LYAG_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LYAG_MOUSE
• UniProt AC: P70699
• Protein Name: Lysosomal alpha-glucosidase
• Gene Name: Gaa
• Organism: Mus musculus (Mouse).
• Sequence Length: 953
• Subcellular Localization: Lysosome . Lysosome membrane .
• Protein Description: Essential for the degradation of glycogen in lysosomes. Has highest activity on alpha-1,4-linked glycosidic linkages, but can also hydrolyze alpha-1,6-linked glucans..
• Protein Sequence: MNIRKPLCSNSVVGACTLISLTTAVILGHLMLRELMLLPQDLHESSSGLWKTYRPHHQEGYKPGPLHIQEQTEQPKEAPTQCDVPPSSRFDCAPDKGISQEQCEARGCCYVPAGQVLKEPQIGQPWCFFPPSYPSYRLENLSSTESGYTATLTRTSPTFFPKDVLTLQLEVLMETDSRLHFKIKDPASKRYEVPLETPRVLSQAPSPLYSVEFSEEPFGVIVRRKLGGRVLLNTTVAPLFFADQFLQLSTSLPSQHITGLGEHLSPLMLSTDWARITLWNRDTPPSQGTNLYGSHPFYLALEDGGLAHGVFLLNSNAMDVILQPSPALTWRSTGGILDVYVFLGPEPKSVVQQYLDVVGYPFMPPYWGLGFHLCRWGYSSTAIVRQVVENMTRTHFPLDVQWNDLDYMDARRDFTFNQDSFADFPDMVRELHQDGRRYMMIVDPAISSAGPAGSYRPYDEGLRRGVFITNETGQPLIGKVWPGTTAFPDFTNPETLDWWQDMVSEFHAQVPFDGMWLDMNEPSNFVRGSQQGCPNNELENPPYVPGVVGGILQAATICASSHQFLSTHYNLHNLYGLTEAIASSRALVKTRGTRPFVISRSTFSGHGRYAGHWTGDVRSSWEHLAYSVPDILQFNLLGVPLVGADICGFIGDTSEELCVRWTQLGAFYPFMRNHNDLNSVPQEPYRFSETAQQAMRKAFALRYALLPYLYTLFHRAHVRGDTVARPLFLEFPEDPSTWSVDRQLLWGPALLITPVLEPGKTEVTGYFPKGTWYNMQMVSVDSLGTLPSPSSASSFRSAVQSKGQWLTLEAPLDTINVHLREGYIIPLQGPSLTTTESRKQPMALAVALTASGEADGELFWDDGESLAVLERGAYTLVTFSAKNNTIVNKLVRVTKEGAELQLREVTVLGVATAPTQVLSNGIPVSNFTYSPDNKSLAIPVSLLMGELFQISWS

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
140	N-linked_Glycosylation	YPSYRLENLSSTESG CCCEEECCCCCCCCC	50.22	19349973
156	Phosphorylation	TATLTRTSPTFFPKD EEEEEECCCCCCCHH	20.74	-
197	Phosphorylation	RYEVPLETPRVLSQA CEECCCCCCCHHCCC	24.87	-
233	N-linked_Glycosylation	LGGRVLLNTTVAPLF CCCEEEEECCCHHHH	29.55	-
333	Phosphorylation	PALTWRSTGGILDVY CCCCCCCCCCEEEEE	30.74	24719451
340	Phosphorylation	TGGILDVYVFLGPEP CCCEEEEEEECCCCC	5.78	24719451
390	N-linked_Glycosylation	IVRQVVENMTRTHFP HHHHHHHHCCCCCCC	26.05	-
438	Phosphorylation	LHQDGRRYMMIVDPA HHHCCCEEEEEECHH	6.95	-
470	N-linked_Glycosylation	RRGVFITNETGQPLI CCCEEEECCCCCCCC	39.76	19349973
604	Phosphorylation	VISRSTFSGHGRYAG EEECCCCCCCCCCCC	29.93	18779572
764	Phosphorylation	EPGKTEVTGYFPKGT CCCCCEEEEECCCCC	21.67	28059163
883	N-linked_Glycosylation	LVTFSAKNNTIVNKL EEEEECCCCCCEEEE	51.06	-
885	Phosphorylation	TFSAKNNTIVNKLVR EEECCCCCCEEEEEE	35.38	18779572
895	Acetylation	NKLVRVTKEGAELQL EEEEECCCCCCEEEE	51.82	22826441
926	N-linked_Glycosylation	SNGIPVSNFTYSPDN CCCCCCCCCEECCCC	33.25	-
933	N-linked_Glycosylation	NFTYSPDNKSLAIPV CCEECCCCCCCHHHH	38.92	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LYAG_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LYAG_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LYAG_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of LYAG_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-470, AND MASSSPECTROMETRY.
PubMed: 19349973