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Q9Y5Z0

- BACE2_HUMAN

UniProt

Q9Y5Z0 - BACE2_HUMAN

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Protein
Beta-secretase 2
Gene
BACE2, AEPLC, ALP56, ASP21, CDA13, UNQ418/PRO852
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

Membrane; Single-pass type I membrane protein. Golgi apparatus. Endoplasmic reticulum. Endosome. Cell surface 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 473453Extracellular Reviewed prediction
Add
BLAST
Transmembranei474 – 49421Helical; Reviewed prediction
Add
BLAST
Topological domaini495 – 51824Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 – 2020 Reviewed prediction
Add
BLAST
Propeptidei21 – 6242
PRO_0000025945Add
BLAST
Chaini63 – 518456Beta-secretase 2
PRO_0000025946Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiQ9Y5Z0.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9595Missing in isoform 5.
VSP_038023Add
BLAST
Alternative sequencei1 – 7979Missing in isoform 4.
VSP_038024Add
BLAST
Alternative sequencei329 – 37850Missing in isoform 2.
VSP_038025Add
BLAST
Alternative sequencei379 – 39618LYIQP…ECYRF → KLQVLQCLKFPGLSQQRM in isoform 3.
VSP_038026Add
BLAST
Alternative sequencei397 – 518122Missing in isoform 3.
VSP_038027Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361A → T in AAF13714. 1 Publication
Sequence conflicti184 – 1841E → G in BAC11682. 1 Publication
Sequence conflicti192 – 1921K → Q in BAC11682. 1 Publication
Sequence conflicti233 – 2331C → R in BAC11682. 1 Publication
Isoform 3 (identifier: Q9Y5Z0-3)
Sequence conflicti381 – 3811Q → R in AAF35836. 1 Publication
Sequence conflicti396 – 3961M → F in AAF35836. 1 Publication

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...

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 139 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

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