BACE1
entrez
23621
canonical
uniprot
P56817
canonical
ensembl
ENSG00000186318
resolver
ensp
ENSP00000318585
resolver
ensp
ENSP00000402228
resolver
ensp
ENSP00000403685
resolver
ensp
ENSP00000422461
resolver
ensp
ENSP00000424536
resolver
ensp
ENSP00000475405
resolver
ensp
ENSP00000506107
resolver
enst
ENST00000680971
resolver
genesymbol
BACE1
resolver
genesymbol_syn
BACE
resolver
genesymbol_syn
KIAA1149
resolver
hgnc
HGNC:933
resolver
uniprot
A0A7P0TAB4
resolver
uniprot
A0M8W7
resolver
uniprot
B0YIU9
resolver
uniprot
B7Z3K2
resolver
uniprot
B7Z3Z4
resolver
uniprot
E9PE65
resolver
uniprot
H7BXJ9
resolver
uniprot
Q9BYB9
resolver
uniprot
Q9BYC0
resolver
uniprot
Q9BYC1
resolver
uniprot
Q9UJT5
resolver
uniprot
Q9ULS1
resolver
uniprot_entry
A0A7P0TAB4_HUMAN
resolver
uniprot_entry
B7Z3K2_HUMAN
resolver
uniprot_entry
B7Z3Z4_HUMAN
resolver
uniprot_entry
BACE1_HUMAN
resolver
uniprot_sec
A0M8W7
resolver
uniprot_sec
B0YIU9
resolver
uniprot_sec
E9PE65
resolver
uniprot_sec
H7BXJ9
resolver
uniprot_sec
Q9BYB9
resolver
uniprot_sec
Q9BYC0
resolver
uniprot_sec
Q9BYC1
resolver
uniprot_sec
Q9UJT5
resolver
uniprot_sec
Q9ULS1
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by RTN3 and RTN4. {ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16965550}.
uniprot
proteins
amino_acid_sequence
MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQWRCLRCLRQQHDDFADDISLLK
uniprot
proteins
ec_number
3.4.23.46
uniprot
proteins
function
FUNCTION: 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 (PubMed:10656250, PubMed:10677483, PubMed:20354142). Cleaves CHL1 (By similarity). {ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:10656250, ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:20354142}.
uniprot
proteins
mass_dalton
55764
uniprot
proteins
mutagenesis
MUTAGEN 93; /note="D->N: Decreases beta-cleaved soluble APP production."; /evidence="ECO:0000269|PubMed:10656250"; MUTAGEN 284; /note="D->N: Almost abolishes beta-cleaved soluble APP production."; /evidence="ECO:0000269|PubMed:10656250"; MUTAGEN 498; /note="S->A: No effect on endocytosis from the cell surface. Increases recycling from endosomes to the cell surface."; /evidence="ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016"; MUTAGEN 498; /note="S->D: No effect on endocytosis form the cell surface. Decreases recycling from endosomes to the cell surface."; /evidence="ECO:0000269|PubMed:15886016"; MUTAGEN 499..500; /note="LL->AA: Impairs endocytosis and produces a delayed retrograde transport to the trans-Golgi network and delivery to the lysosomes, decreasing its degradation. Disrupts location to late endosomes and lysosomes. Locates mainly at the cell surface. No effect on degradation regulated by GGA3. Effects on protein stability and defective internalization increases; when associated with R-501."; /evidence="ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:20484053, ECO:0000269|PubMed:23109336"; MUTAGEN 501; /note="K->R: Inhibits ubiquitination. No effect on endocytosis rate. Induced protein stability and accumulation in early and late endosomes, lysosomes and cell membrane. Effects on protein stability and defective internalization increases; when associated with A-499-500-A."; /evidence="ECO:0000269|PubMed:20484053, ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27302062
uniprot
proteins
post_translational_modification
PTM: N-Glycosylated (PubMed:11083922, PubMed:17425515). Addition of a bisecting N-acetylglucosamine by MGAT3 blocks lysosomal targeting, further degradation and is required for maintaining stability under stress conditions (By similarity). {ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:11083922, ECO:0000269|PubMed:17425515}.; PTM: Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307. 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:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:20826464}.; PTM: Palmitoylation mediates lipid raft localization. {ECO:0000250|UniProtKB:P56818}.; PTM: Ubiquitinated at Lys-501, ubiquitination leads to lysosomal degradation (PubMed:16033761, PubMed:20484053, PubMed:23109336, PubMed:27302062). Monoubiquitinated and 'Lys-63'-linked polyubitinated (PubMed:20484053). Deubiquitnated by USP8; inhibits lysosomal degradation (PubMed:27302062). {ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:20484053, ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27302062}.; 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:0000269|PubMed:15886016}.
uniprot
proteins
protein_family
Peptidase A1 family
uniprot
proteins
pubmed
10531052
uniprot
proteins
pubmed
10574461
uniprot
proteins
pubmed
10591213
uniprot
proteins
pubmed
10591214
uniprot
proteins
pubmed
10656250
uniprot
proteins
pubmed
10677483
uniprot
proteins
pubmed
11021803
uniprot
proteins
pubmed
11083922
uniprot
proteins
pubmed
11466313
uniprot
proteins
pubmed
11516562
uniprot
proteins
pubmed
11953458
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12206667
uniprot
proteins
pubmed
14567678
uniprot
proteins
pubmed
15096037
uniprot
proteins
pubmed
15286784
uniprot
proteins
pubmed
15451669
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15615712
uniprot
proteins
pubmed
15628850
uniprot
proteins
pubmed
15886016
uniprot
proteins
pubmed
16033761
uniprot
proteins
pubmed
16407538
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16965550
uniprot
proteins
pubmed
16979658
uniprot
proteins
pubmed
17425515
uniprot
proteins
pubmed
18660751
uniprot
proteins
pubmed
19011241
uniprot
proteins
pubmed
20354142
uniprot
proteins
pubmed
20484053
uniprot
proteins
pubmed
20826464
uniprot
proteins
pubmed
23109336
uniprot
proteins
pubmed
25663301
uniprot
proteins
pubmed
27084579
uniprot
proteins
pubmed
27179792
uniprot
proteins
pubmed
27302062
uniprot
proteins
sequence_length
501
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11466313}; Single-pass type I membrane protein {ECO:0000305|PubMed:11466313}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:20354142, ECO:0000269|PubMed:23109336}. Endoplasmic reticulum {ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:17425515}. Endosome {ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016}. Cell surface {ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:23109336}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016}; Single-pass type I membrane protein {ECO:0000305|PubMed:11466313}. Membrane raft {ECO:0000250|UniProtKB:P56818}. Lysosome {ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27084579, ECO:0000269|PubMed:27302062}. Late endosome {ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27084579, ECO:0000269|PubMed:27302062}. Early endosome {ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27084579, ECO:0000269|PubMed:27302062}. Recycling endosome {ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:27084579, ECO:0000269|PubMed:27302062}. Cell projection, axon {ECO:0000250|UniProtKB:P56818}. Cell projection, dendrite {ECO:0000250|UniProtKB:P56818}. 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 (PubMed:11466313, PubMed:17425515). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine which blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (PubMed:15886016). {ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17425515}.
uniprot
proteins
transmembrane_region
TRANSMEM 458..478; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins