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Glycogen [starch] synthase, liver (EC 2.4.1.11)

 GYS2_HUMAN              Reviewed;         703 AA.
P54840; A0AVD8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 2.
27-SEP-2017, entry version 156.
RecName: Full=Glycogen [starch] synthase, liver;
EC=2.4.1.11;
Name=GYS2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-363.
TISSUE=Liver;
PubMed=8203908; DOI=10.1006/abbi.1994.1260;
Nuttall F.Q., Gannon M.C., Bai G., Lee E.Y.;
"Primary structure of human liver glycogen synthase deduced by cDNA
cloning.";
Arch. Biochem. Biophys. 311:443-449(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GSD0 SER-39; PRO-339;
VAL-363; ASP-446; GLN-479; PRO-483 AND ARG-491.
PubMed=9691087; DOI=10.1172/JCI2890;
Orho M., Bosshard N.U., Buist N.R.M., Gitzelmann R., Aynsley-Green A.,
Blumel P., Gannon M.C., Nuttall F.Q., Groop L.C.;
"Mutations in the liver glycogen synthase gene in children with
hypoglycemia due to glycogen storage disease type 0.";
J. Clin. Invest. 102:507-515(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-363.
TISSUE=Liver;
Nakabayashi H., Nakayama T.;
"Human liver glycogen synthase cDNA.";
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-363.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627 AND SER-683, 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:0000250}.
-!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
-!- SUBUNIT: Interacts with GYG1 (via C-terminus); required for GYS2-
mediated glycogen synthesis. {ECO:0000250|UniProtKB:Q8VCB3}.
-!- PTM: 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. Dephosphorylation at Ser-641 and Ser-645 by
PP1 activates the enzyme (By similarity). Phosphorylation at Ser-8
is not required for interaction with GYG1 (By similarity).
Interaction with GYG1 does not regulate the phosphorylation at
Ser-8 and Ser-641 (By similarity). {ECO:0000250|UniProtKB:P13807,
ECO:0000250|UniProtKB:P13834, ECO:0000250|UniProtKB:Q8VCB3}.
-!- DISEASE: Glycogen storage disease 0 (GSD0) [MIM:240600]: A
metabolic disorder characterized by fasting hypoglycemia
presenting in infancy or early childhood, high blood ketones and
low alanine and lactate concentrations. Although feeding relieves
symptoms, it often results in postprandial hyperglycemia and
hyperlactatemia. {ECO:0000269|PubMed:9691087}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S70004; AAB30886.1; -; mRNA.
EMBL; AJ003087; CAA05859.1; -; Genomic_DNA.
EMBL; AJ003088; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003089; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003090; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003091; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003092; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003093; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003094; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003095; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003096; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003097; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003098; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003099; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003100; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003101; CAA05859.1; JOINED; Genomic_DNA.
EMBL; AJ003102; CAA05859.1; JOINED; Genomic_DNA.
EMBL; D29685; BAA06154.1; -; mRNA.
EMBL; AC006559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC126310; AAI26311.1; -; mRNA.
EMBL; BC126312; AAI26313.1; -; mRNA.
CCDS; CCDS8690.1; -.
PIR; S45686; S45686.
RefSeq; NP_068776.2; NM_021957.3.
UniGene; Hs.82614; -.
ProteinModelPortal; P54840; -.
SMR; P54840; -.
BioGrid; 109253; 6.
IntAct; P54840; 4.
STRING; 9606.ENSP00000261195; -.
CAZy; GT3; Glycosyltransferase Family 3.
iPTMnet; P54840; -.
PhosphoSitePlus; P54840; -.
BioMuta; GYS2; -.
DMDM; 288558811; -.
EPD; P54840; -.
MaxQB; P54840; -.
PaxDb; P54840; -.
PeptideAtlas; P54840; -.
PRIDE; P54840; -.
DNASU; 2998; -.
Ensembl; ENST00000261195; ENSP00000261195; ENSG00000111713.
GeneID; 2998; -.
KEGG; hsa:2998; -.
UCSC; uc001rfb.3; human.
CTD; 2998; -.
DisGeNET; 2998; -.
EuPathDB; HostDB:ENSG00000111713.2; -.
GeneCards; GYS2; -.
H-InvDB; HIX0036868; -.
HGNC; HGNC:4707; GYS2.
HPA; HPA039482; -.
MalaCards; GYS2; -.
MIM; 138571; gene.
MIM; 240600; phenotype.
neXtProt; NX_P54840; -.
OpenTargets; ENSG00000111713; -.
Orphanet; 2089; Glycogen storage disease due to hepatic glycogen synthase deficiency.
PharmGKB; PA29085; -.
eggNOG; KOG3742; Eukaryota.
eggNOG; COG0438; LUCA.
GeneTree; ENSGT00390000018612; -.
HOGENOM; HOG000160890; -.
HOVERGEN; HBG001960; -.
InParanoid; P54840; -.
KO; K00693; -.
OMA; TADEWGD; -.
OrthoDB; EOG091G0304; -.
PhylomeDB; P54840; -.
TreeFam; TF300306; -.
Reactome; R-HSA-3322077; Glycogen synthesis.
Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
Reactome; R-HSA-3858516; Glycogen storage disease type 0 (liver GYS2).
Reactome; R-HSA-3878781; Glycogen storage disease type IV (GBE1).
UniPathway; UPA00164; -.
ChiTaRS; GYS2; human.
GenomeRNAi; 2998; -.
PRO; PR:P54840; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111713; -.
CleanEx; HS_GYS2; -.
Genevisible; P54840; HS.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0043265; C:ectoplasm; ISS:UniProtKB.
GO; GO:0004373; F:glycogen (starch) synthase activity; IDA:UniProtKB.
GO; GO:0061547; F:glycogen synthase activity, transferring glucose-1-phosphate; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
GO; GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB.
GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
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; Complete proteome; Disease mutation;
Glycogen biosynthesis; Glycogen storage disease; Glycosyltransferase;
Phosphoprotein; Polymorphism; Reference proteome; Transferase.
CHAIN 1 703 Glycogen [starch] synthase, liver.
/FTId=PRO_0000194768.
BINDING 40 40 UDP-glucose. {ECO:0000250}.
MOD_RES 8 8 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P17625}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VCB3}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 641 641 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000250}.
MOD_RES 645 645 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000250}.
MOD_RES 649 649 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000250}.
MOD_RES 653 653 Phosphoserine; by GSK3-alpha and GSK3-
beta. {ECO:0000250}.
MOD_RES 657 657 Phosphoserine; by CK2. {ECO:0000250}.
MOD_RES 683 683 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 39 39 N -> S (in GSD0; dbSNP:rs121918423).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007860.
VARIANT 193 193 A -> T (in dbSNP:rs16924038).
/FTId=VAR_055885.
VARIANT 339 339 A -> P (in GSD0; dbSNP:rs121918421).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007861.
VARIANT 363 363 M -> V (in dbSNP:rs2306180).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8203908,
ECO:0000269|PubMed:9691087,
ECO:0000269|Ref.3}.
/FTId=VAR_058848.
VARIANT 415 415 D -> E (in dbSNP:rs16924002).
/FTId=VAR_055886.
VARIANT 446 446 H -> D (in GSD0; dbSNP:rs121918425).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007862.
VARIANT 479 479 P -> Q (in GSD0; dbSNP:rs121918420).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007863.
VARIANT 483 483 S -> P (in GSD0; dbSNP:rs121918424).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007864.
VARIANT 491 491 M -> R (in GSD0; dbSNP:rs121918422).
{ECO:0000269|PubMed:9691087}.
/FTId=VAR_007865.
CONFLICT 97 97 K -> M (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 178 178 Q -> R (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 186 186 I -> V (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 335 336 SN -> FKT (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 344 344 E -> D (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 441 441 P -> A (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 576 577 KQ -> NM (in Ref. 3; BAA06154).
{ECO:0000305}.
CONFLICT 583 583 I -> F (in Ref. 3; BAA06154).
{ECO:0000305}.
SEQUENCE 703 AA; 80989 MW; 718F000D6D00CA4A CRC64;
MLRGRSLSVT SLGGLPQWEV EELPVEELLL FEVAWEVTNK VGGIYTVIQT KAKTTADEWG
ENYFLIGPYF EHNMKTQVEQ CEPVNDAVRR AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI
GYSAWNLDRW KGDLWEACSV GIPYHDREAN DMLIFGSLTA WFLKEVTDHA DGKYVVAQFH
EWQAGIGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNHLDKFNID KEAGERQIYH
RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY
KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSDI
TVMVFFIMPA KTNNFNVETL KGQAVRKQLW DVAHSVKEKF GKKLYDALLR GEIPDLNDIL
DRDDLTIMKR AIFSTQRQSL PPVTTHNMID DSTDPILSTI RRIGLFNNRT DRVKVILHPE
FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE
HVADPTAYGI YIVDRRFRSP DDSCNQLTKF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY
LGRYYQHARH LTLSRAFPDK FHVELTSPPT TEGFKYPRPS SVPPSPSGSQ ASSPQSSDVE
DEVEDERYDE EEEAERDRLN IKSPFSLSHV PHGKKKLHGE YKN


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