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Q9Z1E4

- GYS1_MOUSE

UniProt

Q9Z1E4 - GYS1_MOUSE

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Protein

Glycogen [starch] synthase, muscle

Gene
Gys1, Gys, Gys3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan By similarity.

Catalytic activityi

UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).

Enzyme regulationi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391UDP-glucose By similarity

GO - Molecular functioni

  1. glucose binding Source: Ensembl
  2. glycogen (starch) synthase activity Source: MGI
  3. protein binding Source: MGI

GO - Biological processi

  1. glycogen biosynthetic process Source: MGI
  2. heart development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

ReactomeiREACT_188939. Glycogen synthesis.
REACT_203841. Myoclonic epilepsy of Lafora.
UniPathwayiUPA00164.

Protein family/group databases

CAZyiGT3. Glycosyltransferase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycogen [starch] synthase, muscle (EC:2.4.1.11)
Gene namesi
Name:Gys1
Synonyms:Gys, Gys3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:101805. Gys1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. inclusion body Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 738737Glycogen [starch] synthase, musclePRO_0000194765Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by AMPK and PKA1 Publication
Modified residuei11 – 111Phosphoserine By similarity
Modified residuei641 – 6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK By similarity
Modified residuei645 – 6451Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei649 – 6491Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-beta By similarity
Modified residuei657 – 6571Phosphoserine; by CK2 By similarity
Modified residuei698 – 6981Phosphoserine By similarity
Modified residuei728 – 7281Phosphoserine By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z1E4.
PaxDbiQ9Z1E4.
PRIDEiQ9Z1E4.

PTM databases

PhosphoSiteiQ9Z1E4.

Expressioni

Gene expression databases

ArrayExpressiQ9Z1E4.
BgeeiQ9Z1E4.
GenevestigatoriQ9Z1E4.

Interactioni

Subunit structurei

Interacts with GYG1 By similarity.

Protein-protein interaction databases

IntActiQ9Z1E4. 4 interactions.
MINTiMINT-4097092.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1E4.
SMRiQ9Z1E4. Positions 23-621.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000018612.
HOGENOMiHOG000160890.
HOVERGENiHBG001960.
InParanoidiQ8VEB0.
KOiK00693.
OMAiFAMKRHG.
OrthoDBiEOG741Z1N.
PhylomeDBiQ9Z1E4.
TreeFamiTF300306.

Family and domain databases

InterProiIPR008631. Glycogen_synth.
[Graphical view]
PANTHERiPTHR10176. PTHR10176. 1 hit.
PfamiPF05693. Glycogen_syn. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z1E4-1 [UniParc]FASTAAdd to Basket

« Hide

MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK    50
AKVTGDEWGD NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK 100
VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND 150
AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH EWLAGVGLCL CRARRLPVAT 200
IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH RYCMERAAAH 250
CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS 300
KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN 350
YLLRVNGSEQ TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF 400
GRKLYESLLV GSLPDMNKML DKEDFTMMKR AIFATQRQSF PPVCTHNMLD 450
DSSDPILTTI RRIGLFNSSA DRVKVIFHPE FLSSTSPLLP VDYEEFVRGC 500
HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE HIADPSAYGI 550
YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY 600
LGRYYMSARH MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR 650
HSSPHQSEDE EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS 700
SSTGGSKRSN SVDTGPSSSL STPTEPLSPT SSLGEERN 738
Length:738
Mass (Da):83,927
Last modified:December 16, 2008 - v2
Checksum:iD1F9252CA908FF69
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31L → R in CAA64322. 1 Publication
Sequence conflicti70 – 701E → V in AAD09457. 1 Publication
Sequence conflicti80 – 801L → M in BAE42275. 1 Publication
Sequence conflicti111 – 1122GP → D in CAA64322. 1 Publication
Sequence conflicti120 – 1201G → A in AAD09457. 1 Publication
Sequence conflicti148 – 1481A → G in AAD09457. 1 Publication
Sequence conflicti154 – 1552FG → YS in AAD09457. 1 Publication
Sequence conflicti191 – 1911C → S in CAA64322. 1 Publication
Sequence conflicti208 – 2081L → V in AAD09457. 1 Publication
Sequence conflicti228 – 2281N → I in AAD09457. 1 Publication
Sequence conflicti581 – 5822QR → HG in CAA64322. 1 Publication
Sequence conflicti640 – 6401A → V in AAD09457. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS21244.1.
RefSeqiNP_109603.2. NM_030678.3.
UniGeneiMm.275654.

Genome annotation databases

EnsembliENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
GeneIDi14936.
KEGGimmu:14936.
UCSCiuc009gve.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS21244.1.
RefSeqi NP_109603.2. NM_030678.3.
UniGenei Mm.275654.

3D structure databases

ProteinModelPortali Q9Z1E4.
SMRi Q9Z1E4. Positions 23-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Z1E4. 4 interactions.
MINTi MINT-4097092.

Protein family/group databases

CAZyi GT3. Glycosyltransferase Family 3.

PTM databases

PhosphoSitei Q9Z1E4.

Proteomic databases

MaxQBi Q9Z1E4.
PaxDbi Q9Z1E4.
PRIDEi Q9Z1E4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003964 ; ENSMUSP00000003964 ; ENSMUSG00000003865 .
GeneIDi 14936.
KEGGi mmu:14936.
UCSCi uc009gve.1. mouse.

Organism-specific databases

CTDi 2997.
MGIi MGI:101805. Gys1.

Phylogenomic databases

eggNOGi COG0438.
GeneTreei ENSGT00390000018612.
HOGENOMi HOG000160890.
HOVERGENi HBG001960.
InParanoidi Q8VEB0.
KOi K00693.
OMAi FAMKRHG.
OrthoDBi EOG741Z1N.
PhylomeDBi Q9Z1E4.
TreeFami TF300306.

Enzyme and pathway databases

UniPathwayi UPA00164 .
Reactomei REACT_188939. Glycogen synthesis.
REACT_203841. Myoclonic epilepsy of Lafora.

Miscellaneous databases

NextBioi 287255.
PROi Q9Z1E4.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z1E4.
Bgeei Q9Z1E4.
Genevestigatori Q9Z1E4.

Family and domain databases

InterProi IPR008631. Glycogen_synth.
[Graphical view ]
PANTHERi PTHR10176. PTHR10176. 1 hit.
Pfami PF05693. Glycogen_syn. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGYS1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1E4
Secondary accession number(s): P54859
, Q3TBN4, Q8BQG4, Q8VEB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: December 16, 2008
Last modified: September 3, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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