Glycogen [starch] synthase, muscle - Homo sapiens (Human)

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P13807 (GYS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycogen [starch] synthase, muscle
EC=2.4.1.11

Gene names

Name:	GYS1
Synonyms:	GYS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	737 AA.
Sequence status	Complete.
Protein existence	Evidence 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.6
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 PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Involvement in disease	Defects in GYS1 are the cause of muscle glycogen storage disease type 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.
Sequence similarities	Belongs to the glycosyltransferase 3 family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Coding sequence diversity	Polymorphism
Disease	Diabetes mellitus Disease mutation
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glucose metabolic process Traceable author statement. Source: Reactome glycogen biosynthetic process Inferred from direct assay Ref.5. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	glycogen (starch) synthase activity Inferred from direct assay Ref.5. Source: UniProtKB protein kinase binding Inferred from physical interaction Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GYG1	P46976	3	EBI-963094,EBI-740533

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 737

737

Glycogen [starch] synthase, muscle

PRO_0000194763

Sites

Binding site

UDP-glucose By similarity

Amino acid modifications

Modified residue

Phosphoserine; by AMPK and PKA By similarity

Modified residue

Phosphoserine By similarity

Modified residue

412

Phosphoserine Ref.10

Modified residue

641

Phosphoserine; by GSK3-alpha, GSK3-beta and PASK By similarity

Modified residue

645

Phosphoserine; by GSK3-alpha and GSK3-beta By similarity

Modified residue

649

Phosphoserine; by GSK3-alpha and GSK3-beta By similarity

Modified residue

653

Phosphoserine; by GSK3-alpha and GSK3-beta By similarity

Modified residue

657

Phosphoserine; by CK2 By similarity

Modified residue

698

Phosphoserine By similarity

Modified residue

710

Phosphoserine Ref.10

Modified residue

727

Phosphoserine Ref.8 Ref.10 Ref.11

Modified residue

729

Phosphothreonine Ref.10

Modified residue

730

Phosphoserine Ref.10

Modified residue

731

Phosphoserine Ref.8 Ref.10

Natural variations

Natural variant

108

I → M.
Corresponds to variant rs5455 [ dbSNP | Ensembl ].

VAR_037958

Natural variant

130

K → E.
Corresponds to variant rs5456 [ dbSNP | Ensembl ].

VAR_014727

Natural variant

283

N → S.
Corresponds to variant rs5461 [ dbSNP | Ensembl ].

VAR_014728

Natural variant

359

E → G.
Corresponds to variant rs5465 [ dbSNP | Ensembl ].

VAR_014729

Natural variant

416

M → V.
Corresponds to variant rs5447 [ dbSNP | Ensembl ].

VAR_014730

Natural variant

464

G → S in NIDDM. Ref.2

VAR_007859

Natural variant

619

E → Q.
Corresponds to variant rs5450 [ dbSNP | Ensembl ].

VAR_014731

Natural variant

691

P → A.
Corresponds to variant rs5453 [ dbSNP | Ensembl ].

VAR_014732

Experimental info

Mutagenesis

641

S → A: Abolishes PASK-mediated phosphorylation. Ref.5

Mutagenesis

645

S → A: Does not affect PASK-mediated phosphorylation. Ref.5

Sequence conflict

136

T → I in AAA88046. Ref.1

Sequence conflict

136

T → I in AAB60385. Ref.3

Sequence conflict

462

Missing in AAB60385. Ref.3

Sequence conflict

608

A → D in AAB60385. Ref.3

Sequence conflict

706

S → R in AAA88046. Ref.1

Sequence conflict

706

S → R in AAB60385. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P13807 [UniParc].

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

737

83,786

        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

References

	« Hide 'large scale' referencesShow '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: 2493642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 7657035] [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: 9010351] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Endometrium.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Skin.
[5]	"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: 16275910] [Abstract] Cited for: PHOSPHORYLATION AT SER-641, MUTAGENESIS OF SER-641 AND SER-645.
[6]	"Interaction between glycogenin and glycogen synthase." Skurat A.V., Dietrich A.D., Roach P.J. Arch. Biochem. Biophys. 456:93-97(2006) [PubMed: 17055998] [Abstract] Cited for: INTERACTION WITH GYG1.
[7]	"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: 17928598] [Abstract] Cited for: INVOLVEMENT IN GSD0B.
[8]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-727 AND SER-731, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; SER-645 AND SER-649, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-710; SER-727; THR-729; SER-730 AND SER-731, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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: 21668450] [Abstract] Cited for: DEPHOSPHORYLATION AT SER-641 AND SER-645 BY PP1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04501 mRNA. Translation: AAA88046.1. Z33622 Z33633 Genomic DNA. Translation: CAA83916.1. U32573 mRNA. Translation: AAB60385.1. BC002617 mRNA. Translation: AAH02617.1. BC007688 mRNA. Translation: AAH07688.1.
IPI	IPI00303868.
PIR	A32156.
RefSeq	NP_001155059.1. NM_001161587.1. NP_002094.2. NM_002103.4.
UniGene	Hs.386225.
3D structure databases
ProteinModelPortal	P13807.
SMR	P13807. Positions 22-623.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13807. 14 interactions.
STRING	P13807.
Protein family/group databases
CAZy	GT3. Glycosyltransferase Family 3.
PTM databases
PhosphoSite	P13807.
Polymorphism databases
DMDM	1351366.
Proteomic databases
PRIDE	P13807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323798; ENSP00000317904; ENSG00000104812.
GeneID	2997.
KEGG	hsa:2997.
UCSC	uc002plp.1. human.
Organism-specific databases
CTD	2997.
GeneCards	GC19M049471.
H-InvDB	HIX0015311.
HGNC	HGNC:4706. GYS1.
HPA	CAB007793.
MIM	138570. gene. 611556. phenotype.
neXtProt	NX_P13807.
Orphanet	137625. Cardiomyopathy-exercise intolerance due to muscle and heart glycogen deficiency.
PharmGKB	PA29084.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17747.
HOGENOM	HBG330297.
HOVERGEN	HBG001960.
InParanoid	P13807.
OMA	LAQSEEK.
OrthoDB	EOG4C2H91.
PhylomeDB	P13807.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11742.
Pathway_Interaction_DB	insulin_glucose_pathway. Insulin-mediated glucose transport.
Reactome	REACT_474. Metabolism of carbohydrates.
Gene expression databases
ArrayExpress	P13807.
Bgee	P13807.
CleanEx	HS_GYS1.
Genevestigator	P13807.
GermOnline	ENSG00000104812. Homo sapiens.
Family and domain databases
InterPro	IPR008631. Glycogen_synth. [Graphical view]
KO	K00693.
PANTHER	PTHR10176. Glycogen_synth. 1 hit.
Pfam	PF05693. Glycogen_syn. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	11884.
SOURCE	Search...

Entry information

Entry name

GYS1_HUMAN

Accession

Primary (citable) accession number: P13807

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents