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P13834 (GYS1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length735 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. Ref.11

Catalytic activity

UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1). Ref.11

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. Ref.11

Pathway

Glycan biosynthesis; glycogen biosynthesis.

Subunit structure

Interacts with GYG1 By similarity.

Post-translational modification

Phosphorylation at Ser-8 is required for modification of Ser-11 by casein kinase I.

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 By similarity. Phosphorylation at Ser-8 by AMPK inactivates the enzyme activity By similarity. Phosphorylated at Ser-641 by DYRK2, leading to inactivation. 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 and GSK3B. Ref.3 Ref.5 Ref.10 Ref.11

Sequence similarities

Belongs to the glycosyltransferase 3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3 Ref.4 Ref.5
Chain2 – 735734Glycogen [starch] synthase, muscle
PRO_0000194767

Sites

Binding site391UDP-glucose By similarity

Amino acid modifications

Modified residue81Phosphoserine; by AMPK and PKA Ref.3 Ref.5
Modified residue111Phosphoserine Ref.5 Ref.8
Modified residue6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK Ref.3 Ref.5 Ref.10 Ref.11
Modified residue6451Phosphoserine; by GSK3-alpha and GSK3-beta Ref.3 Ref.5 Ref.10
Modified residue6491Phosphoserine; by GSK3-alpha and GSK3-beta Ref.3 Ref.5 Ref.10
Modified residue6531Phosphoserine; by GSK3-alpha and GSK3-beta Ref.5 Ref.10
Modified residue6571Phosphoserine; by CK2 Ref.5 Ref.10
Modified residue6981Phosphoserine Ref.5 Ref.8
Modified residue7251Phosphoserine By similarity

Experimental info

Mutagenesis6411S → A: Loss of an inhibitory phosphorylation site. Abolishes phosphorylation by DYRK2. Ref.11
Sequence conflict6921E → Q AA sequence Ref.2
Sequence conflict7261P → S AA sequence Ref.2
Sequence conflict7261P → S AA sequence Ref.5
Sequence conflict7281S → P AA sequence Ref.2
Sequence conflict7281S → P AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P13834 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 53ABE9DBE769ADBC

FASTA73583,601
        10         20         30         40         50         60 
MPLSRTLSVS SLPGLEDWED EFDLENSVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD 

        70         80         90        100        110        120 
NYFLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG 

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

       190        200        210        220        230        240 
EWLAGIGLCL 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 FTYEPHEADA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE 

       670        680        690        700        710        720 
EEPRDGLPEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT SSSGGSKRSN SVDTSSLSTP 

       730 
SEPLSPASSL GEERN 

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References

[1]"Primary structure of rabbit skeletal muscle glycogen synthase deduced from cDNA clones."
Zhang W.M., Browner M.F., Fletterick R.J., DePaoli-Roach A.A., Roach P.J.
FASEB J. 3:2532-2536(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Skeletal muscle.
[2]"Identification of the C-terminus of rabbit skeletal muscle glycogen synthase."
Cohen P., Holmes C.F.B.
Biochem. Biophys. Res. Commun. 137:542-545(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30 AND 612-735.
[3]"Glycogen synthase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase."
Rylatt D.B., Aitken A., Bilham T., Condon G.D., Embi N., Cohen P.
Eur. J. Biochem. 107:529-537(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30, PHOSPHORYLATION AT SER-8; SER-641; SER-645 AND SER-649.
[4]"Effect of proteases on the structure and activity of rabbit skeletal muscle glycogen synthetase."
Huang T.S., Krebs E.G.
FEBS Lett. 98:66-70(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
[5]"Analysis of the in vivo phosphorylation state of rabbit skeletal muscle glycogen synthase by fast-atom-bombardment mass spectrometry."
Poulter L., Ang S.G., Gibson B.W., Williams D.H., Holmes C.F., Caudwell F.B., Pitcher J., Cohen P.
Eur. J. Biochem. 175:497-510(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-15; 639-662 AND 694-735, PHOSPHORYLATION AT SER-8; SER-11; SER-641; SER-645; SER-649; SER-653; SER-657 AND SER-698.
[6]"Catalytic site of rabbit glycogen synthase isozymes. Identification of an active site lysine close to the amino terminus of the subunit."
Mahrenholz A.M., Wang Y.H., Roach P.J.
J. Biol. Chem. 263:10561-10567(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-21; 31-44 AND 286-300.
[7]"Phosphate groups as substrate determinants for casein kinase I action."
Flotow H., Graves P.R., Wang A.Q., Fiol C.J., Roeske R.W., Roach P.J.
J. Biol. Chem. 265:14264-14269(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 665-683.
[8]"Multisite phosphorylation of glycogen synthase from rabbit skeletal muscle. Identification of the sites phosphorylated by casein kinase-I."
Kuret J., Woodgett J.R., Cohen P.
Eur. J. Biochem. 151:39-48(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[9]"Phosphorylation of glycogen synthase by a bovine thymus protein-tyrosine kinase, p40."
Mahrenholz A.M., Votaw P., Roach P.J., Depaoli-Roach A.A., Zioncheck T.F., Harrison M.L., Geahlen R.L.
Biochem. Biophys. Res. Commun. 155:52-58(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 665-683.
[10]"Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3."
Fiol C.J., Mahrenholz A.M., Wang Y., Roeske R.W., Roach P.J.
J. Biol. Chem. 262:14042-14048(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-641; SER-645; SER-649; SER-653 AND SER-657.
[11]"Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases."
Skurat A.V., Dietrich A.D.
J. Biol. Chem. 279:2490-2498(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT SER-641, ENZYME REGULATION, MUTAGENESIS OF SER-641.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017114 mRNA. Translation: AAB69872.1.
PIRA33369.
RefSeqNP_001075492.1. NM_001082023.1.
UniGeneOcu.2171.

3D structure databases

ProteinModelPortalP13834.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13834. 4 interactions.
MINTMINT-8146730.

Protein family/group databases

CAZyGT3. Glycosyltransferase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008660.

Organism-specific databases

CTD2997.

Phylogenomic databases

eggNOGCOG0438.
HOGENOMHOG000160890.
HOVERGENHBG001960.

Enzyme and pathway databases

UniPathwayUPA00164.

Family and domain databases

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

Entry information

Entry nameGYS1_RABIT
AccessionPrimary (citable) accession number: P13834
Secondary accession number(s): O18817
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 101 of the entry and version 4 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