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 09-APR-2025, entry version 276.
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 CNSHA1 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 CNSHA1 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 CNSHA1 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 CNSHA1 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 CNSHA1
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 FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ALDOB AND TP53.
RX PubMed=35122041; DOI=10.1038/s43018-020-0086-7;
RA Li M., He X., Guo W., Yu H., Zhang S., Wang N., Liu G., Sa R., Shen X.,
RA Jiang Y., Tang Y., Zhuo Y., Yin C., Tu Q., Li N., Nie X., Li Y., Hu Z.,
RA Zhu H., Ding J., Li Z., Liu T., Zhang F., Zhou H., Li S., Yue J., Yan Z.,
RA Cheng S., Tao Y., Yin H.;
RT "Aldolase B suppresses hepatocellular carcinogenesis by inhibiting G6PD and
RT pentose phosphate pathways.";
RL Nat. Cancer 1:735-747(2020).
RN [32]
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 [33]
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 [34]
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 [35]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 28-514 IN COMPLEX WITH NADP(+)
RP AND D-GLUCOSE 6-PHOSPHATEE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL 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 [36]
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 [37]
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 [38]
RP VARIANTS CNSHA1 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 [39]
RP VARIANTS CNSHA1 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 [40]
RP VARIANT CNSHA1 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 [41]
RP VARIANT CNSHA1 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 [42]
RP VARIANT CNSHA1 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 [43]
RP VARIANT CNSHA1 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 [44]
RP VARIANT CNSHA1 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 [45]
RP VARIANT CNSHA1 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 [46]
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 [47]
RP VARIANT CNSHA1 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 [48]
RP VARIANTS CNSHA1 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 [49]
RP VARIANT CNSHA1 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 [50]
RP VARIANT SINNAI LEU-12.
RX PubMed=10627140;
RX DOI=10.1002/(sici)1098-1004(1998)12:1<72::aid-humu19>3.0.co;2-t;
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 [51]
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 [52]
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 [53]
RP ASSOCIATION OF VARIANT CNSHA1 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 [54]
RP VARIANT CNSHA1 SER-198, CHARACTERIZATION OF VARIANT CNSHA1 SER-198,
RP FUNCTION, 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 [55]
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 [56]
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 [57]
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 [58]
RP VARIANT CNSHA1 VAL-321, AND CHARACTERIZATION OF VARIANT CNSHA1 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).
RN [59]
RP VARIANT CNSHA1 GLY-219, CHARACTERIZATION OF VARIANT CNSHA1 GLY-219,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=38066190; DOI=10.1038/s42003-023-05599-z;
RA Zgheib O., Chamchoy K., Nouspikel T., Blouin J.L., Cimasoni L.,
RA Quteineh L., Boonyuen U.;
RT "Substitution of arginine 219 by glycine compromises stability,
RT dimerization, and catalytic activity in a G6PD mutant.";
RL Commun. Biol. 6:1245-1245(2023).
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:35122041, ECO:0000269|PubMed:38066190,
CC ECO:0000269|PubMed:743300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-
CC lactone + NADPH + H(+); 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:35122041,
CC ECO:0000269|PubMed:38066190, 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 KM=46.1 uM for glucose 6-phosphate {ECO:0000269|PubMed:38066190};
CC KM=12.9 uM for NADP {ECO:0000269|PubMed:38066190};
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:10745013,
CC PubMed:15858258, PubMed:24769394, PubMed:38066190). Interacts with
CC SIRT2; the interaction is enhanced by H(2)O(2) treatment
CC (PubMed:24769394). Forms a ternary complex with ALDOB and TP53; this
CC interaction is direct. ALDOB stabilizes the complex inhibiting G6PD
CC activity and keeping oxidative pentose phosphate metabolism in check.
CC {ECO:0000269|PubMed:10745013, ECO:0000269|PubMed:15858258,
CC ECO:0000269|PubMed:24769394, ECO:0000269|PubMed:35122041,
CC ECO:0000269|PubMed:38066190}.
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:35122041,
CC ECO:0000269|PubMed:743300}. Membrane; Peripheral membrane protein
CC {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, congenital, non-spherocytic hemolytic, 1 (CNSHA1)
CC [MIM:300908]: An X-linked disease characterized by G6PD deficiency,
CC acute hemolytic anemia, fatigue, back pain, and jaundice. In most
CC patients, the disease is triggered by an exogenous agent, such as some
CC drugs, 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:38066190,
CC ECO:0000269|PubMed:7858267, ECO:0000269|PubMed:7959695,
CC ECO:0000269|PubMed:8193373, ECO:0000269|PubMed:8490627,
CC ECO:0000269|PubMed:8533762, ECO:0000269|PubMed:8733135,
CC ECO:0000269|PubMed:9452072}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Deficiency of G6PD is
CC associated with hemolytic anemia in two different situations. First, in
CC areas in which malaria has been endemic, G6PD-deficiency alleles have
CC reached high frequencies (1% to 50%) and deficient individuals, though
CC essentially asymptomatic in the steady state, have a high risk of acute
CC hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at
CC a very low frequencies, and they usually present a more severe
CC phenotype. Several types of CNSHA1 are recognized. Class-I variants are
CC associated with severe CNSHA1; class-II have an activity <10% of
CC normal; class-III have an activity of 10% to 60% of normal; class-IV
CC 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/";
CC ---------------------------------------------------------------------------
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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_001042351.3. [P11413-1]
DR RefSeq; NP_001346945.1; NM_001360016.2. [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 PDB; 7SEH; X-ray; 2.90 A; A/B=1-515.
DR PDB; 7SEI; X-ray; 3.65 A; A=1-515.
DR PDB; 7SNF; EM; 3.40 A; A/B=1-515.
DR PDB; 7SNG; EM; 2.80 A; A/B/C/D=1-515.
DR PDB; 7SNH; EM; 2.20 A; A/B/C/D=1-515.
DR PDB; 7SNI; EM; 2.50 A; A/B/C/D=1-515.
DR PDB; 7TOE; EM; 3.00 A; A/B/C/D=1-515.
DR PDB; 7TOF; EM; 3.70 A; A/B=1-515.
DR PDB; 7UAG; EM; 3.50 A; A/B=1-515.
DR PDB; 7UAL; EM; 2.90 A; A/B/C/D=1-515.
DR PDB; 7UC2; EM; 2.50 A; A/B/C/D=1-515.
DR PDB; 7ZVD; X-ray; 2.46 A; N=28-511.
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 PDBsum; 7SEH; -.
DR PDBsum; 7SEI; -.
DR PDBsum; 7SNF; -.
DR PDBsum; 7SNG; -.
DR PDBsum; 7SNH; -.
DR PDBsum; 7SNI; -.
DR PDBsum; 7TOE; -.
DR PDBsum; 7TOF; -.
DR PDBsum; 7UAG; -.
DR PDBsum; 7UAL; -.
DR PDBsum; 7UC2; -.
DR PDBsum; 7ZVD; -.
DR AlphaFoldDB; P11413; -.
DR EMDB; EMD-25224; -.
DR EMDB; EMD-25225; -.
DR EMDB; EMD-25226; -.
DR EMDB; EMD-25227; -.
DR EMDB; EMD-26030; -.
DR EMDB; EMD-26031; -.
DR EMDB; EMD-26425; -.
DR EMDB; EMD-26428; -.
DR EMDB; EMD-26442; -.
DR SASBDB; P11413; -.
DR SMR; P11413; -.
DR BioGRID; 108814; 209.
DR IntAct; P11413; 36.
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 GlyCosmos; P11413; 1 site, 1 glycan.
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 CPTAC; CPTAC-204; -.
DR CPTAC; CPTAC-205; -.
DR CPTAC; CPTAC-2734; -.
DR jPOST; P11413; -.
DR MassIVE; P11413; -.
DR PaxDb; 9606-ENSP00000377192; -.
DR PeptideAtlas; P11413; -.
DR ProteomicsDB; 52771; -. [P11413-1]
DR ProteomicsDB; 52772; -. [P11413-2]
DR ProteomicsDB; 52773; -. [P11413-3]
DR Pumba; P11413; -.
DR Antibodypedia; 352; 804 antibodies from 40 providers.
DR DNASU; 2539; -.
DR Ensembl; ENST00000369620.6; ENSP00000358633.2; ENSG00000160211.20. [P11413-2]
DR Ensembl; ENST00000393562.10; ENSP00000377192.3; ENSG00000160211.20. [P11413-1]
DR Ensembl; ENST00000393564.7; ENSP00000377194.2; ENSG00000160211.20. [P11413-1]
DR Ensembl; ENST00000696429.1; ENSP00000512624.1; ENSG00000160211.20. [P11413-1]
DR Ensembl; ENST00000696430.1; ENSP00000512625.1; ENSG00000160211.20. [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 AGR; HGNC:4057; -.
DR CTD; 2539; -.
DR DisGeNET; 2539; -.
DR GeneCards; G6PD; -.
DR HGNC; HGNC:4057; G6PD.
DR HPA; ENSG00000160211; Low tissue specificity.
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 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; ERAGYYE; -.
DR OrthoDB; 60984at2759; -.
DR PhylomeDB; P11413; -.
DR TreeFam; TF300584; -.
DR BioCyc; MetaCyc:HS08467-MONOMER; -.
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-9818028; NFE2L2 regulates pentose phosphate pathway genes.
DR SABIO-RK; P11413; -.
DR SignaLink; P11413; -.
DR SIGNOR; P11413; -.
DR UniPathway; UPA00115; UER00408.
DR BioGRID-ORCS; 2539; 93 hits in 797 CRISPR screens.
DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
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 143 other cell types or tissues.
DR ExpressionAtlas; P11413; baseline and differential.
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:HPA.
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:0005536; F:D-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:UniProtKB.
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 FunFam; 3.30.360.10:FF:000013; Glucose-6-phosphate 1-dehydrogenase; 1.
DR FunFam; 3.40.50.720:FF:000111; Glucose-6-phosphate 1-dehydrogenase; 1.
DR Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR00871; zwf; 1.
DR PANTHER; PTHR23429:SF0; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR23429; GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD; 1.
DR Pfam; PF02781; G6PD_C; 1.
DR Pfam; PF00479; G6PD_N; 1.
DR PIRSF; PIRSF000110; G6PD; 1.
DR PRINTS; PR00079; G6PDHDRGNASE.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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; Proteomics identification; 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="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15858258,
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 201..205
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15858258,
FT ECO:0007744|PDB:2BH9"
FT BINDING 239
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15858258,
FT ECO:0007744|PDB:2BH9"
FT BINDING 258
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
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="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15858258,
FT ECO:0007744|PDB:2BHL"
FT BINDING 365
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
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="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
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 CNSHA1; 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 CNSHA1; Sunderland; class I)"
FT /id="VAR_002452"
FT VARIANT 44
FT /note="A -> G (in CNSHA1; 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 CNSHA1; Aures; class II;
FT dbSNP:rs76645461)"
FT /evidence="ECO:0000269|PubMed:8490627"
FT /id="VAR_002454"
FT VARIANT 58
FT /note="D -> N (in CNSHA1; Metaponto; class III;
FT dbSNP:rs137852315)"
FT /id="VAR_002455"
FT VARIANT 68
FT /note="V -> M (in CNSHA1; A(-) type I; class III; frequent
FT in 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 CNSHA1; Namoru; 4% activity;
FT dbSNP:rs137852349)"
FT /id="VAR_002457"
FT VARIANT 75
FT /note="L -> P (in CNSHA1; Swansea; class I)"
FT /evidence="ECO:0000269|PubMed:7858267"
FT /id="VAR_002458"
FT VARIANT 81
FT /note="R -> C (in CNSHA1; Konan/Ube; class III;
FT dbSNP:rs138687036)"
FT /id="VAR_002460"
FT VARIANT 81
FT /note="R -> H (in CNSHA1; Lagosanto; class III;
FT dbSNP:rs782308266)"
FT /id="VAR_002459"
FT VARIANT 106
FT /note="S -> C (in CNSHA1; 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 CNSHA1; 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 CNSHA1; Ilesha; class III;
FT dbSNP:rs137852313)"
FT /id="VAR_002465"
FT VARIANT 163
FT /note="G -> D (in CNSHA1; Plymouth; class I)"
FT /evidence="ECO:0000269|PubMed:7858267"
FT /id="VAR_002467"
FT VARIANT 163
FT /note="G -> S (in CNSHA1; Mahidol; class III; associated
FT with 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 CNSHA1; Chinese-3; class II;
FT dbSNP:rs137852331)"
FT /id="VAR_002468"
FT VARIANT 166
FT /note="R -> H (in CNSHA1; Naone; 1% activity)"
FT /id="VAR_002469"
FT VARIANT 176
FT /note="D -> G (in CNSHA1; Shinshu; class I)"
FT /evidence="ECO:0000269|PubMed:8193373"
FT /id="VAR_002470"
FT VARIANT 181
FT /note="D -> V (in CNSHA1; Santa Maria; class I;
FT dbSNP:rs5030872)"
FT /id="VAR_002471"
FT VARIANT 182
FT /note="R -> W (in CNSHA1; 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.56"
FT /id="VAR_081894"
FT VARIANT 188
FT /note="S -> F (in CNSHA1; 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 CNSHA1; Santiago; class I;
FT dbSNP:rs137852332)"
FT /evidence="ECO:0000269|PubMed:1611091"
FT /id="VAR_002475"
FT VARIANT 198
FT /note="R -> S (in CNSHA1; Herlev; loss of
FT glucose-6-phosphate dehydrogenase activity)"
FT /evidence="ECO:0000269|PubMed:26479991"
FT /id="VAR_075555"
FT VARIANT 212
FT /note="M -> V (in CNSHA1; Sibari; class III;
FT dbSNP:rs782754619)"
FT /id="VAR_002476"
FT VARIANT 213
FT /note="V -> L (in CNSHA1; Minnesota; class I;
FT dbSNP:rs137852326)"
FT /id="VAR_002477"
FT VARIANT 216
FT /note="F -> L (in CNSHA1; Harilaou; class I;
FT dbSNP:rs137852319)"
FT /id="VAR_002478"
FT VARIANT 219
FT /note="R -> G (in CNSHA1; Meyer; class I; likely
FT pathogenic; disrupts dimer formation; reduces catalytic
FT activity; decreases protein stability; no impact on
FT glucose-6-phosphate binding affinity)"
FT /evidence="ECO:0000269|PubMed:38066190"
FT /id="VAR_088817"
FT VARIANT 227
FT /note="R -> L (in CNSHA1; 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 CNSHA1; Stonybrook; class I)"
FT /id="VAR_002481"
FT VARIANT 257
FT /note="R -> G (in CNSHA1; Wayne; class I)"
FT /id="VAR_002482"
FT VARIANT 274
FT /note="E -> K (in CNSHA1; Corum; class I)"
FT /evidence="ECO:0000269|PubMed:7858267"
FT /id="VAR_002483"
FT VARIANT 278
FT /note="S -> F (in CNSHA1; Wexham; class I)"
FT /evidence="ECO:0000269|PubMed:7858267"
FT /id="VAR_002484"
FT VARIANT 279
FT /note="T -> S (in CNSHA1; Chinese-1; class II)"
FT /id="VAR_002485"
FT VARIANT 282
FT /note="D -> H (in CNSHA1; Seattle; class III;
FT dbSNP:rs137852318)"
FT /evidence="ECO:0000269|PubMed:2912069"
FT /id="VAR_002486"
FT VARIANT 285
FT /note="R -> H (in CNSHA1; Montalbano; class III;
FT dbSNP:rs74575103)"
FT /id="VAR_002487"
FT VARIANT 291
FT /note="V -> M (in CNSHA1; Viangchan/Jammu; class II;
FT dbSNP:rs137852327)"
FT /id="VAR_002488"
FT VARIANT 317
FT /note="E -> K (in CNSHA1; 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 CNSHA1; 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 CNSHA1; A- type 3; class III;
FT dbSNP:rs76723693)"
FT /id="VAR_002490"
FT VARIANT 335
FT /note="A -> T (in CNSHA1; 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 CNSHA1; Loma Linda; class I;
FT dbSNP:rs137852329)"
FT /id="VAR_002494"
FT VARIANT 385
FT /note="C -> R (in CNSHA1; Tomah; class I;
FT dbSNP:rs137852322)"
FT /id="VAR_002495"
FT VARIANT 386
FT /note="K -> E (in CNSHA1; Iowa; class I;
FT dbSNP:rs137852320)"
FT /id="VAR_002496"
FT VARIANT 387
FT /note="R -> C (in CNSHA1; Guadajalara and Mount Sinai;
FT class 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 CNSHA1; Beverly Hills; class I;
FT dbSNP:rs137852321)"
FT /id="VAR_002497"
FT VARIANT 393
FT /note="R -> H (in CNSHA1; 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 CNSHA1; Alhambra; class I;
FT dbSNP:rs137852335)"
FT /evidence="ECO:0000269|PubMed:1611091"
FT /id="VAR_002500"
FT VARIANT 396
FT /note="P -> L (in CNSHA1; Bari; class I;
FT dbSNP:rs1557229683)"
FT /evidence="ECO:0000269|PubMed:7959695"
FT /id="VAR_002501"
FT VARIANT 398
FT /note="E -> K (in CNSHA1; Puerto Limon; class I;
FT dbSNP:rs137852325)"
FT /id="VAR_002502"
FT VARIANT 410
FT /note="G -> C (in CNSHA1; Riverside; class I;
FT dbSNP:rs137852323)"
FT /id="VAR_002503"
FT VARIANT 410
FT /note="G -> D (in CNSHA1; Japan; class I;
FT dbSNP:rs137852336)"
FT /evidence="ECO:0000269|PubMed:1611091"
FT /id="VAR_002504"
FT VARIANT 416
FT /note="E -> K (in CNSHA1; Tokyo; class I)"
FT /id="VAR_002505"
FT VARIANT 439
FT /note="R -> P (in CNSHA1; Pawnee; class I;
FT dbSNP:rs137852337)"
FT /evidence="ECO:0000269|PubMed:1611091"
FT /id="VAR_002506"
FT VARIANT 440
FT /note="L -> F (in CNSHA1; Telti/Kobe; class I;
FT dbSNP:rs1557229599)"
FT /id="VAR_002507"
FT VARIANT 447
FT /note="G -> R (in CNSHA1; Santiago de Cuba; class I;
FT dbSNP:rs137852317)"
FT /id="VAR_002508"
FT VARIANT 449
FT /note="Q -> H (in CNSHA1; Cassano; class II)"
FT /id="VAR_002509"
FT VARIANT 454
FT /note="R -> C (in CNSHA1; 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 CNSHA1; Andalus; class I;
FT dbSNP:rs137852324)"
FT /id="VAR_002511"
FT VARIANT 459
FT /note="R -> L (in CNSHA1; Canton; class II; frequent in
FT China; dbSNP:rs72554665)"
FT /id="VAR_002512"
FT VARIANT 459
FT /note="R -> P (in CNSHA1; 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.56"
FT /id="VAR_002514"
FT VARIANT 488
FT /note="G -> V (in CNSHA1; 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:7SEH"
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 381..383
FT /evidence="ECO:0007829|PDB:7SNF"
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
//