Glycogen [starch] synthase, muscle - Mus musculus (Mouse)

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Q9Z1E4 (GYS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

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

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·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, Gys3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 By similarity.
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 By similarity.
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. Phosphorylated at Ser-641 by PASK, leading to inactivation; phosphorylation by PASK is inhibited by glycogen. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme By similarity. Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity. Ref.6
Sequence similarities	Belongs to the glycosyltransferase 3 family.

Ontologies

Keywords
Biological process	Glycogen biosynthesis
Molecular function	Glycosyltransferase Transferase
PTM	Phosphoprotein
Technical term	Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycogen biosynthetic process Inferred from mutant phenotype PubMed 15282316. Source: MGI heart development Inferred from mutant phenotype PubMed 15282316. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 17908927. Source: MGI inclusion body Inferred from direct assay PubMed 17908927. Source: MGI
Molecular_function	glucose binding Inferred from electronic annotation. Source: Compara glycogen (starch) synthase activity Inferred from mutant phenotype PubMed 15282316. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 738

737

Glycogen [starch] synthase, muscle

PRO_0000194765

Sites

Binding site

UDP-glucose By similarity

Amino acid modifications

Modified residue

Phosphoserine; by AMPK and PKA Ref.6

Modified residue

Phosphoserine By similarity

Modified residue

641

Phosphoserine; by DYRK2, 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

728

Phosphoserine By similarity

Experimental info

Sequence conflict

L → R in CAA64322. Ref.1

Sequence conflict

E → V in AAD09457. Ref.2

Sequence conflict

L → M in BAE42275. Ref.3

Sequence conflict

111 – 112

GP → D in CAA64322. Ref.1

Sequence conflict

120

G → A in AAD09457. Ref.2

Sequence conflict

148

A → G in AAD09457. Ref.2

Sequence conflict

154 – 155

FG → YS in AAD09457. Ref.2

Sequence conflict

191

C → S in CAA64322. Ref.1

Sequence conflict

208

L → V in AAD09457. Ref.2

Sequence conflict

228

N → I in AAD09457. Ref.2

Sequence conflict

581 – 582

QR → HG in CAA64322. Ref.1

Sequence conflict

640

A → V in AAD09457. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z1E4 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: D1F9252CA908FF69
Show »

FASTA

738

83,927

        10         20         30         40         50         60 
MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD 

        70         80         90        100        110        120 
NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 

       130        140        150        160        170        180 
ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH 

       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 MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 

       670        680        690        700        710        720 
EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS SSTGGSKRSN SVDTGPSSSL 

       730 
STPTEPLSPT SSLGEERN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, localization and induction of mouse brain glycogen synthase." Pellegri G., Rossier C., Magistretti P.J., Martin J.-L. Brain Res. Mol. Brain Res. 38:191-199(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss albino. Tissue: Astrocyte.
[2]	"Mouse glycogen synthase gene." Seldin M.F., Xue Z., Rochelle J.M., DeBry R., Surwit R. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Dendritic cell and Embryo.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. Strain: Czech II. Tissue: Mammary tumor.
[6]	"The alpha2-5'AMP-activated protein kinase is a site 2 glycogen synthase kinase in skeletal muscle and is responsive to glucose loading." Jorgensen S.B., Nielsen J.N., Birk J.B., Olsen G.S., Viollet B., Andreelli F., Schjerling P., Vaulont S., Hardie D.G., Hansen B.F., Richter E.A., Wojtaszewski J.F. Diabetes 53:3074-3081(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-8.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94616 mRNA. Translation: CAA64322.1. U53218 mRNA. Translation: AAD09457.1. AK050813 mRNA. Translation: BAC34420.1. AK171148 mRNA. Translation: BAE42275.1. CH466603 Genomic DNA. Translation: EDL22855.1. BC019389 mRNA. Translation: AAH19389.1. BC131687 mRNA. Translation: AAI31688.1. BC131688 mRNA. Translation: AAI31689.1. BC152550 mRNA. Translation: AAI52551.1.
IPI	IPI00130127.
RefSeq	NP_109603.2. NM_030678.3.
UniGene	Mm.275654.
3D structure databases
ProteinModelPortal	Q9Z1E4.
SMR	Q9Z1E4. Positions 23-621.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z1E4. 1 interaction.
Protein family/group databases
CAZy	GT3. Glycosyltransferase Family 3.
PTM databases
PhosphoSite	Q9Z1E4.
Proteomic databases
PaxDb	Q9Z1E4.
PRIDE	Q9Z1E4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
GeneID	14936.
KEGG	mmu:14936.
UCSC	uc009gve.1. mouse.
Organism-specific databases
CTD	2997.
MGI	MGI:101805. Gys1.
Phylogenomic databases
eggNOG	COG0438.
GeneTree	ENSGT00390000018612.
HOGENOM	HOG000160890.
HOVERGEN	HBG001960.
InParanoid	Q8VEB0.
KO	K00693.
OMA	HEWLAGL.
OrthoDB	EOG4C2H91.
Enzyme and pathway databases
UniPathway	UPA00164.
Gene expression databases
ArrayExpress	Q9Z1E4.
Bgee	Q9Z1E4.
Genevestigator	Q9Z1E4.
GermOnline	ENSMUSG00000003865. Mus musculus.
Family and domain databases
InterPro	IPR008631. Glycogen_synth. [Graphical view]
PANTHER	PTHR10176. PTHR10176. 1 hit.
Pfam	PF05693. Glycogen_syn. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	287255.
SOURCE	Search...

Entry information

Entry name

GYS1_MOUSE

Accession

Primary (citable) accession number: Q9Z1E4
Secondary accession number(s): P54859

Q8VEB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM 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