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Protein Page:
BACE (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BACE an integral membrane glycoprotein and aspartic protease that is found mainly in the Golgi. Cleaves APP at the amino terminus of the A-beta peptide sequence, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated carboxy-terminal fragment which is later release by gamma-secretase. Four splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 3.4.23.46; Membrane protein, integral
Cellular Component: Golgi apparatus; multivesicular body; cell surface; cytoplasmic vesicle membrane; axon; endoplasmic reticulum; integral to plasma membrane; late endosome; plasma membrane; integral to membrane; trans-Golgi network; endosome
Molecular Function: protein binding; enzyme binding; beta-amyloid binding; beta-aspartyl-peptidase activity; aspartic-type endopeptidase activity
Biological Process: beta-amyloid metabolic process; membrane protein ectodomain proteolysis; proteolysis
Reference #:  P56817 (UniProtKB)
Alt. Names/Synonyms: APP beta-secretase; Asp 2; ASP2; Aspartyl protease 2; BACE; BACE1; Beta-secretase 1; beta-site amyloid beta A4 precursor protein-cleaving enzyme; Beta-site amyloid precursor protein cleaving enzyme 1; Beta-site APP cleaving enzyme 1; beta-site APP-cleaving enzyme 1; FLJ90568; HSPC104; KIAA1149; Memapsin-2; Membrane-associated aspartic protease 2; transmembrane aspartic proteinase Asp2
Gene Symbols: BACE1
Molecular weight: 55,711 Da
Basal Isoelectric point: 5.24  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BACE

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S498‑p
intracellular localization: S498‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S71-p VDNLRGKsGQGYYVE
1 1 K126-ac STYRDLRkGVYVPYT
0 1 K136-ac YVPYTQGkWEGELGT
0 1 S243 IIGGIDHSLYTGSLW
0 1 Y245 GGIDHSLYTGSLWYT
0 1 Y260-p PIRREWYyEVIIVRV
1 0 K275-ac EINGQDLkMDCkEYN
1 0 K279-ac QDLkMDCkEYNYDkS
1 0 K285-ac CkEYNYDkSIVDSGT
1 0 K299-ac TTNLRLPkkVFEAAV
1 0 K300-ac TNLRLPkkVFEAAVk
1 0 K307-ac kVFEAAVksIKAASS
0 1 S308-p VFEAAVksIKAASST
4 2 S498-p DDFADDIsLLk____
2 0 K501-ub ADDIsLLk_______
  mouse

 
S71 VDNLRGKSGQGYYVE
K126 STYRDLRKGVYVPYT
K136 YVPYTQGKWEGELGT
S243-p IIGGIDHsLyTGSLW
Y245-p GGIDHsLyTGSLWYT
Y260 PIRREWYYEVIIVRV
K275 EINGQDLKMDCKEYN
K279 QDLKMDCKEYNYDKS
K285 CKEYNYDKSIVDSGT
K299 TTNLRLPKKVFEAAV
K300 TNLRLPKKVFEAAVK
K307 KVFEAAVKSIKAASS
S308 VFEAAVKSIKAASST
S498-p DDFADDIsLLK____
K501 ADDIsLLK_______
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