LYAG_HUMAN - dbPTM
LYAG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYAG_HUMAN
UniProt AC P10253
Protein Name Lysosomal alpha-glucosidase
Gene Name GAA
Organism Homo sapiens (Human).
Sequence Length 952
Subcellular Localization Lysosome . Lysosome membrane .
Protein Description Essential for the degradation of glycogen in lysosomes. [PubMed: 1856189]
Protein Sequence MGVRHPPCSHRLLAVCALVSLATAALLGHILLHDFLLVPRELSGSSPVLEETHPAHQQGASRPGPRDAQAHPGRPRAVPTQCDVPPNSRFDCAPDKAITQEQCEARGCCYIPAKQGLQGAQMGQPWCFFPPSYPSYKLENLSSSEMGYTATLTRTTPTFFPKDILTLRLDVMMETENRLHFTIKDPANRRYEVPLETPHVHSRAPSPLYSVEFSEEPFGVIVRRQLDGRVLLNTTVAPLFFADQFLQLSTSLPSQYITGLAEHLSPLMLSTSWTRITLWNRDLAPTPGANLYGSHPFYLALEDGGSAHGVFLLNSNAMDVVLQPSPALSWRSTGGILDVYIFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAITRQVVENMTRAHFPLDVQWNDLDYMDSRRDFTFNKDGFRDFPAMVQELHQGGRRYMMIVDPAISSSGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGSTAFPDFTNPTALAWWEDMVAEFHDQVPFDGMWIDMNEPSNFIRGSEDGCPNNELENPPYVPGVVGGTLQAATICASSHQFLSTHYNLHNLYGLTEAIASHRALVKARGTRPFVISRSTFAGHGRYAGHWTGDVWSSWEQLASSVPEILQFNLLGVPLVGADVCGFLGNTSEELCVRWTQLGAFYPFMRNHNSLLSLPQEPYSFSEPAQQAMRKALTLRYALLPHLYTLFHQAHVAGETVARPLFLEFPKDSSTWTVDHQLLWGEALLITPVLQAGKAEVTGYFPLGTWYDLQTVPVEALGSLPPPPAAPREPAIHSEGQWVTLPAPLDTINVHLRAGYIIPLQGPGLTTTESRQQPMALAVALTKGGEARGELFWDDGESLEVLERGAYTQVIFLARNNTIVNELVRVTSEGAGLQLQKVTVLGVATAPQQVLSNGVPVSNFTYSPDTKVLDICVSLLMGEQFLVSWC
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
46O-linked_GlycosylationPRELSGSSPVLEETH
CHHHCCCCCCCCCCC		23.6655823813
52O-linked_GlycosylationSSPVLEETHPAHQQG
CCCCCCCCCHHHHCC		24.6355823819
61O-linked_GlycosylationPAHQQGASRPGPRDA
HHHHCCCCCCCCCCC		45.9255823825
962-HydroxyisobutyrylationRFDCAPDKAITQEQC
CCCCCCCCCCCHHHH		40.40-
140N-linked_GlycosylationYPSYKLENLSSSEMG
CCCCCCCCCCCCCCC		56.5129061980
140N-linked_GlycosylationYPSYKLENLSSSEMG
CCCCCCCCCCCCCCC		56.5129061980
142PhosphorylationSYKLENLSSSEMGYT
CCCCCCCCCCCCCCE		43.3221406692
142O-linked_GlycosylationSYKLENLSSSEMGYT
CCCCCCCCCCCCCCE		43.3232574038
143PhosphorylationYKLENLSSSEMGYTA
CCCCCCCCCCCCCEE		33.2221406692
144PhosphorylationKLENLSSSEMGYTAT
CCCCCCCCCCCCEEE		28.3821406692
144O-linked_GlycosylationKLENLSSSEMGYTAT
CCCCCCCCCCCCEEE		28.3832574038
148PhosphorylationLSSSEMGYTATLTRT
CCCCCCCCEEEEEEC		7.5921406692
149O-linked_GlycosylationSSSEMGYTATLTRTT
CCCCCCCEEEEEECC		13.8732574038
149PhosphorylationSSSEMGYTATLTRTT
CCCCCCCEEEEEECC		13.8721406692
151PhosphorylationSEMGYTATLTRTTPT
CCCCCEEEEEECCCC		22.3621406692
153PhosphorylationMGYTATLTRTTPTFF
CCCEEEEEECCCCCC		22.9321406692
1622-HydroxyisobutyrylationTTPTFFPKDILTLRL
CCCCCCCHHHEEEEE		52.85-
162UbiquitinationTTPTFFPKDILTLRL
CCCCCCCHHHEEEEE		52.85-
166PhosphorylationFFPKDILTLRLDVMM
CCCHHHEEEEEEEEE		15.3421406692
172SulfoxidationLTLRLDVMMETENRL
EEEEEEEEEECCCEE		1.6830846556
173SulfoxidationTLRLDVMMETENRLH
EEEEEEEEECCCEEE		6.0730846556
175PhosphorylationRLDVMMETENRLHFT
EEEEEEECCCEEEEE		22.2121406692
182PhosphorylationTENRLHFTIKDPANR
CCCEEEEEECCCCCC		19.1721406692
233N-linked_GlycosylationLDGRVLLNTTVAPLF
CCCEEEEECCCHHHH		29.5529061980
235PhosphorylationGRVLLNTTVAPLFFA
CEEEEECCCHHHHCH		17.38-
329PhosphorylationLQPSPALSWRSTGGI
ECCCCCCCCCCCCCE		23.6624719451
390N-linked_GlycosylationITRQVVENMTRAHFP
HHHHHHHHCHHCCCC		26.0529061980
407PhosphorylationVQWNDLDYMDSRRDF
CCCCCCCCCCCCCCC		15.32-
415PhosphorylationMDSRRDFTFNKDGFR
CCCCCCCCCCCCCCC		30.50-
418UbiquitinationRRDFTFNKDGFRDFP
CCCCCCCCCCCCCHH		55.8533845483
4182-HydroxyisobutyrylationRRDFTFNKDGFRDFP
CCCCCCCCCCCCCHH		55.85-
438PhosphorylationLHQGGRRYMMIVDPA
HHHCCCEEEEEECHH		6.9528857561
447PhosphorylationMIVDPAISSSGPAGS
EEECHHHCCCCCCCC		22.1322210691
448PhosphorylationIVDPAISSSGPAGSY
EECHHHCCCCCCCCC		32.9522210691
449PhosphorylationVDPAISSSGPAGSYR
ECHHHCCCCCCCCCC		41.8422210691
454PhosphorylationSSSGPAGSYRPYDEG
CCCCCCCCCCCCCCC		21.7822210691
458PhosphorylationPAGSYRPYDEGLRRG
CCCCCCCCCCCCCCC		20.0328857561
470N-linked_GlycosylationRRGVFITNETGQPLI
CCCEEEECCCCCCCC		39.7629061980
470N-linked_GlycosylationRRGVFITNETGQPLI
CCCEEEECCCCCCCC		39.7629061980
589UbiquitinationASHRALVKARGTRPF
HHCHHHHHHCCCCCE		32.9627667366
652N-linked_GlycosylationDVCGFLGNTSEELCV
EECCCCCCCCHHHHH		42.4529061980
676PhosphorylationPFMRNHNSLLSLPQE
HHHCCCCCHHCCCCC		24.1227251275
679PhosphorylationRNHNSLLSLPQEPYS
CCCCCHHCCCCCCCC		43.2127251275
722PhosphorylationQAHVAGETVARPLFL
HHHHCCCCCCEEEEE		20.6720071362
822PhosphorylationNVHLRAGYIIPLQGP
EEEEECCEEEECCCC		8.4928152594
849UbiquitinationALAVALTKGGEARGE
EEEHHHHCCCCCCCE		66.8124816145
882N-linked_GlycosylationQVIFLARNNTIVNEL
EEEEEECCCHHHHHH		44.3729061980
884O-linked_GlycosylationIFLARNNTIVNELVR
EEEECCCHHHHHHHH		29.8332574038
884PhosphorylationIFLARNNTIVNELVR
EEEECCCHHHHHHHH		29.83-
894PhosphorylationNELVRVTSEGAGLQL
HHHHHHHCCCCCCEE		31.04-
925N-linked_GlycosylationSNGVPVSNFTYSPDT
HCCCCCCCCCCCCCC		33.258435067
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of LYAG_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYAG_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LYAG_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZEP1_HUMANHIVEP1physical
21988832
STAT2_HUMANSTAT2physical
21988832
NUMBL_HUMANNUMBLphysical
21988832
ESTD_HUMANESDphysical
26344197
AATC_HUMANGOT1physical
26344197
MPPA_HUMANPMPCAphysical
26344197
LRC24_HUMANLRRC24physical
28514442
DYR2_HUMANDHFRL1physical
28514442
B4GN3_HUMANB4GALNT3physical
28514442
MANEL_HUMANMANEALphysical
28514442
T132A_HUMANTMEM132Aphysical
28514442
B4GT7_HUMANB4GALT7physical
28514442
EXT1_HUMANEXT1physical
28514442
ENTP7_HUMANENTPD7physical
28514442
MA2A2_HUMANMAN2A2physical
28514442
GALT4_HUMANGALNT4physical
28514442
TM39A_HUMANTMEM39Aphysical
28514442
B3GA3_HUMANB3GAT3physical
28514442
B4GT1_HUMANB4GALT1physical
28514442
LARG1_HUMANLARGEphysical
28514442
AMD_HUMANPAMphysical
28514442
Drug and Disease Associations
Kegg Disease
H00069 Glycogen storage diseases (GSD), including: von Gierke disease (GSD type Ia); Pompe disease (GSD typ
OMIM Disease
232300Glycogen storage disease 2 (GSD2)
Kegg Drug
D00216 Acarbose (JAN/USAN/INN); Precose (TN)
D00625 Miglitol (JAN/USAN/INN); Glyset (TN)
D01665 Voglibose (JP16/USAN/INN); Basen (TN)
D03207 Alglucosidase alfa (genetical recombination) (JAN); Alglucosidase alfa (USAN/INN); Lumizyme (TN); My
D09605 Duvoglustat (USAN/INN); 1-Deoxynojirimycin
D09606 Duvoglustat hydrochloride (USAN)
D09779 Emiglitate (JAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYAG_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple 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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-470; ASN-882 ANDASN-925, AND MASS SPECTROMETRY.
"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).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-390, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-470.
"Human lysosomal alpha-glucosidase: functional characterization of theglycosylation sites.";
Hermans M.M.P., Wisselaar H.A., Kroos M.A., Oostra B.A.,Reuser A.J.J.;
Biochem. J. 289:681-686(1993).
Cited for: GLYCOSYLATION AT ASN-140; ASN-233; ASN-390; ASN-470; ASN-652; ASN-882AND ASN-925.

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