Bace1
entrez
23821
canonical
uniprot
P56818
canonical
ensembl
ENSMUSG00000032086
resolver
ensp
ENSMUSP00000034591
resolver
ensp
ENSMUSP00000077249
resolver
ensp
ENSMUSP00000124960
resolver
enst
ENSMUST00000034591
resolver
enst
ENSMUST00000078111
resolver
genesymbol
Bace1
resolver
genesymbol_syn
Bace
resolver
uniprot
F6ZSV3
resolver
uniprot
Q544D0
resolver
uniprot
Q8C4F4
resolver
uniprot
Q9CUU5
resolver
uniprot_entry
BACE1_MOUSE
resolver
uniprot_entry
F6ZSV3_MOUSE
resolver
uniprot_entry
Q8C4F4_MOUSE
resolver
uniprot_entry
Q9CUU5_MOUSE
resolver
uniprot_sec
Q544D0
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by RTN3 and RTN4. {ECO:0000250|UniProtKB:P56817}.
uniprot
proteins
amino_acid_sequence
MAPALHWLLLWVGSGMLPAQGTHLGIRLPLRSGLAGPPLGLRLPRETDEESEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHIPNIFSLQLCGAGFPLNQTEALASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAVSQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTADMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRHQHDDFADDISLLK
uniprot
proteins
ec_number
3.4.23.46
uniprot
proteins
function
FUNCTION: Responsible for the proteolytic processing of the amyloid precursor protein (APP) (PubMed:29325091). 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 (PubMed:29325091). Cleaves CHL1 (PubMed:29325091). {ECO:0000269|PubMed:29325091}.
uniprot
proteins
mass_dalton
55748
uniprot
proteins
mutagenesis
MUTAGEN 93; /note="D->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:29325091"; MUTAGEN 153; /note="N->S: Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression; when associated with S-223."; /evidence="ECO:0000269|PubMed:26467158"; MUTAGEN 172; /note="N->S: Slightly decreases bisecting N-acetylglucosamine levels."; /evidence="ECO:0000269|PubMed:26467158"; MUTAGEN 223; /note="N->S: Decreases bisecting N-acetylglucosamine levels. Almost abolishes bisecting N-acetylglucosamine levels but has no effect on surface expression; when associated with S-153."; /evidence="ECO:0000269|PubMed:26467158"; MUTAGEN 354; /note="N->S: Slightly decreases bisecting N-acetylglucosamine levels."; /evidence="ECO:0000269|PubMed:26467158"; MUTAGEN 474; /note="C->A: Completely abolishes S-palmitoylation; when associated with A-478; A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-478; A-482 and A-485. Reduces membrane raft association; when associated with A-478; A-482 and A-485. Doesn't affect APP processing; when associated with A-478; A-482 and A-485."; /evidence="ECO:0000269|PubMed:19074428"; MUTAGEN 478; /note="C->A: Significantly reduces S-palmitoylation; when associated with A-482 and A-485. Completely abolishes S-palmitoylation; when associated with A-474; A-482 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-482 and A-485. Reduces membrane raft association; when associated with A-474; A-482 and A-485. Doesn't affect APP processing; when associated with A-474; A-482 and A-485."; /evidence="ECO:0000269|PubMed:19074428"; MUTAGEN 482; /note="C->A: Significantly reduces S-palmitoylation; when associated with A-478 and A-485. Completely abolishes S-palmitoylation; when associated with A-474; A-478 and A-485. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-478 and A-485. Reduces membrane raft association; when associated with A-474; A-478 and A-485. Doesn't affect APP processing; when associated with A-474; A-478 and A-485."; /evidence="ECO:0000269|PubMed:19074428"; MUTAGEN 485; /note="C->A: Significantly reduces S-palmitoylation; when associated with A-478 and A-482. Completely abolishes S-palmitoylation; when associated with A-474; A-478 and A-482. Doesn't affect trans-Golgi network and endosome localization; when associated with A-474; A-478 and A-482. Reduces membrane raft association; when associated with A-474; A-478 and A-482. Doesn't affect APP processing; when associated with A-474; A-478 and A-482."; /evidence="ECO:0000269|PubMed:19074428
uniprot
proteins
post_translational_modification
PTM: N-Glycosylated (By similarity). Addition of a bisecting N-acetylglucosamine by MGAT3 blocks lysosomal targeting, further degradation and is required for maintaining stability under stress conditions (PubMed:25592972, PubMed:26467158). {ECO:0000250, ECO:0000250|UniProtKB:P56817, ECO:0000269|PubMed:25592972, ECO:0000269|PubMed:26467158}.; PTM: Palmitoylation mediates lipid raft localization. {ECO:0000269|PubMed:19074428}.; PTM: Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307 (PubMed:20826464). Acetylation by NAT8 and NAT8B is transient and deacetylation probably occurs in the Golgi. Acetylation regulates the maturation, the transport to the plasma membrane, the stability and the expression of the protein. {ECO:0000250|UniProtKB:P56817, ECO:0000269|PubMed:20826464}.; PTM: Ubiquitinated at Lys-501, ubiquitination leads to lysosomal degradation. Monoubiquitinated and 'Lys-63'-linked polyubitinated. Deubiquitnated by USP8; inhibits lysosomal degradation. {ECO:0000250|UniProtKB:P56817}.; PTM: Phosphorylation at Ser-498 is required for interaction with GGA1 and retrograded transport from endosomal compartments to the trans-Golgi network. Non-phosphorylated BACE1 enters a direct recycling route to the cell surface. {ECO:0000250|UniProtKB:P56817}.
uniprot
proteins
protein_family
Peptidase A1 family
uniprot
proteins
pubmed
10531052
uniprot
proteins
pubmed
10591213
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15987683
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16407538
uniprot
proteins
pubmed
19074428
uniprot
proteins
pubmed
19935654
uniprot
proteins
pubmed
20826464
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23931995
uniprot
proteins
pubmed
25592972
uniprot
proteins
pubmed
26467158
uniprot
proteins
pubmed
29325091
uniprot
proteins
sequence_length
501
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P56817}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:19074428}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P56817}. Endosome {ECO:0000269|PubMed:19074428}. Late endosome {ECO:0000269|PubMed:25592972}. Early endosome {ECO:0000269|PubMed:25592972}. Cell surface {ECO:0000269|PubMed:26467158}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P56817}. Membrane raft {ECO:0000269|PubMed:19074428}. Lysosome {ECO:0000269|PubMed:25592972}. Recycling endosome {ECO:0000269|PubMed:23931995}. Cell projection, axon {ECO:0000269|PubMed:29325091}. Cell projection, dendrite {ECO:0000269|PubMed:29325091}. Note=Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine which blocks targeting to late endosomes and lysosomes (PubMed:25592972). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity). {ECO:0000250|UniProtKB:P56817, ECO:0000269|PubMed:25592972}.
uniprot
proteins
transmembrane_region
TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins