen is to provide critical energy during bursts of activity
and sustained muscle work. {ECO:0000269|PubMed:17928598}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
{ECO:0000320}.
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EMBL; J04501; AAA88046.1; -; mRNA.
EMBL; Z33622; CAA83916.1; -; Genomic_DNA.
EMBL; Z33623; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33609; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33624; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33625; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33626; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33610; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33627; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33628; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33629; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33630; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33631; CAA83916.1; JOINED; Genomic_DNA.
EMBL; Z33633; CAA83916.1; JOINED; Genomic_DNA.
EMBL; U32573; AAB60385.1; -; mRNA.
EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52424.1; -; Genomic_DNA.
EMBL; BC002617; AAH02617.1; -; mRNA.
EMBL; BC003182; AAH03182.1; -; mRNA.
EMBL; BC007688; AAH07688.1; -; mRNA.
CCDS; CCDS12747.1; -. [P13807-1]
CCDS; CCDS54292.1; -. [P13807-2]
PIR; A32156; A32156.
RefSeq; NP_001155059.1; NM_001161587.1. [P13807-2]
RefSeq; NP_002094.2; NM_002103.4. [P13807-1]
UniGene; Hs.386225; -.
ProteinModelPortal; P13807; -.
SMR; P13807; -.
BioGrid; 109252; 36.
IntAct; P13807; 54.
MINT; MINT-1451793; -.
STRING; 9606.ENSP00000317904; -.
BindingDB; P13807; -.
ChEMBL; CHEMBL4000; -.
CAZy; GT3; Glycosyltransferase Family 3.
iPTMnet; P13807; -.
PhosphoSitePlus; P13807; -.
BioMuta; GYS1; -.
DMDM; 1351366; -.
EPD; P13807; -.
MaxQB; P13807; -.
PaxDb; P13807; -.
PeptideAtlas; P13807; -.
PRIDE; P13807; -.
DNASU; 2997; -.
Ensembl; ENST00000263276; ENSP00000263276; ENSG00000104812. [P13807-2]
Ensembl; ENST00000323798; ENSP00000317904; ENSG00000104812. [P13807-1]
GeneID; 2997; -.
KEGG; hsa:2997; -.
UCSC; uc002plp.4; human. [P13807-1]
CTD; 2997; -.
DisGeNET; 2997; -.
EuPathDB; HostDB:ENSG00000104812.14; -.
GeneCards; GYS1; -.
HGNC; HGNC:4706; GYS1.
HPA; CAB007793; -.
HPA; HPA041598; -.
MalaCards; GYS1; -.
MIM; 138570; gene.
MIM; 611556; phenotype.
neXtProt; NX_P13807; -.
OpenTargets; ENSG00000104812; -.
Orphanet; 137625; Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
PharmGKB; PA29084; -.
eggNOG; KOG3742; Eukaryota.
eggNOG; COG0438; LUCA.
GeneTree; ENSGT00390000018612; -.
HOGENOM; HOG000160890; -.
HOVERGEN; HBG001960; -.
InParanoid; P13807; -.
KO; K00693; -.
OMA; KVYFGRW; -.
OrthoDB; EOG091G0304; -.
PhylomeDB; P13807; -.
TreeFam; TF300306; -.
BioCyc; MetaCyc:HS02622-MONOMER; -.
BRENDA; 2.4.1.11; 2681.
Reactome; R-HSA-3322077; Glycogen synthesis.
Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
Reactome; R-HSA-3814836; Glycogen storage disease type XV (GYG1).
Reactome; R-HSA-3828062; Glycogen storage disease type 0 (muscle GYS1).
Reactome; R-HSA-3878781; Glycogen storage disease type IV (GBE1).
SIGNOR; P13807; -.
UniPathway; UPA00164; -.
ChiTaRS; GYS1; human.
GenomeRNAi; 2997; -.
PRO; PR:P13807; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104812; -.
CleanEx; HS_GYS1; -.
ExpressionAtlas; P13807; baseline and differential.
Genevisible; P13807; HS.
GO; GO:0005829; C:cytosol; IBA:Reactome.
GO; GO:0016234; C:inclusion body; RCA:Ensembl.
GO; GO:0016020; C:membrane; HTP:UniProtKB.
GO; GO:0005536; F:glucose binding; RCA:Ensembl.
GO; GO:0004373; F:glycogen (starch) synthase activity; HTP:UniProtKB.
GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; EXP:Reactome.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0005978; P:glycogen biosynthetic process; HTP:UniProtKB.
GO; GO:0007507; P:heart development; RCA:Ensembl.
CDD; cd03793; GT1_Glycogen_synthase_GSY2_lik; 1.
InterPro; IPR008631; Glycogen_synth.
PANTHER; PTHR10176; PTHR10176; 1.
Pfam; PF05693; Glycogen_syn; 1.
1: Evidence at protein level;
Allosteric enzyme; Alternative splicing; Complete proteome;
Diabetes mellitus; Disease mutation; Glycogen biosynthesis;
Glycosyltransferase; Phosphoprotein; Polymorphism; Reference proteome;
Transferase.
CHAIN 1 737 Glycogen [starch] synthase, muscle.
/FTId=PRO_0000194763.
BINDING 39 39 UDP-glucose. {ECO:0007001}.
MOD_RES 8 8 Phosphoserine; by AMPK and PKA.
{ECO:0007001|UniProtKB:Q9Z1E4}.
MOD_RES 11 11 Phosphoserine.
{ECO:0007001|UniProtKB:P13834}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000307|PubMed:23186163,
ECO:0000307|PubMed:24275569}.
MOD_RES 641 641 Phosphoserine.
{ECO:0000269|PubMed:16275910,
ECO:0000307|PubMed:18669648}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000307|PubMed:18669648}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000307|PubMed:18669648}.
MOD_RES 652 652 Phosphoserine.
{ECO:0007001|UniProtKB:A2RRU1}.
MOD_RES 653 653 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0007001|UniProtKB:P13834}.
MOD_RES 657 657 Phosphoserine; by CK2.
{ECO:0007001|UniProtKB:P13834}.
MOD_RES 698 698 Phosphoserine.
{ECO:0007001|UniProtKB:P13834}.
MOD_RES 700 700 Phosphothreonine.
{ECO:0000307|PubMed:24275569}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000307|PubMed:23186163}.
MOD_RES 721 721 Phosphothreonine.
{ECO:0007001|UniProtKB:Q9Z1E4}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000307|PubMed:19690332,
ECO:0000307|PubMed:23186163}.
VAR_SEQ 101 164 Missing (in isoform 2).
{ECO:0000319|PubMed:15489334}.
/FTId=VSP_042745.
VARIANT 108 108 I -> M (in dbSNP:rs5455).
/FTId=VAR_037958.
VARIANT 130 130 K -> E (in dbSNP:rs5456).
/FTId=VAR_014727.
VARIANT 283 283 N -> S (in dbSNP:rs5461).
/FTId=VAR_014728.
VARIANT 359 359 E -> G (in dbSNP:rs5465).
/FTId=VAR_014729.
VARIANT 416 416 M -> V (in dbSNP:rs5447).
/FTId=VAR_014730.
VARIANT 464 464 G -> S (in NIDDM; dbSNP:rs200862074).
{ECO:0000269|PubMed:7657035}.
/FTId=VAR_007859.
VARIANT 619 619 E -> Q (in dbSNP:rs5450).
/FTId=VAR_014731.
VARIANT 691 691 P -> A (in dbSNP:rs5453).
/FTId=VAR_014732.
MUTAGEN 641 641 S->A: Abolishes PASK-mediated
phosphorylation.
{ECO:0000269|PubMed:16275910}.
MUTAGEN 645 645 S->A: Does not affect PASK-mediated
phosphorylation.
{ECO:0000269|PubMed:16275910}.
CONFLICT 136 136 T -> I (in Ref. 1; AAA88046 and 3;
AAB60385). {ECO:0000320}.
CONFLICT 462 462 Missing (in Ref. 3; AAB60385).
{ECO:0000320}.
CONFLICT 608 608 A -> D (in Ref. 3; AAB60385).
{ECO:0000320}.
CONFLICT 706 706 S -> R (in Ref. 1; AAA88046 and 3;
AAB60385). {ECO:0000320}.
SEQUENCE 737 AA; 83786 MW; 0E321BBFDEB0BD7F CRC64;
MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
NYFLVGPYTE QGVRTQVELL EAPTPALKRT 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 VMGIPSISTN LSGFGCFMEE
HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS
TPSEPLSPTS SLGEERN


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CSB-EL010079RA Rat Glycogen [starch] synthase, liver(GYS2) ELISA kit SpeciesRat 96T
CSB-EL010079MO Mouse Glycogen [starch] synthase, liver(GYS2) ELISA kit 96T
CSB-EL010079MO Mouse Glycogen [starch] synthase, liver(GYS2) ELISA kit SpeciesMouse 96T
CSB-EL010079HU Human Glycogen [starch] synthase, liver(GYS2) ELISA kit SpeciesHuman 96T
GYS2_MOUSE ELISA Kit FOR Glycogen [starch] synthase, liver; organism: Mouse; gene name: Gys2 96T
GZF1 GYS1 Gene glycogen synthase 1 (muscle)
Y050445 Anti_Human Muscle Glycogen Synthase phospho_ser640 100ug
AP07589PU-N Glycogen Synthase 1 (Muscle) (GYS1) pSer64 50 µg
201-20-2456 GYS1{glycogen synthase 1 (muscle)}rabbit.pAb 0.2ml


 

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