BACE1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BACE1_MOUSE
• UniProt AC: P56818
• Protein Name: Beta-secretase 1
• Gene Name: Bace1
• Organism: Mus musculus (Mouse).
• Sequence Length: 501
• Subcellular Localization: Membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network . Endoplasmic reticulum. Endosome . Cell surface. Cytoplasmic vesicle membrane. Membrane raft . Predominantly localized to the later Golgi/trans-Golgi network (TGN) a
• Protein Description: Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (By similarity)..
• Protein Sequence: MAPALHWLLLWVGSGMLPAQGTHLGIRLPLRSGLAGPPLGLRLPRETDEESEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHIPNIFSLQLCGAGFPLNQTEALASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAVSQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTADMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRHQHDDFADDISLLK

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
126	Acetylation	STYRDLRKGVYVPYT HHHHHHHCCEEEECC	61.09	17425515
153	N-linked_Glycosylation	VSIPHGPNVTVRANI EECCCCCCCEEEEEE	46.84	26467158
172	N-linked_Glycosylation	ESDKFFINGSNWEGI CCCCEEECCCCHHHH	42.56	26467158
223	N-linked_Glycosylation	CGAGFPLNQTEALAS CCCCCCCCHHHHHHH	47.14	26467158
243	Phosphorylation	IIGGIDHSLYTGSLW EECCCCCCCCCCCCE	21.23	-
245	Phosphorylation	GGIDHSLYTGSLWYT CCCCCCCCCCCCEEE	16.45	-
275	Acetylation	EINGQDLKMDCKEYN EECCEEEEEEHHHHC	40.77	17425515
279	Acetylation	QDLKMDCKEYNYDKS EEEEEEHHHHCCCCC	59.99	17425515
285	Acetylation	CKEYNYDKSIVDSGT HHHHCCCCCCCCCCC	31.55	17425515
299	Acetylation	TTNLRLPKKVFEAAV CCCCCCCHHHHHHHH	67.19	17425515
300	Acetylation	TNLRLPKKVFEAAVK CCCCCCHHHHHHHHH	50.66	17425515
307	Acetylation	KVFEAAVKSIKAASS HHHHHHHHHHHHCCC	41.56	17425515
354	N-linked_Glycosylation	YLMGEVTNQSFRITI HCCEECCCCEEEEEE	40.45	26467158
474	S-palmitoylation	ALFMLPLCLMVCQWR HHHHHHHHHHHHHHH	1.86	19074428
478	S-palmitoylation	LPLCLMVCQWRCLRC HHHHHHHHHHHHHHH	1.68	19074428
482	S-palmitoylation	LMVCQWRCLRCLRHQ HHHHHHHHHHHHHHC	2.27	19074428
485	S-palmitoylation	CQWRCLRCLRHQHDD HHHHHHHHHHHCCCC	2.24	19074428
498	Phosphorylation	DDFADDISLLK---- CCCHHHHHCCC----	34.34	26824392

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
-	K	Ubiquitination	E3 ubiquitin ligase	Fbxo2	Q80UW2	PMID:20854419

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
126	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
275	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
279	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
285	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
299	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
300	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
307	K	Acetylation	Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307.	-
498	S	Phosphorylation	Phosphorylation at Ser-498 is required for interaction with GGA1 and retrograded transport from endosomal compartments to the trans-Golgi network.	21183079
501	K	ubiquitylation	Ubiquitinated at Lys-501, ubiquitination leads to lysosomal degradation.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of BACE1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBX2_MOUSE	Fbxo2	physical	20854419
BRI3_HUMAN	BRI3	physical	15606899
RANB9_HUMAN	RANBP9	physical	15606899
FUBP2_HUMAN	KHSRP	physical	15606899
AT1B1_HUMAN	ATP1B1	physical	15606899
KCY_HUMAN	CMPK1	physical	15606899
SAP_HUMAN	PSAP	physical	15606899

Drug and Disease Associations

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