GLYG2_HUMAN
ID GLYG2_HUMAN Reviewed; 501 AA.
AC O15488; B7WNN6; O15485; O15486; O15487; O15489; O15490;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glycogenin-2;
DE Short=GN-2;
DE Short=GN2;
DE EC=2.4.1.186 {ECO:0000269|PubMed:9346895, ECO:0000269|PubMed:9857012};
GN Name=GYG2;
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], ALTERNATIVE SPLICING, CATALYTIC ACTIVITY,
RP FUNCTION, PATHWAY, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9346895; DOI=10.1074/jbc.272.44.27589;
RA Mu J., Skurat A.V., Roach P.J.;
RT "Glycogenin-2, a novel self-glucosylating protein involved in liver
RT glycogen biosynthesis.";
RL J. Biol. Chem. 272:27589-27597(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA), AND VARIANT ARG-313.
RC TISSUE=Skin;
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 [5]
RP GLYCOSYLATION AT TYR-228, MUTAGENESIS OF TYR-228 AND TYR-230, CATALYTIC
RP ACTIVITY, PATHWAY, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9857012; DOI=10.1074/jbc.273.52.34850;
RA Mu J., Roach P.J.;
RT "Characterization of human glycogenin-2, a self-glucosylating initiator of
RT liver glycogen metabolism.";
RL J. Biol. Chem. 273:34850-34856(1998).
RN [6]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-399 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8] {ECO:0007744|PDB:4UEG}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 35-300.
RA Fairhead M., Strain-Damerell C., Krojer T., Froese D.S., Kopec J.,
RA Nowak R., Burgess-Brown N., von Delft F., Arrowsmith C., Edwards A.,
RA Bountra C., Yue W.W.;
RT "Crystal Structure of Human Glycogenin-2 Catalytic Domain.";
RL Submitted (DEC-2014) to the PDB data bank.
RN [9]
RP VARIANT ARG-194.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
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:9346895, ECO:0000269|PubMed:9857012}.
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:9346895, ECO:0000269|PubMed:9857012};
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:9346895, ECO:0000269|PubMed:9857012};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P46976};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000269|PubMed:9346895, ECO:0000269|PubMed:9857012}.
CC -!- SUBUNIT: Homodimer, tightly complexed to glycogen synthase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=Alpha;
CC IsoId=O15488-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O15488-2; Sequence=VSP_001770;
CC Name=Gamma;
CC IsoId=O15488-3; Sequence=VSP_001771;
CC Name=Delta;
CC IsoId=O15488-4; Sequence=VSP_001772;
CC Name=Epsilon;
CC IsoId=O15488-5; Sequence=VSP_001773;
CC Name=Zeta;
CC IsoId=O15488-6; Sequence=VSP_001774;
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level)
CC (PubMed:9857012). Expressed preferentially in liver, heart, and
CC pancreas (PubMed:9346895). {ECO:0000269|PubMed:9346895,
CC ECO:0000269|PubMed:9857012}.
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-228. {ECO:0000269|PubMed:9857012}.
CC -!- MASS SPECTROMETRY: Mass=55211.89; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. Glycogenin
CC subfamily. {ECO:0000305}.
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DR EMBL; U94362; AAB84377.1; -; mRNA.
DR EMBL; U94363; AAB84378.1; -; mRNA.
DR EMBL; U94364; AAB84379.1; -; mRNA.
DR EMBL; U94357; AAB84373.1; -; mRNA.
DR EMBL; U94358; AAB84374.1; -; mRNA.
DR EMBL; U94360; AAB84375.1; -; mRNA.
DR EMBL; U94361; AAB84376.1; -; mRNA.
DR EMBL; AF179624; AAF61855.1; -; Genomic_DNA.
DR EMBL; AF179615; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179616; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179617; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179618; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179619; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179620; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179621; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179622; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AF179623; AAF61855.1; JOINED; Genomic_DNA.
DR EMBL; AC138085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023152; AAH23152.1; -; mRNA.
DR CCDS; CCDS14121.1; -. [O15488-1]
DR CCDS; CCDS48074.1; -. [O15488-2]
DR CCDS; CCDS55365.1; -. [O15488-4]
DR RefSeq; NP_001073324.1; NM_001079855.1. [O15488-2]
DR RefSeq; NP_001171631.1; NM_001184702.1.
DR RefSeq; NP_001171632.1; NM_001184703.1. [O15488-4]
DR RefSeq; NP_001171633.1; NM_001184704.1.
DR RefSeq; NP_003909.2; NM_003918.2. [O15488-1]
DR RefSeq; XP_011543902.1; XM_011545600.2. [O15488-2]
DR RefSeq; XP_016885416.1; XM_017029927.1. [O15488-1]
DR RefSeq; XP_016885417.1; XM_017029928.1. [O15488-1]
DR PDB; 4UEG; X-ray; 1.93 A; A/B=35-300.
DR PDBsum; 4UEG; -.
DR AlphaFoldDB; O15488; -.
DR SMR; O15488; -.
DR BioGRID; 114422; 30.
DR IntAct; O15488; 14.
DR STRING; 9606.ENSP00000370555; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GlyGen; O15488; 1 site.
DR iPTMnet; O15488; -.
DR PhosphoSitePlus; O15488; -.
DR BioMuta; GYG2; -.
DR EPD; O15488; -.
DR jPOST; O15488; -.
DR MassIVE; O15488; -.
DR MaxQB; O15488; -.
DR PaxDb; O15488; -.
DR PeptideAtlas; O15488; -.
DR PRIDE; O15488; -.
DR ProteomicsDB; 48689; -. [O15488-1]
DR ProteomicsDB; 48690; -. [O15488-2]
DR ProteomicsDB; 48691; -. [O15488-3]
DR ProteomicsDB; 48692; -. [O15488-4]
DR ProteomicsDB; 48693; -. [O15488-5]
DR ProteomicsDB; 48694; -. [O15488-6]
DR Antibodypedia; 486; 174 antibodies from 26 providers.
DR DNASU; 8908; -.
DR Ensembl; ENST00000353656.10; ENSP00000487294.1; ENSG00000056998.20. [O15488-4]
DR Ensembl; ENST00000381163.7; ENSP00000370555.3; ENSG00000056998.20. [O15488-1]
DR Ensembl; ENST00000398806.8; ENSP00000381786.3; ENSG00000056998.20. [O15488-2]
DR GeneID; 8908; -.
DR KEGG; hsa:8908; -.
DR MANE-Select; ENST00000398806.8; ENSP00000381786.3; NM_001079855.2; NP_001073324.1. [O15488-2]
DR UCSC; uc004cqs.2; human. [O15488-1]
DR CTD; 8908; -.
DR DisGeNET; 8908; -.
DR GeneCards; GYG2; -.
DR HGNC; HGNC:4700; GYG2.
DR HPA; ENSG00000056998; Tissue enriched (adipose).
DR MIM; 300198; gene.
DR neXtProt; NX_O15488; -.
DR OpenTargets; ENSG00000056998; -.
DR PharmGKB; PA29078; -.
DR VEuPathDB; HostDB:ENSG00000056998; -.
DR eggNOG; KOG1950; Eukaryota.
DR GeneTree; ENSGT00940000161628; -.
DR InParanoid; O15488; -.
DR OMA; VEHGSFD; -.
DR OrthoDB; 1424146at2759; -.
DR PhylomeDB; O15488; -.
DR TreeFam; TF312839; -.
DR BioCyc; MetaCyc:HS00703-MON; -.
DR BRENDA; 2.4.1.186; 2681.
DR PathwayCommons; O15488; -.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-3858516; Glycogen storage disease type 0 (liver GYS2).
DR Reactome; R-HSA-3878781; Glycogen storage disease type IV (GBE1).
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR SignaLink; O15488; -.
DR UniPathway; UPA00164; -.
DR BioGRID-ORCS; 8908; 12 hits in 698 CRISPR screens.
DR ChiTaRS; GYG2; human.
DR GenomeRNAi; 8908; -.
DR Pharos; O15488; Tbio.
DR PRO; PR:O15488; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15488; protein.
DR Bgee; ENSG00000056998; Expressed in adipose tissue and 127 other tissues.
DR ExpressionAtlas; O15488; baseline and differential.
DR Genevisible; O15488; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0102751; F:UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IDA: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; Alternative splicing; Glycogen biosynthesis; Glycoprotein;
KW Manganese; Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..501
FT /note="Glycogenin-2"
FT /id="PRO_0000215180"
FT BINDING 42..48
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 166..168
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 193..197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 245..251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P46976"
FT SITE 119
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P13280"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 228
FT /note="O-linked (Glc...) tyrosine"
FT /evidence="ECO:0000269|PubMed:9857012"
FT VAR_SEQ 3..42
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000305"
FT /id="VSP_001771"
FT VAR_SEQ 3..33
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001770"
FT VAR_SEQ 378..448
FT /note="Missing (in isoform Delta)"
FT /evidence="ECO:0000305"
FT /id="VSP_001772"
FT VAR_SEQ 407..501
FT /note="Missing (in isoform Epsilon)"
FT /evidence="ECO:0000305"
FT /id="VSP_001773"
FT VAR_SEQ 413..448
FT /note="Missing (in isoform Zeta)"
FT /evidence="ECO:0000305"
FT /id="VSP_001774"
FT VARIANT 7
FT /note="H -> Y (in dbSNP:rs11797037)"
FT /id="VAR_053110"
FT VARIANT 194
FT /note="G -> R (found in a renal cell carcinoma case;
FT somatic mutation; dbSNP:rs200824650)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064717"
FT VARIANT 270
FT /note="A -> V (in dbSNP:rs2306734)"
FT /id="VAR_010401"
FT VARIANT 313
FT /note="H -> R (in dbSNP:rs2306735)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024457"
FT VARIANT 373
FT /note="R -> C (in dbSNP:rs17330993)"
FT /id="VAR_031224"
FT MUTAGEN 228
FT /note="Y->F: Loss of autoglucosylation."
FT /evidence="ECO:0000269|PubMed:9857012"
FT MUTAGEN 230
FT /note="Y->F: No loss of activity."
FT /evidence="ECO:0000269|PubMed:9857012"
FT CONFLICT 413
FT /note="Missing (in Ref. 1; AAB84378)"
FT /evidence="ECO:0000305"
FT CONFLICT 462..464
FT /note="EKV -> AGI (in Ref. 1; AAB84376)"
FT /evidence="ECO:0000305"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4UEG"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:4UEG"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 145..149
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:4UEG"
FT TURN 204..209
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:4UEG"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:4UEG"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:4UEG"
FT HELIX 292..298
FT /evidence="ECO:0007829|PDB:4UEG"
SQ SEQUENCE 501 AA; 55184 MW; 8488A09D6E564693 CRC64;
MSETEFHHGA QAGLELLRSS NSPTSASQSA GMTVTDQAFV TLATNDIYCQ GALVLGQSLR
RHRLTRKLVV LITPQVSSLL RVILSKVFDE VIEVNLIDSA DYIHLAFLKR PELGLTLTKL
HCWTLTHYSK CVFLDADTLV LSNVDELFDR GEFSAAPDPG WPDCFNSGVF VFQPSLHTHK
LLLQHAMEHG SFDGADQGLL NSFFRNWSTT DIHKHLPFIY NLSSNTMYTY SPAFKQFGSS
AKVVHFLGSM KPWNYKYNPQ SGSVLEQGSA SSSQHQAAFL HLWWTVYQNN VLPLYKSVQA
GEARASPGHT LCHSDVGGPC ADSASGVGEP CENSTPSAGV PCANSPLGSN QPAQGLPEPT
QIVDETLSLP EGRRSEDMIA CPETETPAVI TCDPLSQPSP QPADFTETET ILQPANKVES
VSSEETFEPS QELPAEALRD PSLQDALEVD LAVSVSQISI EEKVKELSPE EERRKWEEGR
IDYMGKDAFA RIQEKLDRFL Q
