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Reviewed, UniProtKB/Swiss-Prot Q9Z1E4 (GYS1_MOUSE)

Last modified January 19, 2010. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length738 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 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.

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GYG1P469761EBI-1152696,EBI-740533From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 738738Glycogen [starch] synthase, muscle
PRO_0000194765

Sites

Binding site391UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by PKA By similarity
Modified residue111Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Modified residue6411Phosphoserine Ref.6
Modified residue6451Phosphoserine By similarity
Modified residue6491Phosphoserine By similarity
Modified residue6531Phosphoserine By similarity
Modified residue6571Phosphoserine Ref.7
Modified residue6981Phosphoserine By similarity
Modified residue7281Phosphoserine By similarity
Modified residue7301Phosphothreonine By similarity
Modified residue7311Phosphoserine By similarity
Modified residue7321Phosphoserine 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
Q9Z1E4-1 [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: 8793107] [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[6]"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: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, MASS SPECTROMETRY.
Tissue: Liver.
[7]"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: 18973353] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, MASS SPECTROMETRY.
+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.
IPIIPI00130127.
RefSeqNP_109603.2.
UniGeneMm.275654

3D structure databases

SMRQ9Z1E4. Positions 165-607.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Z1E4. 1 interaction.
STRINGQ9Z1E4.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSiteQ9Z1E4.

Proteomic databases

PRIDEQ9Z1E4.

Genome annotation databases

EnsemblENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865; Mus musculus. [Genome view]
GeneID14936.
KEGGmmu:14936.

Organism-specific databases

CTD14936.
MGIMGI:101805. Gys1.

Phylogenomic databases

eggNOGroNOG07189.
HOGENOMHBG330297.
HOVERGENQ9Z1E4.
InParanoidQ9Z1E4.
OMAKVGGIYS.
PhylomeDBQ9Z1E4.

Enzyme and pathway databases

BRENDA2.4.1.11. 244.

Gene expression databases

ArrayExpressQ9Z1E4.
BgeeQ9Z1E4.
GenevestigatorQ9Z1E4.
GermOnlineENSMUSG00000003865. Mus musculus.

Family and domain databases

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

Other Resources

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: January 19, 2010
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents