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P13834

- GYS1_RABIT

UniProt

P13834 - GYS1_RABIT

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Protein

Glycogen [starch] synthase, muscle

Gene
GYS1, GYS
Organism
Oryctolagus cuniculus (Rabbit)
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.1 Publication

Catalytic activityi

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

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.1 Publication

Pathwayi

Sites

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

GO - Molecular functioni

  1. glycogen (starch) synthase activity Source: UniProtKB

GO - Biological processi

  1. glycogen biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Glycogen biosynthesis

Enzyme and pathway databases

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi641 – 6411S → A: Loss of an inhibitory phosphorylation site. Abolishes phosphorylation by DYRK2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 735734Glycogen [starch] synthase, musclePRO_0000194767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine; by AMPK and PKA2 Publications
Modified residuei11 – 111Phosphoserine2 Publications
Modified residuei641 – 6411Phosphoserine; by DYRK2, GSK3-alpha, GSK3-beta and PASK4 Publications
Modified residuei645 – 6451Phosphoserine; by GSK3-alpha and GSK3-beta3 Publications
Modified residuei649 – 6491Phosphoserine; by GSK3-alpha and GSK3-beta3 Publications
Modified residuei653 – 6531Phosphoserine; by GSK3-alpha and GSK3-beta2 Publications
Modified residuei657 – 6571Phosphoserine; by CK22 Publications
Modified residuei698 – 6981Phosphoserine2 Publications
Modified residuei725 – 7251Phosphoserine By similarity

Post-translational modificationi

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.4 Publications

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Interacts with GYG1 By similarity.

Protein-protein interaction databases

IntActiP13834. 4 interactions.
MINTiMINT-8146730.

Structurei

3D structure databases

ProteinModelPortaliP13834.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0438.
HOGENOMiHOG000160890.
HOVERGENiHBG001960.

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.

P13834-1 [UniParc]FASTAAdd to Basket

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MPLSRTLSVS SLPGLEDWED EFDLENSVLF EVAWEVANKV GGIYTVLQTK    50
AKVTGDEWGD NYFLVGPYTE QGVRTQVELL EPPTPALKRT LDSMNSKGCK 100
VYFGRWLIEG GPLVVLLDVG ASAWALERWK GELWDTCNIG VPWYDREAND 150
AVLFGFLTTW FLGEFLAQNE EKPHVVAHFH EWLAGIGLCL 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 FTYEPHEADA TQGYRYPRPA SVPPSPSLSR 650
HSSPHQSEDE EEPRDGLPEE DGERYDEDEE AAKDRRNIRA PEWPRRASCT 700
SSSGGSKRSN SVDTSSLSTP SEPLSPASSL GEERN 735
Length:735
Mass (Da):83,601
Last modified:January 23, 2007 - v4
Checksum:i53ABE9DBE769ADBC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti692 – 6921E → Q AA sequence 1 Publication
Sequence conflicti726 – 7261P → S AA sequence 1 Publication
Sequence conflicti726 – 7261P → S AA sequence 1 Publication
Sequence conflicti728 – 7281S → P AA sequence 1 Publication
Sequence conflicti728 – 7281S → P AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017114 mRNA. Translation: AAB69872.1.
PIRiA33369.
RefSeqiNP_001075492.1. NM_001082023.1.
UniGeneiOcu.2171.

Genome annotation databases

GeneIDi100008660.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF017114 mRNA. Translation: AAB69872.1 .
PIRi A33369.
RefSeqi NP_001075492.1. NM_001082023.1.
UniGenei Ocu.2171.

3D structure databases

ProteinModelPortali P13834.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13834. 4 interactions.
MINTi MINT-8146730.

Protein family/group databases

CAZyi GT3. Glycosyltransferase Family 3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008660.

Organism-specific databases

CTDi 2997.

Phylogenomic databases

eggNOGi COG0438.
HOGENOMi HOG000160890.
HOVERGENi HBG001960.

Enzyme and pathway databases

UniPathwayi UPA00164 .

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

  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.

Entry informationi

Entry nameiGYS1_RABIT
AccessioniPrimary (citable) accession number: P13834
Secondary accession number(s): O18817
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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