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 24-JAN-2024, entry version 202. DE RecName: Full=Glycogenin-1 {ECO:0000312|HGNC:HGNC:4699}; DE Short=GN-1; DE Short=GN1; DE EC=2.4.1.186 {ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213}; GN Name=GYG1 {ECO:0000312|HGNC:HGNC:4699}; GN Synonyms=GYG {ECO:0000312|HGNC:HGNC:4699}; 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). RN [19] {ECO:0000312|PDB:7ZBN} RP STRUCTURE BY ELECTRON MICROSCOPY (2.62 ANGSTROMS) IN COMPLEX WITH GYS1, RP SUBUNIT, GLYCOSYLATION AT TYR-195, AND MUTAGENESIS OF TYR-195. RX PubMed=35690592; DOI=10.1038/s41467-022-31109-6; RA Marr L., Biswas D., Daly L.A., Browning C., Vial S.C.M., Maskell D.P., RA Hudson C., Bertrand J.A., Pollard J., Ranson N.A., Khatter H., Eyers C.E., RA Sakamoto K., Zeqiraj E.; RT "Mechanism of glycogen synthase inactivation and interaction with RT glycogenin."; RL Nat. Commun. 13:3372-3372(2022). RN [20] {ECO:0000312|PDB:7Q0B, ECO:0000312|PDB:7Q0S, ECO:0000312|PDB:7Q12, ECO:0000312|PDB:7Q13} RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH GYS1, AND RP SUBUNIT. RX PubMed=35835870; DOI=10.1038/s41594-022-00799-3; RA McCorvie T.J., Loria P.M., Tu M., Han S., Shrestha L., Froese D.S., RA Ferreira I.M., Berg A.P., Yue W.W.; RT "Molecular basis for the regulation of human glycogen synthase by RT phosphorylation and glucose-6-phosphate."; RL Nat. Struct. Mol. Biol. 29:628-638(2022). CC -!- FUNCTION: Glycogenin participates in the glycogen biosynthetic process CC along with glycogen synthase and glycogen branching enzyme. It self- CC 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23361; 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56561; 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: Part of the GYS1-GYG1 complex, a heterooctamer composed of a CC tetramer of GYS1 and 2 dimers of GYG1, where each GYS1 protomer binds CC to one GYG1 subunit (via GYG1 C-terminus); the GYS1 tetramer may CC dissociate from GYG1 dimers to continue glycogen polymerization on its CC own (PubMed:17055998, PubMed:22160680, PubMed:35690592, CC PubMed:35835870). May also form a heterooctamer complex with GYS2 (via CC GYG1 C-terminus) (By similarity). {ECO:0000250|UniProtKB:Q9R062, CC ECO:0000269|PubMed:17055998, ECO:0000269|PubMed:22160680, CC ECO:0000269|PubMed:35690592, ECO:0000269|PubMed:35835870}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7OVX; X-ray; 1.70 A; Q=339-350. DR PDB; 7Q0B; EM; 3.00 A; E/F/G/H=1-350. DR PDB; 7Q0S; EM; 4.00 A; E/F/G/H=1-350. DR PDB; 7Q12; EM; 3.70 A; E/F/G/H=1-350. DR PDB; 7Q13; EM; 3.00 A; E/F/G/H=1-350. DR PDB; 7ZBN; EM; 2.62 A; E/F/G/H=1-350. DR PDB; 8CVX; EM; 3.50 A; E/F/G/H=1-350. DR PDB; 8CVY; EM; 3.60 A; E/G/H=1-350. DR PDB; 8CVZ; EM; 3.52 A; E/F/G/H/I/J=1-350. 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 PDBsum; 7OVX; -. DR PDBsum; 7Q0B; -. DR PDBsum; 7Q0S; -. DR PDBsum; 7Q12; -. DR PDBsum; 7Q13; -. DR PDBsum; 7ZBN; -. DR PDBsum; 8CVX; -. DR PDBsum; 8CVY; -. DR PDBsum; 8CVZ; -. DR AlphaFoldDB; P46976; -. DR EMDB; EMD-13743; -. DR EMDB; EMD-13751; -. DR EMDB; EMD-13752; -. DR EMDB; EMD-13753; -. DR EMDB; EMD-14587; -. DR EMDB; EMD-27020; -. DR EMDB; EMD-27021; -. DR EMDB; EMD-27022; -. DR SMR; P46976; -. DR BioGRID; 109247; 41. DR IntAct; P46976; 26. DR STRING; 9606.ENSP00000340736; -. DR DrugBank; DB01861; Uridine diphosphate glucose. DR DrugBank; DB03435; Uridine-5'-Diphosphate. DR CAZy; GT8; Glycosyltransferase Family 8. DR GlyCosmos; P46976; 1 site, No reported glycans. 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; 9606-ENSP00000340736; -. DR PeptideAtlas; P46976; -. DR ProteomicsDB; 12738; -. DR ProteomicsDB; 55779; -. [P46976-1] DR ProteomicsDB; 55780; -. [P46976-2] DR ProteomicsDB; 55781; -. [P46976-3] DR Pumba; P46976; -. DR Antibodypedia; 33551; 229 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 AGR; HGNC:4699; -. 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; TCETVQG; -. DR OrthoDB; 306230at2759; -. DR PhylomeDB; P46976; -. DR TreeFam; TF312839; -. DR BioCyc; MetaCyc:HS08931-MONOMER; -. 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; 17 hits in 1156 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 215 other cell types or tissues. DR ExpressionAtlas; P46976; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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 CDD; cd02537; GT8_Glycogenin; 1. DR InterPro; IPR002495; Glyco_trans_8. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR11183; GLYCOGENIN SUBFAMILY MEMBER; 1. DR PANTHER; PTHR11183:SF164; GLYCOGENIN-1; 1. DR Pfam; PF01501; Glyco_transf_8; 2. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR Genevisible; P46976; HS. 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 ECO:0000269|PubMed:35690592" 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" FT HELIX 319..327 FT /evidence="ECO:0007829|PDB:7ZBN" FT TURN 332..336 FT /evidence="ECO:0007829|PDB:7Q0B" FT HELIX 340..347 FT /evidence="ECO:0007829|PDB:7OVX" 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 //