UniProtKB - P13280 (GLYG_RABIT)
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>sp|P13280|GLYG_RABIT Glycogenin-1 OS=Oryctolagus cuniculus OX=9986 GN=GYG1 PE=1 SV=3 MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTSRRLAVLTTPQVSDTMRKALEIVFDEVIT VDILDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFEREEL SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHVASEQGSFDGGDQGLLNTFFNSWATTDIR KHLPFIYNLSSISIYSYLPAFKAFGANAKVVHFLGQTKPWNYTYDTKTKSVRSEGHDPTM THPQFLNVWWDIFTTSVVPLLQQFGLVQDTCSYQHVEDVSGAVSHLSLGETPATTQPFVS SEERKERWEQGQADYMGADSFDNIKKKLDTYLQCommunity curation ()Add a publicationFeedback
Protein
Glycogenin-1
Gene
GYG1
Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase.
8 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- L-tyrosyl-[glycogenin]EC:2.4.1.186
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- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
L-tyrosyl-[glycogenin]- Search proteins in UniProtKB for this molecule.
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L-tyrosine residuezoom- Search proteins in UniProtKB for this molecule.
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+UDP-α-D-glucose- Search proteins in UniProtKB for this molecule.
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=α-D-glucosyl-L-tyrosyl-[glycogenin]- Search proteins in UniProtKB for this molecule.
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α-D-glucosyl-L-tyrosyl residuezoom- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+UDP- Search proteins in UniProtKB for this molecule.
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- [1,4-α-D-glucosyl](n)-L-tyrosyl-[glycogenin]EC:2.4.1.186
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
[1,4-α-D-glucosyl](n)-L-tyrosyl-[glycogenin]- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
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+UDP-α-D-glucose- Search proteins in UniProtKB for this molecule.
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=[1,4-α-D-glucosyl](n+1)-L-tyrosyl-[glycogenin]- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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+UDP- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mn2+
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.8"Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin."
Gibbons B.J., Roach P.J., Hurley T.D.
J. Mol. Biol. 319:463-477(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, SUBUNIT, COFACTOR. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
Manual assertion based on experiment ini
- Ref.8"Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin."
Gibbons B.J., Roach P.J., Hurley T.D.
J. Mol. Biol. 319:463-477(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, SUBUNIT, COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycogen biosynthesis
This protein is involved in the pathway glycogen biosynthesis, which is part of Glycan biosynthesis.3 PublicationsManual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract] - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163.
View all proteins of this organism that are known to be involved in the pathway glycogen biosynthesis and in Glycan biosynthesis.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 77 | SubstrateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 86 | Important for catalytic activity1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 102 | ManganeseCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 104 | ManganeseCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 212 | ManganeseCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- glycogenin glucosyltransferase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY. - Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract]
- manganese ion binding Source: UniProtKBInferred from direct assayi
- Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract]
- protein homodimerization activity Source: UniProtKB
- UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity Source: UniProtKBInferred from direct assayi
- Ref.3"Structural and functional studies on rabbit liver glycogenin."
Smythe C., Villar-Palasi C., Cohen P.
Eur. J. Biochem. 183:205-209(1989) [PubMed] [Europe PMC] [Abstract]
GO - Biological processi
- glycogen biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Transferase |
| Biological process | Glycogen biosynthesis |
| Ligand | Manganese, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.4.1.186, 1749 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00164 |
Protein family/group databases
Carbohydrate-Active enZymes More...CAZyi | GT8, Glycosyltransferase Family 8 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Glycogenin-1 (EC:2.4.1.186
Manual assertion based on experiment ini
Short name: GN-1 Short name: GN1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:GYG1 Synonyms:GYG |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Oryctolagus cuniculus (Rabbit) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9986 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 83 | T → M: Loss of autoglucosylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 83 | T → S: No effect on autoglucosylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 86 | K → Q: Nearly abolishes enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 160 | D → N or S: Reduced trans-glucosylation activity by at least 260-fold and reduced UDP-glucose hydrolytic activity by 4 to 14-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 163 | D → N: Loss of self-glucosylation activity and ability to trans-glucosylate maltose. Reduces UDP-glucose hydrolytic activity by at least 190-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 163 | D → S: Loss of self-glucosylation activity and 18 to 30-fold reduction in its ability to trans-glucosylate maltose. Reduces UDP-glucose hydrolytic activity by at least 190-fold. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 195 | Y → F or T: Loss of self-glucosylation. No loss of catalytic activity. 4 Publications Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication Manual assertion based on experiment ini
| |||
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000215178 | 2 – 333 | Glycogenin-1CuratedAdd BLAST | 332 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylthreonineBy similarity Manual assertion inferred from sequence similarity toi | 1 | |
| Modified residuei | 44 | Phosphoserine; by PKA; in vitro1 Publication Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 195 | O-linked (Glc...) tyrosine1 Publication Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195.5 Publications
Manual assertion based on experiment ini
- Ref.5"Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity."
Alonso M.D., Lomako J., Lomako W.M., Whelan W.J.
FEBS Lett. 342:38-42(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.6"Mechanism of glycogenin self-glucosylation."
Cao Y., Steinrauf L.K., Roach P.J.
Arch. Biochem. Biophys. 319:293-298(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF TYR-195. - Ref.7"Self-glucosylation of glycogenin, the initiator of glycogen biosynthesis, involves an inter-subunit reaction."
Lin A., Mu J., Yang J., Roach P.J.
Arch. Biochem. Biophys. 363:163-170(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION AT TYR-195, MUTAGENESIS OF LYS-86 AND TYR-195. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
Phosphorylated.1 Publication
Manual assertion based on experiment ini
- Ref.4"The occurrence of serine phosphate in glycogenin: a possible regulatory site."
Lomako J., Whelan W.J.
BioFactors 1:261-264(1988) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE OF 35-48, PHOSPHORYLATION AT SER-44.
Keywords - PTMi
Acetylation, Glycoprotein, PhosphoproteinPTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P13280 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Detected in heart, skeletal muscle, brain and testis, and at lower levels in kidney.1 Publication
Manual assertion based on experiment ini
- Ref.1"Rabbit skeletal muscle glycogenin. Molecular cloning and production of fully functional protein in Escherichia coli."
Viskupic E., Cao Y., Zhang W., Cheng C., Depaoli-Roach A.A., Roach P.J.
J. Biol. Chem. 267:25759-25763(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, TISSUE SPECIFICITY.
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer (PubMed:12051921, PubMed:15849187, PubMed:22226635, PubMed:22128147).
Interacts (via C-terminus) with glycogen synthase GYS1 (By similarity).
Interacts (via C-terminus) with glycogen synthase GYS2 (By similarity). This interaction is required for GYS2-mediated glycogen synthesis (By similarity).
By similarityManual assertion inferred from sequence similarity toi
4 PublicationsManual assertion based on experiment ini
- Ref.8"Crystal structure of the autocatalytic initiator of glycogen biosynthesis, glycogenin."
Gibbons B.J., Roach P.J., Hurley T.D.
J. Mol. Biol. 319:463-477(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH UDP-GLUCOSE AND MANGANESE IONS, SUBUNIT, COFACTOR. - Ref.9"Requirements for catalysis in mammalian glycogenin."
Hurley T.D., Stout S., Miner E., Zhou J., Roach P.J.
J. Biol. Chem. 280:23892-23899(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, SUBUNIT, MUTAGENESIS OF ASP-160 AND ASP-163. - Ref.10"Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation."
Carrizo M.E., Romero J.M., Issoglio F.M., Curtino J.A.
FEBS Lett. 586:254-257(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-271 OF WILD-TYPE AND MUTANT MET-83 IN COMPLEX WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF THR-83. - Ref.11"Mechanisms of monomeric and dimeric glycogenin autoglucosylation."
Issoglio F.M., Carrizo M.E., Romero J.M., Curtino J.A.
J. Biol. Chem. 287:1955-1961(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-271, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-195, GLYCOSYLATION AT TYR-195.
GO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P13280 |
STRING: functional protein association networks More...STRINGi | 9986.ENSOCUP00000019444 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 3 – 12 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 13 – 28 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 16 | |
| Beta strandi | 33 – 39 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 45 – 54 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 56 – 60 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 71 – 76 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 78 – 80 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 81 – 86 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 87 – 91 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 96 – 101 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 105 – 107 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 112 – 116 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 119 – 124 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 126 – 128 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 131 – 139 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 143 – 155 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 159 – 162 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 163 – 170 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 171 – 176 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 179 – 181 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 185 – 187 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 188 – 190 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 193 – 196 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 198 – 204 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 205 – 207 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 209 – 212 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 215 – 217 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 219 – 221 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 222 – 225 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 226 – 229 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 230 – 232 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 243 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Helixi | 257 – 261 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 263 – 265 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P13280 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P13280 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 9 – 15 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 7 | |
| Regioni | 102 – 104 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 3 | |
| Regioni | 133 – 135 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 3 | |
| Regioni | 160 – 164 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 5 | |
| Regioni | 212 – 218 | Substrate bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| 7 | |
| Regioni | 284 – 316 | Interaction with GYS1By similarity Manual assertion inferred from sequence similarity toi Add BLAST | 33 |
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1950, Eukaryota |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P13280 |
Database of Orthologous Groups More...OrthoDBi | 1424146at2759 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.90.550.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR002495, Glyco_trans_8 IPR029044, Nucleotide-diphossugar_trans |
Pfam protein domain database More...Pfami | View protein in Pfam PF01501, Glyco_transf_8, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53448, SSF53448, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P13280-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TSRRLAVLTT PQVSDTMRKA
60 70 80 90 100
LEIVFDEVIT VDILDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF
110 120 130 140 150
MDADTLVLAN IDDLFEREEL SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL
160 170 180 190 200
HVASEQGSFD GGDQGLLNTF FNSWATTDIR KHLPFIYNLS SISIYSYLPA
210 220 230 240 250
FKAFGANAKV VHFLGQTKPW NYTYDTKTKS VRSEGHDPTM THPQFLNVWW
260 270 280 290 300
DIFTTSVVPL LQQFGLVQDT CSYQHVEDVS GAVSHLSLGE TPATTQPFVS
310 320 330
SEERKERWEQ GQADYMGADS FDNIKKKLDT YLQ
Length:333
Mass (Da):37,397
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i7C27F7B428F67571
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 39 | T → L AA sequence (PubMed:3151442).Curated | 1 | |
| Sequence conflicti | 89 | C → S AA sequence (PubMed:2806254).Curated | 1 | |
| Sequence conflicti | 98 | C → L AA sequence (PubMed:2806254).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L01791 mRNA Translation: AAA31404.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A45094 |
NCBI Reference Sequences More...RefSeqi | NP_001075710.1, NM_001082241.1 |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 100009058 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ocu:100009058 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P13280 | Glycogenin-1 | 350 | UniRef90_P13280 | |||
| Glycogenin-1 | 331 | |||||
| +10 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| P13280 | Glycogenin-1 | 350 | UniRef50_P13280 | |||
| GLYG protein (Fragment) | 273 | |||||
| glycogenin-1 isoform X2 | 325 | |||||
| glycogenin-1 isoform X3 | 325 | |||||
| GLYG protein (Fragment) | 309 | |||||
| +117 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L01791 mRNA Translation: AAA31404.1 |
| PIRi | A45094 |
| RefSeqi | NP_001075710.1, NM_001082241.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1LL0 | X-ray | 3.43 | A/B/C/D/E/F/G/H/I/J | 1-333 | [»] | |
| 1LL2 | X-ray | 1.90 | A | 1-333 | [»] | |
| 1LL3 | X-ray | 1.90 | A | 1-333 | [»] | |
| 1ZCT | X-ray | 2.60 | A/B | 1-270 | [»] | |
| 1ZCU | X-ray | 2.00 | A | 1-333 | [»] | |
| 1ZCV | X-ray | 1.98 | A | 1-333 | [»] | |
| 1ZCY | X-ray | 1.99 | A | 1-333 | [»] | |
| 1ZDF | X-ray | 2.45 | A | 1-333 | [»] | |
| 1ZDG | X-ray | 2.30 | A | 1-333 | [»] | |
| 3USQ | X-ray | 2.40 | A | 1-271 | [»] | |
| 3USR | X-ray | 2.10 | A | 1-271 | [»] | |
| 3V8Y | X-ray | 2.15 | A | 1-271 | [»] | |
| 3V8Z | X-ray | 2.20 | A | 1-271 | [»] | |
| 3V90 | X-ray | 2.00 | A | 1-271 | [»] | |
| 3V91 | X-ray | 2.00 | A | 1-271 | [»] | |
| SMRi | P13280 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| CORUMi | P13280 |
| STRINGi | 9986.ENSOCUP00000019444 |
Protein family/group databases
| CAZyi | GT8, Glycosyltransferase Family 8 |
PTM databases
| iPTMneti | P13280 |
Genome annotation databases
| GeneIDi | 100009058 |
| KEGGi | ocu:100009058 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 2992 |
Phylogenomic databases
| eggNOGi | KOG1950, Eukaryota |
| InParanoidi | P13280 |
| OrthoDBi | 1424146at2759 |
Enzyme and pathway databases
| UniPathwayi | UPA00164 |
| BRENDAi | 2.4.1.186, 1749 |
Miscellaneous databases
| EvolutionaryTracei | P13280 |
Family and domain databases
| Gene3Di | 3.90.550.10, 1 hit |
| InterProi | View protein in InterPro IPR002495, Glyco_trans_8 IPR029044, Nucleotide-diphossugar_trans |
| Pfami | View protein in Pfam PF01501, Glyco_transf_8, 1 hit |
| SUPFAMi | SSF53448, SSF53448, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | GLYG_RABIT | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P13280Primary (citable) accession number: P13280 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | June 2, 2021 | |
| This is version 137 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
