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Q9Z1E4 (GYS1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, muscle

EC=2.4.1.11
Gene names
Name:Gys1
Synonyms:Gys, Gys3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length738 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 738737Glycogen [starch] synthase, muscle
PRO_0000194765

Sites

Binding site391UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by AMPK and PKA Ref.6
Modified residue111Phosphoserine By similarity
Modified residue6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK 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 residue6981Phosphoserine By similarity
Modified residue7281Phosphoserine By similarity

Experimental info

Sequence conflict31L → R in CAA64322. Ref.1
Sequence conflict701E → V in AAD09457. Ref.2
Sequence conflict801L → M in BAE42275. Ref.3
Sequence conflict111 – 1122GP → D in CAA64322. Ref.1
Sequence conflict1201G → A in AAD09457. Ref.2
Sequence conflict1481A → G in AAD09457. Ref.2
Sequence conflict154 – 1552FG → YS in AAD09457. Ref.2
Sequence conflict1911C → S in CAA64322. Ref.1
Sequence conflict2081L → V in AAD09457. Ref.2
Sequence conflict2281N → I in AAD09457. Ref.2
Sequence conflict581 – 5822QR → HG in CAA64322. Ref.1
Sequence conflict6401A → V in AAD09457. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z1E4 [UniParc].

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

FASTA73883,927
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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.
+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.
CCDSCCDS21244.1.
RefSeqNP_109603.2. NM_030678.3.
UniGeneMm.275654.

3D structure databases

ProteinModelPortalQ9Z1E4.
SMRQ9Z1E4. Positions 23-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z1E4. 4 interactions.
MINTMINT-4097092.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteQ9Z1E4.

Proteomic databases

MaxQBQ9Z1E4.
PaxDbQ9Z1E4.
PRIDEQ9Z1E4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
GeneID14936.
KEGGmmu:14936.
UCSCuc009gve.1. mouse.

Organism-specific databases

CTD2997.
MGIMGI:101805. Gys1.

Phylogenomic databases

eggNOGCOG0438.
GeneTreeENSGT00390000018612.
HOGENOMHOG000160890.
HOVERGENHBG001960.
InParanoidQ8VEB0.
KOK00693.
OMAFAMKRHG.
OrthoDBEOG741Z1N.
PhylomeDBQ9Z1E4.
TreeFamTF300306.

Enzyme and pathway databases

UniPathwayUPA00164.

Gene expression databases

ArrayExpressQ9Z1E4.
BgeeQ9Z1E4.
GenevestigatorQ9Z1E4.

Family and domain databases

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

Other

NextBio287255.
PROQ9Z1E4.
SOURCESearch...

Entry information

Entry nameGYS1_MOUSE
AccessionPrimary (citable) accession number: Q9Z1E4
Secondary accession number(s): P54859 expand/collapse secondary AC list , Q3TBN4, Q8BQG4, Q8VEB0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot