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P10253 (LYAG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysosomal alpha-glucosidase

EC=3.2.1.20
Alternative name(s):
Acid maltase
Aglucosidase alfa
Gene names
Name:GAA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length952 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.57

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Contains 1 P-type (trefoil) domain.

Ontologies

Keywords
   Cellular componentLysosome
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Glycogen storage disease
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac 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

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

lysosome organization

Inferred from mutant phenotype Ref.27. Source: BHF-UCL

maltose metabolic process

Inferred by curator PubMed 9505277. Source: BHF-UCL

muscle cell cellular homeostasis

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling posture

Inferred from electronic annotation. Source: Ensembl

regulation of the force of heart contraction

Inferred from electronic annotation. Source: Ensembl

sucrose metabolic process

Inferred by curator PubMed 9505277. Source: BHF-UCL

tissue development

Inferred from electronic annotation. Source: Ensembl

vacuolar sequestering

Inferred from mutant phenotype PubMed 10931430. Source: BHF-UCL

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

lysosomal membrane

Inferred from direct assay Ref.14. Source: UniProtKB

lysosome

Inferred from direct assay PubMed 9505277. Source: BHF-UCL

   Molecular_functionalpha-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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 6942
PRO_0000018565
Chain70 – 952883Lysosomal alpha-glucosidase
PRO_0000018566
Chain123 – 95283076 kDa lysosomal alpha-glucosidase
PRO_0000018567
Chain204 – 95274970 kDa lysosomal alpha-glucosidase
PRO_0000018568

Regions

Domain80 – 13152P-type

Sites

Active site5181Nucleophile Ref.9
Active site5211 By similarity

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Ref.10 Ref.15
Glycosylation2331N-linked (GlcNAc...) Ref.10
Glycosylation3901N-linked (GlcNAc...) Ref.10 Ref.13
Glycosylation4701N-linked (GlcNAc...) Ref.10 Ref.11 Ref.15
Glycosylation6521N-linked (GlcNAc...) Ref.10
Glycosylation8821N-linked (GlcNAc...) Ref.10 Ref.15
Glycosylation9251N-linked (GlcNAc...) Ref.10 Ref.15
Disulfide bond82 ↔ 109 By similarity
Disulfide bond92 ↔ 108 By similarity
Disulfide bond103 ↔ 127 By similarity

Natural variations

Natural variant461S → P in GSD2. Ref.52
VAR_068564
Natural variant741R → H. Ref.56
VAR_068565
Natural variant891R → H. Ref.56
VAR_068566
Natural variant911D → 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 variant1031C → 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 variant1031C → R in GSD2. Ref.56
VAR_068567
Natural variant1081C → G in GSD2. Ref.56
VAR_068568
Natural variant1271C → F in GSD2. Ref.56
VAR_068569
Natural variant1901R → H in GSD2. Ref.50
VAR_068570
Natural variant1911Y → C in GSD2; extremely low residual enzymatic activity. Ref.51
VAR_046467
Natural variant1991H → R. Ref.1 Ref.5 Ref.27 Ref.32
Corresponds to variant rs1042393 [ dbSNP | Ensembl ].
VAR_004286
Natural variant2081L → P in GSD2. Ref.37
VAR_029025
Natural variant2171P → L in GSD2. Ref.52
VAR_068571
Natural variant2191G → R in GSD2; infantile form; severe; loss of activity. Ref.38 Ref.42 Ref.51
VAR_018079
Natural variant2201V → L. Ref.56
VAR_068572
Natural variant2221V → M. Ref.56
VAR_068573
Natural variant2231R → H. Ref.1 Ref.5 Ref.27 Ref.32
Corresponds to variant rs1042395 [ dbSNP | Ensembl ].
VAR_004287
Natural variant2241R → P in GSD2. Ref.54
VAR_068574
Natural variant2241R → Q in GSD2. Ref.56
VAR_068575
Natural variant2241R → W in GSD2; infantile; mild partial loss of activity. Ref.39 Ref.41 Ref.51
VAR_029026
Natural variant2341T → K in GSD2. Ref.56 Ref.57
VAR_068576
Natural variant2341T → R in GSD2. Ref.56
VAR_068577
Natural variant2371A → V in GSD2. Ref.45
VAR_029027
Natural variant2511S → L in GSD2. Ref.54
VAR_068578
Natural variant2541S → L in GSD2. Ref.54
VAR_068579
Natural variant2621E → K in GSD2; infantile; severe. Ref.38 Ref.51 Ref.54
Corresponds to variant rs201896815 [ dbSNP | Ensembl ].
VAR_029028
Natural variant2661P → S in GSD2. Ref.54
VAR_068580
Natural variant2711T → A. Ref.54
VAR_068581
Natural variant2851P → R in GSD2; juvenile form; mild; partial loss of activity. Ref.42
VAR_018080
Natural variant2851P → S in GSD2. Ref.50
VAR_068582
Natural variant2901N → D. Ref.56
VAR_068583
Natural variant2911L → F in GSD2. Ref.50
VAR_068584
Natural variant2911L → P in GSD2. Ref.50 Ref.54
VAR_068585
Natural variant2921Y → C in GSD2; juvenile form; mild; partial loss of activity. Ref.42
VAR_018081
Natural variant2931G → R in GSD2; infantile form; severe; almost complete loss of activity. Ref.42 Ref.45 Ref.51
VAR_018082
Natural variant2991L → R in GSD2; infantile form. Ref.27
VAR_004288
Natural variant3081H → L in GSD2. Ref.37
VAR_046468
Natural variant3081H → P in GSD2; infantile form; severe; complete loss of activity. Ref.42
VAR_018083
Natural variant3091G → R in GSD2; severe. Ref.31 Ref.48
VAR_018084
Natural variant3101V → G Found in a patient with GSD2; unknown pathological significance. Ref.56
VAR_068586
Natural variant3121L → R in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018085
Natural variant3161N → I in GSD2. Ref.56
VAR_068587
Natural variant3181M → K in GSD2. Ref.50
VAR_068588
Natural variant3181M → T in GSD2; severe. Ref.18
VAR_004289
Natural variant3241P → L in GSD2. Ref.37
VAR_029029
Natural variant3301W → G in GSD2; infantile form; severe. Ref.46
VAR_029030
Natural variant3351G → E in GSD2. Ref.56
VAR_068589
Natural variant3351G → R in GSD2. Ref.50
VAR_068590
Natural variant3471P → R in GSD2. Ref.50
VAR_068591
Natural variant3551L → P in GSD2; infantile form; severe; loss of activity. Ref.42 Ref.43 Ref.48 Ref.49 Ref.51
VAR_018086
Natural variant3591G → R. Ref.49
VAR_068592
Natural variant3611P → L in GSD2; juvenile form; severe. Ref.40 Ref.48 Ref.56
VAR_029031
Natural variant3741C → R in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018087
Natural variant3751R → L in GSD2; extremely low residual enzymatic activity. Ref.51
VAR_046469
Natural variant3771G → R in GSD2; severe.
VAR_029032
Natural variant3911M → V Found in a patient with GSD2; unknown pathological significance. Ref.56
VAR_068593
Natural variant3971P → L in GSD2. Ref.56
VAR_068594
Natural variant4011Q → R in GSD2; extremely low residual enzymatic activity. Ref.51
VAR_046470
Natural variant4021W → R in GSD2; severe.
VAR_004290
Natural variant4041D → N in GSD2; severe. Ref.47
VAR_029033
Natural variant4051L → P in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018088
Natural variant4081M → V in GSD2; juvenile form; severe. Ref.38 Ref.54
VAR_029034
Natural variant4191D → V in GSD2. Ref.56
VAR_068595
Natural variant431 – 4333Missing in GSD2.
VAR_070017
Natural variant4371R → C in GSD2; juvenile form; severe. Ref.40
VAR_029035
Natural variant4451A → P in GSD2. Ref.48
VAR_029036
Natural variant4551Y → F in GSD2; juvenile form; almost complete loss of activity. Ref.42
VAR_018089
Natural variant4571P → H in GSD2. Ref.56
VAR_068596
Natural variant4571P → L in GSD2; juvenile form. Ref.5
VAR_029040
Natural variant4581Y → C. Ref.56
VAR_068597
Natural variant4591Missing in GSD2; infantile form; severe. Ref.42
VAR_018090
Natural variant4781G → R in GSD2; severe; loss of activity. Ref.42 Ref.54
VAR_004291
Natural variant4811W → R in GSD2; severe; loss of activity. Ref.35 Ref.42
VAR_004292
Natural variant4821P → R in GSD2. Ref.50
VAR_068598
Natural variant4831G → V in GSD2. Ref.50
VAR_068599
Natural variant4861A → P in GSD2. Ref.52
VAR_068600
Natural variant4891D → N in GSD2; severe. Ref.48 Ref.51
VAR_029037
Natural variant5191M → T in GSD2; severe; loss of activity. Ref.42
VAR_004293
Natural variant5191M → V in GSD2. Ref.24
VAR_004294
Natural variant5211E → K in GSD2; severe. Ref.19
VAR_004295
Natural variant5211E → Q in GSD2. Ref.50
VAR_068601
Natural variant5221P → A in GSD2; no residual enzymatic activity. Ref.49 Ref.51
VAR_046471
Natural variant5221P → S in GSD2. Ref.50
VAR_068602
Natural variant5231S → Y in GSD2. Ref.56
VAR_068603
Natural variant5251F → Y in GSD2. Ref.54
VAR_068604
Natural variant5291S → V in GSD2; mild; requires 2 nucleotide substitutions. Ref.29
VAR_004296
Natural variant5451P → L in GSD2; mild; partial loss of activity. Ref.26 Ref.34 Ref.42 Ref.54
VAR_004297
Natural variant5491G → R in GSD2; juvenile form; mild; partial loss of activity. Ref.42 Ref.48
VAR_018091
Natural variant5521L → P in GSD2; infantile/juvenile form; severe; loss of activity. Ref.42 Ref.51
VAR_018092
Natural variant5571I → F in GSD2. Ref.54
VAR_068605
Natural variant5581C → S in GSD2. Ref.53 Ref.56
VAR_068606
Natural variant5661S → P in GSD2; infantile form. Ref.32
VAR_004298
Natural variant5681H → L in GSD2. Ref.57
VAR_070018
Natural variant5701N → K in GSD2. Ref.50
VAR_068607
Natural variant5721H → Q in GSD2. Ref.50
VAR_068608
Natural variant5751Y → C in GSD2. Ref.56
VAR_068609
Natural variant5751Y → S in GSD2; juvenile form. Ref.42
VAR_018093
Natural variant5761G → A.
VAR_004299
Natural variant5761G → R in GSD2. Ref.56
VAR_068610
Natural variant5761G → S Retains about half of the activity compared with the wild-type. Ref.41
Corresponds to variant rs1800307 [ dbSNP | Ensembl ].
VAR_004300
Natural variant5791E → K in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018094
Natural variant5851R → K. Ref.50
VAR_068611
Natural variant5851R → M in GSD2. Ref.37
VAR_046472
Natural variant5941R → H in GSD2. Ref.56
VAR_068612
Natural variant5941R → P in GSD2. Ref.50 Ref.52
VAR_068613
Natural variant5991S → Y in GSD2; no residual enzymatic activity. Ref.51
VAR_046473
Natural variant6001R → C in GSD2; juvenile form; loss of activity. Ref.41 Ref.42
VAR_018095
Natural variant6001R → H in GSD2; infantile form.
VAR_008689
Natural variant6011S → L in GSD2. Ref.56 Ref.57
VAR_068614
Natural variant6021T → A in GSD2. Ref.56
VAR_068615
Natural variant607 – 6126Missing in GSD2.
VAR_046474
Natural variant6071G → D in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018096
Natural variant6101A → V in GSD2. Ref.49
VAR_068616
Natural variant6111G → D Found in a patient with GSD2; unknown pathological significance. Ref.56
VAR_068617
Natural variant6121H → Q in GSD2. Ref.48
VAR_029038
Natural variant6121H → Y in GSD2. Ref.52
VAR_068618
Natural variant6141T → K in GSD2. Ref.50
VAR_068619
Natural variant6151G → R in GSD2; infantile/adult form. Ref.54
VAR_008690
Natural variant6191S → R in GSD2; loss of function of the mutant enzyme. Ref.41
VAR_046475
Natural variant6271S → P in GSD2. Ref.56
VAR_068620
Natural variant6291P → L. Ref.56
VAR_068621
Natural variant6351N → K in GSD2. Ref.52
VAR_068622
Natural variant6381G → V in GSD2. Ref.52
VAR_068623
Natural variant6381G → W in GSD2. Ref.34 Ref.51
VAR_046476
Natural variant6431G → R in GSD2; infantile form. Ref.20 Ref.32 Ref.37 Ref.48 Ref.51
Corresponds to variant rs28937909 [ dbSNP | Ensembl ].
VAR_004301
Natural variant6451D → 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 variant6451D → H in GSD2; almost complete loss of activity. Ref.8
VAR_004303
Natural variant6451D → N in GSD2. Ref.30 Ref.44 Ref.51
VAR_004304
Natural variant6471C → W in GSD2. Ref.25 Ref.30
VAR_004305
Natural variant6481G → D in GSD2. Ref.56
VAR_068624
Natural variant6481G → S in GSD2. Ref.30
VAR_004306
Natural variant6601R → H in GSD2; loss of function of the mutant enzyme. Ref.41
VAR_046477
Natural variant6721R → Q in GSD2. Ref.30
VAR_004307
Natural variant6721R → T in GSD2. Ref.37
VAR_046478
Natural variant6721R → W in GSD2. Ref.30 Ref.48
VAR_004308
Natural variant6751Missing in GSD2; infantile form.
VAR_008692
Natural variant6891E → K in allele GAA*4. Ref.28
Corresponds to variant rs1800309 [ dbSNP | Ensembl ].
VAR_004309
Natural variant700 – 7012Missing Found in a patient with GSD2; unknown pathological significance.
VAR_068625
Natural variant7021R → 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 variant7021R → L in GSD2. Ref.56
VAR_068626
Natural variant7111T → R. Ref.54
VAR_068627
Natural variant7181V → I. Ref.56
VAR_068628
Natural variant7251R → W in GSD2; adult form. Ref.20
Corresponds to variant rs28939100 [ dbSNP | Ensembl ].
VAR_004310
Natural variant7371T → N in GSD2. Ref.50
VAR_068629
Natural variant7431Q → K in GSD2. Ref.56
VAR_068630
Natural variant7461W → C. Ref.48 Ref.54
Corresponds to variant rs1800312 [ dbSNP | Ensembl ].
VAR_004311
Natural variant7461W → G in GSD2. Ref.54
VAR_068631
Natural variant7461W → S in GSD2. Ref.50
VAR_068632
Natural variant7661Y → C in GSD2. Ref.57
VAR_070019
Natural variant7681P → R in GSD2; infantile form. Ref.32
VAR_004312
Natural variant7801V → I. Ref.1 Ref.3 Ref.4 Ref.5 Ref.27
Corresponds to variant rs1126690 [ dbSNP | Ensembl ].
VAR_004313
Natural variant8161V → I. Ref.21 Ref.22 Ref.23
Corresponds to variant rs1800314 [ dbSNP | Ensembl ].
VAR_004314
Natural variant8191R → P in GSD2. Ref.56
VAR_068633
Natural variant8801A → D in GSD2; infantile form; severe; loss of activity. Ref.42
VAR_018097
Natural variant9011L → Q in GSD2; infantile form; severe. Ref.44
VAR_029039
Natural variant9031Missing in GSD2; infantile form; severe; loss of activity. Ref.27
VAR_004315
Natural variant9131P → R in GSD2. Ref.57
VAR_070020
Natural variant9161V → F in GSD2. Ref.56
VAR_068634
Natural variant9251N → NGVPVSN in GSD2.
VAR_004316
Natural variant9271T → I Loss of glycosylation site. Ref.21 Ref.22 Ref.23
Corresponds to variant rs1800315 [ dbSNP | Ensembl ].
VAR_004317
Natural variant9351L → P in GSD2. Ref.50
VAR_068635
Natural variant9491V → D in GSD2.
VAR_004318

Experimental info

Mutagenesis5161W → R: Loss of activity. Ref.9
Mutagenesis5181D → G, N or E: Loss of activity. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P10253 [UniParc].

Last modified January 11, 2011. Version 4.
Checksum: 6E2717BF7201F469

FASTA952105,324
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
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].
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.
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. expand/collapse author list , 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. expand/collapse author list , 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.
[57]"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."
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.
Orphanet J. Rare Dis. 7:35-35(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GSD2 LYS-234; 431-LEU--GLN-433 DEL; LEU-568; LEU-601; CYS-766 AND ARG-913.
+Additional computationally mapped references.

Web resources

GAA

Mutations in alpha-glucosidase

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 expand/collapse EMBL AC list , 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.
CCDSCCDS32760.1.
PIRA32609. A40577.
RefSeqNP_000143.2. NM_000152.3.
NP_001073271.1. NM_001079803.1.
NP_001073272.1. NM_001079804.1.
XP_005257250.1. XM_005257193.1.
XP_005257251.1. XM_005257194.2.
UniGeneHs.1437.

3D structure databases

ProteinModelPortalP10253.
SMRP10253. Positions 89-951.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108823. 14 interactions.
IntActP10253. 7 interactions.
STRING9606.ENSP00000305692.

Chemistry

BindingDBP10253.
ChEMBLCHEMBL2608.
DrugBankDB00284. Acarbose.

Protein family/group databases

Allergome9614. Hom s Glucosidase.
CAZyGH31. Glycoside Hydrolase Family 31.

PTM databases

PhosphoSiteP10253.

Polymorphism databases

DMDM317373572.

Proteomic databases

MaxQBP10253.
PaxDbP10253.
PRIDEP10253.

Protocols and materials databases

DNASU2548.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302262; ENSP00000305692; ENSG00000171298.
ENST00000390015; ENSP00000374665; ENSG00000171298.
GeneID2548.
KEGGhsa:2548.
UCSCuc002jxo.3. human.

Organism-specific databases

CTD2548.
GeneCardsGC17P078075.
GeneReviewsGAA.
HGNCHGNC:4065. GAA.
HPAHPA026970.
MIM232300. phenotype.
606800. gene.
neXtProtNX_P10253.
Orphanet308604. 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.
PharmGKBPA28476.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1501.
HOGENOMHOG000041175.
HOVERGENHBG006297.
InParanoidP10253.
KOK12316.
OMASSEMGYT.
OrthoDBEOG77HDD0.
PhylomeDBP10253.
TreeFamTF314577.

Gene expression databases

ArrayExpressP10253.
BgeeP10253.
CleanExHS_GAA.
GenevestigatorP10253.

Family and domain databases

Gene3D4.10.110.10. 1 hit.
InterProIPR011013. 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]
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
PF00088. Trefoil. 1 hit.
[Graphical view]
SMARTSM00018. PD. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF57492. SSF57492. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS00129. 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]
ProtoNetSearch...

Other

GeneWikiAcid_alpha-glucosidase.
GenomeRNAi2548.
NextBio10047.
PROP10253.
SOURCESearch...

Entry information

Entry nameLYAG_HUMAN
AccessionPrimary (citable) accession number: P10253
Secondary accession number(s): Q09GN4 expand/collapse secondary AC list , Q14351, Q16302, Q8IWE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 172 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries