| Tag | Content |
|---|
| CPLM ID | CPLM-023947 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Beta-secretase 2 |
Protein Synonyms/Alias | Aspartic-like protease 56 kDa; Aspartyl protease 1; ASP1; Asp 1; Beta-site amyloid precursor protein cleaving enzyme 2; Beta-site APP cleaving enzyme 2; Down region aspartic protease; DRAP; Memapsin-1; Membrane-associated aspartic protease 1; Theta-secretase |
Gene Name | BACE2 |
Gene Synonyms/Alias | AEPLC; ALP56; ASP21; CDA13; UNQ418/PRO852 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 314 | TLLRLPQKVFDAVVE | ubiquitination | [1] |
|
Reference | [1] Global identification of modular cullin-RING ligase substrates. Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ. Cell. 2011 Oct 14;147(2):459-74. [ PMID: 21963094] |
Functional Description | Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading 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. It has also been shown that it can cleave APP between residues 671 and 672. |
Sequence Annotation | ACT_SITE 110 110
ACT_SITE 303 303
CARBOHYD 170 170 N-linked (GlcNAc...) (Potential).
CARBOHYD 366 366 N-linked (GlcNAc...) (Potential).
DISULFID 233 433
DISULFID 292 457
DISULFID 344 393 |
Keyword | 3D-structure; Alternative splicing; Aspartyl protease; Autocatalytic cleavage; Complete proteome; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome; Signal; Transmembrane; Transmembrane helix; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 518 AA |
Protein Sequence | MGALARALLL PLLAQWLLRA APELAPAPFT LPLRVAAATN RVVAPTPGPG TPAERHADGL 60
ALALEPALAS PAGAANFLAM VDNLQGDSGR GYYLEMLIGT PPQKLQILVD TGSSNFAVAG 120
TPHSYIDTYF DTERSSTYRS KGFDVTVKYT QGSWTGFVGE DLVTIPKGFN TSFLVNIATI 180
FESENFFLPG IKWNGILGLA YATLAKPSSS LETFFDSLVT QANIPNVFSM QMCGAGLPVA 240
GSGTNGGSLV LGGIEPSLYK GDIWYTPIKE EWYYQIEILK LEIGGQSLNL DCREYNADKA 300
IVDSGTTLLR LPQKVFDAVV EAVARASLIP EFSDGFWTGS QLACWTNSET PWSYFPKISI 360
YLRDENSSRS FRITILPQLY IQPMMGAGLN YECYRFGISP STNALVIGAT VMEGFYVIFD 420
RAQKRVGFAA SPCAEIAGAA VSEISGPFST EDVASNCVPA QSLSEPILWI VSYALMSVCG 480
AILLVLIVLL LLPFRCQRRP RDPEVVNDES SLVRHRWK 518 |
Gene Ontology | GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. GO:0005768; C:endosome; IEA:UniProtKB-SubCell. GO:0005794; C:Golgi apparatus; IDA:UniProtKB. GO:0016021; C:integral to membrane; NAS:UniProtKB. GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB. GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB. GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IMP:UniProtKB. GO:0016486; P:peptide hormone processing; NAS:UniProtKB. |
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PRINTS | |