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P56817

- BACE1_HUMAN

UniProt

P56817 - BACE1_HUMAN

Protein

Beta-secretase 1

Gene

BACE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer amyloid precursor protein.

    Enzyme regulationi

    Inhibited by RTN3 and RTN4.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei93 – 931PROSITE-ProRule annotation
    Active sitei289 – 2891PROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB
    2. beta-amyloid binding Source: Alzheimers_University_of_Toronto
    3. beta-aspartyl-peptidase activity Source: ProtInc
    4. enzyme binding Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. beta-amyloid metabolic process Source: UniProtKB
    2. membrane protein ectodomain proteolysis Source: UniProtKB
    3. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000160610-MONOMER.
    BRENDAi3.4.23.46. 2681.
    SABIO-RKP56817.

    Protein family/group databases

    MEROPSiA01.004.
    TCDBi8.A.32.1.1. the -amyloid cleaving enzyme (bace1) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-secretase 1 (EC:3.4.23.46)
    Alternative name(s):
    Aspartyl protease 2
    Short name:
    ASP2
    Short name:
    Asp 2
    Beta-site amyloid precursor protein cleaving enzyme 1
    Short name:
    Beta-site APP cleaving enzyme 1
    Memapsin-2
    Membrane-associated aspartic protease 2
    Gene namesi
    Name:BACE1
    Synonyms:BACE, KIAA1149
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:933. BACE1.

    Subcellular locationi

    Membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane
    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.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. cell surface Source: UniProtKB-SubCell
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. endosome Source: UniProtKB
    6. Golgi apparatus Source: UniProtKB
    7. integral component of membrane Source: UniProtKB
    8. integral component of plasma membrane Source: UniProtKB
    9. late endosome Source: UniProtKB
    10. multivesicular body Source: UniProtKB
    11. plasma membrane Source: UniProtKB
    12. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25232.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 45241 PublicationPRO_0000025939Add
    BLAST
    Chaini46 – 501456Beta-secretase 1PRO_0000025940Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysine2 Publications
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 4201 Publication
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Modified residuei275 – 2751N6-acetyllysine2 Publications
    Disulfide bondi278 ↔ 4431 Publication
    Modified residuei279 – 2791N6-acetyllysine2 Publications
    Modified residuei285 – 2851N6-acetyllysine2 Publications
    Modified residuei299 – 2991N6-acetyllysine2 Publications
    Modified residuei300 – 3001N6-acetyllysine2 Publications
    Modified residuei307 – 3071N6-acetyllysine2 Publications
    Disulfide bondi330 ↔ 3801 Publication
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-Glycosylated.2 Publications
    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.2 Publications

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP56817.
    PRIDEiP56817.

    PTM databases

    PhosphoSiteiP56817.

    Miscellaneous databases

    PMAP-CutDBP56817.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata.2 Publications

    Gene expression databases

    ArrayExpressiP56817.
    BgeeiP56817.
    CleanExiHS_BACE1.
    GenevestigatoriP56817.

    Organism-specific databases

    HPAiCAB016358.

    Interactioni

    Subunit structurei

    Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Interacts with SNX6. Interacts with PCSK9. Interacts with NAT8 and NAT8B.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLOT2Q142542EBI-2433139,EBI-348613

    Protein-protein interaction databases

    BioGridi117154. 7 interactions.
    DIPiDIP-41388N.
    IntActiP56817. 6 interactions.
    MINTiMINT-242532.
    STRINGi9606.ENSP00000318585.

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi61 – 633
    Beta strandi67 – 704
    Turni71 – 733
    Beta strandi75 – 817
    Turni82 – 854
    Beta strandi86 – 938
    Beta strandi99 – 1024
    Beta strandi109 – 1113
    Helixi115 – 1173
    Beta strandi122 – 13110
    Beta strandi132 – 1343
    Beta strandi136 – 14712
    Beta strandi151 – 1533
    Beta strandi155 – 16814
    Turni172 – 1743
    Beta strandi178 – 1814
    Helixi185 – 1873
    Beta strandi188 – 1903
    Helixi197 – 2048
    Beta strandi211 – 2155
    Helixi224 – 2296
    Beta strandi230 – 23910
    Helixi242 – 2443
    Beta strandi245 – 2539
    Turni257 – 2604
    Beta strandi264 – 2696
    Helixi278 – 2825
    Beta strandi286 – 2883
    Beta strandi294 – 2985
    Helixi299 – 31214
    Turni313 – 3153
    Helixi320 – 3234
    Beta strandi329 – 3324
    Turni333 – 3353
    Helixi338 – 3403
    Beta strandi344 – 3496
    Beta strandi355 – 3617
    Helixi363 – 3664
    Beta strandi367 – 3693
    Helixi373 – 3753
    Beta strandi378 – 3836
    Beta strandi385 – 3906
    Beta strandi392 – 3943
    Helixi396 – 3994
    Beta strandi402 – 4076
    Turni408 – 4114
    Beta strandi412 – 4187
    Beta strandi430 – 4367
    Helixi440 – 4434

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FKNX-ray1.90A/B56-446[»]
    1M4HX-ray2.10A/B56-446[»]
    1PY1X-ray2.60E/F/G/H494-501[»]
    1SGZX-ray2.00A/B/C/D58-446[»]
    1TQFX-ray1.80A43-446[»]
    1UJJX-ray2.60C490-501[»]
    1UJKX-ray1.90C/D490-501[»]
    1W50X-ray1.75A43-453[»]
    1W51X-ray2.55A43-453[»]
    1XN2X-ray1.90A/B/C/D58-446[»]
    1XN3X-ray2.00A/B/C/D58-446[»]
    1XS7X-ray2.80D58-446[»]
    1YM2X-ray2.05A/B/C48-447[»]
    1YM4X-ray2.25A/B/C48-453[»]
    2B8LX-ray1.70A43-446[»]
    2B8VX-ray1.80A43-446[»]
    2F3EX-ray2.11A/B/C48-447[»]
    2F3FX-ray2.30A/B/C48-447[»]
    2FDPX-ray2.50A/B/C59-446[»]
    2G94X-ray1.86A/B/C/D58-446[»]
    2HIZX-ray2.50A/B/C14-453[»]
    2HM1X-ray2.20A57-453[»]
    2IQGX-ray1.70A57-453[»]
    2IRZX-ray1.80A43-446[»]
    2IS0X-ray2.20A43-446[»]
    2NTRX-ray1.80A43-446[»]
    2OAHX-ray1.80A43-446[»]
    2OF0X-ray2.25A45-446[»]
    2OHKX-ray2.20A45-446[»]
    2OHLX-ray2.65A45-446[»]
    2OHMX-ray2.70A45-446[»]
    2OHNX-ray2.15A45-446[»]
    2OHPX-ray2.25A45-446[»]
    2OHQX-ray2.10A45-446[»]
    2OHRX-ray2.25A45-446[»]
    2OHSX-ray2.45A45-446[»]
    2OHTX-ray2.30A45-446[»]
    2OHUX-ray2.35A45-446[»]
    2P4JX-ray2.50A/B/C/D58-446[»]
    2P83X-ray2.50A/B/C14-446[»]
    2P8HX-ray1.80A43-446[»]
    2PH6X-ray2.00A43-446[»]
    2PH8X-ray1.70A43-446[»]
    2Q11X-ray2.40A/B/C59-446[»]
    2Q15X-ray2.40A62-446[»]
    2QK5X-ray2.20A/B55-447[»]
    2QMDX-ray1.65A/B55-447[»]
    2QMFX-ray1.75A/B55-447[»]
    2QMGX-ray1.89A/B55-447[»]
    2QP8X-ray1.50A/B55-447[»]
    2QU2X-ray2.60A46-454[»]
    2QU3X-ray2.00A46-454[»]
    2QZKX-ray1.80A43-446[»]
    2QZLX-ray1.80A43-446[»]
    2VA5X-ray2.75A14-453[»]
    2VA6X-ray2.50A14-453[»]
    2VA7X-ray2.20A14-453[»]
    2VIEX-ray1.90A61-452[»]
    2VIJX-ray1.60A61-452[»]
    2VIYX-ray1.82A61-452[»]
    2VIZX-ray1.60A61-452[»]
    2VJ6X-ray1.80A61-452[»]
    2VJ7X-ray1.60A61-452[»]
    2VJ9X-ray1.60A61-452[»]
    2VKMX-ray2.05A/B/C/D58-446[»]
    2VNMX-ray1.79A61-452[»]
    2VNNX-ray1.87A61-452[»]
    2WEZX-ray1.70A61-452[»]
    2WF0X-ray1.60A61-452[»]
    2WF1X-ray1.60A61-452[»]
    2WF2X-ray1.80A61-452[»]
    2WF3X-ray2.08A61-452[»]
    2WF4X-ray1.80A61-452[»]
    2WJOX-ray2.50A58-460[»]
    2XFIX-ray1.73A61-452[»]
    2XFJX-ray1.80A61-452[»]
    2XFKX-ray1.80A61-452[»]
    2ZDZX-ray2.00A46-454[»]
    2ZE1X-ray2.20A46-454[»]
    2ZHRX-ray2.50A/B45-454[»]
    2ZHSX-ray2.70A45-454[»]
    2ZHTX-ray2.35A45-454[»]
    2ZHUX-ray2.40A45-454[»]
    2ZHVX-ray1.85A45-454[»]
    2ZJHX-ray2.60A43-446[»]
    2ZJIX-ray2.30A43-446[»]
    2ZJJX-ray2.20A43-446[»]
    2ZJKX-ray3.00A/B/C43-446[»]
    2ZJLX-ray2.10A43-446[»]
    2ZJMX-ray1.90A43-446[»]
    2ZJNX-ray2.70A43-446[»]
    3BRAX-ray2.30A46-454[»]
    3BUFX-ray2.30A46-454[»]
    3BUGX-ray2.50A46-454[»]
    3BUHX-ray2.30A46-454[»]
    3CIBX-ray1.72A/B58-447[»]
    3CICX-ray1.75A/B58-447[»]
    3CIDX-ray1.80A/B58-447[»]
    3CKPX-ray2.30A/B/C43-454[»]
    3CKRX-ray2.70A/B/C43-454[»]
    3DM6X-ray2.60A/B/C42-446[»]
    3DUYX-ray1.97A/B/C48-447[»]
    3DV1X-ray2.10A/B/C48-447[»]
    3DV5X-ray2.10A/B/C48-447[»]
    3EXOX-ray2.10A43-454[»]
    3FKTX-ray1.90A43-446[»]
    3H0BX-ray2.70A/B/C43-446[»]
    3HVGX-ray2.26A/B/C46-453[»]
    3HW1X-ray2.48A/B/C46-453[»]
    3I25X-ray2.10A/B/C42-446[»]
    3IGBX-ray2.24A46-454[»]
    3IN3X-ray2.00A46-454[»]
    3IN4X-ray2.30A46-454[»]
    3INDX-ray2.25A46-454[»]
    3INEX-ray2.00A46-454[»]
    3INFX-ray1.85A46-454[»]
    3INHX-ray1.80A46-454[»]
    3IVHX-ray1.80A57-453[»]
    3IVIX-ray2.20A/B/C57-453[»]
    3IXJX-ray2.20A/B/C59-446[»]
    3IXKX-ray2.50A/B/C42-446[»]
    3K5CX-ray2.12A/B/C48-447[»]
    3K5DX-ray2.90A/B/C48-453[»]
    3K5FX-ray2.25A/B/C48-447[»]
    3K5GX-ray2.00A/B/C48-447[»]
    3KMXX-ray1.70A/B53-447[»]
    3KMYX-ray1.90A/B53-447[»]
    3KN0X-ray1.90A/B53-447[»]
    3KYRX-ray2.60A/B/C42-446[»]
    3L38X-ray2.10A46-454[»]
    3L3AX-ray2.36A46-454[»]
    3L58X-ray1.80A/B41-454[»]
    3L59X-ray2.00A/B41-454[»]
    3L5BX-ray1.80A/B41-454[»]
    3L5CX-ray1.80A/B41-454[»]
    3L5DX-ray1.75A/B41-454[»]
    3L5EX-ray1.53A/B41-454[»]
    3L5FX-ray1.70A/B41-454[»]
    3LHGX-ray2.10A46-454[»]
    3LNKX-ray1.80A/B53-447[»]
    3LPIX-ray2.05A/B14-454[»]
    3LPJX-ray1.79A/B14-454[»]
    3LPKX-ray1.93A/B14-454[»]
    3MSJX-ray1.80A/B/C43-453[»]
    3MSKX-ray2.00A48-453[»]
    3MSLX-ray2.40A48-453[»]
    3N4LX-ray2.70A/B/C57-453[»]
    3NSHX-ray2.20A/B/C57-453[»]
    3OHFX-ray2.10A/B14-454[»]
    3OHHX-ray2.01A/B14-454[»]
    3OOZX-ray1.80A46-454[»]
    3PI5X-ray2.40A/B/C48-447[»]
    3QBHX-ray2.24A/B/C48-447[»]
    3QI1X-ray2.30A57-453[»]
    3R1GX-ray2.80B57-453[»]
    3R2FX-ray2.53A/B/D/E14-454[»]
    3RSVX-ray2.50A43-453[»]
    3RSXX-ray2.48A43-453[»]
    3RTHX-ray2.70A43-453[»]
    3RTMX-ray2.76A43-453[»]
    3RTNX-ray2.70A43-453[»]
    3RU1X-ray2.30A43-453[»]
    3RVIX-ray2.65A43-453[»]
    3S2OX-ray2.60A48-453[»]
    3S7LX-ray2.16A46-454[»]
    3S7MX-ray2.20A46-454[»]
    3SKFX-ray3.00A/B14-454[»]
    3SKGX-ray2.88A/B/D/E14-454[»]
    3TPJX-ray1.61A43-454[»]
    3TPLX-ray2.50A/B/C43-454[»]
    3TPPX-ray1.60A43-454[»]
    3TPRX-ray2.55A43-454[»]
    3U6AX-ray2.20A/B/C58-446[»]
    3UDHX-ray1.70A58-453[»]
    3UDJX-ray1.80A58-453[»]
    3UDKX-ray2.51A58-453[»]
    3UDMX-ray1.94A58-453[»]
    3UDNX-ray2.19A58-453[»]
    3UDPX-ray1.95A58-453[»]
    3UDQX-ray2.73A58-453[»]
    3UDRX-ray1.95A58-453[»]
    3UDYX-ray2.00A58-453[»]
    3UFLX-ray1.90A58-446[»]
    3UQPX-ray1.77A43-454[»]
    3UQRX-ray3.06A/B/C43-454[»]
    3UQUX-ray1.70A43-454[»]
    3UQWX-ray2.20A43-454[»]
    3UQXX-ray1.70A43-454[»]
    3VEUX-ray1.52A48-447[»]
    3VF3X-ray1.48A48-447[»]
    3VG1X-ray1.77A48-447[»]
    3VV6X-ray2.05A43-454[»]
    3VV7X-ray2.10A43-454[»]
    3VV8X-ray2.50A43-454[»]
    3WB4X-ray2.25A43-454[»]
    3WB5X-ray2.50A43-454[»]
    3ZMGX-ray1.74A46-454[»]
    3ZOVX-ray2.10A46-454[»]
    4ACUX-ray1.75A43-453[»]
    4ACXX-ray2.00A43-453[»]
    4AZYX-ray1.79A43-453[»]
    4B00X-ray1.83A43-453[»]
    4B05X-ray1.80A43-453[»]
    4B0QX-ray1.87A62-445[»]
    4B1CX-ray1.95A58-445[»]
    4B1DX-ray1.95A58-445[»]
    4B1EX-ray1.95A58-445[»]
    4B70X-ray1.60A61-445[»]
    4B72X-ray1.60A58-445[»]
    4B77X-ray1.80A58-445[»]
    4B78X-ray1.50A62-445[»]
    4BEKX-ray2.39A46-454[»]
    4BFDX-ray2.30A46-454[»]
    4D83X-ray2.40A/B/C48-447[»]
    4D85X-ray2.65A48-453[»]
    4D88X-ray1.70A48-447[»]
    4D89X-ray1.65A48-447[»]
    4D8CX-ray2.07A/B/C48-447[»]
    4DH6X-ray2.50A43-453[»]
    4DI2X-ray2.00A/B/C43-453[»]
    4DJUX-ray1.80A/B41-454[»]
    4DJVX-ray1.73A/B41-454[»]
    4DJWX-ray1.90A/B41-454[»]
    4DJXX-ray1.50A/B41-454[»]
    4DJYX-ray1.86A/B41-454[»]
    4DPFX-ray1.80A57-446[»]
    4DPIX-ray1.90A57-446[»]
    4DUSX-ray2.50A43-453[»]
    4DV9X-ray2.08A43-454[»]
    4DVFX-ray1.80A/B43-454[»]
    4EWOX-ray1.80A61-446[»]
    4EXGX-ray1.80A61-446[»]
    4FCOX-ray1.76A43-454[»]
    4FGXX-ray1.59A43-454[»]
    4FM7X-ray1.56A58-453[»]
    4FM8X-ray1.90A58-453[»]
    4FRIX-ray2.30A43-453[»]
    4FRJX-ray1.95A43-453[»]
    4FRKX-ray2.10A43-453[»]
    4FRSX-ray1.70A/B53-447[»]
    4FS4X-ray1.74A/B58-447[»]
    4FSEX-ray2.65A/B/D/E14-454[»]
    4FSLX-ray2.50A/B/D/E43-453[»]
    4GIDX-ray2.00A/B/C/D59-446[»]
    4GMIX-ray1.80A57-446[»]
    4H1EX-ray1.90A/B41-454[»]
    4H3FX-ray1.70A/B41-454[»]
    4H3GX-ray1.85A/B41-454[»]
    4H3IX-ray1.96A/B41-454[»]
    4H3JX-ray1.60A/B41-454[»]
    4HA5X-ray1.83A/B41-454[»]
    4HZTX-ray1.80A57-453[»]
    4I0DX-ray1.91A57-453[»]
    4I0EX-ray1.70A57-453[»]
    4I0FX-ray1.80A57-453[»]
    4I0GX-ray1.78A57-453[»]
    4I0HX-ray2.20A/B/C57-453[»]
    4I0IX-ray2.20A/B/C57-453[»]
    4I0JX-ray1.99A57-453[»]
    4I0ZX-ray1.80A57-453[»]
    4I10X-ray2.07A57-453[»]
    4I11X-ray1.89A57-453[»]
    4I12X-ray1.78A57-453[»]
    4I1CX-ray2.00A57-453[»]
    4IVSX-ray2.64A43-454[»]
    4IVTX-ray1.60A43-454[»]
    4J0PX-ray1.97A46-454[»]
    4J0TX-ray2.05A46-454[»]
    4J0VX-ray1.94A46-454[»]
    4J0YX-ray1.77A46-454[»]
    4J0ZX-ray2.13A46-454[»]
    4J17X-ray1.81A46-454[»]
    4J1CX-ray2.01A46-454[»]
    4J1EX-ray1.78A46-454[»]
    4J1FX-ray2.25A46-454[»]
    4J1HX-ray2.20A46-454[»]
    4J1IX-ray2.05A46-454[»]
    4J1KX-ray2.18A46-454[»]
    4JOOX-ray1.80A57-453[»]
    4JP9X-ray1.80A57-453[»]
    4JPCX-ray1.80A57-453[»]
    4JPEX-ray1.80A57-453[»]
    4K8SX-ray2.39A/B/C59-446[»]
    4K9HX-ray2.29A/B/C59-446[»]
    4KE0X-ray2.30A/B/C43-453[»]
    4KE1X-ray1.91A43-453[»]
    4L7GX-ray1.38A57-453[»]
    4L7HX-ray1.85A57-453[»]
    4L7JX-ray1.65A57-453[»]
    4LC7X-ray1.70A57-453[»]
    4LXAX-ray1.95A/B/C48-447[»]
    4LXKX-ray2.05A/B/C48-447[»]
    4LXMX-ray2.30A/B/C48-447[»]
    4N00X-ray1.80A57-453[»]
    4PZWX-ray1.80A57-453[»]
    4PZXX-ray1.80A57-453[»]
    ProteinModelPortaliP56817.
    SMRiP56817. Positions 58-447.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56817.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 457436ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini479 – 50123CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei458 – 47821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni479 – 50123Interaction with RTN3Add
    BLAST

    Domaini

    The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71700.
    HOVERGENiHBG059578.
    KOiK04521.
    OMAiPDMEDCG.
    OrthoDBiEOG7DNNVW.
    PhylomeDBiP56817.
    TreeFamiTF329595.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR009119. Pept_A1_BACE.
    IPR009120. Pept_A1_BACE1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR01816. BACE1.
    PR01815. BACEFAMILY.
    PR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: P56817-1) [UniParc]FASTAAdd to Basket

    Also known as: BACE-1A, BAC-501

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE    50
    PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA 100
    VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH 150
    GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS 200
    LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW 250
    YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK 300
    VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG 350
    EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME 400
    GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT 450
    DESTLMTIAY VMAAICALFM LPLCLMVCQW CCLRCLRQQH DDFADDISLL 500
    K 501
    Length:501
    Mass (Da):55,711
    Last modified:May 18, 2010 - v2
    Checksum:i377CE4C838C09F05
    GO
    Isoform B (identifier: P56817-2) [UniParc]FASTAAdd to Basket

    Also known as: BACE-1B, BACE-I-476

    The sequence of this isoform differs from the canonical sequence as follows:
         190-214: Missing.

    Show »
    Length:476
    Mass (Da):52,855
    Checksum:i6C8C87F8B53FDF66
    GO
    Isoform C (identifier: P56817-3) [UniParc]FASTAAdd to Basket

    Also known as: BACE-1C, BACE-I-457

    The sequence of this isoform differs from the canonical sequence as follows:
         146-189: Missing.

    Show »
    Length:457
    Mass (Da):51,015
    Checksum:iC794C9A9F43397A2
    GO
    Isoform D (identifier: P56817-4) [UniParc]FASTAAdd to Basket

    Also known as: BACE-1D, BACE-I-432

    The sequence of this isoform differs from the canonical sequence as follows:
         146-189: Missing.
         190-214: Missing.

    Show »
    Length:432
    Mass (Da):48,159
    Checksum:i96FC81E6EC82A01B
    GO
    Isoform 5 (identifier: P56817-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
         21-120: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:401
    Mass (Da):44,964
    Checksum:iA8D5B1112614B521
    GO
    Isoform 6 (identifier: P56817-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
         21-120: Missing.
         190-214: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:376
    Mass (Da):42,107
    Checksum:i93E4D8C54F8E4716
    GO

    Sequence cautioni

    The sequence BAA86463.2 differs from that shown. Reason: Frameshift at position 34.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti265 – 2651V → A.1 Publication
    Corresponds to variant rs28989503 [ dbSNP | Ensembl ].
    VAR_060692
    Natural varianti481 – 4811C → R.12 Publications
    Corresponds to variant rs539765 [ dbSNP | Ensembl ].
    VAR_051509

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2020MAQAL…VLPAH → MVPFIYLQAHFTLCSGWSST in isoform 5 and isoform 6. CuratedVSP_047092Add
    BLAST
    Alternative sequencei21 – 120100Missing in isoform 5 and isoform 6. CuratedVSP_047093Add
    BLAST
    Alternative sequencei146 – 18944Missing in isoform C and isoform D. 2 PublicationsVSP_005222Add
    BLAST
    Alternative sequencei190 – 21425Missing in isoform B, isoform D and isoform 6. 2 PublicationsVSP_005223Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190725 mRNA. Translation: AAF04142.1.
    AF201468 mRNA. Translation: AAF18982.1.
    AF200343 mRNA. Translation: AAF17079.1.
    AF204943 mRNA. Translation: AAF26367.1.
    AF338816 mRNA. Translation: AAK38374.1.
    AF338817 mRNA. Translation: AAK38375.1.
    AB050436 mRNA. Translation: BAB40931.1.
    AB050437 mRNA. Translation: BAB40932.1.
    AB050438 mRNA. Translation: BAB40933.1.
    AB032975 mRNA. Translation: BAA86463.2. Frameshift.
    DQ007053 Genomic DNA. Translation: AAY16982.1.
    EF444940 Genomic DNA. Translation: ACA05927.1.
    AP000892 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67313.1.
    BC065492 mRNA. Translation: AAH65492.1.
    AF200193 mRNA. Translation: AAF13715.1.
    CCDSiCCDS44739.1. [P56817-2]
    CCDS44740.1. [P56817-3]
    CCDS44741.1. [P56817-4]
    CCDS55786.1. [P56817-6]
    CCDS55787.1. [P56817-5]
    CCDS8383.1. [P56817-1]
    PIRiA59090.
    RefSeqiNP_001193978.1. NM_001207049.1.
    NP_036236.1. NM_012104.4.
    NP_620427.1. NM_138971.3.
    NP_620428.1. NM_138972.3.
    NP_620429.1. NM_138973.3.
    UniGeneiHs.504003.

    Genome annotation databases

    EnsembliENST00000313005; ENSP00000318585; ENSG00000186318. [P56817-1]
    ENST00000392937; ENSP00000475405; ENSG00000186318. [P56817-5]
    ENST00000428381; ENSP00000402228; ENSG00000186318. [P56817-4]
    ENST00000445823; ENSP00000403685; ENSG00000186318. [P56817-3]
    ENST00000510630; ENSP00000422461; ENSG00000186318. [P56817-6]
    ENST00000513780; ENSP00000424536; ENSG00000186318. [P56817-2]
    GeneIDi23621.
    KEGGihsa:23621.
    UCSCiuc001pqw.3. human. [P56817-2]
    uc001pqx.3. human. [P56817-4]
    uc001pqy.3. human. [P56817-3]
    uc001pqz.3. human. [P56817-1]

    Polymorphism databases

    DMDMi296434407.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF190725 mRNA. Translation: AAF04142.1 .
    AF201468 mRNA. Translation: AAF18982.1 .
    AF200343 mRNA. Translation: AAF17079.1 .
    AF204943 mRNA. Translation: AAF26367.1 .
    AF338816 mRNA. Translation: AAK38374.1 .
    AF338817 mRNA. Translation: AAK38375.1 .
    AB050436 mRNA. Translation: BAB40931.1 .
    AB050437 mRNA. Translation: BAB40932.1 .
    AB050438 mRNA. Translation: BAB40933.1 .
    AB032975 mRNA. Translation: BAA86463.2 . Frameshift.
    DQ007053 Genomic DNA. Translation: AAY16982.1 .
    EF444940 Genomic DNA. Translation: ACA05927.1 .
    AP000892 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67313.1 .
    BC065492 mRNA. Translation: AAH65492.1 .
    AF200193 mRNA. Translation: AAF13715.1 .
    CCDSi CCDS44739.1. [P56817-2 ]
    CCDS44740.1. [P56817-3 ]
    CCDS44741.1. [P56817-4 ]
    CCDS55786.1. [P56817-6 ]
    CCDS55787.1. [P56817-5 ]
    CCDS8383.1. [P56817-1 ]
    PIRi A59090.
    RefSeqi NP_001193978.1. NM_001207049.1.
    NP_036236.1. NM_012104.4.
    NP_620427.1. NM_138971.3.
    NP_620428.1. NM_138972.3.
    NP_620429.1. NM_138973.3.
    UniGenei Hs.504003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FKN X-ray 1.90 A/B 56-446 [» ]
    1M4H X-ray 2.10 A/B 56-446 [» ]
    1PY1 X-ray 2.60 E/F/G/H 494-501 [» ]
    1SGZ X-ray 2.00 A/B/C/D 58-446 [» ]
    1TQF X-ray 1.80 A 43-446 [» ]
    1UJJ X-ray 2.60 C 490-501 [» ]
    1UJK X-ray 1.90 C/D 490-501 [» ]
    1W50 X-ray 1.75 A 43-453 [» ]
    1W51 X-ray 2.55 A 43-453 [» ]
    1XN2 X-ray 1.90 A/B/C/D 58-446 [» ]
    1XN3 X-ray 2.00 A/B/C/D 58-446 [» ]
    1XS7 X-ray 2.80 D 58-446 [» ]
    1YM2 X-ray 2.05 A/B/C 48-447 [» ]
    1YM4 X-ray 2.25 A/B/C 48-453 [» ]
    2B8L X-ray 1.70 A 43-446 [» ]
    2B8V X-ray 1.80 A 43-446 [» ]
    2F3E X-ray 2.11 A/B/C 48-447 [» ]
    2F3F X-ray 2.30 A/B/C 48-447 [» ]
    2FDP X-ray 2.50 A/B/C 59-446 [» ]
    2G94 X-ray 1.86 A/B/C/D 58-446 [» ]
    2HIZ X-ray 2.50 A/B/C 14-453 [» ]
    2HM1 X-ray 2.20 A 57-453 [» ]
    2IQG X-ray 1.70 A 57-453 [» ]
    2IRZ X-ray 1.80 A 43-446 [» ]
    2IS0 X-ray 2.20 A 43-446 [» ]
    2NTR X-ray 1.80 A 43-446 [» ]
    2OAH X-ray 1.80 A 43-446 [» ]
    2OF0 X-ray 2.25 A 45-446 [» ]
    2OHK X-ray 2.20 A 45-446 [» ]
    2OHL X-ray 2.65 A 45-446 [» ]
    2OHM X-ray 2.70 A 45-446 [» ]
    2OHN X-ray 2.15 A 45-446 [» ]
    2OHP X-ray 2.25 A 45-446 [» ]
    2OHQ X-ray 2.10 A 45-446 [» ]
    2OHR X-ray 2.25 A 45-446 [» ]
    2OHS X-ray 2.45 A 45-446 [» ]
    2OHT X-ray 2.30 A 45-446 [» ]
    2OHU X-ray 2.35 A 45-446 [» ]
    2P4J X-ray 2.50 A/B/C/D 58-446 [» ]
    2P83 X-ray 2.50 A/B/C 14-446 [» ]
    2P8H X-ray 1.80 A 43-446 [» ]
    2PH6 X-ray 2.00 A 43-446 [» ]
    2PH8 X-ray 1.70 A 43-446 [» ]
    2Q11 X-ray 2.40 A/B/C 59-446 [» ]
    2Q15 X-ray 2.40 A 62-446 [» ]
    2QK5 X-ray 2.20 A/B 55-447 [» ]
    2QMD X-ray 1.65 A/B 55-447 [» ]
    2QMF X-ray 1.75 A/B 55-447 [» ]
    2QMG X-ray 1.89 A/B 55-447 [» ]
    2QP8 X-ray 1.50 A/B 55-447 [» ]
    2QU2 X-ray 2.60 A 46-454 [» ]
    2QU3 X-ray 2.00 A 46-454 [» ]
    2QZK X-ray 1.80 A 43-446 [» ]
    2QZL X-ray 1.80 A 43-446 [» ]
    2VA5 X-ray 2.75 A 14-453 [» ]
    2VA6 X-ray 2.50 A 14-453 [» ]
    2VA7 X-ray 2.20 A 14-453 [» ]
    2VIE X-ray 1.90 A 61-452 [» ]
    2VIJ X-ray 1.60 A 61-452 [» ]
    2VIY X-ray 1.82 A 61-452 [» ]
    2VIZ X-ray 1.60 A 61-452 [» ]
    2VJ6 X-ray 1.80 A 61-452 [» ]
    2VJ7 X-ray 1.60 A 61-452 [» ]
    2VJ9 X-ray 1.60 A 61-452 [» ]
    2VKM X-ray 2.05 A/B/C/D 58-446 [» ]
    2VNM X-ray 1.79 A 61-452 [» ]
    2VNN X-ray 1.87 A 61-452 [» ]
    2WEZ X-ray 1.70 A 61-452 [» ]
    2WF0 X-ray 1.60 A 61-452 [» ]
    2WF1 X-ray 1.60 A 61-452 [» ]
    2WF2 X-ray 1.80 A 61-452 [» ]
    2WF3 X-ray 2.08 A 61-452 [» ]
    2WF4 X-ray 1.80 A 61-452 [» ]
    2WJO X-ray 2.50 A 58-460 [» ]
    2XFI X-ray 1.73 A 61-452 [» ]
    2XFJ X-ray 1.80 A 61-452 [» ]
    2XFK X-ray 1.80 A 61-452 [» ]
    2ZDZ X-ray 2.00 A 46-454 [» ]
    2ZE1 X-ray 2.20 A 46-454 [» ]
    2ZHR X-ray 2.50 A/B 45-454 [» ]
    2ZHS X-ray 2.70 A 45-454 [» ]
    2ZHT X-ray 2.35 A 45-454 [» ]
    2ZHU X-ray 2.40 A 45-454 [» ]
    2ZHV X-ray 1.85 A 45-454 [» ]
    2ZJH X-ray 2.60 A 43-446 [» ]
    2ZJI X-ray 2.30 A 43-446 [» ]
    2ZJJ X-ray 2.20 A 43-446 [» ]
    2ZJK X-ray 3.00 A/B/C 43-446 [» ]
    2ZJL X-ray 2.10 A 43-446 [» ]
    2ZJM X-ray 1.90 A 43-446 [» ]
    2ZJN X-ray 2.70 A 43-446 [» ]
    3BRA X-ray 2.30 A 46-454 [» ]
    3BUF X-ray 2.30 A 46-454 [» ]
    3BUG X-ray 2.50 A 46-454 [» ]
    3BUH X-ray 2.30 A 46-454 [» ]
    3CIB X-ray 1.72 A/B 58-447 [» ]
    3CIC X-ray 1.75 A/B 58-447 [» ]
    3CID X-ray 1.80 A/B 58-447 [» ]
    3CKP X-ray 2.30 A/B/C 43-454 [» ]
    3CKR X-ray 2.70 A/B/C 43-454 [» ]
    3DM6 X-ray 2.60 A/B/C 42-446 [» ]
    3DUY X-ray 1.97 A/B/C 48-447 [» ]
    3DV1 X-ray 2.10 A/B/C 48-447 [» ]
    3DV5 X-ray 2.10 A/B/C 48-447 [» ]
    3EXO X-ray 2.10 A 43-454 [» ]
    3FKT X-ray 1.90 A 43-446 [» ]
    3H0B X-ray 2.70 A/B/C 43-446 [» ]
    3HVG X-ray 2.26 A/B/C 46-453 [» ]
    3HW1 X-ray 2.48 A/B/C 46-453 [» ]
    3I25 X-ray 2.10 A/B/C 42-446 [» ]
    3IGB X-ray 2.24 A 46-454 [» ]
    3IN3 X-ray 2.00 A 46-454 [» ]
    3IN4 X-ray 2.30 A 46-454 [» ]
    3IND X-ray 2.25 A 46-454 [» ]
    3INE X-ray 2.00 A 46-454 [» ]
    3INF X-ray 1.85 A 46-454 [» ]
    3INH X-ray 1.80 A 46-454 [» ]
    3IVH X-ray 1.80 A 57-453 [» ]
    3IVI X-ray 2.20 A/B/C 57-453 [» ]
    3IXJ X-ray 2.20 A/B/C 59-446 [» ]
    3IXK X-ray 2.50 A/B/C 42-446 [» ]
    3K5C X-ray 2.12 A/B/C 48-447 [» ]
    3K5D X-ray 2.90 A/B/C 48-453 [» ]
    3K5F X-ray 2.25 A/B/C 48-447 [» ]
    3K5G X-ray 2.00 A/B/C 48-447 [» ]
    3KMX X-ray 1.70 A/B 53-447 [» ]
    3KMY X-ray 1.90 A/B 53-447 [» ]
    3KN0 X-ray 1.90 A/B 53-447 [» ]
    3KYR X-ray 2.60 A/B/C 42-446 [» ]
    3L38 X-ray 2.10 A 46-454 [» ]
    3L3A X-ray 2.36 A 46-454 [» ]
    3L58 X-ray 1.80 A/B 41-454 [» ]
    3L59 X-ray 2.00 A/B 41-454 [» ]
    3L5B X-ray 1.80 A/B 41-454 [» ]
    3L5C X-ray 1.80 A/B 41-454 [» ]
    3L5D X-ray 1.75 A/B 41-454 [» ]
    3L5E X-ray 1.53 A/B 41-454 [» ]
    3L5F X-ray 1.70 A/B 41-454 [» ]
    3LHG X-ray 2.10 A 46-454 [» ]
    3LNK X-ray 1.80 A/B 53-447 [» ]
    3LPI X-ray 2.05 A/B 14-454 [» ]
    3LPJ X-ray 1.79 A/B 14-454 [» ]
    3LPK X-ray 1.93 A/B 14-454 [» ]
    3MSJ X-ray 1.80 A/B/C 43-453 [» ]
    3MSK X-ray 2.00 A 48-453 [» ]
    3MSL X-ray 2.40 A 48-453 [» ]
    3N4L X-ray 2.70 A/B/C 57-453 [» ]
    3NSH X-ray 2.20 A/B/C 57-453 [» ]
    3OHF X-ray 2.10 A/B 14-454 [» ]
    3OHH X-ray 2.01 A/B 14-454 [» ]
    3OOZ X-ray 1.80 A 46-454 [» ]
    3PI5 X-ray 2.40 A/B/C 48-447 [» ]
    3QBH X-ray 2.24 A/B/C 48-447 [» ]
    3QI1 X-ray 2.30 A 57-453 [» ]
    3R1G X-ray 2.80 B 57-453 [» ]
    3R2F X-ray 2.53 A/B/D/E 14-454 [» ]
    3RSV X-ray 2.50 A 43-453 [» ]
    3RSX X-ray 2.48 A 43-453 [» ]
    3RTH X-ray 2.70 A 43-453 [» ]
    3RTM X-ray 2.76 A 43-453 [» ]
    3RTN X-ray 2.70 A 43-453 [» ]
    3RU1 X-ray 2.30 A 43-453 [» ]
    3RVI X-ray 2.65 A 43-453 [» ]
    3S2O X-ray 2.60 A 48-453 [» ]
    3S7L X-ray 2.16 A 46-454 [» ]
    3S7M X-ray 2.20 A 46-454 [» ]
    3SKF X-ray 3.00 A/B 14-454 [» ]
    3SKG X-ray 2.88 A/B/D/E 14-454 [» ]
    3TPJ X-ray 1.61 A 43-454 [» ]
    3TPL X-ray 2.50 A/B/C 43-454 [» ]
    3TPP X-ray 1.60 A 43-454 [» ]
    3TPR X-ray 2.55 A 43-454 [» ]
    3U6A X-ray 2.20 A/B/C 58-446 [» ]
    3UDH X-ray 1.70 A 58-453 [» ]
    3UDJ X-ray 1.80 A 58-453 [» ]
    3UDK X-ray 2.51 A 58-453 [» ]
    3UDM X-ray 1.94 A 58-453 [» ]
    3UDN X-ray 2.19 A 58-453 [» ]
    3UDP X-ray 1.95 A 58-453 [» ]
    3UDQ X-ray 2.73 A 58-453 [» ]
    3UDR X-ray 1.95 A 58-453 [» ]
    3UDY X-ray 2.00 A 58-453 [» ]
    3UFL X-ray 1.90 A 58-446 [» ]
    3UQP X-ray 1.77 A 43-454 [» ]
    3UQR X-ray 3.06 A/B/C 43-454 [» ]
    3UQU X-ray 1.70 A 43-454 [» ]
    3UQW X-ray 2.20 A 43-454 [» ]
    3UQX X-ray 1.70 A 43-454 [» ]
    3VEU X-ray 1.52 A 48-447 [» ]
    3VF3 X-ray 1.48 A 48-447 [» ]
    3VG1 X-ray 1.77 A 48-447 [» ]
    3VV6 X-ray 2.05 A 43-454 [» ]
    3VV7 X-ray 2.10 A 43-454 [» ]
    3VV8 X-ray 2.50 A 43-454 [» ]
    3WB4 X-ray 2.25 A 43-454 [» ]
    3WB5 X-ray 2.50 A 43-454 [» ]
    3ZMG X-ray 1.74 A 46-454 [» ]
    3ZOV X-ray 2.10 A 46-454 [» ]
    4ACU X-ray 1.75 A 43-453 [» ]
    4ACX X-ray 2.00 A 43-453 [» ]
    4AZY X-ray 1.79 A 43-453 [» ]
    4B00 X-ray 1.83 A 43-453 [» ]
    4B05 X-ray 1.80 A 43-453 [» ]
    4B0Q X-ray 1.87 A 62-445 [» ]
    4B1C X-ray 1.95 A 58-445 [» ]
    4B1D X-ray 1.95 A 58-445 [» ]
    4B1E X-ray 1.95 A 58-445 [» ]
    4B70 X-ray 1.60 A 61-445 [» ]
    4B72 X-ray 1.60 A 58-445 [» ]
    4B77 X-ray 1.80 A 58-445 [» ]
    4B78 X-ray 1.50 A 62-445 [» ]
    4BEK X-ray 2.39 A 46-454 [» ]
    4BFD X-ray 2.30 A 46-454 [» ]
    4D83 X-ray 2.40 A/B/C 48-447 [» ]
    4D85 X-ray 2.65 A 48-453 [» ]
    4D88 X-ray 1.70 A 48-447 [» ]
    4D89 X-ray 1.65 A 48-447 [» ]
    4D8C X-ray 2.07 A/B/C 48-447 [» ]
    4DH6 X-ray 2.50 A 43-453 [» ]
    4DI2 X-ray 2.00 A/B/C 43-453 [» ]
    4DJU X-ray 1.80 A/B 41-454 [» ]
    4DJV X-ray 1.73 A/B 41-454 [» ]
    4DJW X-ray 1.90 A/B 41-454 [» ]
    4DJX X-ray 1.50 A/B 41-454 [» ]
    4DJY X-ray 1.86 A/B 41-454 [» ]
    4DPF X-ray 1.80 A 57-446 [» ]
    4DPI X-ray 1.90 A 57-446 [» ]
    4DUS X-ray 2.50 A 43-453 [» ]
    4DV9 X-ray 2.08 A 43-454 [» ]
    4DVF X-ray 1.80 A/B 43-454 [» ]
    4EWO X-ray 1.80 A 61-446 [» ]
    4EXG X-ray 1.80 A 61-446 [» ]
    4FCO X-ray 1.76 A 43-454 [» ]
    4FGX X-ray 1.59 A 43-454 [» ]
    4FM7 X-ray 1.56 A 58-453 [» ]
    4FM8 X-ray 1.90 A 58-453 [» ]
    4FRI X-ray 2.30 A 43-453 [» ]
    4FRJ X-ray 1.95 A 43-453 [» ]
    4FRK X-ray 2.10 A 43-453 [» ]
    4FRS X-ray 1.70 A/B 53-447 [» ]
    4FS4 X-ray 1.74 A/B 58-447 [» ]
    4FSE X-ray 2.65 A/B/D/E 14-454 [» ]
    4FSL X-ray 2.50 A/B/D/E 43-453 [» ]
    4GID X-ray 2.00 A/B/C/D 59-446 [» ]
    4GMI X-ray 1.80 A 57-446 [» ]
    4H1E X-ray 1.90 A/B 41-454 [» ]
    4H3F X-ray 1.70 A/B 41-454 [» ]
    4H3G X-ray 1.85 A/B 41-454 [» ]
    4H3I X-ray 1.96 A/B 41-454 [» ]
    4H3J X-ray 1.60 A/B 41-454 [» ]
    4HA5 X-ray 1.83 A/B 41-454 [» ]
    4HZT X-ray 1.80 A 57-453 [» ]
    4I0D X-ray 1.91 A 57-453 [» ]
    4I0E X-ray 1.70 A 57-453 [» ]
    4I0F X-ray 1.80 A 57-453 [» ]
    4I0G X-ray 1.78 A 57-453 [» ]
    4I0H X-ray 2.20 A/B/C 57-453 [» ]
    4I0I X-ray 2.20 A/B/C 57-453 [» ]
    4I0J X-ray 1.99 A 57-453 [» ]
    4I0Z X-ray 1.80 A 57-453 [» ]
    4I10 X-ray 2.07 A 57-453 [» ]
    4I11 X-ray 1.89 A 57-453 [» ]
    4I12 X-ray 1.78 A 57-453 [» ]
    4I1C X-ray 2.00 A 57-453 [» ]
    4IVS X-ray 2.64 A 43-454 [» ]
    4IVT X-ray 1.60 A 43-454 [» ]
    4J0P X-ray 1.97 A 46-454 [» ]
    4J0T X-ray 2.05 A 46-454 [» ]
    4J0V X-ray 1.94 A 46-454 [» ]
    4J0Y X-ray 1.77 A 46-454 [» ]
    4J0Z X-ray 2.13 A 46-454 [» ]
    4J17 X-ray 1.81 A 46-454 [» ]
    4J1C X-ray 2.01 A 46-454 [» ]
    4J1E X-ray 1.78 A 46-454 [» ]
    4J1F X-ray 2.25 A 46-454 [» ]
    4J1H X-ray 2.20 A 46-454 [» ]
    4J1I X-ray 2.05 A 46-454 [» ]
    4J1K X-ray 2.18 A 46-454 [» ]
    4JOO X-ray 1.80 A 57-453 [» ]
    4JP9 X-ray 1.80 A 57-453 [» ]
    4JPC X-ray 1.80 A 57-453 [» ]
    4JPE X-ray 1.80 A 57-453 [» ]
    4K8S X-ray 2.39 A/B/C 59-446 [» ]
    4K9H X-ray 2.29 A/B/C 59-446 [» ]
    4KE0 X-ray 2.30 A/B/C 43-453 [» ]
    4KE1 X-ray 1.91 A 43-453 [» ]
    4L7G X-ray 1.38 A 57-453 [» ]
    4L7H X-ray 1.85 A 57-453 [» ]
    4L7J X-ray 1.65 A 57-453 [» ]
    4LC7 X-ray 1.70 A 57-453 [» ]
    4LXA X-ray 1.95 A/B/C 48-447 [» ]
    4LXK X-ray 2.05 A/B/C 48-447 [» ]
    4LXM X-ray 2.30 A/B/C 48-447 [» ]
    4N00 X-ray 1.80 A 57-453 [» ]
    4PZW X-ray 1.80 A 57-453 [» ]
    4PZX X-ray 1.80 A 57-453 [» ]
    ProteinModelPortali P56817.
    SMRi P56817. Positions 58-447.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117154. 7 interactions.
    DIPi DIP-41388N.
    IntActi P56817. 6 interactions.
    MINTi MINT-242532.
    STRINGi 9606.ENSP00000318585.

    Chemistry

    BindingDBi P56817.
    ChEMBLi CHEMBL4822.
    GuidetoPHARMACOLOGYi 2330.

    Protein family/group databases

    MEROPSi A01.004.
    TCDBi 8.A.32.1.1. the -amyloid cleaving enzyme (bace1) family.

    PTM databases

    PhosphoSitei P56817.

    Polymorphism databases

    DMDMi 296434407.

    Proteomic databases

    PaxDbi P56817.
    PRIDEi P56817.

    Protocols and materials databases

    DNASUi 23621.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313005 ; ENSP00000318585 ; ENSG00000186318 . [P56817-1 ]
    ENST00000392937 ; ENSP00000475405 ; ENSG00000186318 . [P56817-5 ]
    ENST00000428381 ; ENSP00000402228 ; ENSG00000186318 . [P56817-4 ]
    ENST00000445823 ; ENSP00000403685 ; ENSG00000186318 . [P56817-3 ]
    ENST00000510630 ; ENSP00000422461 ; ENSG00000186318 . [P56817-6 ]
    ENST00000513780 ; ENSP00000424536 ; ENSG00000186318 . [P56817-2 ]
    GeneIDi 23621.
    KEGGi hsa:23621.
    UCSCi uc001pqw.3. human. [P56817-2 ]
    uc001pqx.3. human. [P56817-4 ]
    uc001pqy.3. human. [P56817-3 ]
    uc001pqz.3. human. [P56817-1 ]

    Organism-specific databases

    CTDi 23621.
    GeneCardsi GC11M117156.
    HGNCi HGNC:933. BACE1.
    HPAi CAB016358.
    MIMi 604252. gene.
    neXtProti NX_P56817.
    PharmGKBi PA25232.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG71700.
    HOVERGENi HBG059578.
    KOi K04521.
    OMAi PDMEDCG.
    OrthoDBi EOG7DNNVW.
    PhylomeDBi P56817.
    TreeFami TF329595.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000160610-MONOMER.
    BRENDAi 3.4.23.46. 2681.
    SABIO-RK P56817.

    Miscellaneous databases

    EvolutionaryTracei P56817.
    GeneWikii Beta-secretase_1.
    GenomeRNAii 23621.
    NextBioi 35501710.
    PMAP-CutDB P56817.
    PROi P56817.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56817.
    Bgeei P56817.
    CleanExi HS_BACE1.
    Genevestigatori P56817.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR009119. Pept_A1_BACE.
    IPR009120. Pept_A1_BACE1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR01816. BACE1.
    PR01815. BACEFAMILY.
    PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, CHARACTERIZATION, VARIANT ARG-481.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
    5. "New beta-site APP cleaving enzyme isoform (BACE-1B) obtained from human brain and pancreas."
      Michel B., De Pietri Tonelli D., Zacchetti D., Keller P.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT ARG-481.
      Tissue: Brain and Pancreas.
    6. "New beta-site APP cleaving enzyme isoform (BACE-1C) obtained from human pancreas."
      Zacchetti D., De Pietri Tonelli D., Schnurbus R.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), VARIANT ARG-481.
      Tissue: Pancreas.
    7. "Three novel alternatively spliced isoforms of the human beta-site amyloid precursor protein cleaving enzyme (BACE) and their effect on amyloid beta-peptide production."
      Tanahashi H., Tabira T.
      Neurosci. Lett. 307:9-12(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D), VARIANT ARG-481.
      Tissue: Brain.
    8. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
      Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
      DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ARG-481.
      Tissue: Brain.
    9. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    10. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-265 AND ARG-481.
    11. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-481.
    14. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ARG-481.
      Tissue: Lung.
    15. "Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein."
      Lin X., Koelsch G., Wu S., Downs D., Dashti A., Tang J.
      Proc. Natl. Acad. Sci. U.S.A. 97:1456-1460(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-501 (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, VARIANT ARG-481.
    16. Cited for: TISSUE SPECIFICITY, GLYCOSYLATION.
    17. "The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate."
      Yan R., Han P., Miao H., Greengard P., Xu H.
      J. Biol. Chem. 276:36788-36796(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DOMAIN.
    18. "The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity."
      Fischer F., Molinari M., Bodendorf U., Paganetti P.
      J. Neurochem. 80:1079-1088(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    19. "Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins."
      He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.
      Biochemistry 42:12174-12180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GGA1; GGA2 AND GGA3.
    20. "Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
      He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
      Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
    21. "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
      Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
      Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
    22. "Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
      He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
      J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTN3.
    23. "A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1."
      Costantini C., Ko M.H., Jonas M.C., Puglielli L.
      Biochem. J. 407:383-395(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307, GLYCOSYLATION.
    24. "PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1."
      Jonas M.C., Costantini C., Puglielli L.
      EMBO Rep. 9:916-922(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCSK9.
    25. "Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels."
      Ko M.H., Puglielli L.
      J. Biol. Chem. 284:2482-2492(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307 BY NAT8 AND NAT8B, DEACETYLATION, INTERACTION WITH NAT8 AND NAT8B.
    26. "Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing."
      Okada H., Zhang W., Peterhoff C., Hwang J.C., Nixon R.A., Ryu S.H., Kim T.W.
      FASEB J. 24:2783-2794(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNX6, SUBCELLULAR LOCATION.
    27. "Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor."
      Hong L., Koelsch G., Lin X., Wu S., Terzyan S., Ghosh A.K., Zhang X.C., Tang J.
      Science 290:150-153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
    28. "Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3."
      Hong L., Turner R.T. III, Koelsch G., Shin D., Ghosh A.K., Tang J.
      Biochemistry 41:10963-10967(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
    29. "Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis."
      Hong L., Tang J.
      Biochemistry 43:4689-4695(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
    30. "Apo and inhibitor complex structures of BACE (beta-secretase)."
      Patel S., Vuillard L., Cleasby A., Murray C.W., Yon J.
      J. Mol. Biol. 343:407-416(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-453 IN COMPLEX WITH SUBSTRATE ANALOG.
    31. "Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase)."
      Turner R.T. III, Hong L., Koelsch G., Ghosh A.K., Tang J.
      Biochemistry 44:105-112(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.

    Entry informationi

    Entry nameiBACE1_HUMAN
    AccessioniPrimary (citable) accession number: P56817
    Secondary accession number(s): A0M8W7
    , B0YIU9, E9PE65, H7BXJ9, Q9BYB9, Q9BYC0, Q9BYC1, Q9UJT5, Q9ULS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3