Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lysosomal alpha-glucosidase (EC 3.2.1.20) (Acid maltase) (Aglucosidase alfa) [Cleaved into: 76 kDa lysosomal alpha-glucosidase; 70 kDa lysosomal alpha-glucosidase]

 LYAG_HUMAN              Reviewed;         952 AA.
P10253; Q09GN4; Q14351; Q16302; Q8IWE7;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 4.
25-OCT-2017, entry version 204.
RecName: Full=Lysosomal alpha-glucosidase;
EC=3.2.1.20;
AltName: Full=Acid maltase;
AltName: Full=Aglucosidase alfa;
Contains:
RecName: Full=76 kDa lysosomal alpha-glucosidase;
Contains:
RecName: Full=70 kDa lysosomal alpha-glucosidase;
Flags: Precursor;
Name=GAA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 70-89; 123-145;
204-215; 230-249; 332-345; 349-370; 394-409; 480-513; 520-545;
703-719; 726-731 AND 795-803, AND VARIANTS ARG-199; HIS-223 AND
ILE-780.
TISSUE=Placenta, Testis, and Urine;
PubMed=3049072;
Hoefsloot L.H., Hoogeveen-Westerveld M., Kroos M.A., van Beeumen J.,
Reuser A.J.J., Oostra B.A.;
"Primary structure and processing of lysosomal alpha-glucosidase;
homology with the intestinal sucrase-isomaltase complex.";
EMBO J. 7:1697-1704(1988).
[2]
SEQUENCE REVISION.
Reuser A.J.J.;
Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-780.
PubMed=2268276; DOI=10.1042/bj2720493;
Hoefsloot L.H., Hoogeveen-Westerveld M., Reuser A.J.J., Oostra B.A.;
"Characterization of the human lysosomal alpha-glucosidase gene.";
Biochem. J. 272:493-497(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-780.
PubMed=2111708; DOI=10.1089/dna.1990.9.85;
Martiniuk F., Mehler M., Tzall S., Meredith G., Hirschhorn R.;
"Sequence of the cDNA and 5'-flanking region for human acid alpha-
glucosidase, detection of an intron in the 5' untranslated leader
sequence, definition of 18-bp polymorphisms, and differences with
previous cDNA and amino acid sequences.";
DNA Cell Biol. 9:85-94(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD2 LEU-457, AND VARIANTS
ARG-199; HIS-223 AND ILE-780.
Ghaffari S.R., Sabokbar T., Tahmasebi S., Dastan J.;
"Identification of a novel mutation in the acid alpha glucosidase gene
causing juvenile form of Pompe disease in Iranian population.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 631-680, AND VARIANT GSD2 HIS-645.
PubMed=7695647; DOI=10.1006/bbrc.1995.1418;
Lin C.-Y., Shieh J.-J.;
"Identification of a de novo point mutation resulting in infantile
form of Pompe's disease.";
Biochem. Biophys. Res. Commun. 208:886-893(1995).
[9]
MUTAGENESIS OF TRP-516 AND ASP-518, AND ACTIVE SITE.
PubMed=1856189;
Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A.,
Reuser A.J.J.;
"Human lysosomal alpha-glucosidase. Characterization of the catalytic
site.";
J. Biol. Chem. 266:13507-13512(1991).
[10]
GLYCOSYLATION AT ASN-140; ASN-233; ASN-390; ASN-470; ASN-652; ASN-882
AND ASN-925.
PubMed=8435067; DOI=10.1042/bj2890681;
Hermans M.M.P., Wisselaar H.A., Kroos M.A., Oostra B.A.,
Reuser A.J.J.;
"Human lysosomal alpha-glucosidase: functional characterization of the
glycosylation sites.";
Biochem. J. 289:681-686(1993).
[11]
GLYCOSYLATION AT ASN-470.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[12]
REVIEW ON VARIANTS.
PubMed=7603530; DOI=10.1002/mus.880181414;
Reuser A.J.J., Kroos M.A., Hermans M.M.P., Bijvoet A.G.A.,
Verbeet M.P., van Diggelen O.P., Kleijer W.J., van der Ploeg A.T.;
"Glycogenosis type II (acid maltase deficiency).";
Muscle Nerve 3:S61-S69(1995).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-390.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-470; ASN-882 AND
ASN-925.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
VARIANT ASN-91.
PubMed=2203258;
Martiniuk F., Bodkin M., Tzall S., Hirschhorn R.;
"Identification of the base-pair substitution responsible for a human
acid alpha glucosidase allele with lower 'affinity' for glycogen (GAA
2) and transient gene expression in deficient cells.";
Am. J. Hum. Genet. 47:440-445(1990).
[20]
VARIANT GSD2 THR-318.
PubMed=1652892;
Zhong N., Martiniuk F., Tzall S., Hirschhorn R.;
"Identification of a missense mutation in one allele of a patient with
Pompe disease, and use of endonuclease digestion of PCR-amplified RNA
to demonstrate lack of mRNA expression from the second allele.";
Am. J. Hum. Genet. 49:635-645(1991).
[21]
VARIANT GSD2 LYS-521.
PubMed=1898413; DOI=10.1016/0006-291X(91)91906-S;
Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A., Oostra B.A.,
Reuser A.J.J.;
"Identification of a point mutation in the human lysosomal alpha-
glucosidase gene causing infantile glycogenosis type II.";
Biochem. Biophys. Res. Commun. 179:919-926(1991).
[22]
VARIANTS GSD2 ARG-643 AND TRP-725.
PubMed=8401535; DOI=10.1002/humu.1380020406;
Hermans M.M.P., Kroos M.A., de Graaff E., Oostra B.A., Reuser A.J.J.;
"Two mutations affecting the transport and maturation of lysosomal
alpha-glucosidase in an adult case of glycogen storage disease type
II.";
Hum. Mutat. 2:268-273(1993).
[23]
VARIANT GSD2 GLU-645, AND VARIANTS ILE-816 AND ILE-927.
PubMed=8094613; DOI=10.1042/bj2890687;
Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A.,
Willemsen R., Oostra B.A., Reuser A.J.J.;
"The conservative substitution Asp-645-->Glu in lysosomal alpha-
glucosidase affects transport and phosphorylation of the enzyme in an
adult patient with glycogen-storage disease type II.";
Biochem. J. 289:687-693(1993).
[24]
VARIANT GSD2 GLU-645, AND VARIANTS ILE-816 AND ILE-927.
PubMed=1684505; DOI=10.1089/dna.1991.10.681;
Martiniuk F., Mehler M., Bodkin M., Tzall S., Hirschhorn K., Zhong N.,
Hirschhorn R.;
"Identification of a missense mutation in an adult-onset patient with
glycogenosis type II expressing only one allele.";
DNA Cell Biol. 10:681-687(1991).
[25]
VARIANTS ILE-816 AND ILE-927.
PubMed=8486380; DOI=10.1006/geno.1993.1185;
Hermans M.M.P., Svetkey L.P., Oostra B.A., Chen Y.T., Reuser A.J.J.;
"The loss of a polymorphic glycosylation site caused by Thr-927-->Ile
is linked to a second polymorphic Val-816-->Ile substitution in
lysosomal alpha-glucosidase of American blacks.";
Genomics 16:300-301(1993).
[26]
VARIANT GSD2 VAL-519.
PubMed=7866409; DOI=10.1002/humu.1380040410;
Huie M.L., Hirschhorn R., Chen A.S., Martiniuk F., Zhong N.;
"Mutation at the catalytic site (M519V) in glycogen storage disease
type II (Pompe disease).";
Hum. Mutat. 4:291-293(1994).
[27]
VARIANT GSD2 TRP-647.
PubMed=7981676; DOI=10.1093/hmg/3.7.1081;
Huie M.L., Chen A.S., Brooks S.S., Grix A., Hirschhorn R.;
"A de novo 13 nt deletion, a newly identified C647W missense mutation
and a deletion of exon 18 in infantile onset glycogen storage disease
type II (GSDII).";
Hum. Mol. Genet. 3:1081-1087(1994).
[28]
VARIANT GSD2 LEU-545.
PubMed=7881422; DOI=10.1093/hmg/3.12.2213;
Hermans M.M.P., de Graaff E., Kroos M.A., Mohkamsing S., Eussen B.J.,
Joosse M., Willemsen R., Kleijer W.J., Oostra B.A., Reuser A.J.J.;
"The effect of a single base pair deletion (delta T525) and a C1634T
missense mutation (Pro545Leu) on the expression of lysosomal alpha-
glucosidase in patients with glycogen storage disease type II.";
Hum. Mol. Genet. 3:2213-2218(1994).
[29]
VARIANTS GSD2 ARG-299 AND LYS-903 DEL, AND VARIANTS ARG-199; HIS-223
AND ILE-780.
PubMed=7717400;
Boerkoel C.F., Exelbert R., Nicastri C., Nichols R.C., Miller F.W.,
Plotz P.H., Raben N.;
"Leaky splicing mutation in the acid maltase gene is associated with
delayed onset of glycogenosis type II.";
Am. J. Hum. Genet. 56:887-897(1995).
[30]
VARIANT LYS-689.
PubMed=8912788; DOI=10.1111/j.1469-1809.1996.tb00433.x;
Huie M.L., Menaker M., McAlpine P.J., Hirschhorn R.;
"Identification of an E689K substitution as the molecular basis of the
human acid alpha-glucosidase type 4 allozyme (GAA*4).";
Ann. Hum. Genet. 60:365-368(1996).
[31]
VARIANT GSD2 VAL-529.
PubMed=8834250; DOI=10.1007/BF02267074;
Tsunoda H., Ohshima T., Tohyama J., Sasaki M., Sakuragawa N.,
Martiniuk F.;
"Acid alpha-glucosidase deficiency: identification and expression of a
missense mutation (S529V) in a Japanese adult phenotype.";
Hum. Genet. 97:496-499(1996).
[32]
VARIANTS GSD2 ASN-645; TRP-647; SER-648; GLN-672 AND TRP-672.
PubMed=9535769; DOI=10.1006/bbrc.1998.8255;
Huie M.L., Tsujino S., Brooks S.S., Engel A., Elias E., Bonthron D.T.,
Bessley C., Shanske S., Dimauro S., Goto Y., Hirschhorn R.;
"Glycogen storage disease type II: identification of four novel
missense mutations (D645N, G648S, R672W, R672Q) and two
insertions/deletions in the acid alpha-glucosidase locus of patients
of differing phenotype.";
Biochem. Biophys. Res. Commun. 244:921-927(1998).
[33]
VARIANT GSD2 ARG-309.
PubMed=9660056;
Kroos M.A., van Leenen D., Verbiest J., Reuser A.J.J., Hermans M.M.P.;
"Glycogen storage disease type II: identification of a dinucleotide
deletion and a common missense mutation in the lysosomal alpha-
glucosidase gene.";
Clin. Genet. 53:379-382(1998).
[34]
VARIANTS GSD2 PRO-566; ARG-643 AND ARG-768, AND VARIANTS ASN-91;
ARG-199 AND HIS-223.
PubMed=9521422;
DOI=10.1002/(SICI)1098-1004(1998)11:3<209::AID-HUMU5>3.3.CO;2-R;
Hermans M.M.P., Kroos M.A., Smeitink J.A.M., van der Ploeg A.T.,
Kleijer W.J., Reuser A.J.J.;
"Glycogen storage disease type II: genetic and biochemical analysis of
novel mutations in infantile patients from Turkish ancestry.";
Hum. Mutat. 11:209-215(1998).
[35]
VARIANT GSD2 GLY-VAL-PRO-VAL-SER-ASN-925 INS.
PubMed=10206684;
DOI=10.1002/(SICI)1098-1004(1998)11:5<413::AID-HUMU16>3.0.CO;2-I;
Beesley C.E., Child A.H., Yacoub M.Y.;
"The identification of five novel mutations in the lysosomal acid
alpha-(1,4) glucosidase gene from patients with glycogen storage
disease type II.";
Hum. Mutat. 11:413-413(1998).
[36]
VARIANTS GSD2 LEU-545 AND TRP-638.
PubMed=10737124; DOI=10.1007/s100480050030;
Vorgerd M., Burwinkel B., Reichmann H., Malin J.-P., Kilimann M.W.;
"Adult-onset glycogen storage disease type II: phenotypic and allelic
heterogeneity in German patients.";
Neurogenetics 1:205-211(1998).
[37]
VARIANT GSD2 ARG-481.
PubMed=10189220;
DOI=10.1002/(SICI)1098-1004(1999)13:1<83::AID-HUMU13>3.0.CO;2-2;
Raben N., Lee E., Lee L., Hirschhorn R., Plotz P.H.;
"Novel mutations in African American patients with glycogen storage
disease Type II.";
Hum. Mutat. 13:83-84(1999).
[38]
VARIANTS GSD2, AND VARIANTS.
PubMed=10338092;
DOI=10.1002/(SICI)1098-1004(1999)13:5<380::AID-HUMU6>3.0.CO;2-A;
Ko T.-M., Hwu W.-L., Lin Y.-W., Tseng L.-H., Hwa H.-L., Wang T.-R.,
Chuang S.-M.;
"Molecular genetic study of Pompe disease in Chinese patients in
Taiwan.";
Hum. Mutat. 13:380-384(1999).
[39]
VARIANTS GSD2 PRO-208; LEU-308; LEU-324; MET-585; 607-GLY--HIS-612
DEL; ARG-643 AND THR-672.
PubMed=11071489; DOI=10.1212/WNL.55.8.1122;
Laforet P., Nicolino M., Eymard P.B., Puech J.P., Caillaud C.,
Poenaru L., Fardeau M.;
"Juvenile and adult-onset acid maltase deficiency in France: genotype-
phenotype correlation.";
Neurology 55:1122-1128(2000).
[40]
VARIANTS GSD2 ARG-219; LYS-262 AND VAL-408.
PubMed=11738358; DOI=10.1016/S0960-8966(01)00247-4;
Fernandez-Hojas R., Huie M.L., Navarro C., Dominguez C., Roig M.,
Lopez-Coronas D., Teijeira S., Anyane-Yeboa K., Hirschhorn R.;
"Identification of six novel mutations in the acid alpha-glucosidase
gene in three Spanish patients with infantile onset glycogen storage
disease type II (Pompe disease).";
Neuromuscul. Disord. 12:159-166(2002).
[41]
VARIANT GSD2 TRP-224, AND CHARACTERIZATION OF VARIANT GSD2 TRP-224.
PubMed=12923862; DOI=10.1002/ajmg.a.20164;
Pittis M.G., Montalvo A.L., Miocic S., Martini C., Deganuto M.,
Candusso M., Ciana G., Bembi B.;
"Identification of four novel mutations in the alpha glucosidase gene
in five Italian patients with infantile onset glycogen storage disease
type II.";
Am. J. Med. Genet. A 121:225-230(2003).
[42]
VARIANTS GSD2 LEU-361 AND CYS-437.
PubMed=12601120; DOI=10.1212/01.WNL.0000048661.95327.BF;
Lam C.W., Yuen Y.P., Chan K.Y., Tong S.F., Lai C.K., Chow T.C.,
Lee K.C., Chan Y.W., Martiniuk F.;
"Juvenile-onset glycogen storage disease type II with novel mutations
in acid alpha-glucosidase gene.";
Neurology 60:715-717(2003).
[43]
VARIANTS GSD2 TRP-224; CYS-600; ARG-619 AND HIS-660, CHARACTERIZATION
OF VARIANTS GSD2 TRP-224; ARG-619 AND HIS-660, AND CHARACTERIZATION OF
VARIANT SER-576.
PubMed=14643388; DOI=10.1016/S0887-8994(03)00267-4;
Pipo J.R., Feng J.-H., Yamamoto T., Ohsaki Y., Nanba E., Tsujino S.,
Sakuragawa N., Martiniuk F., Ninomiya H., Oka A., Ohno K.;
"New GAA mutations in Japanese patients with GSDII (Pompe disease).";
Pediatr. Neurol. 29:284-287(2003).
[44]
VARIANTS GSD2 GLY-103; ARG-219; ARG-285; CYS-292; ARG-293; PRO-308;
ARG-312; PRO-355; ARG-374; PRO-405; PHE-455; ASP-459 DEL; ARG-478;
ARG-481; THR-519; LEU-545; ARG-549; PRO-552; SER-575; LYS-579;
CYS-600; ASP-607 AND ASP-880, AND CHARACTERIZATION OF VARIANTS.
PubMed=14695532; DOI=10.1002/humu.10286;
Hermans M.M.P., van Leenen D., Kroos M.A., Beesley C.E.,
Van der Ploeg A.T., Sakuraba H., Wevers R., Kleijer W.J.,
Michelakakis H., Kirk E.P., Fletcher J., Bosshard N.,
Basel-Vanagaite L., Besley G., Reuser A.J.J.;
"Twenty-two novel mutations in the lysosomal alpha-glucosidase gene
(GAA) underscore the genotype-phenotype correlation in glycogen
storage disease type II.";
Hum. Mutat. 23:47-56(2004).
[45]
VARIANTS GSD2 PRO-355 AND CYS-702, AND CHARACTERIZATION OF VARIANTS
GSD2 PRO-355 AND CYS-702.
PubMed=14972326; DOI=10.1016/j.ymgme.2003.11.011;
Montalvo A.L.E., Cariati R., Deganuto M., Guerci V., Garcia R.,
Ciana G., Bembi B., Pittis M.G.;
"Glycogenosis type II: identification and expression of three novel
mutations in the acid alpha-glucosidase gene causing the infantile
form of the disease.";
Mol. Genet. Metab. 81:203-208(2004).
[46]
VARIANT GSD2 GLN-901, AND VARIANT ASN-645.
PubMed=15145338; DOI=10.1016/j.nmd.2004.02.012;
Kroos M.A., Kirschner J., Gellerich F.N., Hermans M.M.,
Van der Ploeg A.T., Reuser A.J., Korinthenberg R.;
"A case of childhood Pompe disease demonstrating phenotypic
variability of p.Asp645Asn.";
Neuromuscul. Disord. 14:371-374(2004).
[47]
VARIANTS GSD2 VAL-237 AND ARG-293.
PubMed=15668445; DOI=10.1212/01.WNL.0000149528.95362.20;
Anneser J.M., Pongratz D.E., Podskarbi T., Shin Y.S., Schoser B.G.;
"Mutations in the acid alpha-glucosidase gene (M. Pompe) in a patient
with an unusual phenotype.";
Neurology 64:368-370(2005).
[48]
VARIANT GSD2 GLY-330.
PubMed=16782080; DOI=10.1016/j.cca.2006.04.007;
Dou W., Gu X., Fu L., Peng C., Zheng J., Martiniuk F., Sheng H.Z.;
"A novel missense mutation in the acid alpha-glucosidase gene causing
the classic infantile form of Pompe disease.";
Clin. Chim. Acta 374:145-146(2006).
[49]
VARIANT GSD2 GLY-ASN-404.
PubMed=16433701; DOI=10.1111/j.1399-0004.2005.00557.x;
Amartino H., Painceira D., Pomponio R.J., Niizawa G., Sabio Paz V.,
Blanco M., Chamoles N.;
"Two clinical forms of glycogen-storage disease type II in two
generations of the same family.";
Clin. Genet. 69:187-188(2006).
[50]
VARIANTS GSD2 ARG-309; PRO-355; LEU-361; PRO-445; ASN-489; ARG-549;
GLN-612; ARG-643; TRP-672 AND CYS-746.
PubMed=16917947; DOI=10.1002/humu.20374;
Montalvo A.L., Bembi B., Donnarumma M., Filocamo M., Parenti G.,
Rossi M., Merlini L., Buratti E., De Filippi P., Dardis A.,
Stroppiano M., Ciana G., Pittis M.G.;
"Mutation profile of the GAA gene in 40 Italian patients with late
onset glycogen storage disease type II.";
Hum. Mutat. 27:999-1006(2006).
[51]
VARIANTS GSD2 PRO-355; ALA-522 AND VAL-610, AND VARIANT ARG-359.
PubMed=17643989; DOI=10.1016/j.nmd.2007.06.002;
Muller-Felber W., Horvath R., Gempel K., Podskarbi T., Shin Y.,
Pongratz D., Walter M.C., Baethmann M., Schlotter-Weigel B.,
Lochmuller H., Schoser B.;
"Late onset Pompe disease: clinical and neurophysiological spectrum of
38 patients including long-term follow-up in 18 patients.";
Neuromuscul. Disord. 17:698-706(2007).
[52]
VARIANTS GSD2 HIS-190; SER-285; PHE-291; PRO-291; LYS-318; ARG-335;
ARG-347; ARG-482; VAL-483; GLN-521; SER-522; LYS-570; GLN-572;
PRO-594; LYS-614; ASN-737; SER-746 AND PRO-935, AND VARIANT LYS-585.
PubMed=18425781; DOI=10.1002/humu.20745;
Kroos M., Pomponio R.J., van Vliet L., Palmer R.E., Phipps M.,
Van der Helm R., Halley D., Reuser A.;
"Update of the Pompe disease mutation database with 107 sequence
variants and a format for severity rating.";
Hum. Mutat. 29:E13-E26(2008).
[53]
VARIANTS GSD2 GLY-103; CYS-191; ARG-219; TRP-224; LYS-262; ARG-293;
PRO-355; LEU-375; ARG-401; ASN-489; ALA-522; PRO-552; TYR-599;
TRP-638; ARG-643 AND ASN-645, AND CHARACTERIZATION OF VARIANTS GSD2
CYS-191; LEU-375; ARG-401; ALA-522 AND TYR-599.
PubMed=18429042; DOI=10.1002/humu.20753;
Pittis M.G., Donnarumma M., Montalvo A.L.E., Dominissini S., Kroos M.,
Rosano C., Stroppiano M., Bianco M.G., Donati M.A., Parenti G.,
D'Amico A., Ciana G., Di Rocco M., Reuser A., Bembi B., Filocamo M.;
"Molecular and functional characterization of eight novel GAA
mutations in Italian infants with Pompe disease.";
Hum. Mutat. 29:E27-E36(2008).
[54]
VARIANTS GSD2 PRO-46; LEU-217; PRO-486; PRO-594; TYR-612; LYS-635 AND
VAL-638.
PubMed=19588081; DOI=10.1007/s00415-009-5219-y;
Oba-Shinjo S.M., da Silva R., Andrade F.G., Palmer R.E.,
Pomponio R.J., Ciociola K.M., Carvalho S.M., Gutierrez P.S., Porta G.,
Marrone C.D., Munoz V., Grzesiuk A.K., Llerena J.C. Jr.,
Berditchevsky C.R., Sobreira C., Horovitz D., Hatem T.P., Frota E.R.,
Pecchini R., Kouyoumdjian J.A., Werneck L., Amado V.M.,
Camelo J.S. Jr., Mattaliano R.J., Marie S.K.;
"Pompe disease in a Brazilian series: clinical and molecular analyses
with identification of nine new mutations.";
J. Neurol. 256:1881-1890(2009).
[55]
VARIANT GSD2 SER-558.
PubMed=20350966; DOI=10.1177/0883073809356035;
Alcantara-Ortigoza M.A., Gonzalez-del Angel A., Barrientos-Rios R.,
Cupples C., Garrido-Garcia L.M., de Leon-Bojorge B.,
Alva-Chaire Adel C.;
"Screening of late-onset Pompe disease in a sample of Mexican patients
with myopathies of unknown etiology: identification of a novel
mutation in the acid alpha-glucosidase gene.";
J. Child Neurol. 25:1034-1037(2010).
[56]
VARIANTS GSD2 PRO-224; LEU-251; LEU-254; LYS-262; SER-266; PRO-291;
VAL-408; ARG-478; TYR-525; LEU-545; PHE-557; ARG-615; GLU-645; GLY-746
AND CYS-746, AND VARIANTS ALA-271 AND ARG-711.
PubMed=20080426; DOI=10.1016/j.ymgme.2009.12.014;
Labrousse P., Chien Y.H., Pomponio R.J., Keutzer J., Lee N.C.,
Akmaev V.R., Scholl T., Hwu W.L.;
"Genetic heterozygosity and pseudodeficiency in the Pompe disease
newborn screening pilot program.";
Mol. Genet. Metab. 99:379-383(2010).
[57]
VARIANT GSD2 GLY-103, AND VARIANT ASN-91.
PubMed=21109266; DOI=10.1016/j.jns.2010.10.031;
Fidzianska A., Lugowska A., Tylki-Szymanska A.;
"Late form of Pompe disease with glycogen storage in peripheral nerves
axons.";
J. Neurol. Sci. 301:59-62(2011).
[58]
VARIANTS HIS-74; HIS-89; LEU-220; MET-222; ASP-290; GLY-310; VAL-391;
CYS-458; ASP-611; LEU-629; 700-THR-LEU-701 DEL AND ILE-718, AND
VARIANTS GSD2 ARG-103; GLY-108; PHE-127; GLN-224; ARG-234; LYS-234;
ILE-316; GLU-335; LEU-361; LEU-397; VAL-419; HIS-457; TYR-523;
SER-558; CYS-575; ARG-576; HIS-594; LEU-601; ALA-602; PRO-627;
ASP-648; LEU-702; LYS-743; PRO-819 AND PHE-916.
PubMed=22644586; DOI=10.1002/humu.22108;
Kroos M., Hoogeveen-Westerveld M., Michelakakis H., Pomponio R.,
Van der Ploeg A., Halley D., Reuser A., Augoustides-Savvopoulou P.,
Ausems M., Llona J.B., Bautista Lorite J., van der Beek N., Bonafe L.,
Cuk M., D'Hooghe M., Engelen B., Farouk A., Fumic K.,
Garcia-Delgado E., Herzog A., Hurst J., Jones S., Kariminejad M.H.,
Kucukcongar A., Lissens W., Lund A., Majoor-Krakauer D., Kumamoto S.,
Maravi E., Marie S., Mengel E., Mavridou I., Munteis Olivas E.,
Najmabadi H., Okumiya T., Peric S., Paschke E., Plecko B.,
Robberecht W., Serdaroglu P., Shboul M., Tansek M.Z., Tarnutzer A.,
Stojanovic V.R., Tylki-Szymanska A., Venancio M., Verhoeven K.;
"Update of the pompe disease mutation database with 60 novel GAA
sequence variants and additional studies on the functional effect of
34 previously reported variants.";
Hum. Mutat. 33:1161-1165(2012).
[59]
VARIANTS GSD2 LYS-234; 431-LEU--GLN-433 DEL; LEU-568; LEU-601; CYS-766
AND ARG-913.
PubMed=22676651; DOI=10.1186/1750-1172-7-35;
Herzog A., Hartung R., Reuser A.J., Hermanns P., Runz H., Karabul N.,
Goekce S., Pohlenz J., Kampmann C., Lampe C., Beck M., Mengel E.;
"A cross-sectional single-centre study on the spectrum of Pompe
disease, German patients: molecular analysis of the GAA gene,
manifestation and genotype-phenotype correlations.";
Orphanet J. Rare Dis. 7:35-35(2012).
[60]
VARIANTS GSD2 VAL-391; HIS-437; PRO-552; ASP-611; VAL-641; TRP-647 AND
PRO-705, AND VARIANTS ASN-91; ARG-199; HIS-223; SER-576; LYS-689;
ILE-780 AND ILE-816.
PubMed=25681614; DOI=10.1016/j.gene.2015.02.023;
Turaca L.T., de Faria D.O., Kyosen S.O., Teixeira V.D., Motta F.L.,
Pessoa J.G., Rodrigues E Silva M., de Almeida S.S., D'Almeida V.,
Munoz Rojas M.V., Martins A.M., Pesquero J.B.;
"Novel GAA mutations in patients with Pompe disease.";
Gene 561:124-131(2015).
-!- FUNCTION: Essential for the degradation of glygogen to glucose in
lysosomes.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing (1->4)-
linked alpha-D-glucose residues with release of alpha-D-glucose.
-!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:17897319}.
Lysosome membrane {ECO:0000269|PubMed:17897319}.
-!- PTM: The different forms of acid glucosidase are obtained by
proteolytic processing.
-!- PTM: Phosphorylation of mannose residues ensures efficient
transport of the enzyme to the lysosomes via the mannose 6-
phosphate receptor.
-!- POLYMORPHISM: There are three common alleles of GAA: GAA*1, GAA*2
and GAA*4. The sequence shown is that of allele GAA*1, which is
the most common. Alleles GAA*2 and GAA*4 are much rarer.
{ECO:0000269|PubMed:21109266, ECO:0000269|PubMed:2203258,
ECO:0000269|PubMed:25681614, ECO:0000269|PubMed:8912788,
ECO:0000269|PubMed:9521422}.
-!- DISEASE: Glycogen storage disease 2 (GSD2) [MIM:232300]: A
metabolic disorder with a broad clinical spectrum. The severe
infantile form, or Pompe disease, presents at birth with massive
accumulation of glycogen in muscle, heart and liver.
Cardiomyopathy and muscular hypotonia are the cardinal features of
this form whose life expectancy is less than two years. The
juvenile and adult forms present as limb-girdle muscular dystrophy
beginning in the lower limbs. Final outcome depends on respiratory
muscle failure. Patients with the adult form can be free of
clinical symptoms for most of their life but finally develop a
slowly progressive myopathy. {ECO:0000269|PubMed:10189220,
ECO:0000269|PubMed:10206684, ECO:0000269|PubMed:10338092,
ECO:0000269|PubMed:10737124, ECO:0000269|PubMed:11071489,
ECO:0000269|PubMed:11738358, ECO:0000269|PubMed:12601120,
ECO:0000269|PubMed:12923862, ECO:0000269|PubMed:14643388,
ECO:0000269|PubMed:14695532, ECO:0000269|PubMed:14972326,
ECO:0000269|PubMed:15145338, ECO:0000269|PubMed:15668445,
ECO:0000269|PubMed:16433701, ECO:0000269|PubMed:1652892,
ECO:0000269|PubMed:16782080, ECO:0000269|PubMed:1684505,
ECO:0000269|PubMed:16917947, ECO:0000269|PubMed:17643989,
ECO:0000269|PubMed:18425781, ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:1898413, ECO:0000269|PubMed:19588081,
ECO:0000269|PubMed:20080426, ECO:0000269|PubMed:20350966,
ECO:0000269|PubMed:21109266, ECO:0000269|PubMed:22644586,
ECO:0000269|PubMed:22676651, ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:7695647, ECO:0000269|PubMed:7717400,
ECO:0000269|PubMed:7866409, ECO:0000269|PubMed:7881422,
ECO:0000269|PubMed:7981676, ECO:0000269|PubMed:8094613,
ECO:0000269|PubMed:8401535, ECO:0000269|PubMed:8834250,
ECO:0000269|PubMed:9521422, ECO:0000269|PubMed:9535769,
ECO:0000269|PubMed:9660056, ECO:0000269|Ref.5}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=GAA; Note=Mutations in alpha-glucosidase;
URL="http://cluster15.erasmusmc.nl/klgn/pompe/mutations.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-glucosidase entry;
URL="https://en.wikipedia.org/wiki/Alpha-glucosidase";
-!- WEB RESOURCE: Name=Glucosidase, alpha, acid (Pompe disease) (GAA);
Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/GAA";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00839; CAA68763.1; -; mRNA.
EMBL; Y00839; CAA68764.1; -; mRNA.
EMBL; X55080; CAC12967.1; -; Genomic_DNA.
EMBL; X55081; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55095; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55082; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55084; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55083; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55098; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55085; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55086; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55087; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55088; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55089; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55090; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55096; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55091; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55092; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55093; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55094; CAC12967.1; JOINED; Genomic_DNA.
EMBL; X55097; CAC12967.1; JOINED; Genomic_DNA.
EMBL; M34424; AAA52506.1; -; mRNA.
EMBL; DQ907243; ABI53718.1; -; mRNA.
EMBL; AC087741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040431; AAH40431.1; -; mRNA.
EMBL; S76893; AAB33842.1; -; mRNA.
CCDS; CCDS32760.1; -.
PIR; A40577; A32609.
RefSeq; NP_000143.2; NM_000152.4.
RefSeq; NP_001073271.1; NM_001079803.2.
RefSeq; NP_001073272.1; NM_001079804.2.
RefSeq; XP_005257250.1; XM_005257193.2.
RefSeq; XP_005257251.1; XM_005257194.4.
UniGene; Hs.1437; -.
UniGene; Hs.733627; -.
PDB; 5KZW; X-ray; 2.00 A; A=79-952.
PDB; 5KZX; X-ray; 2.00 A; A=79-952.
PDBsum; 5KZW; -.
PDBsum; 5KZX; -.
ProteinModelPortal; P10253; -.
SMR; P10253; -.
BioGrid; 108823; 46.
IntAct; P10253; 8.
STRING; 9606.ENSP00000305692; -.
BindingDB; P10253; -.
ChEMBL; CHEMBL2608; -.
DrugBank; DB00284; Acarbose.
DrugBank; DB05200; AT2220.
DrugBank; DB00491; Miglitol.
GuidetoPHARMACOLOGY; 2611; -.
Allergome; 9614; Hom s Glucosidase.
CAZy; GH31; Glycoside Hydrolase Family 31.
iPTMnet; P10253; -.
PhosphoSitePlus; P10253; -.
UniCarbKB; P10253; -.
BioMuta; GAA; -.
DMDM; 317373572; -.
EPD; P10253; -.
MaxQB; P10253; -.
PaxDb; P10253; -.
PeptideAtlas; P10253; -.
PRIDE; P10253; -.
DNASU; 2548; -.
Ensembl; ENST00000302262; ENSP00000305692; ENSG00000171298.
Ensembl; ENST00000390015; ENSP00000374665; ENSG00000171298.
GeneID; 2548; -.
KEGG; hsa:2548; -.
UCSC; uc002jxo.4; human.
CTD; 2548; -.
DisGeNET; 2548; -.
EuPathDB; HostDB:ENSG00000171298.12; -.
GeneCards; GAA; -.
GeneReviews; GAA; -.
HGNC; HGNC:4065; GAA.
HPA; HPA026970; -.
HPA; HPA029126; -.
MalaCards; GAA; -.
MIM; 232300; phenotype.
MIM; 606800; gene.
neXtProt; NX_P10253; -.
OpenTargets; ENSG00000171298; -.
Orphanet; 308604; Glycogen storage disease due to acid maltase deficiency, adult onset.
Orphanet; 308552; Glycogen storage disease due to acid maltase deficiency, infantile onset.
Orphanet; 308573; Glycogen storage disease due to acid maltase deficiency, juvenile onset.
PharmGKB; PA28476; -.
eggNOG; KOG1065; Eukaryota.
eggNOG; COG1501; LUCA.
GeneTree; ENSGT00760000119229; -.
HOGENOM; HOG000041175; -.
HOVERGEN; HBG006297; -.
InParanoid; P10253; -.
KO; K12316; -.
OMA; HWTGDVW; -.
OrthoDB; EOG091G030L; -.
PhylomeDB; P10253; -.
TreeFam; TF314577; -.
BRENDA; 3.2.1.20; 2681.
Reactome; R-HSA-5357572; Lysosomal glycogen catabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
GeneWiki; Acid_alpha-glucosidase; -.
GenomeRNAi; 2548; -.
PRO; PR:P10253; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171298; -.
CleanEx; HS_GAA; -.
ExpressionAtlas; P10253; baseline and differential.
Genevisible; P10253; HS.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:BHF-UCL.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0004574; F:oligo-1,6-glucosidase activity; EXP:Reactome.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0002086; P:diaphragm contraction; IMP:BHF-UCL.
GO; GO:0006006; P:glucose metabolic process; IC:BHF-UCL.
GO; GO:0005980; P:glycogen catabolic process; IDA:BHF-UCL.
GO; GO:0003007; P:heart morphogenesis; IEA:Ensembl.
GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
GO; GO:0007040; P:lysosome organization; IMP:BHF-UCL.
GO; GO:0000023; P:maltose metabolic process; IC:BHF-UCL.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
GO; GO:0005985; P:sucrose metabolic process; IC:BHF-UCL.
GO; GO:0009888; P:tissue development; IEA:Ensembl.
GO; GO:0043181; P:vacuolar sequestering; IMP:BHF-UCL.
CDD; cd00111; Trefoil; 1.
InterPro; IPR031727; Gal_mutarotase_N.
InterPro; IPR011013; Gal_mutarotase_SF_dom.
InterPro; IPR000322; Glyco_hydro_31.
InterPro; IPR030458; Glyco_hydro_31_AS.
InterPro; IPR030459; Glyco_hydro_31_CS.
InterPro; IPR025887; Glyco_hydro_31_N_dom.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR017957; P_trefoil_CS.
InterPro; IPR000519; P_trefoil_dom.
Pfam; PF13802; Gal_mutarotas_2; 1.
Pfam; PF01055; Glyco_hydro_31; 1.
Pfam; PF16863; NtCtMGAM_N; 1.
Pfam; PF00088; Trefoil; 1.
SMART; SM00018; PD; 1.
SUPFAM; SSF51445; SSF51445; 2.
SUPFAM; SSF74650; SSF74650; 1.
PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PROSITE; PS00025; P_TREFOIL_1; 1.
PROSITE; PS51448; P_TREFOIL_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycogen storage disease;
Glycoprotein; Glycosidase; Hydrolase; Lysosome; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Signal.
SIGNAL 1 27 {ECO:0000255}.
PROPEP 28 69 {ECO:0000269|PubMed:3049072}.
/FTId=PRO_0000018565.
CHAIN 70 952 Lysosomal alpha-glucosidase.
/FTId=PRO_0000018566.
CHAIN 123 952 76 kDa lysosomal alpha-glucosidase.
/FTId=PRO_0000018567.
CHAIN 204 952 70 kDa lysosomal alpha-glucosidase.
/FTId=PRO_0000018568.
DOMAIN 80 131 P-type. {ECO:0000255|PROSITE-
ProRule:PRU00779}.
ACT_SITE 518 518 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10066,
ECO:0000269|PubMed:1856189}.
ACT_SITE 521 521 {ECO:0000250}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8435067}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8435067}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:8435067}.
CARBOHYD 470 470 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8435067}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8435067}.
CARBOHYD 882 882 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8435067}.
CARBOHYD 925 925 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8435067}.
DISULFID 82 109 {ECO:0000255|PROSITE-ProRule:PRU00779}.
DISULFID 92 108 {ECO:0000255|PROSITE-ProRule:PRU00779}.
DISULFID 103 127 {ECO:0000255|PROSITE-ProRule:PRU00779}.
VARIANT 46 46 S -> P (in GSD2; dbSNP:rs777215354).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068564.
VARIANT 74 74 R -> H (in dbSNP:rs764797280).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068565.
VARIANT 89 89 R -> H (in dbSNP:rs200586324).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068566.
VARIANT 91 91 D -> N (in allele GAA*2; lower affinity
for glycogen and starch but not for
lower-molecular weight substrates;
dbSNP:rs1800299).
{ECO:0000269|PubMed:21109266,
ECO:0000269|PubMed:2203258,
ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:9521422}.
/FTId=VAR_004285.
VARIANT 103 103 C -> G (in GSD2; infantile form; severe;
loss of activity; shows enzyme
localization primarily in the ER-Golgi
compartment suggesting that mutation
could affect the normal processing and
stability of the enzyme;
dbSNP:rs398123174).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:21109266}.
/FTId=VAR_018078.
VARIANT 103 103 C -> R (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068567.
VARIANT 108 108 C -> G (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068568.
VARIANT 127 127 C -> F (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068569.
VARIANT 190 190 R -> H (in GSD2; dbSNP:rs528367092).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068570.
VARIANT 191 191 Y -> C (in GSD2; extremely low residual
enzymatic activity).
{ECO:0000269|PubMed:18429042}.
/FTId=VAR_046467.
VARIANT 199 199 H -> R (in dbSNP:rs1042393).
{ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:3049072,
ECO:0000269|PubMed:7717400,
ECO:0000269|PubMed:9521422,
ECO:0000269|Ref.5}.
/FTId=VAR_004286.
VARIANT 208 208 L -> P (in GSD2).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_029025.
VARIANT 217 217 P -> L (in GSD2).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068571.
VARIANT 219 219 G -> R (in GSD2; infantile form; severe;
loss of activity; dbSNP:rs370950728).
{ECO:0000269|PubMed:11738358,
ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_018079.
VARIANT 220 220 V -> L (in dbSNP:rs530478036).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068572.
VARIANT 222 222 V -> M (in dbSNP:rs374569672).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068573.
VARIANT 223 223 R -> H (in dbSNP:rs1042395).
{ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:3049072,
ECO:0000269|PubMed:7717400,
ECO:0000269|PubMed:9521422,
ECO:0000269|Ref.5}.
/FTId=VAR_004287.
VARIANT 224 224 R -> P (in GSD2).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068574.
VARIANT 224 224 R -> Q (in GSD2; dbSNP:rs200210219).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068575.
VARIANT 224 224 R -> W (in GSD2; infantile; mild partial
loss of activity; dbSNP:rs757700700).
{ECO:0000269|PubMed:12923862,
ECO:0000269|PubMed:14643388,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_029026.
VARIANT 234 234 T -> K (in GSD2).
{ECO:0000269|PubMed:22644586,
ECO:0000269|PubMed:22676651}.
/FTId=VAR_068576.
VARIANT 234 234 T -> R (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068577.
VARIANT 237 237 A -> V (in GSD2; dbSNP:rs121907944).
{ECO:0000269|PubMed:15668445}.
/FTId=VAR_029027.
VARIANT 251 251 S -> L (in GSD2; dbSNP:rs200856561).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068578.
VARIANT 254 254 S -> L (in GSD2; dbSNP:rs577915581).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068579.
VARIANT 262 262 E -> K (in GSD2; infantile; severe;
dbSNP:rs201896815).
{ECO:0000269|PubMed:11738358,
ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:20080426}.
/FTId=VAR_029028.
VARIANT 266 266 P -> S (in GSD2).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068580.
VARIANT 271 271 T -> A. {ECO:0000269|PubMed:20080426}.
/FTId=VAR_068581.
VARIANT 285 285 P -> R (in GSD2; juvenile form; mild;
partial loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018080.
VARIANT 285 285 P -> S (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068582.
VARIANT 290 290 N -> D (in dbSNP:rs552929702).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068583.
VARIANT 291 291 L -> F (in GSD2; dbSNP:rs773417785).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068584.
VARIANT 291 291 L -> P (in GSD2).
{ECO:0000269|PubMed:18425781,
ECO:0000269|PubMed:20080426}.
/FTId=VAR_068585.
VARIANT 292 292 Y -> C (in GSD2; juvenile form; mild;
partial loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018081.
VARIANT 293 293 G -> R (in GSD2; infantile form; severe;
almost complete loss of activity;
dbSNP:rs121907945).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:15668445,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_018082.
VARIANT 299 299 L -> R (in GSD2; infantile form;
dbSNP:rs121907940).
{ECO:0000269|PubMed:7717400}.
/FTId=VAR_004288.
VARIANT 308 308 H -> L (in GSD2).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_046468.
VARIANT 308 308 H -> P (in GSD2; infantile form; severe;
complete loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018083.
VARIANT 309 309 G -> R (in GSD2; severe;
dbSNP:rs543300039).
{ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:9660056}.
/FTId=VAR_018084.
VARIANT 310 310 V -> G (found in a patient with GSD2;
unknown pathological significance;
dbSNP:rs763091901).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068586.
VARIANT 312 312 L -> R (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018085.
VARIANT 316 316 N -> I (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068587.
VARIANT 318 318 M -> K (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068588.
VARIANT 318 318 M -> T (in GSD2; severe;
dbSNP:rs121907936).
{ECO:0000269|PubMed:1652892}.
/FTId=VAR_004289.
VARIANT 324 324 P -> L (in GSD2; dbSNP:rs750030887).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_029029.
VARIANT 330 330 W -> G (in GSD2; infantile form; severe).
{ECO:0000269|PubMed:16782080}.
/FTId=VAR_029030.
VARIANT 335 335 G -> E (in GSD2; dbSNP:rs730880022).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068589.
VARIANT 335 335 G -> R (in GSD2; dbSNP:rs202095215).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068590.
VARIANT 347 347 P -> R (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068591.
VARIANT 355 355 L -> P (in GSD2; infantile form; severe;
loss of activity; dbSNP:rs766074609).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:14972326,
ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:17643989,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_018086.
VARIANT 359 359 G -> R. {ECO:0000269|PubMed:17643989}.
/FTId=VAR_068592.
VARIANT 361 361 P -> L (in GSD2; juvenile form; severe;
dbSNP:rs755253527).
{ECO:0000269|PubMed:12601120,
ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:22644586}.
/FTId=VAR_029031.
VARIANT 374 374 C -> R (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018087.
VARIANT 375 375 R -> L (in GSD2; extremely low residual
enzymatic activity; dbSNP:rs142752477).
{ECO:0000269|PubMed:18429042}.
/FTId=VAR_046469.
VARIANT 377 377 G -> R (in GSD2; severe;
dbSNP:rs752002666).
/FTId=VAR_029032.
VARIANT 391 391 M -> V (found in a patient with GSD2;
unknown pathological significance;
dbSNP:rs778634337).
{ECO:0000269|PubMed:22644586,
ECO:0000269|PubMed:25681614}.
/FTId=VAR_068593.
VARIANT 397 397 P -> L (in GSD2; dbSNP:rs776008078).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068594.
VARIANT 401 401 Q -> R (in GSD2; extremely low residual
enzymatic activity).
{ECO:0000269|PubMed:18429042}.
/FTId=VAR_046470.
VARIANT 402 402 W -> R (in GSD2; severe).
/FTId=VAR_004290.
VARIANT 404 404 D -> N (in GSD2; severe;
dbSNP:rs141533320).
/FTId=VAR_029033.
VARIANT 405 405 L -> P (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018088.
VARIANT 408 408 M -> V (in GSD2; juvenile form; severe;
dbSNP:rs560575383).
{ECO:0000269|PubMed:11738358,
ECO:0000269|PubMed:20080426}.
/FTId=VAR_029034.
VARIANT 419 419 D -> V (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068595.
VARIANT 431 433 Missing (in GSD2).
{ECO:0000269|PubMed:22676651}.
/FTId=VAR_070017.
VARIANT 437 437 R -> C (in GSD2; juvenile form; severe;
dbSNP:rs770610356).
{ECO:0000269|PubMed:12601120}.
/FTId=VAR_029035.
VARIANT 437 437 R -> H (in GSD2; unknown pathological
significance; dbSNP:rs150868652).
{ECO:0000269|PubMed:25681614}.
/FTId=VAR_074277.
VARIANT 445 445 A -> P (in GSD2).
{ECO:0000269|PubMed:16917947}.
/FTId=VAR_029036.
VARIANT 455 455 Y -> F (in GSD2; juvenile form; almost
complete loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018089.
VARIANT 457 457 P -> H (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068596.
VARIANT 457 457 P -> L (in GSD2; juvenile form).
{ECO:0000269|Ref.5}.
/FTId=VAR_029040.
VARIANT 458 458 Y -> C. {ECO:0000269|PubMed:22644586}.
/FTId=VAR_068597.
VARIANT 459 459 Missing (in GSD2; infantile form;
severe). {ECO:0000269|PubMed:14695532}.
/FTId=VAR_018090.
VARIANT 478 478 G -> R (in GSD2; severe; loss of
activity; dbSNP:rs778068209).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:20080426}.
/FTId=VAR_004291.
VARIANT 481 481 W -> R (in GSD2; severe; loss of
activity; dbSNP:rs772883420).
{ECO:0000269|PubMed:10189220,
ECO:0000269|PubMed:14695532}.
/FTId=VAR_004292.
VARIANT 482 482 P -> R (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068598.
VARIANT 483 483 G -> V (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068599.
VARIANT 486 486 A -> P (in GSD2).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068600.
VARIANT 489 489 D -> N (in GSD2; severe;
dbSNP:rs398123169).
{ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_029037.
VARIANT 519 519 M -> T (in GSD2; severe; loss of
activity; dbSNP:rs786204720).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_004293.
VARIANT 519 519 M -> V (in GSD2).
{ECO:0000269|PubMed:7866409}.
/FTId=VAR_004294.
VARIANT 521 521 E -> K (in GSD2; severe;
dbSNP:rs121907937).
{ECO:0000269|PubMed:1898413}.
/FTId=VAR_004295.
VARIANT 521 521 E -> Q (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068601.
VARIANT 522 522 P -> A (in GSD2; no residual enzymatic
activity). {ECO:0000269|PubMed:17643989,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_046471.
VARIANT 522 522 P -> S (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068602.
VARIANT 523 523 S -> Y (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068603.
VARIANT 525 525 F -> Y (in GSD2).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068604.
VARIANT 529 529 S -> V (in GSD2; mild; requires 2
nucleotide substitutions;
dbSNP:rs121907941).
{ECO:0000269|PubMed:8834250}.
/FTId=VAR_004296.
VARIANT 545 545 P -> L (in GSD2; mild; partial loss of
activity; dbSNP:rs121907942).
{ECO:0000269|PubMed:10737124,
ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:20080426,
ECO:0000269|PubMed:7881422}.
/FTId=VAR_004297.
VARIANT 549 549 G -> R (in GSD2; juvenile form; mild;
partial loss of activity).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:16917947}.
/FTId=VAR_018091.
VARIANT 552 552 L -> P (in GSD2; infantile/juvenile form;
severe; loss of activity;
dbSNP:rs779556619).
{ECO:0000269|PubMed:14695532,
ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:25681614}.
/FTId=VAR_018092.
VARIANT 557 557 I -> F (in GSD2).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068605.
VARIANT 558 558 C -> S (in GSD2).
{ECO:0000269|PubMed:20350966,
ECO:0000269|PubMed:22644586}.
/FTId=VAR_068606.
VARIANT 566 566 S -> P (in GSD2; infantile form).
{ECO:0000269|PubMed:9521422}.
/FTId=VAR_004298.
VARIANT 568 568 H -> L (in GSD2).
{ECO:0000269|PubMed:22676651}.
/FTId=VAR_070018.
VARIANT 570 570 N -> K (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068607.
VARIANT 572 572 H -> Q (in GSD2; dbSNP:rs772962666).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068608.
VARIANT 575 575 Y -> C (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068609.
VARIANT 575 575 Y -> S (in GSD2; juvenile form).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018093.
VARIANT 576 576 G -> A.
/FTId=VAR_004299.
VARIANT 576 576 G -> R (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068610.
VARIANT 576 576 G -> S (retains about half of the
activity compared with the wild-type;
dbSNP:rs1800307).
{ECO:0000269|PubMed:14643388,
ECO:0000269|PubMed:25681614}.
/FTId=VAR_004300.
VARIANT 579 579 E -> K (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018094.
VARIANT 585 585 R -> K (in dbSNP:rs747373179).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068611.
VARIANT 585 585 R -> M (in GSD2).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_046472.
VARIANT 594 594 R -> H (in GSD2; dbSNP:rs775450536).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068612.
VARIANT 594 594 R -> P (in GSD2; dbSNP:rs775450536).
{ECO:0000269|PubMed:18425781,
ECO:0000269|PubMed:19588081}.
/FTId=VAR_068613.
VARIANT 599 599 S -> Y (in GSD2; no residual enzymatic
activity; dbSNP:rs753505203).
{ECO:0000269|PubMed:18429042}.
/FTId=VAR_046473.
VARIANT 600 600 R -> C (in GSD2; juvenile form; loss of
activity; dbSNP:rs764670084).
{ECO:0000269|PubMed:14643388,
ECO:0000269|PubMed:14695532}.
/FTId=VAR_018095.
VARIANT 600 600 R -> H (in GSD2; infantile form;
dbSNP:rs377544304).
/FTId=VAR_008689.
VARIANT 601 601 S -> L (in GSD2).
{ECO:0000269|PubMed:22644586,
ECO:0000269|PubMed:22676651}.
/FTId=VAR_068614.
VARIANT 602 602 T -> A (in GSD2; dbSNP:rs781484283).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068615.
VARIANT 607 612 Missing (in GSD2).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_046474.
VARIANT 607 607 G -> D (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018096.
VARIANT 610 610 A -> V (in GSD2).
{ECO:0000269|PubMed:17643989}.
/FTId=VAR_068616.
VARIANT 611 611 G -> D (found in a patient with GSD2;
unknown pathological significance).
{ECO:0000269|PubMed:22644586,
ECO:0000269|PubMed:25681614}.
/FTId=VAR_068617.
VARIANT 612 612 H -> Q (in GSD2).
{ECO:0000269|PubMed:16917947}.
/FTId=VAR_029038.
VARIANT 612 612 H -> Y (in GSD2).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068618.
VARIANT 614 614 T -> K (in GSD2; dbSNP:rs369531647).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068619.
VARIANT 615 615 G -> R (in GSD2; infantile/adult form;
dbSNP:rs549029029).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_008690.
VARIANT 619 619 S -> R (in GSD2; loss of function of the
mutant enzyme).
{ECO:0000269|PubMed:14643388}.
/FTId=VAR_046475.
VARIANT 627 627 S -> P (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068620.
VARIANT 629 629 P -> L (in dbSNP:rs746961289).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068621.
VARIANT 635 635 N -> K (in GSD2).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068622.
VARIANT 638 638 G -> V (in GSD2).
{ECO:0000269|PubMed:19588081}.
/FTId=VAR_068623.
VARIANT 638 638 G -> W (in GSD2; dbSNP:rs757617999).
{ECO:0000269|PubMed:10737124,
ECO:0000269|PubMed:18429042}.
/FTId=VAR_046476.
VARIANT 641 641 L -> V (in GSD2; unknown pathological
significance).
{ECO:0000269|PubMed:25681614}.
/FTId=VAR_074278.
VARIANT 643 643 G -> R (in GSD2; infantile form;
dbSNP:rs28937909).
{ECO:0000269|PubMed:11071489,
ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:8401535,
ECO:0000269|PubMed:9521422}.
/FTId=VAR_004301.
VARIANT 645 645 D -> E (in GSD2; infantile form; most
common mutation; deficient in
phosphorylation and in proteolytic
processing; dbSNP:rs28940868).
{ECO:0000269|PubMed:1684505,
ECO:0000269|PubMed:20080426,
ECO:0000269|PubMed:8094613}.
/FTId=VAR_004302.
VARIANT 645 645 D -> H (in GSD2; almost complete loss of
activity; dbSNP:rs368438393).
{ECO:0000269|PubMed:7695647}.
/FTId=VAR_004303.
VARIANT 645 645 D -> N (in GSD2; dbSNP:rs368438393).
{ECO:0000269|PubMed:15145338,
ECO:0000269|PubMed:18429042,
ECO:0000269|PubMed:9535769}.
/FTId=VAR_004304.
VARIANT 647 647 C -> W (in GSD2; dbSNP:rs776948121).
{ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:7981676,
ECO:0000269|PubMed:9535769}.
/FTId=VAR_004305.
VARIANT 648 648 G -> D (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068624.
VARIANT 648 648 G -> S (in GSD2; dbSNP:rs536906561).
{ECO:0000269|PubMed:9535769}.
/FTId=VAR_004306.
VARIANT 660 660 R -> H (in GSD2; loss of function of the
mutant enzyme; dbSNP:rs374143224).
{ECO:0000269|PubMed:14643388}.
/FTId=VAR_046477.
VARIANT 672 672 R -> Q (in GSD2; dbSNP:rs778418246).
{ECO:0000269|PubMed:9535769}.
/FTId=VAR_004307.
VARIANT 672 672 R -> T (in GSD2).
{ECO:0000269|PubMed:11071489}.
/FTId=VAR_046478.
VARIANT 672 672 R -> W (in GSD2; dbSNP:rs757111744).
{ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:9535769}.
/FTId=VAR_004308.
VARIANT 675 675 Missing (in GSD2; infantile form).
/FTId=VAR_008692.
VARIANT 689 689 E -> K (in allele GAA*4;
dbSNP:rs1800309).
{ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:8912788}.
/FTId=VAR_004309.
VARIANT 700 701 Missing (found in a patient with GSD2;
unknown pathological significance).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068625.
VARIANT 702 702 R -> C (in GSD2; no enzymatic activity;
shows enzyme localization primarily in
the ER-Golgi compartment suggesting that
mutation could affect the normal
processing and stability of the enzyme;
dbSNP:rs786204645).
{ECO:0000269|PubMed:14972326}.
/FTId=VAR_046479.
VARIANT 702 702 R -> L (in GSD2; dbSNP:rs398123172).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068626.
VARIANT 705 705 L -> P (in GSD2; unknown pathological
significance).
{ECO:0000269|PubMed:25681614}.
/FTId=VAR_074279.
VARIANT 711 711 T -> R (in dbSNP:rs759292700).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068627.
VARIANT 718 718 V -> I (in dbSNP:rs141017311).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068628.
VARIANT 725 725 R -> W (in GSD2; adult form;
dbSNP:rs28939100).
{ECO:0000269|PubMed:8401535}.
/FTId=VAR_004310.
VARIANT 737 737 T -> N (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068629.
VARIANT 743 743 Q -> K (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068630.
VARIANT 746 746 W -> C (in dbSNP:rs1800312).
{ECO:0000269|PubMed:16917947,
ECO:0000269|PubMed:20080426}.
/FTId=VAR_004311.
VARIANT 746 746 W -> G (in GSD2).
{ECO:0000269|PubMed:20080426}.
/FTId=VAR_068631.
VARIANT 746 746 W -> S (in GSD2; dbSNP:rs752921215).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068632.
VARIANT 766 766 Y -> C (in GSD2; dbSNP:rs144016984).
{ECO:0000269|PubMed:22676651}.
/FTId=VAR_070019.
VARIANT 768 768 P -> R (in GSD2; infantile form).
{ECO:0000269|PubMed:9521422}.
/FTId=VAR_004312.
VARIANT 780 780 V -> I (in dbSNP:rs1126690).
{ECO:0000269|PubMed:2111708,
ECO:0000269|PubMed:2268276,
ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:3049072,
ECO:0000269|PubMed:7717400,
ECO:0000269|Ref.5}.
/FTId=VAR_004313.
VARIANT 816 816 V -> I (in dbSNP:rs1800314).
{ECO:0000269|PubMed:1684505,
ECO:0000269|PubMed:25681614,
ECO:0000269|PubMed:8094613,
ECO:0000269|PubMed:8486380}.
/FTId=VAR_004314.
VARIANT 819 819 R -> P (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068633.
VARIANT 880 880 A -> D (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:14695532}.
/FTId=VAR_018097.
VARIANT 901 901 L -> Q (in GSD2; infantile form; severe).
{ECO:0000269|PubMed:15145338}.
/FTId=VAR_029039.
VARIANT 903 903 Missing (in GSD2; infantile form; severe;
loss of activity).
{ECO:0000269|PubMed:7717400}.
/FTId=VAR_004315.
VARIANT 913 913 P -> R (in GSD2).
{ECO:0000269|PubMed:22676651}.
/FTId=VAR_070020.
VARIANT 916 916 V -> F (in GSD2).
{ECO:0000269|PubMed:22644586}.
/FTId=VAR_068634.
VARIANT 925 925 N -> NGVPVSN (in GSD2).
{ECO:0000269|PubMed:10206684}.
/FTId=VAR_004316.
VARIANT 927 927 T -> I (loss of glycosylation site;
dbSNP:rs1800315).
{ECO:0000269|PubMed:1684505,
ECO:0000269|PubMed:8094613,
ECO:0000269|PubMed:8486380}.
/FTId=VAR_004317.
VARIANT 935 935 L -> P (in GSD2).
{ECO:0000269|PubMed:18425781}.
/FTId=VAR_068635.
VARIANT 949 949 V -> D (in GSD2).
/FTId=VAR_004318.
MUTAGEN 516 516 W->R: Loss of activity.
{ECO:0000269|PubMed:1856189}.
MUTAGEN 518 518 D->G,N,E: Loss of activity.
{ECO:0000269|PubMed:1856189}.
SEQUENCE 952 AA; 105324 MW; 6E2717BF7201F469 CRC64;
MGVRHPPCSH RLLAVCALVS LATAALLGHI LLHDFLLVPR ELSGSSPVLE ETHPAHQQGA
SRPGPRDAQA HPGRPRAVPT QCDVPPNSRF DCAPDKAITQ EQCEARGCCY IPAKQGLQGA
QMGQPWCFFP PSYPSYKLEN LSSSEMGYTA TLTRTTPTFF PKDILTLRLD VMMETENRLH
FTIKDPANRR YEVPLETPHV HSRAPSPLYS VEFSEEPFGV IVRRQLDGRV LLNTTVAPLF
FADQFLQLST SLPSQYITGL AEHLSPLMLS TSWTRITLWN RDLAPTPGAN LYGSHPFYLA
LEDGGSAHGV FLLNSNAMDV VLQPSPALSW RSTGGILDVY IFLGPEPKSV VQQYLDVVGY
PFMPPYWGLG FHLCRWGYSS TAITRQVVEN MTRAHFPLDV QWNDLDYMDS RRDFTFNKDG
FRDFPAMVQE LHQGGRRYMM IVDPAISSSG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV
WPGSTAFPDF TNPTALAWWE DMVAEFHDQV PFDGMWIDMN EPSNFIRGSE DGCPNNELEN
PPYVPGVVGG TLQAATICAS SHQFLSTHYN LHNLYGLTEA IASHRALVKA RGTRPFVISR
STFAGHGRYA GHWTGDVWSS WEQLASSVPE ILQFNLLGVP LVGADVCGFL GNTSEELCVR
WTQLGAFYPF MRNHNSLLSL PQEPYSFSEP AQQAMRKALT LRYALLPHLY TLFHQAHVAG
ETVARPLFLE FPKDSSTWTV DHQLLWGEAL LITPVLQAGK AEVTGYFPLG TWYDLQTVPV
EALGSLPPPP AAPREPAIHS EGQWVTLPAP LDTINVHLRA GYIIPLQGPG LTTTESRQQP
MALAVALTKG GEARGELFWD DGESLEVLER GAYTQVIFLA RNNTIVNELV RVTSEGAGLQ
LQKVTVLGVA TAPQQVLSNG VPVSNFTYSP DTKVLDICVS LLMGEQFLVS WC


Related products :

Catalog number Product name Quantity
E0177h ELISA Acid maltase,Aglucosidase alfa,GAA,Homo sapiens,Human,Lysosomal alpha-glucosidase 96T
U0177h CLIA Acid maltase,Aglucosidase alfa,GAA,Homo sapiens,Human,Lysosomal alpha-glucosidase 96T
E0177h ELISA kit Acid maltase,Aglucosidase alfa,GAA,Homo sapiens,Human,Lysosomal alpha-glucosidase 96T
E0177m ELISA Acid maltase,Gaa,Lysosomal alpha-glucosidase,Mouse,Mus musculus 96T
E0177m ELISA kit Acid maltase,Gaa,Lysosomal alpha-glucosidase,Mouse,Mus musculus 96T
E0177r ELISA kit Acid maltase,Gaa,Lysosomal alpha-glucosidase,Rat,Rattus norvegicus 96T
U0177m CLIA Acid maltase,Gaa,Lysosomal alpha-glucosidase,Mouse,Mus musculus 96T
E0177b ELISA Acid maltase,Bos taurus,Bovine,GAA,Lysosomal alpha-glucosidase 96T
U0177r CLIA Acid maltase,Gaa,Lysosomal alpha-glucosidase,Rat,Rattus norvegicus 96T
E0177b ELISA kit Acid maltase,Bos taurus,Bovine,GAA,Lysosomal alpha-glucosidase 96T
E0177r ELISA Acid maltase,Gaa,Lysosomal alpha-glucosidase,Rat,Rattus norvegicus 96T
U0177b CLIA Acid maltase,Bos taurus,Bovine,GAA,Lysosomal alpha-glucosidase 96T
EH747 Lysosomal alpha-glucosidase Elisa Kit 96T
EM343 Lysosomal alpha-glucosidase Elisa Kit 96T
ER245 Lysosomal alpha-glucosidase Elisa Kit 96T
CSB-EL009125BO Bovine Lysosomal alpha-glucosidase(GAA) ELISA kit 96T
CSB-EL009125HU Human Lysosomal alpha-glucosidase(GAA) ELISA kit 96T
gen4212 LYAG_RAT Lysosomal alpha-glucosidase ELISA tesk kit 1
gen4209 LYAG_MOUSE Lysosomal alpha-glucosidase ELISA tesk kit 1
CSB-EL009125BO Bovine Lysosomal alpha-glucosidase(GAA) ELISA kit SpeciesBovine 96T
gen4206 LYAG_HUMAN Lysosomal alpha-glucosidase ELISA tesk kit 1
gen4202 LYAG_BOVIN Lysosomal alpha-glucosidase ELISA tesk kit 1
CSB-EL009125HU Human Lysosomal alpha-glucosidase(GAA) ELISA kit SpeciesHuman 96T
E0177m ELISA Kit FOR Lysosomal alpha-glucosidase; organism: Mouse; gene name: Gaa 96T
18-272-195667 alpha Glucosidase II - Rabbit polyclonal to alpha Glucosidase II; EC 3.2.1.84; Glucosidase II subunit alpha Polyclonal 0.05 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur