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P13807 (GYS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycogen [starch] synthase, muscle

EC=2.4.1.11
Gene names
Name:GYS1
Synonyms:GYS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

Interacts with GYG1. Ref.8

Post-translational modification

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. Ref.7 Ref.15

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

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GSK3BP498413EBI-740553,EBI-373586
GYG1P469764EBI-740553,EBI-740533

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13807-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P13807-2)

The sequence of this isoform differs from the canonical sequence as follows:
     101-164: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 737736Glycogen [starch] synthase, muscle
PRO_0000194763

Sites

Binding site391UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by AMPK and PKA By similarity
Modified residue111Phosphoserine By similarity
Modified residue6411Phosphoserine Ref.7 Ref.11 Ref.15
Modified residue6451Phosphoserine Ref.11 Ref.15
Modified residue6491Phosphoserine Ref.11
Modified residue6531Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residue6571Phosphoserine; by CK2 By similarity
Modified residue6981Phosphoserine By similarity
Modified residue7271Phosphoserine Ref.13

Natural variations

Alternative sequence101 – 16464Missing in isoform 2.
VSP_042745
Natural variant1081I → M.
Corresponds to variant rs5455 [ dbSNP | Ensembl ].
VAR_037958
Natural variant1301K → E.
Corresponds to variant rs5456 [ dbSNP | Ensembl ].
VAR_014727
Natural variant2831N → S.
Corresponds to variant rs5461 [ dbSNP | Ensembl ].
VAR_014728
Natural variant3591E → G.
Corresponds to variant rs5465 [ dbSNP | Ensembl ].
VAR_014729
Natural variant4161M → V.
Corresponds to variant rs5447 [ dbSNP | Ensembl ].
VAR_014730
Natural variant4641G → S in NIDDM. Ref.2
VAR_007859
Natural variant6191E → Q.
Corresponds to variant rs5450 [ dbSNP | Ensembl ].
VAR_014731
Natural variant6911P → A.
Corresponds to variant rs5453 [ dbSNP | Ensembl ].
VAR_014732

Experimental info

Mutagenesis6411S → A: Abolishes PASK-mediated phosphorylation. Ref.7
Mutagenesis6451S → A: Does not affect PASK-mediated phosphorylation. Ref.7
Sequence conflict1361T → I in AAA88046. Ref.1
Sequence conflict1361T → I in AAB60385. Ref.3
Sequence conflict4621Missing in AAB60385. Ref.3
Sequence conflict6081A → D in AAB60385. Ref.3
Sequence conflict7061S → R in AAA88046. Ref.1
Sequence conflict7061S → R in AAB60385. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 0E321BBFDEB0BD7F

FASTA73783,786
        10         20         30         40         50         60 
MPLNRTLSMS SLPGLEDWED EFDLENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD 

        70         80         90        100        110        120 
NYFLVGPYTE QGVRTQVELL EAPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 

       130        140        150        160        170        180 
ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQSE EKPHVVAHFH 

       190        200        210        220        230        240 
EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH 

       250        260        270        280        290        300 
RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 

       310        320        330        340        350        360 
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ 

       370        380        390        400        410        420 
TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML 

       430        440        450        460        470        480 
DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE 

       490        500        510        520        530        540 
FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE 

       550        560        570        580        590        600 
HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 

       610        620        630        640        650        660 
LGRYYMSARH MALSKAFPEH FTYEPNEADA AQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 

       670        680        690        700        710        720 
EDPRNGPLEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSTSGSKRNS VDTATSSSLS 

       730 
TPSEPLSPTS SLGEERN 

« Hide

Isoform 2 [UniParc].

Checksum: 8C059070E0D075FC
Show »

FASTA67376,483

References

« Hide 'large scale' references
[1]"Human muscle glycogen synthase cDNA sequence: a negatively charged protein with an asymmetric charge distribution."
Browner M.F., Nakano K., Bang A.G., Fletterick R.J.
Proc. Natl. Acad. Sci. U.S.A. 86:1443-1447(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Muscle.
[2]"Isolation and characterization of the human muscle glycogen synthase gene."
Orho M., Nikula-Ijas P., Schalin-Jantti C., Permutt M.A., Groop L.C.
Diabetes 44:1099-1105(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NIDDM SER-464.
[3]"Cloning and characterization of a glycogen synthase cDNA from human endometrium."
Su X., Schuler L., Shapiro S.S.
J. Steroid Biochem. Mol. Biol. 59:459-465(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Endometrium.
[4]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Kidney, Lymph and Skin.
[7]"Control of mammalian glycogen synthase by PAS kinase."
Wilson W.A., Skurat A.V., Probst B., de Paoli-Roach A., Roach P.J., Rutter J.
Proc. Natl. Acad. Sci. U.S.A. 102:16596-16601(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-641, MUTAGENESIS OF SER-641 AND SER-645.
[8]"Interaction between glycogenin and glycogen synthase."
Skurat A.V., Dietrich A.D., Roach P.J.
Arch. Biochem. Biophys. 456:93-97(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GYG1.
[9]"Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0."
Kollberg G., Tulinius M., Gilljam T., Oestman-Smith I., Forsander G., Jotorp P., Oldfors A., Holme E.
N. Engl. J. Med. 357:1507-1514(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN GSD0B.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND SER-649, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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."
Kelsall I.R., Voss M., Munro S., Cuthbertson D.J., Cohen P.T.
J. Neurochem. 118:596-610(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04501 mRNA. Translation: AAA88046.1.
Z33622 expand/collapse EMBL AC list , Z33623, Z33609, Z33624, Z33625, Z33626, Z33610, Z33627, Z33628, Z33629, Z33630, Z33631, Z33633 Genomic DNA. Translation: CAA83916.1.
U32573 mRNA. Translation: AAB60385.1.
AC008687 Genomic DNA. No translation available.
AC026803 Genomic DNA. No translation available.
AC098792 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52424.1.
BC002617 mRNA. Translation: AAH02617.1.
BC003182 mRNA. Translation: AAH03182.1.
BC007688 mRNA. Translation: AAH07688.1.
CCDSCCDS12747.1. [P13807-1]
CCDS54292.1. [P13807-2]
PIRA32156.
RefSeqNP_001155059.1. NM_001161587.1. [P13807-2]
NP_002094.2. NM_002103.4. [P13807-1]
UniGeneHs.386225.

3D structure databases

ProteinModelPortalP13807.
SMRP13807. Positions 23-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109252. 18 interactions.
IntActP13807. 17 interactions.
MINTMINT-1451793.
STRING9606.ENSP00000317904.

Chemistry

BindingDBP13807.
ChEMBLCHEMBL4000.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteP13807.

Polymorphism databases

DMDM1351366.

Proteomic databases

MaxQBP13807.
PaxDbP13807.
PRIDEP13807.

Protocols and materials databases

DNASU2997.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263276; ENSP00000263276; ENSG00000104812. [P13807-2]
ENST00000323798; ENSP00000317904; ENSG00000104812. [P13807-1]
GeneID2997.
KEGGhsa:2997.
UCSCuc002plp.3. human. [P13807-1]
uc010emm.3. human. [P13807-2]

Organism-specific databases

CTD2997.
GeneCardsGC19M049471.
HGNCHGNC:4706. GYS1.
HPACAB007793.
HPA041598.
MIM138570. gene.
611556. phenotype.
neXtProtNX_P13807.
Orphanet137625. Glycogen storage disease due to muscle and heart glycogen synthase deficiency.
PharmGKBPA29084.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000160890.
HOVERGENHBG001960.
InParanoidP13807.
KOK00693.
OMAFAMKRHG.
OrthoDBEOG741Z1N.
PhylomeDBP13807.
TreeFamTF300306.

Enzyme and pathway databases

BioCycMetaCyc:HS02622-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00164.

Gene expression databases

ArrayExpressP13807.
BgeeP13807.
CleanExHS_GYS1.
GenevestigatorP13807.

Family and domain databases

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

Other

ChiTaRSGYS1. human.
GenomeRNAi2997.
NextBio11884.
PROP13807.
SOURCESearch...

Entry information

Entry nameGYS1_HUMAN
AccessionPrimary (citable) accession number: P13807
Secondary accession number(s): Q9BTT9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 147 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 19

Human chromosome 19: entries, gene names and cross-references to MIM