P10253 (LYAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysosomal alpha-glucosidase
EC=3.2.1.20

Alternative name(s):
Acid maltase
Aglucosidase alfa

Cleaved into the following 2 chains:

1. 76 kDa lysosomal alpha-glucosidase
2. 70 kDa lysosomal alpha-glucosidase

Gene names

Name:

GAA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	952 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Lysosome membrane Ref.14.
Post-translational modification	The different forms of acid glucosidase are obtained by proteolytic processing. 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.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.8 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56
Sequence similarities	Belongs to the glycosyl hydrolase 31 family. Contains 1 P-type (trefoil) domain.

Ontologies

Keywords
Cellular component	Lysosome Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Glycogen storage disease
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle contraction Inferred from mutant phenotype PubMed 10931430. Source: BHF-UCL diaphragm contraction Inferred from mutant phenotype Ref.48. Source: BHF-UCL glucose metabolic process Inferred by curator PubMed 9505277. Source: BHF-UCL glycogen catabolic process Inferred from direct assay PubMed 9505277. Source: BHF-UCL locomotory behavior Inferred from electronic annotation. Source: Compara lysosome organization Inferred from mutant phenotype Ref.27. Source: BHF-UCL maltose metabolic process Inferred by curator PubMed 9505277. Source: BHF-UCL muscle cell homeostasis Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara neuromuscular process controlling posture Inferred from electronic annotation. Source: Compara regulation of the force of heart contraction Inferred from electronic annotation. Source: Compara sucrose metabolic process Inferred by curator PubMed 9505277. Source: BHF-UCL tongue morphogenesis Inferred from mutant phenotype PubMed 10931430. Source: BHF-UCL vacuolar sequestering Inferred from mutant phenotype PubMed 10931430. Source: BHF-UCL ventricular cardiac muscle tissue morphogenesis Inferred from mutant phenotype PubMed 10931430. Source: BHF-UCL
Cellular_component	lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 9505277. Source: BHF-UCL
Molecular_function	alpha-glucosidase activity Inferred from direct assay PubMed 9505277. Source: BHF-UCL carbohydrate binding Inferred from electronic annotation. Source: InterPro maltose alpha-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Propeptide	28 – 69	42			PRO_0000018565
	Chain	70 – 952	883	Lysosomal alpha-glucosidase		PRO_0000018566
	Chain	123 – 952	830	76 kDa lysosomal alpha-glucosidase		PRO_0000018567
	Chain	204 – 952	749	70 kDa lysosomal alpha-glucosidase		PRO_0000018568
Regions
	Domain	80 – 131	52	P-type
Sites
	Active site	518	1	Nucleophile Ref.9
	Active site	521	1	By similarity
Amino acid modifications
	Glycosylation	140	1	N-linked (GlcNAc...) Ref.10 Ref.15
	Glycosylation	233	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	390	1	N-linked (GlcNAc...) Ref.10 Ref.13
	Glycosylation	470	1	N-linked (GlcNAc...) Ref.10 Ref.11 Ref.15
	Glycosylation	652	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	882	1	N-linked (GlcNAc...) Ref.10 Ref.15
	Glycosylation	925	1	N-linked (GlcNAc...) Ref.10 Ref.15
	Disulfide bond	82 ↔ 109		By similarity
	Disulfide bond	92 ↔ 108		By similarity
	Disulfide bond	103 ↔ 127		By similarity
Natural variations
	Natural variant	46	1	S → P in GSD2. Ref.52		VAR_068564
	Natural variant	74	1	R → H. Ref.56		VAR_068565
	Natural variant	89	1	R → H. Ref.56		VAR_068566
	Natural variant	91	1	D → N in allele GAA*2; lower affinity for glycogen and starch but not for lower-molecular weight substrates. Ref.17 Ref.32 Ref.55 Corresponds to variant rs1800299 [ dbSNP | Ensembl ].		VAR_004285
	Natural variant	103	1	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. Ref.42 Ref.51 Ref.55		VAR_018078
	Natural variant	103	1	C → R in GSD2. Ref.56		VAR_068567
	Natural variant	108	1	C → G in GSD2. Ref.56		VAR_068568
	Natural variant	127	1	C → F in GSD2. Ref.56		VAR_068569
	Natural variant	190	1	R → H in GSD2. Ref.50		VAR_068570
	Natural variant	191	1	Y → C in GSD2; extremely low residual enzymatic activity. Ref.51		VAR_046467
	Natural variant	199	1	H → R. Ref.1 Ref.5 Ref.27 Ref.32 Corresponds to variant rs1042393 [ dbSNP | Ensembl ].		VAR_004286
	Natural variant	208	1	L → P in GSD2. Ref.37		VAR_029025
	Natural variant	217	1	P → L in GSD2. Ref.52		VAR_068571
	Natural variant	219	1	G → R in GSD2; infantile form; severe; loss of activity. Ref.38 Ref.42 Ref.51		VAR_018079
	Natural variant	220	1	V → L. Ref.56		VAR_068572
	Natural variant	222	1	V → M. Ref.56		VAR_068573
	Natural variant	223	1	R → H. Ref.1 Ref.5 Ref.27 Ref.32 Corresponds to variant rs1042395 [ dbSNP | Ensembl ].		VAR_004287
	Natural variant	224	1	R → P in GSD2. Ref.54		VAR_068574
	Natural variant	224	1	R → Q in GSD2. Ref.56		VAR_068575
	Natural variant	224	1	R → W in GSD2; infantile; mild partial loss of activity. Ref.39 Ref.41 Ref.51		VAR_029026
	Natural variant	234	1	T → K in GSD2. Ref.56		VAR_068576
	Natural variant	234	1	T → R in GSD2. Ref.56		VAR_068577
	Natural variant	237	1	A → V in GSD2. Ref.45		VAR_029027
	Natural variant	251	1	S → L in GSD2. Ref.54		VAR_068578
	Natural variant	254	1	S → L in GSD2. Ref.54		VAR_068579
	Natural variant	262	1	E → K in GSD2; infantile; severe. Ref.38 Ref.51 Ref.54		VAR_029028
	Natural variant	266	1	P → S in GSD2. Ref.54		VAR_068580
	Natural variant	271	1	T → A. Ref.54		VAR_068581
	Natural variant	285	1	P → R in GSD2; juvenile form; mild; partial loss of activity. Ref.42		VAR_018080
	Natural variant	285	1	P → S in GSD2. Ref.50		VAR_068582
	Natural variant	290	1	N → D. Ref.56		VAR_068583
	Natural variant	291	1	L → F in GSD2. Ref.50		VAR_068584
	Natural variant	291	1	L → P in GSD2. Ref.50 Ref.54		VAR_068585
	Natural variant	292	1	Y → C in GSD2; juvenile form; mild; partial loss of activity. Ref.42		VAR_018081
	Natural variant	293	1	G → R in GSD2; infantile form; severe; almost complete loss of activity. Ref.42 Ref.45 Ref.51		VAR_018082
	Natural variant	299	1	L → R in GSD2; infantile form. Ref.27		VAR_004288
	Natural variant	308	1	H → L in GSD2. Ref.37		VAR_046468
	Natural variant	308	1	H → P in GSD2; infantile form; severe; complete loss of activity. Ref.42		VAR_018083
	Natural variant	309	1	G → R in GSD2; severe. Ref.31 Ref.48		VAR_018084
	Natural variant	310	1	V → G Found in a patient with GSD2; unknown pathological significance. Ref.56		VAR_068586
	Natural variant	312	1	L → R in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018085
	Natural variant	316	1	N → I in GSD2. Ref.56		VAR_068587
	Natural variant	318	1	M → K in GSD2. Ref.50		VAR_068588
	Natural variant	318	1	M → T in GSD2; severe. Ref.18		VAR_004289
	Natural variant	324	1	P → L in GSD2. Ref.37		VAR_029029
	Natural variant	330	1	W → G in GSD2; infantile form; severe. Ref.46		VAR_029030
	Natural variant	335	1	G → E in GSD2. Ref.56		VAR_068589
	Natural variant	335	1	G → R in GSD2. Ref.50		VAR_068590
	Natural variant	347	1	P → R in GSD2. Ref.50		VAR_068591
	Natural variant	355	1	L → P in GSD2; infantile form; severe; loss of activity. Ref.42 Ref.43 Ref.48 Ref.49 Ref.51		VAR_018086
	Natural variant	359	1	G → R. Ref.49		VAR_068592
	Natural variant	361	1	P → L in GSD2; juvenile form; severe. Ref.40 Ref.48 Ref.56		VAR_029031
	Natural variant	374	1	C → R in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018087
	Natural variant	375	1	R → L in GSD2; extremely low residual enzymatic activity. Ref.51		VAR_046469
	Natural variant	377	1	G → R in GSD2; severe.		VAR_029032
	Natural variant	391	1	M → V Found in a patient with GSD2; unknown pathological significance. Ref.56		VAR_068593
	Natural variant	397	1	P → L in GSD2. Ref.56		VAR_068594
	Natural variant	401	1	Q → R in GSD2; extremely low residual enzymatic activity. Ref.51		VAR_046470
	Natural variant	402	1	W → R in GSD2; severe.		VAR_004290
	Natural variant	404	1	D → N in GSD2; severe. Ref.47		VAR_029033
	Natural variant	405	1	L → P in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018088
	Natural variant	408	1	M → V in GSD2; juvenile form; severe. Ref.38 Ref.54		VAR_029034
	Natural variant	419	1	D → V in GSD2. Ref.56		VAR_068595
	Natural variant	437	1	R → C in GSD2; juvenile form; severe. Ref.40		VAR_029035
	Natural variant	445	1	A → P in GSD2. Ref.48		VAR_029036
	Natural variant	455	1	Y → F in GSD2; juvenile form; almost complete loss of activity. Ref.42		VAR_018089
	Natural variant	457	1	P → H in GSD2. Ref.56		VAR_068596
	Natural variant	457	1	P → L in GSD2; juvenile form. Ref.5		VAR_029040
	Natural variant	458	1	Y → C. Ref.56		VAR_068597
	Natural variant	459	1	Missing in GSD2; infantile form; severe. Ref.42		VAR_018090
	Natural variant	478	1	G → R in GSD2; severe; loss of activity. Ref.42 Ref.54		VAR_004291
	Natural variant	481	1	W → R in GSD2; severe; loss of activity. Ref.35 Ref.42		VAR_004292
	Natural variant	482	1	P → R in GSD2. Ref.50		VAR_068598
	Natural variant	483	1	G → V in GSD2. Ref.50		VAR_068599
	Natural variant	486	1	A → P in GSD2. Ref.52		VAR_068600
	Natural variant	489	1	D → N in GSD2; severe. Ref.48 Ref.51		VAR_029037
	Natural variant	519	1	M → T in GSD2; severe; loss of activity. Ref.42		VAR_004293
	Natural variant	519	1	M → V in GSD2. Ref.24		VAR_004294
	Natural variant	521	1	E → K in GSD2; severe. Ref.19		VAR_004295
	Natural variant	521	1	E → Q in GSD2. Ref.50		VAR_068601
	Natural variant	522	1	P → A in GSD2; no residual enzymatic activity. Ref.49 Ref.51		VAR_046471
	Natural variant	522	1	P → S in GSD2. Ref.50		VAR_068602
	Natural variant	523	1	S → Y in GSD2. Ref.56		VAR_068603
	Natural variant	525	1	F → Y in GSD2. Ref.54		VAR_068604
	Natural variant	529	1	S → V in GSD2; mild; requires 2 nucleotide substitutions. Ref.29		VAR_004296
	Natural variant	545	1	P → L in GSD2; mild; partial loss of activity. Ref.26 Ref.34 Ref.42 Ref.54		VAR_004297
	Natural variant	549	1	G → R in GSD2; juvenile form; mild; partial loss of activity. Ref.42 Ref.48		VAR_018091
	Natural variant	552	1	L → P in GSD2; infantile/juvenile form; severe; loss of activity. Ref.42 Ref.51		VAR_018092
	Natural variant	557	1	I → F in GSD2. Ref.54		VAR_068605
	Natural variant	558	1	C → S in GSD2. Ref.53 Ref.56		VAR_068606
	Natural variant	566	1	S → P in GSD2; infantile form. Ref.32		VAR_004298
	Natural variant	570	1	N → K in GSD2. Ref.50		VAR_068607
	Natural variant	572	1	H → Q in GSD2. Ref.50		VAR_068608
	Natural variant	575	1	Y → C in GSD2. Ref.56		VAR_068609
	Natural variant	575	1	Y → S in GSD2; juvenile form. Ref.42		VAR_018093
	Natural variant	576	1	G → A.		VAR_004299
	Natural variant	576	1	G → R in GSD2. Ref.56		VAR_068610
	Natural variant	576	1	G → S Retains about half of the activity compared with the wild-type. Ref.41 Corresponds to variant rs1800307 [ dbSNP | Ensembl ].		VAR_004300
	Natural variant	579	1	E → K in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018094
	Natural variant	585	1	R → K. Ref.50		VAR_068611
	Natural variant	585	1	R → M in GSD2. Ref.37		VAR_046472
	Natural variant	594	1	R → H in GSD2. Ref.56		VAR_068612
	Natural variant	594	1	R → P in GSD2. Ref.50 Ref.52		VAR_068613
	Natural variant	599	1	S → Y in GSD2; no residual enzymatic activity. Ref.51		VAR_046473
	Natural variant	600	1	R → C in GSD2; juvenile form; loss of activity. Ref.41 Ref.42		VAR_018095
	Natural variant	600	1	R → H in GSD2; infantile form.		VAR_008689
	Natural variant	601	1	S → L in GSD2. Ref.56		VAR_068614
	Natural variant	602	1	T → A in GSD2. Ref.56		VAR_068615
	Natural variant	607 – 612	6	Missing in GSD2.		VAR_046474
	Natural variant	607	1	G → D in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018096
	Natural variant	610	1	A → V in GSD2. Ref.49		VAR_068616
	Natural variant	611	1	G → D Found in a patient with GSD2; unknown pathological significance. Ref.56		VAR_068617
	Natural variant	612	1	H → Q in GSD2. Ref.48		VAR_029038
	Natural variant	612	1	H → Y in GSD2. Ref.52		VAR_068618
	Natural variant	614	1	T → K in GSD2. Ref.50		VAR_068619
	Natural variant	615	1	G → R in GSD2; infantile/adult form. Ref.54		VAR_008690
	Natural variant	619	1	S → R in GSD2; loss of function of the mutant enzyme. Ref.41		VAR_046475
	Natural variant	627	1	S → P in GSD2. Ref.56		VAR_068620
	Natural variant	629	1	P → L. Ref.56		VAR_068621
	Natural variant	635	1	N → K in GSD2. Ref.52		VAR_068622
	Natural variant	638	1	G → V in GSD2. Ref.52		VAR_068623
	Natural variant	638	1	G → W in GSD2. Ref.34 Ref.51		VAR_046476
	Natural variant	643	1	G → R in GSD2; infantile form. Ref.20 Ref.32 Ref.37 Ref.48 Ref.51 Corresponds to variant rs28937909 [ dbSNP | Ensembl ].		VAR_004301
	Natural variant	645	1	D → E in GSD2; infantile form; most common mutation; deficient in phosphorylation and in proteolytic processing. Ref.21 Ref.22 Ref.54 Corresponds to variant rs28940868 [ dbSNP | Ensembl ].		VAR_004302
	Natural variant	645	1	D → H in GSD2; almost complete loss of activity. Ref.8		VAR_004303
	Natural variant	645	1	D → N in GSD2. Ref.30 Ref.44 Ref.51		VAR_004304
	Natural variant	647	1	C → W in GSD2. Ref.25 Ref.30		VAR_004305
	Natural variant	648	1	G → D in GSD2. Ref.56		VAR_068624
	Natural variant	648	1	G → S in GSD2. Ref.30		VAR_004306
	Natural variant	660	1	R → H in GSD2; loss of function of the mutant enzyme. Ref.41		VAR_046477
	Natural variant	672	1	R → Q in GSD2. Ref.30		VAR_004307
	Natural variant	672	1	R → T in GSD2. Ref.37		VAR_046478
	Natural variant	672	1	R → W in GSD2. Ref.30 Ref.48		VAR_004308
	Natural variant	675	1	Missing in GSD2; infantile form.		VAR_008692
	Natural variant	689	1	E → K in allele GAA*4. Ref.28 Corresponds to variant rs1800309 [ dbSNP | Ensembl ].		VAR_004309
	Natural variant	700 – 701	2	Missing Found in a patient with GSD2; unknown pathological significance.		VAR_068625
	Natural variant	702	1	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. Ref.43		VAR_046479
	Natural variant	702	1	R → L in GSD2. Ref.56		VAR_068626
	Natural variant	711	1	T → R. Ref.54		VAR_068627
	Natural variant	718	1	V → I. Ref.56		VAR_068628
	Natural variant	725	1	R → W in GSD2; adult form. Ref.20 Corresponds to variant rs28939100 [ dbSNP | Ensembl ].		VAR_004310
	Natural variant	737	1	T → N in GSD2. Ref.50		VAR_068629
	Natural variant	743	1	Q → K in GSD2. Ref.56		VAR_068630
	Natural variant	746	1	W → C. Ref.48 Ref.54 Corresponds to variant rs1800312 [ dbSNP | Ensembl ].		VAR_004311
	Natural variant	746	1	W → G in GSD2. Ref.54		VAR_068631
	Natural variant	746	1	W → S in GSD2. Ref.50		VAR_068632
	Natural variant	768	1	P → R in GSD2; infantile form. Ref.32		VAR_004312
	Natural variant	780	1	V → I. Ref.1 Ref.3 Ref.4 Ref.5 Ref.27 Corresponds to variant rs1126690 [ dbSNP | Ensembl ].		VAR_004313
	Natural variant	816	1	V → I. Ref.21 Ref.22 Ref.23 Corresponds to variant rs1800314 [ dbSNP | Ensembl ].		VAR_004314
	Natural variant	819	1	R → P in GSD2. Ref.56		VAR_068633
	Natural variant	880	1	A → D in GSD2; infantile form; severe; loss of activity. Ref.42		VAR_018097
	Natural variant	901	1	L → Q in GSD2; infantile form; severe. Ref.44		VAR_029039
	Natural variant	903	1	Missing in GSD2; infantile form; severe; loss of activity. Ref.27		VAR_004315
	Natural variant	916	1	V → F in GSD2. Ref.56		VAR_068634
	Natural variant	925	1	N → NGVPVSN in GSD2.		VAR_004316
	Natural variant	927	1	T → I Loss of glycosylation site. Ref.21 Ref.22 Ref.23 Corresponds to variant rs1800315 [ dbSNP | Ensembl ].		VAR_004317
	Natural variant	935	1	L → P in GSD2. Ref.50		VAR_068635
	Natural variant	949	1	V → D in GSD2.		VAR_004318
Experimental info
	Mutagenesis	516	1	W → R: Loss of activity. Ref.9
	Mutagenesis	518	1	D → G, N or E: Loss of activity. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P10253 [UniParc]. Last modified January 11, 2011. Version 4. Checksum: 6E2717BF7201F469	FASTA	952	105,324
	10 20 30 40 50 60 MGVRHPPCSH RLLAVCALVS LATAALLGHI LLHDFLLVPR ELSGSSPVLE ETHPAHQQGA 70 80 90 100 110 120 SRPGPRDAQA HPGRPRAVPT QCDVPPNSRF DCAPDKAITQ EQCEARGCCY IPAKQGLQGA 130 140 150 160 170 180 QMGQPWCFFP PSYPSYKLEN LSSSEMGYTA TLTRTTPTFF PKDILTLRLD VMMETENRLH 190 200 210 220 230 240 FTIKDPANRR YEVPLETPHV HSRAPSPLYS VEFSEEPFGV IVRRQLDGRV LLNTTVAPLF 250 260 270 280 290 300 FADQFLQLST SLPSQYITGL AEHLSPLMLS TSWTRITLWN RDLAPTPGAN LYGSHPFYLA 310 320 330 340 350 360 LEDGGSAHGV FLLNSNAMDV VLQPSPALSW RSTGGILDVY IFLGPEPKSV VQQYLDVVGY 370 380 390 400 410 420 PFMPPYWGLG FHLCRWGYSS TAITRQVVEN MTRAHFPLDV QWNDLDYMDS RRDFTFNKDG 430 440 450 460 470 480 FRDFPAMVQE LHQGGRRYMM IVDPAISSSG PAGSYRPYDE GLRRGVFITN ETGQPLIGKV 490 500 510 520 530 540 WPGSTAFPDF TNPTALAWWE DMVAEFHDQV PFDGMWIDMN EPSNFIRGSE DGCPNNELEN 550 560 570 580 590 600 PPYVPGVVGG TLQAATICAS SHQFLSTHYN LHNLYGLTEA IASHRALVKA RGTRPFVISR 610 620 630 640 650 660 STFAGHGRYA GHWTGDVWSS WEQLASSVPE ILQFNLLGVP LVGADVCGFL GNTSEELCVR 670 680 690 700 710 720 WTQLGAFYPF MRNHNSLLSL PQEPYSFSEP AQQAMRKALT LRYALLPHLY TLFHQAHVAG 730 740 750 760 770 780 ETVARPLFLE FPKDSSTWTV DHQLLWGEAL LITPVLQAGK AEVTGYFPLG TWYDLQTVPV 790 800 810 820 830 840 EALGSLPPPP AAPREPAIHS EGQWVTLPAP LDTINVHLRA GYIIPLQGPG LTTTESRQQP 850 860 870 880 890 900 MALAVALTKG GEARGELFWD DGESLEVLER GAYTQVIFLA RNNTIVNELV RVTSEGAGLQ 910 920 930 940 950 LQKVTVLGVA TAPQQVLSNG VPVSNFTYSP DTKVLDICVS LLMGEQFLVS WC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrase-isomaltase complex." Hoefsloot L.H., Hoogeveen-Westerveld M., Kroos M.A., van Beeumen J., Reuser A.J.J., Oostra B.A. EMBO J. 7:1697-1704(1988) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANTS ARG-199; HIS-223 AND ILE-780. Tissue: Placenta, Testis and Urine.
[2]	Reuser A.J.J. Submitted (JUN-1990) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Characterization of the human lysosomal alpha-glucosidase gene." Hoefsloot L.H., Hoogeveen-Westerveld M., Reuser A.J.J., Oostra B.A. Biochem. J. 272:493-497(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-780.
[4]	"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." Martiniuk F., Mehler M., Tzall S., Meredith G., Hirschhorn R. DNA Cell Biol. 9:85-94(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-780.
[5]	"Identification of a novel mutation in the acid alpha glucosidase gene causing juvenile form of Pompe disease in Iranian population." Ghaffari S.R., Sabokbar T., Tahmasebi S., Dastan J. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GSD2 LEU-457, VARIANTS ARG-199; HIS-223 AND ILE-780.
[6]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." 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. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum.
[8]	"Identification of a de novo point mutation resulting in infantile form of Pompe's disease." Lin C.-Y., Shieh J.-J. Biochem. Biophys. Res. Commun. 208:886-893(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 631-680, VARIANT GSD2 HIS-645.
[9]	"Human lysosomal alpha-glucosidase. Characterization of the catalytic site." Hermans M.M.P., Kroos M.A., van Beeumen J., Oostra B.A., Reuser A.J.J. J. Biol. Chem. 266:13507-13512(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TRP-516 AND ASP-518, ACTIVE SITE.
[10]	"Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites." Hermans M.M.P., Wisselaar H.A., Kroos M.A., Oostra B.A., Reuser A.J.J. Biochem. J. 289:681-686(1993) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-140; ASN-233; ASN-390; ASN-470; ASN-652; ASN-882 AND ASN-925.
[11]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-470.
[12]	"Glycogenosis type II (acid maltase deficiency)." 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. Muscle Nerve 3:S61-S69(1995) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[13]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-390, MASS SPECTROMETRY. Tissue: Plasma.
[14]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[15]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-470; ASN-882 AND ASN-925, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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." Martiniuk F., Bodkin M., Tzall S., Hirschhorn R. Am. J. Hum. Genet. 47:440-445(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASN-91.
[18]	"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." Zhong N., Martiniuk F., Tzall S., Hirschhorn R. Am. J. Hum. Genet. 49:635-645(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 THR-318.
[19]	"Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II." Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A., Oostra B.A., Reuser A.J.J. Biochem. Biophys. Res. Commun. 179:919-926(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 LYS-521.
[20]	"Two mutations affecting the transport and maturation of lysosomal alpha-glucosidase in an adult case of glycogen storage disease type II." Hermans M.M.P., Kroos M.A., de Graaff E., Oostra B.A., Reuser A.J.J. Hum. Mutat. 2:268-273(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 ARG-643 AND TRP-725.
[21]	"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." Hermans M.M.P., de Graaff E., Kroos M.A., Wisselaar H.A., Willemsen R., Oostra B.A., Reuser A.J.J. Biochem. J. 289:687-693(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLU-645, VARIANTS ILE-816 AND ILE-927.
[22]	"Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele." Martiniuk F., Mehler M., Bodkin M., Tzall S., Hirschhorn K., Zhong N., Hirschhorn R. DNA Cell Biol. 10:681-687(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLU-645, VARIANTS ILE-816 AND ILE-927.
[23]	"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." Hermans M.M.P., Svetkey L.P., Oostra B.A., Chen Y.T., Reuser A.J.J. Genomics 16:300-301(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ILE-816 AND ILE-927.
[24]	"Mutation at the catalytic site (M519V) in glycogen storage disease type II (Pompe disease)." Huie M.L., Hirschhorn R., Chen A.S., Martiniuk F., Zhong N. Hum. Mutat. 4:291-293(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 VAL-519.
[25]	"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)." Huie M.L., Chen A.S., Brooks S.S., Grix A., Hirschhorn R. Hum. Mol. Genet. 3:1081-1087(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 TRP-647.
[26]	"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." 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. Hum. Mol. Genet. 3:2213-2218(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 LEU-545.
[27]	"Leaky splicing mutation in the acid maltase gene is associated with delayed onset of glycogenosis type II." Boerkoel C.F., Exelbert R., Nicastri C., Nichols R.C., Miller F.W., Plotz P.H., Raben N. Am. J. Hum. Genet. 56:887-897(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 ARG-299 AND LYS-903 DEL, VARIANTS ARG-199; HIS-223 AND ILE-780.
[28]	"Identification of an E689K substitution as the molecular basis of the human acid alpha-glucosidase type 4 allozyme (GAA*4)." Huie M.L., Menaker M., McAlpine P.J., Hirschhorn R. Ann. Hum. Genet. 60:365-368(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LYS-689.
[29]	"Acid alpha-glucosidase deficiency: identification and expression of a missense mutation (S529V) in a Japanese adult phenotype." Tsunoda H., Ohshima T., Tohyama J., Sasaki M., Sakuragawa N., Martiniuk F. Hum. Genet. 97:496-499(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 VAL-529.
[30]	"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." 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. Biochem. Biophys. Res. Commun. 244:921-927(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 ASN-645; TRP-647; SER-648; GLN-672 AND TRP-672.
[31]	"Glycogen storage disease type II: identification of a dinucleotide deletion and a common missense mutation in the lysosomal alpha-glucosidase gene." Kroos M.A., van Leenen D., Verbiest J., Reuser A.J.J., Hermans M.M.P. Clin. Genet. 53:379-382(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 ARG-309.
[32]	"Glycogen storage disease type II: genetic and biochemical analysis of novel mutations in infantile patients from Turkish ancestry." Hermans M.M.P., Kroos M.A., Smeitink J.A.M., van der Ploeg A.T., Kleijer W.J., Reuser A.J.J. Hum. Mutat. 11:209-215(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 PRO-566; ARG-643 AND ARG-768, VARIANTS ASN-91; ARG-199 AND HIS-223.
[33]	"The identification of five novel mutations in the lysosomal acid alpha-(1,4) glucosidase gene from patients with glycogen storage disease type II." Beesley C.E., Child A.H., Yacoub M.Y. Hum. Mutat. 11:413-413(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLY-VAL-PRO-VAL-SER-ASN-925 INS.
[34]	"Adult-onset glycogen storage disease type II: phenotypic and allelic heterogeneity in German patients." Vorgerd M., Burwinkel B., Reichmann H., Malin J.-P., Kilimann M.W. Neurogenetics 1:205-211(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 LEU-545 AND TRP-638.
[35]	"Novel mutations in African American patients with glycogen storage disease Type II." Raben N., Lee E., Lee L., Hirschhorn R., Plotz P.H. Hum. Mutat. 13:83-84(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 ARG-481.
[36]	"Molecular genetic study of Pompe disease in Chinese patients in Taiwan." Ko T.-M., Hwu W.-L., Lin Y.-W., Tseng L.-H., Hwa H.-L., Wang T.-R., Chuang S.-M. Hum. Mutat. 13:380-384(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2, VARIANTS.
[37]	"Juvenile and adult-onset acid maltase deficiency in France: genotype-phenotype correlation." Laforet P., Nicolino M., Eymard P.B., Puech J.P., Caillaud C., Poenaru L., Fardeau M. Neurology 55:1122-1128(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 PRO-208; LEU-308; LEU-324; MET-585; 607-GLY--HIS-612 DEL; ARG-643 AND THR-672.
[38]	"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)." Fernandez-Hojas R., Huie M.L., Navarro C., Dominguez C., Roig M., Lopez-Coronas D., Teijeira S., Anyane-Yeboa K., Hirschhorn R. Neuromuscul. Disord. 12:159-166(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 ARG-219; LYS-262 AND VAL-408.
[39]	"Identification of four novel mutations in the alpha glucosidase gene in five Italian patients with infantile onset glycogen storage disease type II." Pittis M.G., Montalvo A.L., Miocic S., Martini C., Deganuto M., Candusso M., Ciana G., Bembi B. Am. J. Med. Genet. A 121:225-230(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 TRP-224, CHARACTERIZATION OF VARIANT GSD2 TRP-224.
[40]	"Juvenile-onset glycogen storage disease type II with novel mutations in acid alpha-glucosidase gene." 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. Neurology 60:715-717(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 LEU-361 AND CYS-437.
[41]	"New GAA mutations in Japanese patients with GSDII (Pompe disease)." Pipo J.R., Feng J.-H., Yamamoto T., Ohsaki Y., Nanba E., Tsujino S., Sakuragawa N., Martiniuk F., Ninomiya H., Oka A., Ohno K. Pediatr. Neurol. 29:284-287(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 TRP-224; CYS-600; ARG-619 AND HIS-660, CHARACTERIZATION OF VARIANTS GSD2 TRP-224; ARG-619 AND HIS-660, CHARACTERIZATION OF VARIANT SER-576.
[42]	"Twenty-two novel mutations in the lysosomal alpha-glucosidase gene (GAA) underscore the genotype-phenotype correlation in glycogen storage disease type II." 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. Hum. Mutat. 23:47-56(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 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, CHARACTERIZATION OF VARIANTS.
[43]	"Glycogenosis type II: identification and expression of three novel mutations in the acid alpha-glucosidase gene causing the infantile form of the disease." Montalvo A.L.E., Cariati R., Deganuto M., Guerci V., Garcia R., Ciana G., Bembi B., Pittis M.G. Mol. Genet. Metab. 81:203-208(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 PRO-355 AND CYS-702, CHARACTERIZATION OF VARIANTS GSD2 PRO-355 AND CYS-702.
[44]	"A case of childhood Pompe disease demonstrating phenotypic variability of p.Asp645Asn." Kroos M.A., Kirschner J., Gellerich F.N., Hermans M.M., Van der Ploeg A.T., Reuser A.J., Korinthenberg R. Neuromuscul. Disord. 14:371-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLN-901, VARIANT ASN-645.
[45]	"Mutations in the acid alpha-glucosidase gene (M. Pompe) in a patient with an unusual phenotype." Anneser J.M., Pongratz D.E., Podskarbi T., Shin Y.S., Schoser B.G. Neurology 64:368-370(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 VAL-237 AND ARG-293.
[46]	"A novel missense mutation in the acid alpha-glucosidase gene causing the classic infantile form of Pompe disease." Dou W., Gu X., Fu L., Peng C., Zheng J., Martiniuk F., Sheng H.Z. Clin. Chim. Acta 374:145-146(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLY-330.
[47]	"Two clinical forms of glycogen-storage disease type II in two generations of the same family." Amartino H., Painceira D., Pomponio R.J., Niizawa G., Sabio Paz V., Blanco M., Chamoles N. Clin. Genet. 69:187-188(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLY-ASN-404.
[48]	"Mutation profile of the GAA gene in 40 Italian patients with late onset glycogen storage disease type II." 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. Hum. Mutat. 27:999-1006(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 ARG-309; PRO-355; LEU-361; PRO-445; ASN-489; ARG-549; GLN-612; ARG-643; TRP-672 AND CYS-746.
[49]	"Late onset Pompe disease: clinical and neurophysiological spectrum of 38 patients including long-term follow-up in 18 patients." 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. Neuromuscul. Disord. 17:698-706(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 PRO-355; ALA-522 AND VAL-610, VARIANT ARG-359.
[50]	"Update of the Pompe disease mutation database with 107 sequence variants and a format for severity rating." Kroos M., Pomponio R.J., van Vliet L., Palmer R.E., Phipps M., Van der Helm R., Halley D., Reuser A. Hum. Mutat. 29:E13-E26(2008) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT LYS-585.
[51]	"Molecular and functional characterization of eight novel GAA mutations in Italian infants with Pompe disease." 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. Hum. Mutat. 29:E27-E36(2008) [PubMed] [Europe PMC] [Abstract] Cited for: 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, CHARACTERIZATION OF VARIANTS GSD2 CYS-191; LEU-375; ARG-401; ALA-522 AND TYR-599.
[52]	"Pompe disease in a Brazilian series: clinical and molecular analyses with identification of nine new mutations." 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. J. Neurol. 256:1881-1890(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GSD2 PRO-46; LEU-217; PRO-486; PRO-594; TYR-612; LYS-635 AND VAL-638.
[53]	"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." 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. J. Child Neurol. 25:1034-1037(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 SER-558.
[54]	"Genetic heterozygosity and pseudodeficiency in the Pompe disease newborn screening pilot program." Labrousse P., Chien Y.H., Pomponio R.J., Keutzer J., Lee N.C., Akmaev V.R., Scholl T., Hwu W.L. Mol. Genet. Metab. 99:379-383(2010) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANTS ALA-271 AND ARG-711.
[55]	"Late form of Pompe disease with glycogen storage in peripheral nerves axons." Fidzianska A., Lugowska A., Tylki-Szymanska A. J. Neurol. Sci. 301:59-62(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GSD2 GLY-103, VARIANT ASN-91.
[56]	"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." 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. Hum. Mutat. 33:1161-1165(2012) [PubMed] [Europe PMC] [Abstract] Cited for: 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, 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.
+	Additional computationally mapped references.

Web resources

GAA

Mutations in alpha-glucosidase

GeneReviews

Wikipedia

Alpha-glucosidase entry

Glucosidase, alpha, acid (Pompe disease) (GAA)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y00839 mRNA. Translation: CAA68763.1. Y00839 mRNA. Translation: CAA68764.1. X55080 , X55081, X55095, X55082, X55084, X55083, X55098, X55085, X55086, X55087, X55088, X55089, X55090, X55096, X55091, X55092, X55093, X55094, X55097 Genomic DNA. Translation: CAC12967.1. M34424 mRNA. Translation: AAA52506.1. DQ907243 mRNA. Translation: ABI53718.1. AC087741 Genomic DNA. No translation available. BC040431 mRNA. Translation: AAH40431.1. S76893 mRNA. Translation: AAB33842.1.
IPI	IPI00293088.
PIR	A32609. A40577.
RefSeq	NP_000143.2. NM_000152.3. NP_001073271.1. NM_001079803.1. NP_001073272.1. NM_001079804.1.
UniGene	Hs.1437.
3D structure databases
ProteinModelPortal	P10253.
SMR	P10253. Positions 89-951.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10253. 6 interactions.
STRING	9606.ENSP00000305692.
Protein family/group databases
Allergome	9614. Hom s Glucosidase.
CAZy	GH31. Glycoside Hydrolase Family 31.
PTM databases
PhosphoSite	P10253.
Polymorphism databases
DMDM	251757460.
Proteomic databases
PaxDb	P10253.
PRIDE	P10253.
Protocols and materials databases
DNASU	2548.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302262; ENSP00000305692; ENSG00000171298. ENST00000390015; ENSP00000374665; ENSG00000171298.
GeneID	2548.
KEGG	hsa:2548.
UCSC	uc002jxo.3. human.
Organism-specific databases
CTD	2548.
GeneCards	GC17P078075.
HGNC	HGNC:4065. GAA.
HPA	HPA026970.
MIM	232300. phenotype. 606800. gene.
neXtProt	NX_P10253.
Orphanet	308604. Glycogen storage disease due to acid maltase deficiency, adult onset. 308552. Glycogen storage disease due to acid maltase deficiency, infantile onset. 308573. Glycogen storage disease due to acid maltase deficiency, juvenile onset.
PharmGKB	PA28476.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1501.
HOGENOM	HOG000041175.
HOVERGEN	HBG006297.
InParanoid	P10253.
KO	K12316.
OMA	RGCCYIP.
OrthoDB	EOG4MKNFR.
Gene expression databases
ArrayExpress	P10253.
Bgee	P10253.
CleanEx	HS_GAA.
Genevestigator	P10253.
GermOnline	ENSG00000171298. Homo sapiens.
Family and domain databases
Gene3D	4.10.110.10. 1 hit.
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR000322. Glyco_hydro_31. IPR025887. Glyco_hydro_31_N_dom. IPR017853. Glycoside_hydrolase_SF. IPR000519. P_trefoil. IPR017957. P_trefoil_CS. [Graphical view]
PANTHER	PTHR22762. PTHR22762. 1 hit.
Pfam	PF13802. Gal_mutarotas_2. 1 hit. PF01055. Glyco_hydro_31. 1 hit. PF00088. Trefoil. 1 hit. [Graphical view]
SMART	SM00018. PD. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit. PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit. PS00025. P_TREFOIL_1. 1 hit. PS51448. P_TREFOIL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P10253.
ChEMBL	CHEMBL2608.
DrugBank	DB00284. Acarbose.
GenomeRNAi	2548.
NextBio	10047.
SOURCE	Search...

Entry information

Entry name

LYAG_HUMAN

Accession

Primary (citable) accession number: P10253
Secondary accession number(s): Q09GN4 , Q14351, Q16302, Q8IWE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 11, 2011
Last modified:	May 29, 2013
This is version 159 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.