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G6PD_HUMAN
ID   G6PD_HUMAN              Reviewed;         515 AA.
AC   P11413; D3DWX9; Q16000; Q16765; Q8IU70; Q8IU88; Q8IUA6; Q96PQ2;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 261.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49 {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:743300};
GN   Name=G6PD;
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 SHORT).
RX   PubMed=3515319; DOI=10.1093/nar/14.6.2511;
RA   Persico M.G., Viglietto G., Martini G., Toniolo D., Paonessa G.,
RA   Moscatelli C., Dono R., Vulliamy T.J., Luzzatto L., D'Urso M.;
RT   "Isolation of human glucose-6-phosphate dehydrogenase (G6PD) cDNA clones:
RT   primary structure of the protein and unusual 5' non-coding region.";
RL   Nucleic Acids Res. 14:2511-2522(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2428611; DOI=10.1002/j.1460-2075.1986.tb04436.x;
RA   Martini G., Toniolo D., Vulliamy T., Luzzatto L., Dono R., Viglietto G.,
RA   Paonessa G., D'Urso M., Persico M.G.;
RT   "Structural analysis of the X-linked gene encoding human glucose 6-
RT   phosphate dehydrogenase.";
RL   EMBO J. 5:1849-1855(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL NUCLEOTIDE SEQUENCE
RP   [MRNA] (ISOFORM LONG), VARIANT NSHA MET-68, AND VARIANT ASP-126.
RX   PubMed=2836867; DOI=10.1073/pnas.85.11.3951;
RA   Hirono A., Beutler E.;
RT   "Molecular cloning and nucleotide sequence of cDNA for human glucose-6-
RT   phosphate dehydrogenase variant A(-).";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3951-3954(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NSHA MET-68, AND VARIANT
RP   ASP-126.
RX   PubMed=1889820; DOI=10.1016/0888-7543(91)90465-q;
RA   Chen E.Y., Cheng A., Lee A., Kuang W., Hillier L., Green P.,
RA   Schlessinger D., Ciccodicola A., D'Urso M.;
RT   "Sequence of human glucose-6-phosphate dehydrogenase cloned in plasmids and
RT   a yeast artificial chromosome.";
RL   Genomics 10:792-800(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NSHA MET-68, AND VARIANT
RP   ASP-126.
RX   PubMed=8733135; DOI=10.1093/hmg/5.5.659;
RA   Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L.,
RA   Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.;
RT   "Long-range sequence analysis in Xq28: thirteen known and six candidate
RT   genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci.";
RL   Hum. Mol. Genet. 5:659-668(1996).
RN   [6]
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   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Lung;
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   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-71.
RX   PubMed=2758468; DOI=10.1016/0092-8674(89)90440-6;
RA   Kanno H., Huang I.Y., Kan Y.W., Yoshida A.;
RT   "Two structural genes on different chromosomes are required for encoding
RT   the major subunit of human red cell glucose-6-phosphate dehydrogenase.";
RL   Cell 58:595-606(1989).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-71 (ISOFORM 3).
RX   PubMed=8466644; DOI=10.1089/dna.1993.12.209;
RA   Kanno H., Kondoh T., Yoshida A.;
RT   "5' structure and expression of human glucose-6-phosphate dehydrogenase
RT   mRNA.";
RL   DNA Cell Biol. 12:209-215(1993).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX   PubMed=1874446; DOI=10.1016/0378-1119(91)90078-p;
RA   Toniolo D., Filippi M., Dono R., Lettieri T., Martini G.;
RT   "The CpG island in the 5' region of the G6PD gene of man and mouse.";
RL   Gene 102:197-203(1991).
RN   [12]
RP   PROTEIN SEQUENCE OF 2-9.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-34, AND VARIANT NSHA ARG-32.
RX   PubMed=1945893; DOI=10.1093/nar/19.21.6056;
RA   Chao L.T., Du C.S., Louie E., Zuo L., Chen E., Lubin B., Chiu D.T.;
RT   "A to G substitution identified in exon 2 of the G6PD gene among G6PD
RT   deficient Chinese.";
RL   Nucleic Acids Res. 19:6056-6056(1991).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-515 (ISOFORM SHORT), VARIANT NSHA
RP   MET-68, AND VARIANT ASP-126.
RX   PubMed=12524354; DOI=10.1093/genetics/162.4.1849;
RA   Saunders M.A., Hammer M.F., Nachman M.W.;
RT   "Nucleotide variability at G6pd and the signature of malarial selection in
RT   humans.";
RL   Genetics 162:1849-1861(2002).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 154-515 (ISOFORM SHORT).
RX   PubMed=3012556; DOI=10.1073/pnas.83.12.4157;
RA   Takizawa T., Huang I.-Y., Ikuta T., Yoshida A.;
RT   "Human glucose-6-phosphate dehydrogenase: primary structure and cDNA
RT   cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:4157-4161(1986).
RN   [16]
RP   PROTEIN SEQUENCE OF 199-215.
RX   PubMed=3126064; DOI=10.1111/j.1432-1033.1988.tb13815.x;
RA   Camardella L., Caruso C., Rutigliano B., Romano M., di Prisco G.,
RA   Descalzi-Cancedda F.;
RT   "Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a
RT   reactive lysyl residue labelled with pyridoxal 5'-phosphate.";
RL   Eur. J. Biochem. 171:485-489(1988).
RN   [17]
RP   PROTEIN SEQUENCE OF 509-515.
RX   PubMed=6696761; DOI=10.1016/0006-291x(84)91105-7;
RA   Descalzi-Cancedda F., Caruso C., Romano M., di Prisco G., Camardella L.;
RT   "Amino acid sequence of the carboxy-terminal end of human erythrocyte
RT   glucose-6-phosphate dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 118:332-338(1984).
RN   [18]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX   PubMed=743300; DOI=10.1016/0006-291x(78)91147-6;
RA   Benatti U., Morelli A., Frascio M., Melloni E., Salamino F., Sparatore B.,
RA   Pontremoli S., De Flora A.;
RT   "Glucose 6-phosphate dehydrogenase activity in membranes of erythrocytes
RT   from normal individuals and subjects with Mediterranean G6PD deficiency.";
RL   Biochem. Biophys. Res. Commun. 85:1318-1324(1978).
RN   [19]
RP   ALTERNATIVE SPLICING.
RX   PubMed=2910917; DOI=10.1172/jci113881;
RA   Hirono A., Beutler E.;
RT   "Alternative splicing of human glucose-6-phosphate dehydrogenase messenger
RT   RNA in different tissues.";
RL   J. Clin. Invest. 83:343-346(1989).
RN   [20]
RP   ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=7857286; DOI=10.1006/bbrc.1995.1192;
RA   Camardella L., Damonte G., Carratore V., Benatti U., Tonetti M., Moneti G.;
RT   "Glucose 6-phosphate dehydrogenase from human erythrocytes: identification
RT   of N-acetyl-alanine at the N-terminus of the mature protein.";
RL   Biochem. Biophys. Res. Commun. 207:331-338(1995).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 (ISOFORM 3), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [22]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [23]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89; LYS-171; LYS-403; LYS-432 AND
RP   LYS-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [24]
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   [25]
RP   REVIEW.
RX   PubMed=22431005; DOI=10.1002/iub.1017;
RA   Stanton R.C.;
RT   "Glucose-6-phosphate dehydrogenase, NADPH, and cell survival.";
RL   IUBMB Life 64:362-369(2012).
RN   [26]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-10 AND TYR-503, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [29]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ACETYLATION AT LYS-403 BY ELP3,
RP   DEACETYLATION AT LYS-403 BY SIRT2, INTERACTION WITH SIRT2, MUTAGENESIS OF
RP   LYS-171; LYS-386 AND LYS-403, AND SUBUNIT.
RX   PubMed=24769394; DOI=10.1002/embj.201387224;
RA   Wang Y.P., Zhou L.S., Zhao Y.Z., Wang S.W., Chen L.L., Liu L.X., Ling Z.Q.,
RA   Hu F.J., Sun Y.P., Zhang J.Y., Yang C., Yang Y., Xiong Y., Guan K.L.,
RA   Ye D.;
RT   "Regulation of G6PD acetylation by KAT9/SIRT2 modulates NADPH homeostasis
RT   and cell survival during oxidative stress.";
RL   EMBO J. 33:1304-1320(2014).
RN   [30]
RP   HYDROXYBUTYRYLATION AT LYS-171.
RX   PubMed=29192674; DOI=10.1038/cr.2017.149;
RA   Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA   Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT   "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT   pathway.";
RL   Cell Res. 28:111-125(2018).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF VARIANT CANTON IN COMPLEX WITH
RP   NADP, AND SUBUNIT.
RX   PubMed=10745013; DOI=10.1016/s0969-2126(00)00104-0;
RA   Au S.W., Gover S., Lam V.M., Adams M.J.;
RT   "Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a
RT   structural NADP(+) molecule and provides insights into enzyme deficiency.";
RL   Structure 8:293-303(2000).
RN   [32]
RP   REVIEW ON VARIANTS.
RX   PubMed=8364584; DOI=10.1002/humu.1380020302;
RA   Vulliamy T., Beutler E., Luzzatto L.;
RT   "Variants of glucose-6-phosphate dehydrogenase are due to missense
RT   mutations spread throughout the coding region of the gene.";
RL   Hum. Mutat. 2:159-167(1993).
RN   [33]
RP   REVIEW ON VARIANTS.
RX   PubMed=11857737; DOI=10.1002/humu.10036;
RA   Kwok C.J., Martin A.C., Au S.W., Lam V.M.;
RT   "G6PDdb, an integrated database of glucose-6-phosphate dehydrogenase (G6PD)
RT   mutations.";
RL   Hum. Mutat. 19:217-224(2002).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 28-514 IN COMPLEX WITH NADP AND
RP   GLUCOSE 6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=15858258; DOI=10.1107/s0907444905002350;
RA   Kotaka M., Gover S., Vandeputte-Rutten L., Au S.W., Lam V.M., Adams M.J.;
RT   "Structural studies of glucose-6-phosphate and NADP+ binding to human
RT   glucose-6-phosphate dehydrogenase.";
RL   Acta Crystallogr. D 61:495-504(2005).
RN   [35]
RP   VARIANT ASP-126.
RX   PubMed=3446582; DOI=10.1016/0888-7543(87)90048-6;
RA   Takizawa T., Yoneyama Y., Miwa S., Yoshida A.;
RT   "A single nucleotide base transition is the basis of the common human
RT   glucose-6-phosphate dehydrogenase variant A (+).";
RL   Genomics 1:228-231(1987).
RN   [36]
RP   VARIANTS.
RX   PubMed=3393536; DOI=10.1073/pnas.85.14.5171;
RA   Vulliamy T.J., D'Urso M., Battistuzzi G., Estrada M., Foulkes N.S.,
RA   Martini G., Calabro V., Poggi V., Giordano R., Town M., Luzzatto L.,
RA   Persico M.G.;
RT   "Diverse point mutations in the human glucose-6-phosphate dehydrogenase
RT   gene cause enzyme deficiency and mild or severe hemolytic anemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:5171-5175(1988).
RN   [37]
RP   VARIANTS NSHA PHE-188 AND HIS-282.
RX   PubMed=2912069;
RA   de Vita G., Alcalay M., Sampietro M., Cappelini M.D., Fiorelli G.,
RA   Toniolo D.;
RT   "Two point mutations are responsible for G6PD polymorphism in Sardinia.";
RL   Am. J. Hum. Genet. 44:233-240(1989).
RN   [38]
RP   VARIANTS NSHA PRO-198; CYS-387; LEU-394; ASP-410 AND PRO-439, VARIANT
RP   MEXICO CITY GLN-227, AND VARIANT IERAPETRA SER-353.
RX   PubMed=1611091;
RA   Beutler E., Westwood B., Prchal J.T., Vaca C.S., Bartsocas C.S.,
RA   Baronciani L.;
RT   "New glucose-6-phosphate dehydrogenase mutations from various ethnic
RT   groups.";
RL   Blood 80:255-256(1992).
RN   [39]
RP   VARIANT NSHA HIS-393.
RX   PubMed=1536798; DOI=10.1111/j.1365-2141.1992.tb06409.x;
RA   Filosa S., Calabro V., Vallone D., Poggi V., Mason P., Pagnini D.,
RA   Alfinito F., Rotoli B., Martini G., Luzzatto L., Battistuzzi G.;
RT   "Molecular basis of chronic non-spherocytic haemolytic anaemia: a new G6PD
RT   variant (393arg-to-his) with abnormal K(m) G6P and marked in vivo
RT   instability.";
RL   Br. J. Haematol. 80:111-116(1992).
RN   [40]
RP   VARIANT NSHA CYS-454.
RX   PubMed=1303180; DOI=10.1093/hmg/1.3.205;
RA   Perng L.-I., Chiou S.-S., Liu T.-C., Chang J.-G.;
RT   "A novel C to T substitution at nucleotide 1360 of cDNA which abolishes a
RT   natural Hha I site accounts for a new G6PD deficiency gene in Chinese.";
RL   Hum. Mol. Genet. 1:205-205(1992).
RN   [41]
RP   VARIANT NSHA LYS-317.
RX   PubMed=1303182; DOI=10.1093/hmg/1.3.209;
RA   Ahluwalia A., Corcoran C.M., Vulliamy T.J., Ishwad C.S., Naidu J.M.,
RA   Stevens D.J., Mason P.J., Luzzatto L.;
RT   "G6PD Kalyan and G6PD Kerala; two deficient variants in India caused by the
RT   same 317 Glu-->Lys mutation.";
RL   Hum. Mol. Genet. 1:209-210(1992).
RN   [42]
RP   VARIANT NSHA THR-48.
RX   PubMed=8490627; DOI=10.1093/hmg/2.1.81;
RA   Nafa K., Reghis A., Osmani N., Baghli L., Benabadji M., Kaplan J.-C.,
RA   Vulliamy T.J., Luzzatto L.;
RT   "G6PD Aures: a new mutation (48 Ile-->Thr) causing mild G6PD deficiency is
RT   associated with favism.";
RL   Hum. Mol. Genet. 2:81-82(1993).
RN   [43]
RP   VARIANT NSHA GLY-176.
RX   PubMed=8193373;
RA   Hirono A., Miwa S., Fujii H., Ishida F., Yamada K., Kubota K.;
RT   "Molecular study of eight Japanese cases of glucose-6-phosphate
RT   dehydrogenase deficiency by nonradioisotopic single-strand conformation
RT   polymorphism analysis.";
RL   Blood 83:3363-3368(1994).
RN   [44]
RP   VARIANT NSHA LEU-396.
RX   PubMed=7959695; DOI=10.1007/bf00211027;
RA   Filosa S., Cai W., Galanello R., Cao A., de Mattia D., Schettini F.,
RA   Martini G.;
RT   "A novel single-base mutation in the glucose 6-phosphate dehydrogenase gene
RT   is associated with chronic non-spherocytic haemolytic anaemia.";
RL   Hum. Genet. 94:560-562(1994).
RN   [45]
RP   VARIANTS NAMORU; VANUA LAVA; NAONE AND UNION.
RX   PubMed=7825590;
RA   Ganczakowski M., Town M., Bowden D.K., Vulliamy T.J., Kaneko A.,
RA   Clegg J.B., Weatherall D.J., Luzzatto L.;
RT   "Multiple glucose 6-phosphate dehydrogenase-deficient variants correlate
RT   with malaria endemicity in the Vanuatu archipelago (southwestern
RT   Pacific).";
RL   Am. J. Hum. Genet. 56:294-301(1995).
RN   [46]
RP   VARIANT NSHA GLY-44.
RX   PubMed=8533762;
RA   Kaeda J.S., Chhotray G.P., Ranjit M.R., Bautista J.M., Reddy P.H.,
RA   Stevens D., Naidu J.M., Britt R.P., Vulliamy T.J., Luzzatto L., Mason P.J.;
RT   "A new glucose-6-phosphate dehydrogenase variant, G6PD Orissa (44
RT   Ala-->Gly), is the major polymorphic variant in tribal populations in
RT   India.";
RL   Am. J. Hum. Genet. 57:1335-1341(1995).
RN   [47]
RP   VARIANTS NSHA PRO-75; ASP-163; LYS-274 AND PHE-278.
RX   PubMed=7858267;
RA   Mason P.J., Sonati M.F., Macdonald D., Lanza C., Busutil D., Town M.,
RA   Corcoran C.M., Kaeda J.S., Stevens D.J., Al-Ismail S., Altay C., Hatton C.,
RA   Lewis D.S., McMullin M.F., Meloni T., Paul B., Pippard M., Prentice A.G.,
RA   Vulliamy T.J., Luzzatto L.;
RT   "New glucose-6-phosphate dehydrogenase mutations associated with chronic
RT   anemia.";
RL   Blood 85:1377-1380(1995).
RN   [48]
RP   VARIANT NSHA CYS-387, AND VARIANT ASP-126.
RX   PubMed=9452072; DOI=10.1002/humu.1380110151;
RA   Vlachos A., Westwood B., Lipton J.M., Beutler E.;
RT   "G6PD Mount Sinai: a new severe hemolytic variant characterized by dual
RT   mutations at nucleotides 376G and 1159T (N126D).";
RL   Hum. Mutat. Suppl. 1:S154-S155(1998).
RN   [49]
RP   VARIANT SINNAI LEU-12.
RX   PubMed=10627140;
RA   Galanello R., Loi D., Sollaino C., Dessi S., Cao A., Melis M.A.;
RT   "A new glucose 6 phosphate dehydrogenase variant, G6PD Sinnai (34 G->T).";
RL   Hum. Mutat. 12:72-73(1998).
RN   [50]
RP   VARIANT REHOVOT HIS-322.
RX   PubMed=11112389; DOI=10.1006/bcmd.2000.0334;
RA   Iancovici-Kidon M., Sthoeger D., Abrahamov A., Volach B., Beutler E.,
RA   Gelbart T., Barak Y.;
RT   "A new exon 9 glucose-6-phosphate dehydrogenase mutation (G6PD 'Rehovot')
RT   in a Jewish Ethiopian family with variable phenotypes.";
RL   Blood Cells Mol. Dis. 26:567-571(2000).
RN   [51]
RP   VARIANT NILGIRIS HIS-198, AND VARIANT COIMBRA CYS-198.
RX   PubMed=18043863; DOI=10.1007/s10038-007-0225-3;
RA   Chalvam R., Kedar P.S., Colah R.B., Ghosh K., Mukherjee M.B.;
RT   "A novel R198H mutation in the glucose-6-phosphate dehydrogenase gene in
RT   the tribal groups of the Nilgiris in Southern India.";
RL   J. Hum. Genet. 53:181-184(2008).
RN   [52]
RP   ASSOCIATION OF VARIANT NSHA SER-163 WITH REDUCED DENSITY OF PLASMODIUM
RP   VIVAX.
RX   PubMed=20007901; DOI=10.1126/science.1178849;
RA   Louicharoen C., Patin E., Paul R., Nuchprayoon I., Witoonpanich B.,
RA   Peerapittayamongkol C., Casademont I., Sura T., Laird N.M.,
RA   Singhasivanon P., Quintana-Murci L., Sakuntabhai A.;
RT   "Positively selected G6PD-Mahidol mutation reduces Plasmodium vivax density
RT   in Southeast Asians.";
RL   Science 326:1546-1549(2009).
RN   [53]
RP   VARIANT NSHA SER-198, CHARACTERIZATION OF VARIANT NSHA SER-198, FUNCTION,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=26479991; DOI=10.1097/mph.0000000000000435;
RA   Warny M., Lausen B., Birgens H., Knabe N., Petersen J.;
RT   "Severe G6PD Deficiency Due to a New Missense Mutation in an Infant of
RT   Northern European Descent.";
RL   J. Pediatr. Hematol. Oncol. 37:E497-E499(2015).
RN   [54]
RP   VARIANT ASP-126.
RX   PubMed=27535533; DOI=10.1038/nature19057;
RG   Exome Aggregation Consortium;
RA   Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA   O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA   Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA   Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA   Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA   Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA   Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA   Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA   Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA   Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA   Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA   McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA   Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA   Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA   Daly M.J., MacArthur D.G.;
RT   "Analysis of protein-coding genetic variation in 60,706 humans.";
RL   Nature 536:285-291(2016).
RN   [55]
RP   VARIANT DINDORI PHE-184, CHARACTERIZATION OF VARIANT DINDORI PHE-184, AND
RP   VARIANT KAIPING HIS-463.
RA   Devendra R., Shanmugam R., Singh M.P.S.S., Vishwakarma C.P., Godbhole S.,
RA   Singh N., Gupta V., Kedar P., Mukherjee M.B.;
RT   "Identification of a novel S184F mutation causing glucose-6-phosphate-
RT   dehydrogenase deficiency in a tribal family of Madhya Pradesh, Central
RT   India.";
RL   Meta Gene 12:130-133(2017).
RN   [56]
RP   VARIANT NILGIRIS HIS-198.
RX   PubMed=29333274; DOI=10.1038/hgv.2017.57;
RA   Canu G., Mazzuccato G., Urbani A., Minucci A.;
RT   "Report of an Italian family carrying a typical Indian variant of the
RT   Nilgiris tribal groups resulting from a de novo occurrence.";
RL   Hum. Genome Var. 5:17057-17057(2018).
RN   [57]
RP   VARIANT NSHA VAL-321, AND CHARACTERIZATION OF VARIANT NSHA VAL-321.
RX   PubMed=30988594; DOI=10.1007/s12288-018-1049-3;
RA   Devendra R., Warang P., Gupta V., Chiddarwar A., Kedar P., Agarwal M.B.,
RA   Mukherjee M.B.;
RT   "A novel G6PD p.Gly321Val mutation causing severe hemolysis in an Indian
RT   infant.";
RL   Indian J. Hematol. Blood Transfus. 35:399-401(2019).
CC   -!- FUNCTION: Catalyzes the rate-limiting step of the oxidative pentose-
CC       phosphate pathway, which represents a route for the dissimilation of
CC       carbohydrates besides glycolysis. The main function of this enzyme is
CC       to provide reducing power (NADPH) and pentose phosphates for fatty acid
CC       and nucleic acid synthesis. {ECO:0000269|PubMed:15858258,
CC       ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:26479991,
CC       ECO:0000269|PubMed:743300}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC         lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:61548; EC=1.1.1.49;
CC         Evidence={ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394,
CC         ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:743300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842;
CC         Evidence={ECO:0000269|PubMed:26479991};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.07 uM for NADP {ECO:0000269|PubMed:15858258};
CC         KM=52 uM for glucose 6-phosphate {ECO:0000269|PubMed:15858258};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       1/3. {ECO:0000269|PubMed:15858258, ECO:0000269|PubMed:24769394,
CC       ECO:0000269|PubMed:26479991, ECO:0000269|PubMed:743300}.
CC   -!- SUBUNIT: Homotetramer; dimer of dimers (PubMed:24769394,
CC       PubMed:10745013, PubMed:15858258). Interacts with SIRT2; the
CC       interaction is enhanced by H(2)O(2) treatment (PubMed:24769394).
CC       {ECO:0000269|PubMed:10745013, ECO:0000269|PubMed:15858258,
CC       ECO:0000269|PubMed:24769394}.
CC   -!- INTERACTION:
CC       P11413; P11413: G6PD; NbExp=3; IntAct=EBI-4289891, EBI-4289891;
CC       P11413; P04792: HSPB1; NbExp=2; IntAct=EBI-4289891, EBI-352682;
CC       P11413; Q8IXJ6: SIRT2; NbExp=3; IntAct=EBI-4289891, EBI-477232;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:743300}.
CC       Membrane; Peripheral membrane protein {ECO:0000269|PubMed:743300}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Short;
CC         IsoId=P11413-1; Sequence=Displayed;
CC       Name=Long;
CC         IsoId=P11413-2; Sequence=VSP_001592;
CC       Name=3;
CC         IsoId=P11413-3; Sequence=VSP_037802;
CC   -!- TISSUE SPECIFICITY: Isoform Long is found in lymphoblasts, granulocytes
CC       and sperm.
CC   -!- PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its
CC       homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403;
CC       deacetylation stimulates its enzyme activity.
CC       {ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:7857286}.
CC   -!- POLYMORPHISM: The sequence shown is that of variant B, the most common
CC       variant.
CC   -!- DISEASE: Anemia, non-spherocytic hemolytic, due to G6PD deficiency
CC       (NSHA) [MIM:300908]: A disease characterized by G6PD deficiency, acute
CC       hemolytic anemia, fatigue, back pain, and jaundice. In most patients,
CC       the disease is triggered by an exogenous agent, such as some drugs,
CC       food, or infection. Increased unconjugated bilirubin, lactate
CC       dehydrogenase, and reticulocytosis are markers of the disorder.
CC       Although G6PD deficiency can be life-threatening, most patients are
CC       asymptomatic throughout their life. {ECO:0000269|PubMed:12524354,
CC       ECO:0000269|PubMed:1303180, ECO:0000269|PubMed:1303182,
CC       ECO:0000269|PubMed:1536798, ECO:0000269|PubMed:1611091,
CC       ECO:0000269|PubMed:1889820, ECO:0000269|PubMed:1945893,
CC       ECO:0000269|PubMed:20007901, ECO:0000269|PubMed:26479991,
CC       ECO:0000269|PubMed:2836867, ECO:0000269|PubMed:2912069,
CC       ECO:0000269|PubMed:30988594, ECO:0000269|PubMed:7858267,
CC       ECO:0000269|PubMed:7959695, ECO:0000269|PubMed:8193373,
CC       ECO:0000269|PubMed:8490627, ECO:0000269|PubMed:8533762,
CC       ECO:0000269|PubMed:8733135, ECO:0000269|PubMed:9452072}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry. Deficiency of G6PD is associated with hemolytic anemia in two
CC       different situations. First, in areas in which malaria has been
CC       endemic, G6PD-deficiency alleles have reached high frequencies (1% to
CC       50%) and deficient individuals, though essentially asymptomatic in the
CC       steady state, have a high risk of acute hemolytic attacks. Secondly,
CC       sporadic cases of G6PD deficiency occur at a very low frequencies, and
CC       they usually present a more severe phenotype. Several types of NSHA are
CC       recognized. Class-I variants are associated with severe NSHA; class-II
CC       have an activity <10% of normal; class-III have an activity of 10% to
CC       60% of normal; class-IV have near normal activity.
CC   -!- MISCELLANEOUS: Binds two molecules of NADP. The first one is a
CC       cosubstrate (bound to the N-terminal domain), the second is bound to
CC       the C-terminal domain and functions as a structural element.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA63175.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=G6PDdb; Note=G6PD mutation database;
CC       URL="http://www.bioinf.org.uk/mutations/g6pd/";
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DR   EMBL; X03674; CAA27309.1; -; mRNA.
DR   EMBL; M65234; AAA63175.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M26749; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M26750; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65225; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65226; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65227; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65228; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65229; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65230; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65231; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65233; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M65232; AAA63175.1; JOINED; Genomic_DNA.
DR   EMBL; M21248; AAA52500.1; -; mRNA.
DR   EMBL; M19866; AAA52501.1; -; mRNA.
DR   EMBL; X55448; CAA39089.1; -; Genomic_DNA.
DR   EMBL; L44140; AAA92653.1; -; Genomic_DNA.
DR   EMBL; AF277315; AAL27011.1; -; Genomic_DNA.
DR   EMBL; CH471172; EAW72682.1; -; Genomic_DNA.
DR   EMBL; CH471172; EAW72686.1; -; Genomic_DNA.
DR   EMBL; BC000337; AAH00337.1; -; mRNA.
DR   EMBL; M27940; AAA52504.1; -; mRNA.
DR   EMBL; S58359; AAB26169.1; -; mRNA.
DR   EMBL; X53815; CAA37811.1; -; Genomic_DNA.
DR   EMBL; S64462; AAB20299.1; -; Genomic_DNA.
DR   EMBL; AY158096; AAN76367.1; -; Genomic_DNA.
DR   EMBL; AY158097; AAN76368.1; -; Genomic_DNA.
DR   EMBL; AY158098; AAN76369.1; -; Genomic_DNA.
DR   EMBL; AY158099; AAN76370.1; -; Genomic_DNA.
DR   EMBL; AY158100; AAN76371.1; -; Genomic_DNA.
DR   EMBL; AY158101; AAN76372.1; -; Genomic_DNA.
DR   EMBL; AY158102; AAN76373.1; -; Genomic_DNA.
DR   EMBL; AY158103; AAN76374.1; -; Genomic_DNA.
DR   EMBL; AY158104; AAN76375.1; -; Genomic_DNA.
DR   EMBL; AY158105; AAN76376.1; -; Genomic_DNA.
DR   EMBL; AY158106; AAN76377.1; -; Genomic_DNA.
DR   EMBL; AY158107; AAN76378.1; -; Genomic_DNA.
DR   EMBL; AY158108; AAN76379.1; -; Genomic_DNA.
DR   EMBL; AY158109; AAN76380.1; -; Genomic_DNA.
DR   EMBL; AY158110; AAN76381.1; -; Genomic_DNA.
DR   EMBL; AY158111; AAN76382.1; -; Genomic_DNA.
DR   EMBL; AY158112; AAN76383.1; -; Genomic_DNA.
DR   EMBL; AY158113; AAN76384.1; -; Genomic_DNA.
DR   EMBL; AY158114; AAN76385.1; -; Genomic_DNA.
DR   EMBL; AY158115; AAN76386.1; -; Genomic_DNA.
DR   EMBL; AY158116; AAN76387.1; -; Genomic_DNA.
DR   EMBL; AY158117; AAN76388.1; -; Genomic_DNA.
DR   EMBL; AY158118; AAN76389.1; -; Genomic_DNA.
DR   EMBL; AY158119; AAN76390.1; -; Genomic_DNA.
DR   EMBL; AY158120; AAN76391.1; -; Genomic_DNA.
DR   EMBL; AY158121; AAN76392.1; -; Genomic_DNA.
DR   EMBL; AY158122; AAN76393.1; -; Genomic_DNA.
DR   EMBL; AY158123; AAN76394.1; -; Genomic_DNA.
DR   EMBL; AY158124; AAN76395.1; -; Genomic_DNA.
DR   EMBL; AY158125; AAN76396.1; -; Genomic_DNA.
DR   EMBL; AY158126; AAN76397.1; -; Genomic_DNA.
DR   EMBL; AY158127; AAN76398.1; -; Genomic_DNA.
DR   EMBL; AY158128; AAN76399.1; -; Genomic_DNA.
DR   EMBL; AY158129; AAN76400.1; -; Genomic_DNA.
DR   EMBL; AY158130; AAN76401.1; -; Genomic_DNA.
DR   EMBL; AY158131; AAN76402.1; -; Genomic_DNA.
DR   EMBL; AY158132; AAN76403.1; -; Genomic_DNA.
DR   EMBL; AY158133; AAN76404.1; -; Genomic_DNA.
DR   EMBL; AY158134; AAN76405.1; -; Genomic_DNA.
DR   EMBL; AY158135; AAN76406.1; -; Genomic_DNA.
DR   EMBL; AY158136; AAN76407.1; -; Genomic_DNA.
DR   EMBL; AY158137; AAN76408.1; -; Genomic_DNA.
DR   EMBL; AY158138; AAN76409.1; -; Genomic_DNA.
DR   EMBL; AY158139; AAN76410.1; -; Genomic_DNA.
DR   EMBL; AY158140; AAN76411.1; -; Genomic_DNA.
DR   EMBL; AY158141; AAN76412.1; -; Genomic_DNA.
DR   EMBL; AY158142; AAN76413.1; -; Genomic_DNA.
DR   EMBL; M12996; AAA52499.1; -; mRNA.
DR   EMBL; M23423; AAB59390.1; -; Genomic_DNA.
DR   CCDS; CCDS44023.1; -. [P11413-1]
DR   PIR; A40309; DEHUG6.
DR   RefSeq; NP_000393.4; NM_000402.4. [P11413-3]
DR   RefSeq; NP_001035810.1; NM_001042351.2. [P11413-1]
DR   PDB; 1QKI; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-515.
DR   PDB; 2BH9; X-ray; 2.50 A; A=27-515.
DR   PDB; 2BHL; X-ray; 2.90 A; A/B=28-515.
DR   PDB; 5UKW; X-ray; 2.65 A; A=29-511.
DR   PDB; 6E07; X-ray; 2.60 A; B/C/F/L/N/Q/T/W=1-515.
DR   PDB; 6E08; X-ray; 1.90 A; L=1-515.
DR   PDB; 6JYU; X-ray; 1.89 A; A=29-513.
DR   PDB; 6VA0; X-ray; 3.10 A; A=1-515.
DR   PDB; 6VA7; X-ray; 3.07 A; A=1-515.
DR   PDB; 6VA8; X-ray; 3.95 A; A=1-515.
DR   PDB; 6VA9; X-ray; 3.95 A; A=1-515.
DR   PDB; 6VAQ; X-ray; 2.95 A; A=1-515.
DR   PDBsum; 1QKI; -.
DR   PDBsum; 2BH9; -.
DR   PDBsum; 2BHL; -.
DR   PDBsum; 5UKW; -.
DR   PDBsum; 6E07; -.
DR   PDBsum; 6E08; -.
DR   PDBsum; 6JYU; -.
DR   PDBsum; 6VA0; -.
DR   PDBsum; 6VA7; -.
DR   PDBsum; 6VA8; -.
DR   PDBsum; 6VA9; -.
DR   PDBsum; 6VAQ; -.
DR   AlphaFoldDB; P11413; -.
DR   SMR; P11413; -.
DR   BioGRID; 108814; 116.
DR   IntAct; P11413; 27.
DR   MINT; P11413; -.
DR   STRING; 9606.ENSP00000377192; -.
DR   BindingDB; P11413; -.
DR   ChEMBL; CHEMBL5347; -.
DR   DrugBank; DB05107; 16-Bromoepiandrosterone.
DR   DrugBank; DB11638; Artenimol.
DR   DrugBank; DB03085; Glycolic acid.
DR   DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR   DrugCentral; P11413; -.
DR   GlyGen; P11413; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P11413; -.
DR   MetOSite; P11413; -.
DR   PhosphoSitePlus; P11413; -.
DR   SwissPalm; P11413; -.
DR   BioMuta; G6PD; -.
DR   DMDM; 116242483; -.
DR   REPRODUCTION-2DPAGE; IPI00289800; -.
DR   SWISS-2DPAGE; P11413; -.
DR   CPTAC; CPTAC-204; -.
DR   CPTAC; CPTAC-205; -.
DR   EPD; P11413; -.
DR   jPOST; P11413; -.
DR   MassIVE; P11413; -.
DR   MaxQB; P11413; -.
DR   PaxDb; P11413; -.
DR   PeptideAtlas; P11413; -.
DR   PRIDE; P11413; -.
DR   ProteomicsDB; 52771; -. [P11413-1]
DR   ProteomicsDB; 52772; -. [P11413-2]
DR   ProteomicsDB; 52773; -. [P11413-3]
DR   Antibodypedia; 352; 752 antibodies from 40 providers.
DR   DNASU; 2539; -.
DR   Ensembl; ENST00000369620.6; ENSP00000358633.2; ENSG00000160211.19. [P11413-2]
DR   Ensembl; ENST00000393562.10; ENSP00000377192.3; ENSG00000160211.19. [P11413-1]
DR   Ensembl; ENST00000393564.6; ENSP00000377194.2; ENSG00000160211.19. [P11413-1]
DR   GeneID; 2539; -.
DR   KEGG; hsa:2539; -.
DR   MANE-Select; ENST00000393562.10; ENSP00000377192.3; NM_001360016.2; NP_001346945.1.
DR   UCSC; uc004flx.3; human. [P11413-1]
DR   CTD; 2539; -.
DR   DisGeNET; 2539; -.
DR   GeneCards; G6PD; -.
DR   HGNC; HGNC:4057; G6PD.
DR   HPA; ENSG00000160211; Tissue enhanced (bone).
DR   MalaCards; G6PD; -.
DR   MIM; 300908; phenotype.
DR   MIM; 305900; gene.
DR   neXtProt; NX_P11413; -.
DR   OpenTargets; ENSG00000160211; -.
DR   Orphanet; 466026; Class I glucose-6-phosphate dehydrogenase deficiency.
DR   Orphanet; 362; NON RARE IN EUROPE: Glucose-6-phosphate-dehydrogenase deficiency.
DR   PharmGKB; PA28469; -.
DR   VEuPathDB; HostDB:ENSG00000160211; -.
DR   eggNOG; KOG0563; Eukaryota.
DR   GeneTree; ENSGT00530000063435; -.
DR   HOGENOM; CLU_013524_2_3_1; -.
DR   InParanoid; P11413; -.
DR   OMA; VEICVYE; -.
DR   OrthoDB; 383995at2759; -.
DR   PhylomeDB; P11413; -.
DR   TreeFam; TF300584; -.
DR   BioCyc; MetaCyc:HS08467-MON; -.
DR   BRENDA; 1.1.1.49; 2681.
DR   PathwayCommons; P11413; -.
DR   Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-HSA-71336; Pentose phosphate pathway.
DR   Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR   SABIO-RK; P11413; -.
DR   SignaLink; P11413; -.
DR   SIGNOR; P11413; -.
DR   UniPathway; UPA00115; UER00408.
DR   BioGRID-ORCS; 2539; 67 hits in 716 CRISPR screens.
DR   ChiTaRS; G6PD; human.
DR   EvolutionaryTrace; P11413; -.
DR   GeneWiki; Glucose-6-phosphate_dehydrogenase; -.
DR   GenomeRNAi; 2539; -.
DR   Pharos; P11413; Tchem.
DR   PRO; PR:P11413; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P11413; protein.
DR   Bgee; ENSG00000160211; Expressed in stromal cell of endometrium and 141 other tissues.
DR   ExpressionAtlas; P11413; baseline and differential.
DR   Genevisible; P11413; HS.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005536; F:glucose binding; IDA:BHF-UCL.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0050661; F:NADP binding; IDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:BHF-UCL.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0043249; P:erythrocyte maturation; IMP:BHF-UCL.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:BHF-UCL.
DR   GO; GO:0006629; P:lipid metabolic process; TAS:BHF-UCL.
DR   GO; GO:0006739; P:NADP metabolic process; IDA:UniProtKB.
DR   GO; GO:0006740; P:NADPH regeneration; IMP:BHF-UCL.
DR   GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:0010734; P:negative regulation of protein glutathionylation; IMP:BHF-UCL.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0019322; P:pentose biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IDA:BHF-UCL.
DR   GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IMP:BHF-UCL.
DR   GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; IEA:Ensembl.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0032094; P:response to food; IEA:Ensembl.
DR   GO; GO:0010041; P:response to iron(III) ion; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0046390; P:ribose phosphate biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   HAMAP; MF_00966; G6PD; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23429; PTHR23429; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00871; zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW   Cytoplasm; Direct protein sequencing; Disease variant; Glucose metabolism;
KW   Hereditary hemolytic anemia; Hydroxylation; Membrane; NADP; Oxidoreductase;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0000269|PubMed:7857286, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..515
FT                   /note="Glucose-6-phosphate 1-dehydrogenase"
FT                   /id="PRO_0000068083"
FT   ACT_SITE        263
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P11411"
FT   BINDING         38..45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         147
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         171
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         201..205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         357
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BHL"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BHL"
FT   BINDING         366
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         370
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         393
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15858258,
FT                   ECO:0007744|PDB:2BHL"
FT   BINDING         401..403
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         421..423
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         487
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         503
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   BINDING         509
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:10745013,
FT                   ECO:0000269|PubMed:15858258, ECO:0007744|PDB:1QKI,
FT                   ECO:0007744|PDB:2BH9"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7857286,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         10
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         89
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         171
FT                   /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT                   /evidence="ECO:0000269|PubMed:29192674"
FT   MOD_RES         171
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         403
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:24769394,
FT                   ECO:0007744|PubMed:19608861"
FT   MOD_RES         432
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         497
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         503
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1
FT                   /note="M -> MGRRGSAPGNGRTLRGCERGGRRRRSADSVM (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:8466644"
FT                   /id="VSP_037802"
FT   VAR_SEQ         257
FT                   /note="R -> RGPGRQGGSGSESCSLSLGSLVWGPHALEPGEQGGELRRALASSVPR
FT                   (in isoform Long)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001592"
FT   VARIANT         12
FT                   /note="V -> L (in Sinnai)"
FT                   /evidence="ECO:0000269|PubMed:10627140"
FT                   /id="VAR_002450"
FT   VARIANT         32
FT                   /note="H -> R (in NSHA; Gahoe; class III; frequent in
FT                   Chinese; dbSNP:rs137852340)"
FT                   /evidence="ECO:0000269|PubMed:1945893"
FT                   /id="VAR_002451"
FT   VARIANT         35
FT                   /note="Missing (in NSHA; Sunderland; class I)"
FT                   /id="VAR_002452"
FT   VARIANT         44
FT                   /note="A -> G (in NSHA; Orissa; class III; frequent in
FT                   Indian tribal populations; dbSNP:rs78478128)"
FT                   /evidence="ECO:0000269|PubMed:8533762"
FT                   /id="VAR_002453"
FT   VARIANT         48
FT                   /note="I -> T (in NSHA; Aures; class II; dbSNP:rs76645461)"
FT                   /evidence="ECO:0000269|PubMed:8490627"
FT                   /id="VAR_002454"
FT   VARIANT         58
FT                   /note="D -> N (in NSHA; Metaponto; class III;
FT                   dbSNP:rs137852315)"
FT                   /id="VAR_002455"
FT   VARIANT         68
FT                   /note="V -> M (in NSHA; A(-) type I; class III; frequent in
FT                   African population; dbSNP:rs1050828)"
FT                   /evidence="ECO:0000269|PubMed:12524354,
FT                   ECO:0000269|PubMed:1889820, ECO:0000269|PubMed:2836867,
FT                   ECO:0000269|PubMed:8733135"
FT                   /id="VAR_002456"
FT   VARIANT         70
FT                   /note="Y -> H (in NSHA; Namoru; 4% activity;
FT                   dbSNP:rs137852349)"
FT                   /id="VAR_002457"
FT   VARIANT         75
FT                   /note="L -> P (in NSHA; Swansea; class I)"
FT                   /evidence="ECO:0000269|PubMed:7858267"
FT                   /id="VAR_002458"
FT   VARIANT         81
FT                   /note="R -> C (in NSHA; Konan/Ube; class III;
FT                   dbSNP:rs138687036)"
FT                   /id="VAR_002460"
FT   VARIANT         81
FT                   /note="R -> H (in NSHA; Lagosanto; class III;
FT                   dbSNP:rs782308266)"
FT                   /id="VAR_002459"
FT   VARIANT         106
FT                   /note="S -> C (in NSHA; Vancouver; class I;
FT                   dbSNP:rs267606835)"
FT                   /id="VAR_002461"
FT   VARIANT         126
FT                   /note="N -> D (found in Santa Maria and Mount Sinai;
FT                   associated with C-387 in Mount Sinai; class IV and class I;
FT                   dbSNP:rs1050829)"
FT                   /evidence="ECO:0000269|PubMed:12524354,
FT                   ECO:0000269|PubMed:1889820, ECO:0000269|PubMed:27535533,
FT                   ECO:0000269|PubMed:2836867, ECO:0000269|PubMed:3446582,
FT                   ECO:0000269|PubMed:8733135, ECO:0000269|PubMed:9452072"
FT                   /id="VAR_002462"
FT   VARIANT         128
FT                   /note="L -> P (in NSHA; Vanua Lava; 4% activity;
FT                   dbSNP:rs78365220)"
FT                   /id="VAR_002463"
FT   VARIANT         131
FT                   /note="G -> V (in Chinese-4; dbSNP:rs137852341)"
FT                   /id="VAR_002464"
FT   VARIANT         156
FT                   /note="E -> K (in NSHA; Ilesha; class III;
FT                   dbSNP:rs137852313)"
FT                   /id="VAR_002465"
FT   VARIANT         163
FT                   /note="G -> D (in NSHA; Plymouth; class I)"
FT                   /evidence="ECO:0000269|PubMed:7858267"
FT                   /id="VAR_002467"
FT   VARIANT         163
FT                   /note="G -> S (in NSHA; Mahidol; class III; associated with
FT                   reduced density of Plasmodium vivax but not Plasmodium
FT                   falciparum in Southeast Asians; reduced activity;
FT                   dbSNP:rs137852314)"
FT                   /id="VAR_002466"
FT   VARIANT         165
FT                   /note="N -> D (in NSHA; Chinese-3; class II;
FT                   dbSNP:rs137852331)"
FT                   /id="VAR_002468"
FT   VARIANT         166
FT                   /note="R -> H (in NSHA; Naone; 1% activity)"
FT                   /id="VAR_002469"
FT   VARIANT         176
FT                   /note="D -> G (in NSHA; Shinshu; class I)"
FT                   /evidence="ECO:0000269|PubMed:8193373"
FT                   /id="VAR_002470"
FT   VARIANT         181
FT                   /note="D -> V (in NSHA; Santa Maria; class I;
FT                   dbSNP:rs5030872)"
FT                   /id="VAR_002471"
FT   VARIANT         182
FT                   /note="R -> W (in NSHA; Vancouver; class I;
FT                   dbSNP:rs267606836)"
FT                   /id="VAR_002472"
FT   VARIANT         184
FT                   /note="S -> F (in Dindori; class II; 5% of activity;
FT                   dbSNP:rs782315572)"
FT                   /evidence="ECO:0000269|Ref.55"
FT                   /id="VAR_081894"
FT   VARIANT         188
FT                   /note="S -> F (in NSHA; Sassari/Cagliari; class II;
FT                   frequent in the Mediterranean; dbSNP:rs5030868)"
FT                   /evidence="ECO:0000269|PubMed:2912069"
FT                   /id="VAR_002473"
FT   VARIANT         198
FT                   /note="R -> C (in Coimbra; class II; dbSNP:rs137852330)"
FT                   /evidence="ECO:0000269|PubMed:18043863"
FT                   /id="VAR_002474"
FT   VARIANT         198
FT                   /note="R -> H (in Nilgiris; class II; dbSNP:rs137852332)"
FT                   /evidence="ECO:0000269|PubMed:18043863,
FT                   ECO:0000269|PubMed:29333274"
FT                   /id="VAR_081895"
FT   VARIANT         198
FT                   /note="R -> P (in NSHA; Santiago; class I;
FT                   dbSNP:rs137852332)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002475"
FT   VARIANT         198
FT                   /note="R -> S (in NSHA; Herlev; loss of glucose-6-phosphate
FT                   dehydrogenase activity)"
FT                   /evidence="ECO:0000269|PubMed:26479991"
FT                   /id="VAR_075555"
FT   VARIANT         212
FT                   /note="M -> V (in NSHA; Sibari; class III;
FT                   dbSNP:rs782754619)"
FT                   /id="VAR_002476"
FT   VARIANT         213
FT                   /note="V -> L (in NSHA; Minnesota; class I;
FT                   dbSNP:rs137852326)"
FT                   /id="VAR_002477"
FT   VARIANT         216
FT                   /note="F -> L (in NSHA; Harilaou; class I;
FT                   dbSNP:rs137852319)"
FT                   /id="VAR_002478"
FT   VARIANT         227
FT                   /note="R -> L (in NSHA; A- type 2; class III;
FT                   dbSNP:rs137852328)"
FT                   /id="VAR_002480"
FT   VARIANT         227
FT                   /note="R -> Q (in Mexico City; class III;
FT                   dbSNP:rs137852328)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002479"
FT   VARIANT         242..243
FT                   /note="Missing (in NSHA; Stonybrook; class I)"
FT                   /id="VAR_002481"
FT   VARIANT         257
FT                   /note="R -> G (in NSHA; Wayne; class I)"
FT                   /id="VAR_002482"
FT   VARIANT         274
FT                   /note="E -> K (in NSHA; Corum; class I)"
FT                   /evidence="ECO:0000269|PubMed:7858267"
FT                   /id="VAR_002483"
FT   VARIANT         278
FT                   /note="S -> F (in NSHA; Wexham; class I)"
FT                   /evidence="ECO:0000269|PubMed:7858267"
FT                   /id="VAR_002484"
FT   VARIANT         279
FT                   /note="T -> S (in NSHA; Chinese-1; class II)"
FT                   /id="VAR_002485"
FT   VARIANT         282
FT                   /note="D -> H (in NSHA; Seattle; class III;
FT                   dbSNP:rs137852318)"
FT                   /evidence="ECO:0000269|PubMed:2912069"
FT                   /id="VAR_002486"
FT   VARIANT         285
FT                   /note="R -> H (in NSHA; Montalbano; class III;
FT                   dbSNP:rs74575103)"
FT                   /id="VAR_002487"
FT   VARIANT         291
FT                   /note="V -> M (in NSHA; Viangchan/Jammu; class II;
FT                   dbSNP:rs137852327)"
FT                   /id="VAR_002488"
FT   VARIANT         317
FT                   /note="E -> K (in NSHA; Kalyan/Kerala; class III;
FT                   dbSNP:rs137852339)"
FT                   /evidence="ECO:0000269|PubMed:1303182"
FT                   /id="VAR_002489"
FT   VARIANT         321
FT                   /note="G -> V (in NSHA; Bhavnagar; decreased enzyme
FT                   stability)"
FT                   /evidence="ECO:0000269|PubMed:30988594"
FT                   /id="VAR_081896"
FT   VARIANT         322
FT                   /note="Y -> H (in Rehovot; dbSNP:rs137852347)"
FT                   /evidence="ECO:0000269|PubMed:11112389"
FT                   /id="VAR_020535"
FT   VARIANT         323
FT                   /note="L -> P (in NSHA; A- type 3; class III;
FT                   dbSNP:rs76723693)"
FT                   /id="VAR_002490"
FT   VARIANT         335
FT                   /note="A -> T (in NSHA; Chatham; class III;
FT                   dbSNP:rs5030869)"
FT                   /id="VAR_002491"
FT   VARIANT         342
FT                   /note="L -> F (in Chinese-5; dbSNP:rs137852342)"
FT                   /id="VAR_002492"
FT   VARIANT         353
FT                   /note="P -> S (in Ierapetra; class II; dbSNP:rs137852333)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002493"
FT   VARIANT         363
FT                   /note="N -> K (in NSHA; Loma Linda; class I;
FT                   dbSNP:rs137852329)"
FT                   /id="VAR_002494"
FT   VARIANT         385
FT                   /note="C -> R (in NSHA; Tomah; class I; dbSNP:rs137852322)"
FT                   /id="VAR_002495"
FT   VARIANT         386
FT                   /note="K -> E (in NSHA; Iowa; class I; dbSNP:rs137852320)"
FT                   /id="VAR_002496"
FT   VARIANT         387
FT                   /note="R -> C (in NSHA; Guadajalara and Mount Sinai; class
FT                   I; dbSNP:rs137852334)"
FT                   /evidence="ECO:0000269|PubMed:1611091,
FT                   ECO:0000269|PubMed:9452072"
FT                   /id="VAR_002498"
FT   VARIANT         387
FT                   /note="R -> H (in NSHA; Beverly Hills; class I;
FT                   dbSNP:rs137852321)"
FT                   /id="VAR_002497"
FT   VARIANT         393
FT                   /note="R -> H (in NSHA; Nashville/Anaheim; class I;
FT                   dbSNP:rs137852316)"
FT                   /evidence="ECO:0000269|PubMed:1536798"
FT                   /id="VAR_002499"
FT   VARIANT         394
FT                   /note="V -> L (in NSHA; Alhambra; class I;
FT                   dbSNP:rs137852335)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002500"
FT   VARIANT         396
FT                   /note="P -> L (in NSHA; Bari; class I; dbSNP:rs1557229683)"
FT                   /evidence="ECO:0000269|PubMed:7959695"
FT                   /id="VAR_002501"
FT   VARIANT         398
FT                   /note="E -> K (in NSHA; Puerto Limon; class I;
FT                   dbSNP:rs137852325)"
FT                   /id="VAR_002502"
FT   VARIANT         410
FT                   /note="G -> C (in NSHA; Riverside; class I;
FT                   dbSNP:rs137852323)"
FT                   /id="VAR_002503"
FT   VARIANT         410
FT                   /note="G -> D (in NSHA; Japan; class I; dbSNP:rs137852336)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002504"
FT   VARIANT         416
FT                   /note="E -> K (in NSHA; Tokyo; class I)"
FT                   /id="VAR_002505"
FT   VARIANT         439
FT                   /note="R -> P (in NSHA; Pawnee; class I;
FT                   dbSNP:rs137852337)"
FT                   /evidence="ECO:0000269|PubMed:1611091"
FT                   /id="VAR_002506"
FT   VARIANT         440
FT                   /note="L -> F (in NSHA; Telti/Kobe; class I;
FT                   dbSNP:rs1557229599)"
FT                   /id="VAR_002507"
FT   VARIANT         447
FT                   /note="G -> R (in NSHA; Santiago de Cuba; class I;
FT                   dbSNP:rs137852317)"
FT                   /id="VAR_002508"
FT   VARIANT         449
FT                   /note="Q -> H (in NSHA; Cassano; class II)"
FT                   /id="VAR_002509"
FT   VARIANT         454
FT                   /note="R -> C (in NSHA; Chinese-II/Maewo/Union; class II;
FT                   <1% activity; dbSNP:rs398123546)"
FT                   /evidence="ECO:0000269|PubMed:1303180"
FT                   /id="VAR_002510"
FT   VARIANT         454
FT                   /note="R -> H (in NSHA; Andalus; class I;
FT                   dbSNP:rs137852324)"
FT                   /id="VAR_002511"
FT   VARIANT         459
FT                   /note="R -> L (in NSHA; Canton; class II; frequent in
FT                   China; dbSNP:rs72554665)"
FT                   /id="VAR_002512"
FT   VARIANT         459
FT                   /note="R -> P (in NSHA; Cosenza; class II;
FT                   dbSNP:rs72554665)"
FT                   /id="VAR_002513"
FT   VARIANT         463
FT                   /note="R -> H (in Kaiping; class II; dbSNP:rs72554664)"
FT                   /evidence="ECO:0000269|Ref.55"
FT                   /id="VAR_002514"
FT   VARIANT         488
FT                   /note="G -> V (in NSHA; Campinas; class I)"
FT                   /id="VAR_002515"
FT   MUTAGEN         171
FT                   /note="K->Q: Inhibits catalytic activity. Does not impair
FT                   dimerization."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   MUTAGEN         171
FT                   /note="K->R: Inhibits catalytic activity. Does not impair
FT                   dimerization."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   MUTAGEN         386
FT                   /note="K->Q: Impairs dimerization and reduces catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   MUTAGEN         386
FT                   /note="K->R: Does not impair dimerization and catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   MUTAGEN         403
FT                   /note="K->Q: Impairs dimerization and reduces catalytic
FT                   activity in cells under oxidative stress."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   MUTAGEN         403
FT                   /note="K->R: Does not impair dimerization and catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24769394"
FT   CONFLICT        11
FT                   /note="Q -> H (in Ref. 1; CAA27309, 2; AAA63175 and 3;
FT                   AAA52500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        435..436
FT                   /note="DA -> EP (in Ref. 15; AAA52499)"
FT                   /evidence="ECO:0000305"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            38..40
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           42..46
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           48..57
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          63..73
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           77..84
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           95..103
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           115..126
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            127..133
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           147..157
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          165..169
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           201..204
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           206..216
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           219..221
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          222..226
FT                   /evidence="ECO:0007829|PDB:2BHL"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          230..238
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            251..253
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           254..258
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           263..272
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           281..292
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           300..302
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          303..309
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          312..314
FT                   /evidence="ECO:0007829|PDB:6VA7"
FT   HELIX           316..319
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          326..328
FT                   /evidence="ECO:0007829|PDB:2BHL"
FT   STRAND          336..344
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            347..351
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          353..364
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          366..373
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          389..397
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          399..407
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          414..423
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           424..427
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   TURN            428..430
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           436..446
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   HELIX           449..451
FT                   /evidence="ECO:0007829|PDB:1QKI"
FT   HELIX           455..475
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          480..483
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   STRAND          486..488
FT                   /evidence="ECO:0007829|PDB:2BH9"
FT   HELIX           490..499
FT                   /evidence="ECO:0007829|PDB:6JYU"
FT   MOD_RES         P11413-3:26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
SQ   SEQUENCE   515 AA;  59257 MW;  F2B775340640A96F CRC64;
     MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL
     LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR
     LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS
     DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP
     FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA
     NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK
     ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL
     DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI
     PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL
 
 
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