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Q9Y5Z0

- BACE2_HUMAN

UniProt

Q9Y5Z0 - BACE2_HUMAN

Protein

Beta-secretase 2

Gene

BACE2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    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 672.5 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei110 – 1101
    Active sitei303 – 3031

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. membrane protein ectodomain proteolysis Source: UniProtKB
    2. negative regulation of amyloid precursor protein biosynthetic process Source: UniProtKB
    3. peptide hormone processing Source: UniProtKB
    4. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BioCyciMetaCyc:G66-33964-MONOMER.
    BRENDAi3.4.23.45. 2681.

    Protein family/group databases

    MEROPSiA01.041.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-secretase 2 (EC:3.4.23.45)
    Alternative name(s):
    Aspartic-like protease 56 kDa
    Aspartyl protease 1
    Short name:
    ASP1
    Short name:
    Asp 1
    Beta-site amyloid precursor protein cleaving enzyme 2
    Short name:
    Beta-site APP cleaving enzyme 2
    Down region aspartic protease
    Short name:
    DRAP
    Memapsin-1
    Membrane-associated aspartic protease 1
    Theta-secretase
    Gene namesi
    Name:BACE2
    Synonyms:AEPLC, ALP56, ASP21
    ORF Names:CDA13, UNQ418/PRO852
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:934. BACE2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: UniProtKB-SubCell
    3. endosome Source: UniProtKB-SubCell
    4. Golgi apparatus Source: UniProtKB
    5. integral component of membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi110 – 1101D → A or N: Loss of autoproteolytic cleavage. 2 Publications
    Mutagenesisi303 – 3031D → A: Loss of autoproteolytic cleavage. 1 Publication

    Organism-specific databases

    PharmGKBiPA25233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 62425 PublicationsPRO_0000025945Add
    BLAST
    Chaini63 – 518456Beta-secretase 2PRO_0000025946Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi233 ↔ 4331 Publication
    Disulfide bondi292 ↔ 4571 Publication
    Disulfide bondi344 ↔ 3931 Publication
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Undergoes autoproteolytic cleavage.
    Glycosylated.2 Publications

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ9Y5Z0.
    PaxDbiQ9Y5Z0.
    PRIDEiQ9Y5Z0.

    PTM databases

    PhosphoSiteiQ9Y5Z0.

    Miscellaneous databases

    PMAP-CutDBQ9Y5Z0.

    Expressioni

    Tissue specificityi

    Brain. Present in neurons within the hippocampus, frontal cortex and temporal cortex (at protein level). Expressed at low levels in most peripheral tissues and at higher levels in colon, kidney, pancreas, placenta, prostate, stomach and trachea. Expressed at low levels in the brain. Found in spinal cord, medulla oblongata, substantia nigra and locus coruleus. Expressed in the ductal epithelium of both normal and malignant prostate.7 Publications

    Inductioni

    Up-regulated in primary breast and colon tumors and liver metastasis.1 Publication

    Gene expression databases

    BgeeiQ9Y5Z0.
    CleanExiHS_BACE2.
    GenevestigatoriQ9Y5Z0.

    Organism-specific databases

    HPAiCAB008975.

    Interactioni

    Subunit structurei

    Monomer. Interacts ith RTN3 and RTN4.2 Publications

    Protein-protein interaction databases

    BioGridi117353. 3 interactions.
    STRINGi9606.ENSP00000332979.

    Structurei

    Secondary structure

    1
    518
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi78 – 803
    Beta strandi84 – 874
    Helixi88 – 903
    Beta strandi91 – 988
    Turni99 – 1024
    Beta strandi103 – 1108
    Beta strandi116 – 1194
    Helixi132 – 1343
    Beta strandi139 – 14911
    Beta strandi152 – 16413
    Turni166 – 1683
    Beta strandi173 – 18513
    Beta strandi194 – 1985
    Helixi202 – 2043
    Beta strandi205 – 2073
    Helixi214 – 2229
    Beta strandi228 – 2325
    Beta strandi247 – 2537
    Helixi256 – 2583
    Beta strandi264 – 2674
    Turni271 – 2744
    Beta strandi278 – 2836
    Helixi292 – 2954
    Beta strandi300 – 3023
    Beta strandi308 – 3125
    Helixi313 – 32614
    Beta strandi327 – 3293
    Helixi334 – 3374
    Helixi339 – 3424
    Beta strandi343 – 3464
    Helixi347 – 3493
    Helixi352 – 3543
    Beta strandi358 – 3636
    Beta strandi369 – 3757
    Helixi377 – 3804
    Beta strandi381 – 3844
    Beta strandi391 – 40313
    Beta strandi405 – 4073
    Helixi409 – 4124
    Beta strandi415 – 4206
    Turni421 – 4244
    Beta strandi425 – 4306
    Beta strandi435 – 4384
    Beta strandi439 – 44911
    Beta strandi451 – 4533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EWYX-ray3.10A/B/C/D78-460[»]
    3ZKGX-ray1.90A/B75-460[»]
    3ZKIX-ray2.40A/B75-460[»]
    3ZKMX-ray1.85A/B75-460[»]
    3ZKNX-ray2.00A/B75-460[»]
    3ZKQX-ray1.51A75-460[»]
    3ZKSX-ray2.11A75-460[»]
    3ZKXX-ray2.37A75-460[»]
    3ZL7X-ray3.20A75-460[»]
    3ZLQX-ray2.10A/B75-460[»]
    4BELX-ray1.85A/B75-460[»]
    4BFBX-ray2.21A/B75-460[»]
    ProteinModelPortaliQ9Y5Z0.
    SMRiQ9Y5Z0. Positions 76-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5Z0.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 473453ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini495 – 51824CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei474 – 49421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG267436.
    HOVERGENiHBG059578.
    InParanoidiQ9Y5Z0.
    KOiK07747.
    OMAiMEGFYVI.
    OrthoDBiEOG7DNNVW.
    PhylomeDBiQ9Y5Z0.
    TreeFamiTF329595.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR009119. Pept_A1_BACE.
    IPR009121. Pept_A1_BACE2.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 1 hit.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR01817. BACE2.
    PR01815. BACEFAMILY.
    PR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y5Z0-1) [UniParc]FASTAAdd to Basket

    Also known as: Isoform A

    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

    MGALARALLL PLLAQWLLRA APELAPAPFT LPLRVAAATN RVVAPTPGPG    50
    TPAERHADGL ALALEPALAS PAGAANFLAM VDNLQGDSGR GYYLEMLIGT 100
    PPQKLQILVD TGSSNFAVAG TPHSYIDTYF DTERSSTYRS KGFDVTVKYT 150
    QGSWTGFVGE DLVTIPKGFN TSFLVNIATI FESENFFLPG IKWNGILGLA 200
    YATLAKPSSS LETFFDSLVT QANIPNVFSM QMCGAGLPVA GSGTNGGSLV 250
    LGGIEPSLYK GDIWYTPIKE EWYYQIEILK LEIGGQSLNL DCREYNADKA 300
    IVDSGTTLLR LPQKVFDAVV EAVARASLIP EFSDGFWTGS QLACWTNSET 350
    PWSYFPKISI YLRDENSSRS FRITILPQLY IQPMMGAGLN YECYRFGISP 400
    STNALVIGAT VMEGFYVIFD RAQKRVGFAA SPCAEIAGAA VSEISGPFST 450
    EDVASNCVPA QSLSEPILWI VSYALMSVCG AILLVLIVLL LLPFRCQRRP 500
    RDPEVVNDES SLVRHRWK 518
    Length:518
    Mass (Da):56,180
    Last modified:November 1, 1999 - v1
    Checksum:i2E903150823760D3
    GO
    Isoform 2 (identifier: Q9Y5Z0-2) [UniParc]FASTAAdd to Basket

    Also known as: Isoform C

    The sequence of this isoform differs from the canonical sequence as follows:
         329-378: Missing.

    Show »
    Length:468
    Mass (Da):50,325
    Checksum:i717E0920126A0142
    GO
    Isoform 3 (identifier: Q9Y5Z0-3) [UniParc]FASTAAdd to Basket

    Also known as: Isoform B

    The sequence of this isoform differs from the canonical sequence as follows:
         379-396: LYIQPMMGAGLNYECYRF → KLQVLQCLKFPGLSQQRM
         397-518: Missing.

    Show »
    Length:396
    Mass (Da):42,985
    Checksum:iEDB3A7AF391CEACA
    GO
    Isoform 4 (identifier: Q9Y5Z0-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: Missing.

    Show »
    Length:439
    Mass (Da):48,275
    Checksum:i02EC0E0E50F11602
    GO
    Isoform 5 (identifier: Q9Y5Z0-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Show »
    Length:423
    Mass (Da):46,476
    Checksum:i675FBF380B57CE7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361A → T in AAF13714. (PubMed:10677483)Curated
    Sequence conflicti184 – 1841E → G in BAC11682. (PubMed:14702039)Curated
    Sequence conflicti192 – 1921K → Q in BAC11682. (PubMed:14702039)Curated
    Sequence conflicti233 – 2331C → R in BAC11682. (PubMed:14702039)Curated
    Isoform 3 (identifier: Q9Y5Z0-3)
    Sequence conflicti381 – 3811Q → R in AAF35836. (PubMed:10965118)Curated
    Sequence conflicti396 – 3961M → F in AAF35836. (PubMed:10965118)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9595Missing in isoform 5. 1 PublicationVSP_038023Add
    BLAST
    Alternative sequencei1 – 7979Missing in isoform 4. 1 PublicationVSP_038024Add
    BLAST
    Alternative sequencei329 – 37850Missing in isoform 2. 1 PublicationVSP_038025Add
    BLAST
    Alternative sequencei379 – 39618LYIQP…ECYRF → KLQVLQCLKFPGLSQQRM in isoform 3. 1 PublicationVSP_038026Add
    BLAST
    Alternative sequencei397 – 518122Missing in isoform 3. 1 PublicationVSP_038027Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200342 mRNA. Translation: AAF17078.1.
    AF117892 mRNA. Translation: AAD45240.1.
    AF178532 mRNA. Translation: AAF29494.1.
    AF188276 mRNA. Translation: AAF35835.1.
    AF188277 mRNA. Translation: AAF35836.1.
    AF050171 mRNA. Translation: AAD45963.1.
    AF204944 mRNA. Translation: AAF26368.1.
    AF200192 mRNA. Translation: AAF13714.1.
    AF212252 mRNA. Translation: AAG41783.1.
    AY358927 mRNA. Translation: AAQ89286.1.
    AK075539 mRNA. Translation: BAC11682.1.
    AK292056 mRNA. Translation: BAF84745.1.
    AL163284 Genomic DNA. Translation: CAB90458.1.
    AL163285 Genomic DNA. Translation: CAB90554.1.
    CH471079 Genomic DNA. Translation: EAX09611.1.
    CH471079 Genomic DNA. Translation: EAX09613.1.
    BC014453 mRNA. Translation: AAH14453.1.
    AY769996 Genomic DNA. Translation: AAX14808.1.
    CCDSiCCDS13668.1. [Q9Y5Z0-1]
    CCDS13669.1. [Q9Y5Z0-2]
    CCDS13670.1. [Q9Y5Z0-3]
    RefSeqiNP_036237.2. NM_012105.4. [Q9Y5Z0-1]
    NP_620476.1. NM_138991.2. [Q9Y5Z0-2]
    NP_620477.1. NM_138992.2. [Q9Y5Z0-3]
    UniGeneiHs.43047.
    Hs.529408.

    Genome annotation databases

    EnsembliENST00000328735; ENSP00000333854; ENSG00000182240. [Q9Y5Z0-3]
    ENST00000330333; ENSP00000332979; ENSG00000182240. [Q9Y5Z0-1]
    ENST00000347667; ENSP00000327528; ENSG00000182240. [Q9Y5Z0-2]
    GeneIDi25825.
    KEGGihsa:25825.
    UCSCiuc002yyw.3. human. [Q9Y5Z0-1]
    uc002yyx.3. human. [Q9Y5Z0-2]
    uc002yyy.3. human. [Q9Y5Z0-3]

    Polymorphism databases

    DMDMi6685260.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF200342 mRNA. Translation: AAF17078.1 .
    AF117892 mRNA. Translation: AAD45240.1 .
    AF178532 mRNA. Translation: AAF29494.1 .
    AF188276 mRNA. Translation: AAF35835.1 .
    AF188277 mRNA. Translation: AAF35836.1 .
    AF050171 mRNA. Translation: AAD45963.1 .
    AF204944 mRNA. Translation: AAF26368.1 .
    AF200192 mRNA. Translation: AAF13714.1 .
    AF212252 mRNA. Translation: AAG41783.1 .
    AY358927 mRNA. Translation: AAQ89286.1 .
    AK075539 mRNA. Translation: BAC11682.1 .
    AK292056 mRNA. Translation: BAF84745.1 .
    AL163284 Genomic DNA. Translation: CAB90458.1 .
    AL163285 Genomic DNA. Translation: CAB90554.1 .
    CH471079 Genomic DNA. Translation: EAX09611.1 .
    CH471079 Genomic DNA. Translation: EAX09613.1 .
    BC014453 mRNA. Translation: AAH14453.1 .
    AY769996 Genomic DNA. Translation: AAX14808.1 .
    CCDSi CCDS13668.1. [Q9Y5Z0-1 ]
    CCDS13669.1. [Q9Y5Z0-2 ]
    CCDS13670.1. [Q9Y5Z0-3 ]
    RefSeqi NP_036237.2. NM_012105.4. [Q9Y5Z0-1 ]
    NP_620476.1. NM_138991.2. [Q9Y5Z0-2 ]
    NP_620477.1. NM_138992.2. [Q9Y5Z0-3 ]
    UniGenei Hs.43047.
    Hs.529408.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EWY X-ray 3.10 A/B/C/D 78-460 [» ]
    3ZKG X-ray 1.90 A/B 75-460 [» ]
    3ZKI X-ray 2.40 A/B 75-460 [» ]
    3ZKM X-ray 1.85 A/B 75-460 [» ]
    3ZKN X-ray 2.00 A/B 75-460 [» ]
    3ZKQ X-ray 1.51 A 75-460 [» ]
    3ZKS X-ray 2.11 A 75-460 [» ]
    3ZKX X-ray 2.37 A 75-460 [» ]
    3ZL7 X-ray 3.20 A 75-460 [» ]
    3ZLQ X-ray 2.10 A/B 75-460 [» ]
    4BEL X-ray 1.85 A/B 75-460 [» ]
    4BFB X-ray 2.21 A/B 75-460 [» ]
    ProteinModelPortali Q9Y5Z0.
    SMRi Q9Y5Z0. Positions 76-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117353. 3 interactions.
    STRINGi 9606.ENSP00000332979.

    Chemistry

    BindingDBi Q9Y5Z0.
    ChEMBLi CHEMBL2111390.
    GuidetoPHARMACOLOGYi 2331.

    Protein family/group databases

    MEROPSi A01.041.

    PTM databases

    PhosphoSitei Q9Y5Z0.

    Polymorphism databases

    DMDMi 6685260.

    Proteomic databases

    MaxQBi Q9Y5Z0.
    PaxDbi Q9Y5Z0.
    PRIDEi Q9Y5Z0.

    Protocols and materials databases

    DNASUi 25825.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328735 ; ENSP00000333854 ; ENSG00000182240 . [Q9Y5Z0-3 ]
    ENST00000330333 ; ENSP00000332979 ; ENSG00000182240 . [Q9Y5Z0-1 ]
    ENST00000347667 ; ENSP00000327528 ; ENSG00000182240 . [Q9Y5Z0-2 ]
    GeneIDi 25825.
    KEGGi hsa:25825.
    UCSCi uc002yyw.3. human. [Q9Y5Z0-1 ]
    uc002yyx.3. human. [Q9Y5Z0-2 ]
    uc002yyy.3. human. [Q9Y5Z0-3 ]

    Organism-specific databases

    CTDi 25825.
    GeneCardsi GC21P042539.
    HGNCi HGNC:934. BACE2.
    HPAi CAB008975.
    MIMi 605668. gene.
    neXtProti NX_Q9Y5Z0.
    PharmGKBi PA25233.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG267436.
    HOVERGENi HBG059578.
    InParanoidi Q9Y5Z0.
    KOi K07747.
    OMAi MEGFYVI.
    OrthoDBi EOG7DNNVW.
    PhylomeDBi Q9Y5Z0.
    TreeFami TF329595.

    Enzyme and pathway databases

    BioCyci MetaCyc:G66-33964-MONOMER.
    BRENDAi 3.4.23.45. 2681.

    Miscellaneous databases

    ChiTaRSi BACE2. human.
    EvolutionaryTracei Q9Y5Z0.
    GeneWikii Beta-secretase_2.
    GenomeRNAii 25825.
    NextBioi 47099.
    PMAP-CutDB Q9Y5Z0.
    PROi Q9Y5Z0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y5Z0.
    CleanExi HS_BACE2.
    Genevestigatori Q9Y5Z0.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR009119. Pept_A1_BACE.
    IPR009121. Pept_A1_BACE2.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR01817. BACE2.
    PR01815. BACEFAMILY.
    PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, TISSUE SPECIFICITY.
    2. "Identification of a novel aspartic-like protease differentially expressed in human breast cancer cell lines."
      Xin H., Stephans J.C., Duan X., Harrowe G., Kim E., Grieshammer U., Kingsley C., Giese K.
      Biochim. Biophys. Acta 1501:125-137(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AUTOCATALYTIC CLEAVAGE, INDUCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-110 AND ASP-303.
      Tissue: Bone marrow.
    3. "A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase."
      Solans A., Estivill X., de La Luna S.
      Cytogenet. Cell Genet. 89:177-184(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
    4. "The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region."
      Acquati F., Accarino M.P., Nucci C., Fumagalli P., Jovine L., Ottolenghi S., Taramelli R.
      FEBS Lett. 468:59-64(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
    7. "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] (ISOFORM 1), TISSUE SPECIFICITY.
    8. Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Pheochromocytoma.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
      Tissue: Ovary and Stomach.
    11. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    13. "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 1).
      Tissue: Skin.
    14. "Distinct transcriptional regulation and function of the human BACE2 and BACE1 genes."
      Sun X., Wang Y., Qing H., Christensen M.A., Liu Y., Zhou W., Tong Y., Xiao C., Huang Y., Zhang S., Liu X., Song W.
      FASEB J. 19:739-749(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47, FUNCTION.
    15. "BACE2 functions as an alternative alpha-secretase in cells."
      Yan R., Munzner J.B., Shuck M.E., Bienkowski M.J.
      J. Biol. Chem. 276:34019-34027(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, AUTOCATALYTIC CLEAVAGE, FUNCTION, SUBCELLULAR LOCATION.
    16. "BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome."
      Sun X., He G., Song W.
      FASEB J. 20:1369-1376(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION.
    17. "Crystal structure of human BACE2 in complex with a hydroxyethylamine transition-state inhibitor."
      Ostermann N., Eder J., Eidhoff U., Zink F., Hassiepen U., Worpenberg S., Maibaum J., Simic O., Hommel U., Gerhartz B.
      J. Mol. Biol. 355:249-261(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 78-460, SUBUNIT, DISULFIDE BONDS.
    18. Cited for: AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF ASP-110.
    19. "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.

    Entry informationi

    Entry nameiBACE2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5Z0
    Secondary accession number(s): A8K7P1
    , Q5DIH8, Q8N2D4, Q9H2V8, Q9NZL1, Q9NZL2, Q9UJT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3