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P54840 (GYS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen [starch] synthase, liver

EC=2.4.1.11
Gene names
Name:GYS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.

Catalytic activity

UDP-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.

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Post-translational modification

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.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Ontologies

Keywords
   Biological processGlycogen biosynthesis
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Glycogen storage disease
   Molecular functionGlycosyltransferase
Transferase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

generation of precursor metabolites and energy

Traceable author statement Ref.2. Source: ProtInc

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen biosynthetic process

Inferred from direct assay PubMed 1731614. Source: UniProtKB

response to glucose

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cortical actin cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

ectoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionglycogen (starch) synthase activity

Inferred from direct assay PubMed 1731614. Source: UniProtKB

glycogen synthase activity, transferring glucose-1-phosphate

Traceable author statement. Source: Reactome

protein homodimerization activity

Traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 703703Glycogen [starch] synthase, liver
PRO_0000194768

Sites

Binding site401UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by PKA By similarity
Modified residue6411Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6451Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6491Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6531Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6571Phosphoserine; by CK2 By similarity
Modified residue6831Phosphoserine By similarity

Natural variations

Natural variant391N → S in GSD0. Ref.2
VAR_007860
Natural variant1931A → T.
Corresponds to variant rs16924038 [ dbSNP | Ensembl ].
VAR_055885
Natural variant3391A → P in GSD0. Ref.2
VAR_007861
Natural variant3631M → V. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs2306180 [ dbSNP | Ensembl ].
VAR_058848
Natural variant4151D → E.
Corresponds to variant rs16924002 [ dbSNP | Ensembl ].
VAR_055886
Natural variant4461H → D in GSD0. Ref.2
VAR_007862
Natural variant4791P → Q in GSD0. Ref.2
VAR_007863
Natural variant4831S → P in GSD0. Ref.2
VAR_007864
Natural variant4911M → R in GSD0. Ref.2
VAR_007865

Experimental info

Sequence conflict971K → M in BAA06154. Ref.3
Sequence conflict1781Q → R in BAA06154. Ref.3
Sequence conflict1861I → V in BAA06154. Ref.3
Sequence conflict335 – 3362SN → FKT in BAA06154. Ref.3
Sequence conflict3441E → D in BAA06154. Ref.3
Sequence conflict4411P → A in BAA06154. Ref.3
Sequence conflict576 – 5772KQ → NM in BAA06154. Ref.3
Sequence conflict5831I → F in BAA06154. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P54840 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: 718F000D6D00CA4A

FASTA70380,989
        10         20         30         40         50         60 
MLRGRSLSVT SLGGLPQWEV EELPVEELLL FEVAWEVTNK VGGIYTVIQT KAKTTADEWG 

        70         80         90        100        110        120 
ENYFLIGPYF EHNMKTQVEQ CEPVNDAVRR AVDAMNKHGC QVHFGRWLIE GSPYVVLFDI 

       130        140        150        160        170        180 
GYSAWNLDRW KGDLWEACSV GIPYHDREAN DMLIFGSLTA WFLKEVTDHA DGKYVVAQFH 

       190        200        210        220        230        240 
EWQAGIGLIL SRARKLPIAT IFTTHATLLG RYLCAANIDF YNHLDKFNID KEAGERQIYH 

       250        260        270        280        290        300 
RYCMERASVH CAHVFTTVSE ITAIEAEHML KRKPDVVTPN GLNVKKFSAV HEFQNLHAMY 

       310        320        330        340        350        360 
KARIQDFVRG HFYGHLDFDL EKTLFLFIAG RYEFSNKGAD IFLESLSRLN FLLRMHKSDI 

       370        380        390        400        410        420 
TVMVFFIMPA KTNNFNVETL KGQAVRKQLW DVAHSVKEKF GKKLYDALLR GEIPDLNDIL 

       430        440        450        460        470        480 
DRDDLTIMKR AIFSTQRQSL PPVTTHNMID DSTDPILSTI RRIGLFNNRT DRVKVILHPE 

       490        500        510        520        530        540 
FLSSTSPLLP MDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSVTTN LSGFGCFMQE 

       550        560        570        580        590        600 
HVADPTAYGI YIVDRRFRSP DDSCNQLTKF LYGFCKQSRR QRIIQRNRTE RLSDLLDWRY 

       610        620        630        640        650        660 
LGRYYQHARH LTLSRAFPDK FHVELTSPPT TEGFKYPRPS SVPPSPSGSQ ASSPQSSDVE 

       670        680        690        700 
DEVEDERYDE EEEAERDRLN IKSPFSLSHV PHGKKKLHGE YKN 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of human liver glycogen synthase deduced by cDNA cloning."
Nuttall F.Q., Gannon M.C., Bai G., Lee E.Y.
Arch. Biochem. Biophys. 311:443-449(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-363.
Tissue: Liver.
[2]"Mutations in the liver glycogen synthase gene in children with hypoglycemia due to glycogen storage disease type 0."
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.
J. Clin. Invest. 102:507-515(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GSD0 SER-39; PRO-339; VAL-363; ASP-446; GLN-479; PRO-483 AND ARG-491.
[3]"Human liver glycogen synthase cDNA."
Nakabayashi H., Nakayama T.
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-363.
Tissue: Liver.
[4]"The finished DNA sequence of human chromosome 12."
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. expand/collapse author list , 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.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-363.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S70004 mRNA. Translation: AAB30886.1.
AJ003087 expand/collapse EMBL AC list , AJ003088, AJ003089, AJ003090, AJ003091, AJ003092, AJ003093, AJ003094, AJ003095, AJ003096, AJ003097, AJ003098, AJ003099, AJ003100, AJ003101, AJ003102 Genomic DNA. Translation: CAA05859.1.
D29685 mRNA. Translation: BAA06154.1.
AC006559 Genomic DNA. No translation available.
AC010197 Genomic DNA. No translation available.
AC022072 Genomic DNA. No translation available.
BC126310 mRNA. Translation: AAI26311.1.
BC126312 mRNA. Translation: AAI26313.1.
CCDSCCDS8690.1.
PIRS45686.
RefSeqNP_068776.2. NM_021957.3.
XP_005253409.1. XM_005253352.1.
XP_006719125.1. XM_006719062.1.
UniGeneHs.82614.

3D structure databases

ProteinModelPortalP54840.
SMRP54840. Positions 29-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109253. 3 interactions.
IntActP54840. 3 interactions.
STRING9606.ENSP00000261195.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteP54840.

Polymorphism databases

DMDM288558811.

Proteomic databases

MaxQBP54840.
PaxDbP54840.
PRIDEP54840.

Protocols and materials databases

DNASU2998.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261195; ENSP00000261195; ENSG00000111713.
GeneID2998.
KEGGhsa:2998.
UCSCuc001rfb.3. human.

Organism-specific databases

CTD2998.
GeneCardsGC12M021689.
H-InvDBHIX0036868.
HGNCHGNC:4707. GYS2.
HPAHPA039482.
MIM138571. gene.
240600. phenotype.
neXtProtNX_P54840.
Orphanet2089. Glycogen storage disease due to hepatic glycogen synthase deficiency.
PharmGKBPA29085.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000160890.
HOVERGENHBG001960.
InParanoidP54840.
KOK00693.
OMAEVSWEVT.
OrthoDBEOG741Z1N.
PhylomeDBP54840.
TreeFamTF300306.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00164.

Gene expression databases

BgeeP54840.
CleanExHS_GYS2.
GenevestigatorP54840.

Family and domain databases

InterProIPR008631. Glycogen_synth.
[Graphical view]
PANTHERPTHR10176. PTHR10176. 1 hit.
PfamPF05693. Glycogen_syn. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGYS2. human.
GenomeRNAi2998.
NextBio11888.
PROP54840.
SOURCESearch...

Entry information

Entry nameGYS2_HUMAN
AccessionPrimary (citable) accession number: P54840
Secondary accession number(s): A0AVD8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 9, 2010
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM