GLYG_HUMAN
ID GLYG_HUMAN Reviewed; 350 AA.
AC P46976; D3DNH0; D3DNH1; D3DNH2; Q6FHZ1; Q9UNV0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Glycogenin-1;
DE Short=GN-1;
DE Short=GN1;
DE EC=2.4.1.186 {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213};
GN Name=GYG1; Synonyms=GYG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GN-1), AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=8602861; DOI=10.1006/bbrc.1996.0359;
RA Barbetti F., Rocchi M., Bossolasco M., Cordera R., Sbraccia P., Finelli P.,
RA Consalez G.G.;
RT "The human skeletal muscle glycogenin gene: cDNA, tissue expression and
RT chromosomal localization.";
RL Biochem. Biophys. Res. Commun. 220:72-77(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GN-1).
RX PubMed=8661012; DOI=10.1006/geno.1996.0228;
RA Lomako J., Mazuruk K., Lomako W.M., Alonso M.D., Whelan W.J.,
RA Rodriguez I.R.;
RT "The human intron-containing gene for glycogenin maps to chromosome 3, band
RT q24.";
RL Genomics 33:519-522(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GN-1S).
RC TISSUE=Skin;
RA Leffers H., Wiemann S., Ansorge W.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM GN-1).
RX PubMed=10395894; DOI=10.1016/s0378-1119(99)00211-5;
RA van Maanen M.-H., Fournier P.A., Palmer T.N., Abraham L.J.;
RT "Characterization of the human glycogenin-1 gene: identification of a
RT muscle-specific regulatory domain.";
RL Gene 234:217-226(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GN-1L), AND ALTERNATIVE SPLICING.
RX PubMed=10721716; DOI=10.1016/s0378-1119(99)00520-x;
RA Zhai L., Mu J., Zong H., DePaoli-Roach A.A., Roach P.J.;
RT "Structure and chromosomal localization of the human glycogenin-2 gene
RT GYG2.";
RL Gene 242:229-235(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GN-1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GN-1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP INTERACTION WITH GYS1.
RX PubMed=17055998; DOI=10.1016/j.abb.2006.09.024;
RA Skurat A.V., Dietrich A.D., Roach P.J.;
RT "Interaction between glycogenin and glycogen synthase.";
RL Arch. Biochem. Biophys. 456:93-97(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP INVOLVEMENT IN PGBM2, AND VARIANTS PGBM2 PRO-16 AND HIS-102.
RX PubMed=25272951; DOI=10.1002/ana.24284;
RA Malfatti E., Nilsson J., Hedberg-Oldfors C., Hernandez-Lain A., Michel F.,
RA Dominguez-Gonzalez C., Viennet G., Akman H.O., Kornblum C.,
RA Van den Bergh P., Romero N.B., Engel A.G., DiMauro S., Oldfors A.;
RT "A new muscle glycogen storage disease associated with glycogenin-1
RT deficiency.";
RL Ann. Neurol. 76:891-898(2014).
RN [15] {ECO:0007744|PDB:3Q4S, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-262 OF WILD-TYPE AND VARIANT
RP GSD15 MET-83 IN COMPLEXES WITH MANGANESE; UDP AND UDP-ALPHA-D-GLUCOSE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, GLYCOSYLATION AT TYR-195,
RP COFACTOR, MUTAGENESIS OF TYR-195, AND CHARACTERIZATION OF VARIANT GSD15
RP MET-83.
RX PubMed=22160680; DOI=10.1073/pnas.1113921108;
RA Chaikuad A., Froese D.S., Berridge G., von Delft F., Oppermann U.,
RA Yue W.W.;
RT "Conformational plasticity of glycogenin and its maltosaccharide substrate
RT during glycogen biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:21028-21033(2011).
RN [16] {ECO:0007744|PDB:3U2X}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 1-262 IN COMPLEX WITH
RP 1,5-ANHYDRO-D-GLUCITOL; MANGANESE AND UDP.
RA Chaikuad A., Froese D.S., Krysztofinska E., von Delft F., Weigelt J.,
RA Arrowsmith C.H., Edwards A.M., Bountra C., Oppermann U., Yue W.W.;
RT "Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese,
RT UDP and 1'-deoxyglucose.";
RL Submitted (OCT-2011) to the PDB data bank.
RN [17] {ECO:0007744|PDB:6EQJ, ECO:0007744|PDB:6EQL}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) OF 1-262 IN COMPLEXES WITH UDP AND
RP MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, GLYCOSYLATION
RP AT TYR-195, AND ACTIVITY REGULATION.
RX PubMed=30356213; DOI=10.1038/s41586-018-0644-7;
RA Bilyard M.K., Bailey H.J., Raich L., Gafitescu M.A., Machida T.,
RA Iglesias-Fernandez J., Lee S.S., Spicer C.D., Rovira C., Yue W.W.,
RA Davis B.G.;
RT "Palladium-mediated enzyme activation suggests multiphase initiation of
RT glycogenesis.";
RL Nature 563:235-240(2018).
RN [18]
RP VARIANT GSD15 MET-83, AND CHARACTERIZATION OF VARIANT GSD15 MET-83.
RX PubMed=20357282; DOI=10.1056/nejmoa0900661;
RA Moslemi A.R., Lindberg C., Nilsson J., Tajsharghi H., Andersson B.,
RA Oldfors A.;
RT "Glycogenin-1 deficiency and inactivated priming of glycogen synthesis.";
RL N. Engl. J. Med. 362:1203-1210(2010).
CC -!- FUNCTION: Self-glucosylates, via an inter-subunit mechanism, to form an
CC oligosaccharide primer that serves as substrate for glycogen synthase.
CC {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-
CC glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360,
CC Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140573; EC=2.4.1.186;
CC Evidence={ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[1,4-alpha-D-glucosyl](n)-L-tyrosyl-[glycogenin] + UDP-alpha-
CC D-glucose = [1,4-alpha-D-glucosyl](n+1)-L-tyrosyl-[glycogenin] + H(+)
CC + UDP; Xref=Rhea:RHEA:56560, Rhea:RHEA-COMP:14606, Rhea:RHEA-
CC COMP:14607, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:140574; EC=2.4.1.186;
CC Evidence={ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213};
CC Note=Divalent metal ions. Required for self-glucosylation. Manganese is
CC the most effective.;
CC -!- ACTIVITY REGULATION: Inhibited by palladium ions.
CC {ECO:0000269|PubMed:30356213}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}.
CC -!- SUBUNIT: Homodimer (PubMed:22160680). Interacts (via C-terminus) with
CC glycogen synthase GYS1 (PubMed:17055998). Interacts (via C-terminus)
CC with glycogen synthase GYS2 (By similarity). This interaction is
CC required for GYS2-mediated glycogen synthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9R062, ECO:0000269|PubMed:17055998,
CC ECO:0000269|PubMed:22160680}.
CC -!- INTERACTION:
CC P46976; P13807: GYS1; NbExp=7; IntAct=EBI-740533, EBI-740553;
CC P46976-2; P13807: GYS1; NbExp=3; IntAct=EBI-12017394, EBI-740553;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=GN-1L;
CC IsoId=P46976-1; Sequence=Displayed;
CC Name=GN-1;
CC IsoId=P46976-2; Sequence=VSP_001769;
CC Name=GN-1S;
CC IsoId=P46976-3; Sequence=VSP_001768;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle and heart, with
CC lower levels in brain, lung, kidney and pancreas.
CC {ECO:0000269|PubMed:8602861}.
CC -!- PTM: Self-glycosylated by the transfer of glucose residues from UDP-
CC glucose to itself, forming an alpha-1,4-glycan of around 10 residues
CC attached to Tyr-195. {ECO:0000269|PubMed:22160680,
CC ECO:0000269|PubMed:30356213}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
CC -!- DISEASE: Glycogen storage disease 15 (GSD15) [MIM:613507]: A metabolic
CC disorder resulting in muscle weakness, associated with the glycogen
CC depletion in skeletal muscle, and cardiac arrhythmia, associated with
CC the accumulation of abnormal storage material in the heart. The
CC skeletal muscle shows a marked predominance of slow-twitch, oxidative
CC muscle fibers and mitochondrial proliferation.
CC {ECO:0000269|PubMed:20357282, ECO:0000269|PubMed:22160680}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Polyglucosan body myopathy 2 (PGBM2) [MIM:616199]: A glycogen
CC storage disease characterized by polyglucosan accumulation in muscle,
CC and skeletal myopathy without cardiac involvement. Most patients
CC manifest slowly progressive, hip girdle, shoulder girdle, and/or hand
CC and leg muscle weakness. Polyglucosan contains abnormally long and
CC poorly branched glucosyl chains and is variably resistant to digestion
CC by alpha-amylase. {ECO:0000269|PubMed:25272951}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; U44131; AAB00114.1; -; mRNA.
DR EMBL; U31525; AAB09752.1; -; mRNA.
DR EMBL; X79537; CAA56073.1; -; mRNA.
DR EMBL; AF065481; AAD31084.1; -; Genomic_DNA.
DR EMBL; AF065476; AAD31084.1; JOINED; Genomic_DNA.
DR EMBL; AF065477; AAD31084.1; JOINED; Genomic_DNA.
DR EMBL; AF065478; AAD31084.1; JOINED; Genomic_DNA.
DR EMBL; AF065479; AAD31084.1; JOINED; Genomic_DNA.
DR EMBL; AF065480; AAD31084.1; JOINED; Genomic_DNA.
DR EMBL; AF087942; AAD52093.1; -; mRNA.
DR EMBL; CR536547; CAG38784.1; -; mRNA.
DR EMBL; AC021059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78894.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78895.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78896.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78898.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78900.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78901.1; -; Genomic_DNA.
DR EMBL; BC000033; AAH00033.1; -; mRNA.
DR CCDS; CCDS3139.1; -. [P46976-1]
DR CCDS; CCDS54654.1; -. [P46976-2]
DR CCDS; CCDS54655.1; -. [P46976-3]
DR PIR; JC4695; JC4695.
DR RefSeq; NP_001171649.1; NM_001184720.1. [P46976-2]
DR RefSeq; NP_001171650.1; NM_001184721.1. [P46976-3]
DR RefSeq; NP_004121.2; NM_004130.3. [P46976-1]
DR PDB; 3Q4S; X-ray; 1.98 A; A=1-262.
DR PDB; 3QVB; X-ray; 2.26 A; A=1-262.
DR PDB; 3RMV; X-ray; 1.82 A; A=1-262.
DR PDB; 3RMW; X-ray; 1.93 A; A=1-262.
DR PDB; 3T7M; X-ray; 1.80 A; A/B=1-262.
DR PDB; 3T7N; X-ray; 1.98 A; A/B=1-262.
DR PDB; 3T7O; X-ray; 1.85 A; A/B=1-262.
DR PDB; 3U2T; X-ray; 2.05 A; A=1-262.
DR PDB; 3U2U; X-ray; 1.45 A; A/B=1-262.
DR PDB; 3U2V; X-ray; 1.50 A; A/B=1-262.
DR PDB; 3U2W; X-ray; 1.68 A; A/B=1-262.
DR PDB; 3U2X; X-ray; 1.77 A; A/B=1-262.
DR PDB; 6EQJ; X-ray; 2.18 A; A=1-262.
DR PDB; 6EQL; X-ray; 2.38 A; A/B=1-262.
DR PDBsum; 3Q4S; -.
DR PDBsum; 3QVB; -.
DR PDBsum; 3RMV; -.
DR PDBsum; 3RMW; -.
DR PDBsum; 3T7M; -.
DR PDBsum; 3T7N; -.
DR PDBsum; 3T7O; -.
DR PDBsum; 3U2T; -.
DR PDBsum; 3U2U; -.
DR PDBsum; 3U2V; -.
DR PDBsum; 3U2W; -.
DR PDBsum; 3U2X; -.
DR PDBsum; 6EQJ; -.
DR PDBsum; 6EQL; -.
DR AlphaFoldDB; P46976; -.
DR SMR; P46976; -.
DR BioGRID; 109247; 29.
DR IntAct; P46976; 25.
DR STRING; 9606.ENSP00000340736; -.
DR DrugBank; DB01861; Uridine diphosphate glucose.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; P46976; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P46976; -.
DR MetOSite; P46976; -.
DR PhosphoSitePlus; P46976; -.
DR BioMuta; GYG1; -.
DR EPD; P46976; -.
DR jPOST; P46976; -.
DR MassIVE; P46976; -.
DR MaxQB; P46976; -.
DR PaxDb; P46976; -.
DR PeptideAtlas; P46976; -.
DR PRIDE; P46976; -.
DR ProteomicsDB; 12738; -.
DR ProteomicsDB; 55779; -. [P46976-1]
DR ProteomicsDB; 55780; -. [P46976-2]
DR ProteomicsDB; 55781; -. [P46976-3]
DR Antibodypedia; 33551; 210 antibodies from 28 providers.
DR DNASU; 2992; -.
DR Ensembl; ENST00000296048.10; ENSP00000296048.6; ENSG00000163754.18. [P46976-2]
DR Ensembl; ENST00000345003.9; ENSP00000340736.4; ENSG00000163754.18. [P46976-1]
DR Ensembl; ENST00000484197.5; ENSP00000420683.1; ENSG00000163754.18. [P46976-3]
DR GeneID; 2992; -.
DR KEGG; hsa:2992; -.
DR MANE-Select; ENST00000345003.9; ENSP00000340736.4; NM_004130.4; NP_004121.2.
DR UCSC; uc003ewn.4; human. [P46976-1]
DR CTD; 2992; -.
DR DisGeNET; 2992; -.
DR GeneCards; GYG1; -.
DR HGNC; HGNC:4699; GYG1.
DR HPA; ENSG00000163754; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; GYG1; -.
DR MIM; 603942; gene.
DR MIM; 613507; phenotype.
DR MIM; 616199; phenotype.
DR neXtProt; NX_P46976; -.
DR OpenTargets; ENSG00000163754; -.
DR Orphanet; 263297; Glycogen storage disease with severe cardiomyopathy due to glycogenin deficiency.
DR Orphanet; 456369; Polyglucosan body myopathy type 2.
DR PharmGKB; PA29077; -.
DR VEuPathDB; HostDB:ENSG00000163754; -.
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000154674; -.
DR InParanoid; P46976; -.
DR OMA; GFCRKEG; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; P46976; -.
DR TreeFam; TF312839; -.
DR BioCyc; MetaCyc:HS08931-MON; -.
DR BRENDA; 2.4.1.186; 2681.
DR PathwayCommons; P46976; -.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR Reactome; R-HSA-3814836; Glycogen storage disease type XV (GYG1).
DR Reactome; R-HSA-3828062; Glycogen storage disease type 0 (muscle GYS1).
DR Reactome; R-HSA-5357609; Glycogen storage disease type II (GAA).
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; P46976; -.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 2992; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; GYG1; human.
DR EvolutionaryTrace; P46976; -.
DR GenomeRNAi; 2992; -.
DR Pharos; P46976; Tbio.
DR PRO; PR:P46976; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P46976; protein.
DR Bgee; ENSG00000163754; Expressed in biceps brachii and 213 other tissues.
DR ExpressionAtlas; P46976; baseline and differential.
DR Genevisible; P46976; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0008466; F:glycogenin glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Glycogen biosynthesis; Glycogen storage disease; Glycoprotein; Manganese;
KW Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..350
FT /note="Glycogenin-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000215176"
FT REGION 301..333
FT /note="Interaction with GYS1"
FT /evidence="ECO:0000269|PubMed:17055998"
FT BINDING 9..15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW,
FT ECO:0007744|PDB:3T7O"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N,
FT ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U,
FT ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W,
FT ECO:0007744|PDB:3U2X"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB,
FT ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW,
FT ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N,
FT ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T,
FT ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V,
FT ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB,
FT ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW,
FT ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N,
FT ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T,
FT ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V,
FT ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"
FT BINDING 133..135
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O"
FT BINDING 212..218
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW,
FT ECO:0007744|PDB:3T7O"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB,
FT ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW,
FT ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N,
FT ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T,
FT ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V,
FT ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X"
FT SITE 86
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT CARBOHYD 195
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000269|PubMed:22160680,
FT ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U,
FT ECO:0007744|PDB:3U2V"
FT VAR_SEQ 204..350
FT /note="FGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNMTHPEFLILWWNIFTT
FT NVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAISHLSLGEIPAMAQP
FT FVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ -> KMSQEPYHICPLGRSQLWH
FT SRLYPRKNGRNDGNRARLIIWEQIPLTTSRGNLTLTSSRNTAFFCEHIHFTSLVSDT
FT (in isoform GN-1S)"
FT /evidence="ECO:0000305"
FT /id="VSP_001768"
FT VAR_SEQ 277..293
FT /note="Missing (in isoform GN-1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8602861, ECO:0000303|PubMed:8661012,
FT ECO:0000303|Ref.6"
FT /id="VSP_001769"
FT VARIANT 16
FT /note="A -> P (in PGBM2; dbSNP:rs200947378)"
FT /evidence="ECO:0000269|PubMed:25272951"
FT /id="VAR_072706"
FT VARIANT 83
FT /note="T -> M (in GSD15; loss of autoglucosylation;
FT dbSNP:rs267606858)"
FT /evidence="ECO:0000269|PubMed:20357282,
FT ECO:0000269|PubMed:22160680"
FT /id="VAR_063768"
FT VARIANT 102
FT /note="D -> H (in PGBM2; dbSNP:rs143137713)"
FT /evidence="ECO:0000269|PubMed:25272951"
FT /id="VAR_072707"
FT MUTAGEN 195
FT /note="Y->F: Loss of glucosylation."
FT /evidence="ECO:0000269|PubMed:22160680"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3U2W"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3RMV"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:3U2U"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3U2U"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:3U2U"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:3U2U"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:3U2U"
SQ SEQUENCE 350 AA; 39384 MW; ABAEEB7160DEC4DF CRC64;
MTDQAFVTLT TNDAYAKGAL VLGSSLKQHR TTRRLVVLAT PQVSDSMRKV LETVFDEVIM
VDVLDSGDSA HLTLMKRPEL GVTLTKLHCW SLTQYSKCVF MDADTLVLAN IDDLFDREEL
SAAPDPGWPD CFNSGVFVYQ PSVETYNQLL HLASEQGSFD GGDQGILNTF FSSWATTDIR
KHLPFIYNLS SISIYSYLPA FKVFGASAKV VHFLGRVKPW NYTYDPKTKS VKSEAHDPNM
THPEFLILWW NIFTTNVLPL LQQFGLVKDT CSYVNVLSDL VYTLAFSCGF CRKEDVSGAI
SHLSLGEIPA MAQPFVSSEE RKERWEQGQA DYMGADSFDN IKRKLDTYLQ
