Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y5Z0 (BACE2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:BACE2
Synonyms:AEPLC, ALP56, ASP21
ORF Names:CDA13, UNQ418/PRO852
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.14 Ref.15 Ref.16

Catalytic activity

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

Subunit structure

Monomer. Interacts ith RTN3 and RTN4. Ref.17 Ref.19

Subcellular location

Membrane; Single-pass type I membrane protein. Golgi apparatus. Endoplasmic reticulum. Endosome. Cell surface Ref.6 Ref.15.

Tissue specificity

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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7

Induction

Up-regulated in primary breast and colon tumors and liver metastasis. Ref.2

Post-translational modification

Undergoes autoproteolytic cleavage.

Glycosylated. Ref.4 Ref.6

Sequence similarities

Belongs to the peptidase A1 family.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y5Z0-1)

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.
Isoform 2 (identifier: Q9Y5Z0-2)

Also known as: Isoform C;

The sequence of this isoform differs from the canonical sequence as follows:
     329-378: Missing.
Isoform 3 (identifier: Q9Y5Z0-3)

Also known as: Isoform B;

The sequence of this isoform differs from the canonical sequence as follows:
     379-396: LYIQPMMGAGLNYECYRF → KLQVLQCLKFPGLSQQRM
     397-518: Missing.
Isoform 4 (identifier: Q9Y5Z0-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
Isoform 5 (identifier: Q9Y5Z0-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 6242
PRO_0000025945
Chain63 – 518456Beta-secretase 2
PRO_0000025946

Regions

Topological domain21 – 473453Extracellular Potential
Transmembrane474 – 49421Helical; Potential
Topological domain495 – 51824Cytoplasmic Potential

Sites

Active site1101
Active site3031

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...) Potential
Disulfide bond233 ↔ 433 Ref.17
Disulfide bond292 ↔ 457 Ref.17
Disulfide bond344 ↔ 393 Ref.17

Natural variations

Alternative sequence1 – 9595Missing in isoform 5.
VSP_038023
Alternative sequence1 – 7979Missing in isoform 4.
VSP_038024
Alternative sequence329 – 37850Missing in isoform 2.
VSP_038025
Alternative sequence379 – 39618LYIQP…ECYRF → KLQVLQCLKFPGLSQQRM in isoform 3.
VSP_038026
Alternative sequence397 – 518122Missing in isoform 3.
VSP_038027

Experimental info

Mutagenesis1101D → A or N: Loss of autoproteolytic cleavage. Ref.2 Ref.18
Mutagenesis3031D → A: Loss of autoproteolytic cleavage. Ref.2
Sequence conflict361A → T in AAF13714. Ref.7
Sequence conflict1841E → G in BAC11682. Ref.10
Sequence conflict1921K → Q in BAC11682. Ref.10
Sequence conflict2331C → R in BAC11682. Ref.10
Isoform 3:
Sequence conflict3811Q → R in AAF35836. Ref.3
Sequence conflict3961M → F in AAF35836. Ref.3

Secondary structure

.............................................................................. 518
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Isoform A) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 2E903150823760D3

FASTA51856,180
        10         20         30         40         50         60 
MGALARALLL PLLAQWLLRA APELAPAPFT LPLRVAAATN RVVAPTPGPG TPAERHADGL 

        70         80         90        100        110        120 
ALALEPALAS PAGAANFLAM VDNLQGDSGR GYYLEMLIGT PPQKLQILVD TGSSNFAVAG 

       130        140        150        160        170        180 
TPHSYIDTYF DTERSSTYRS KGFDVTVKYT QGSWTGFVGE DLVTIPKGFN TSFLVNIATI 

       190        200        210        220        230        240 
FESENFFLPG IKWNGILGLA YATLAKPSSS LETFFDSLVT QANIPNVFSM QMCGAGLPVA 

       250        260        270        280        290        300 
GSGTNGGSLV LGGIEPSLYK GDIWYTPIKE EWYYQIEILK LEIGGQSLNL DCREYNADKA 

       310        320        330        340        350        360 
IVDSGTTLLR LPQKVFDAVV EAVARASLIP EFSDGFWTGS QLACWTNSET PWSYFPKISI 

       370        380        390        400        410        420 
YLRDENSSRS FRITILPQLY IQPMMGAGLN YECYRFGISP STNALVIGAT VMEGFYVIFD 

       430        440        450        460        470        480 
RAQKRVGFAA SPCAEIAGAA VSEISGPFST EDVASNCVPA QSLSEPILWI VSYALMSVCG 

       490        500        510 
AILLVLIVLL LLPFRCQRRP RDPEVVNDES SLVRHRWK 

« Hide

Isoform 2 (Isoform C) [UniParc].

Checksum: 717E0920126A0142
Show »

FASTA46850,325
Isoform 3 (Isoform B) [UniParc].

Checksum: EDB3A7AF391CEACA
Show »

FASTA39642,985
Isoform 4 [UniParc].

Checksum: 02EC0E0E50F11602
Show »

FASTA43948,275
Isoform 5 [UniParc].

Checksum: 675FBF380B57CE7D
Show »

FASTA42346,476

References

« Hide 'large scale' references
[1]"Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity."
Yan R., Bienkowski M.J., Shuck M.E., Miao H., Tory M.C., Pauley A.M., Brashier J.R., Stratman N.C., Mathews W.R., Buhl A.E., Carter D.B., Tomasselli A.G., Parodi L.A., Heinrikson R.L., Gurney M.E.
Nature 402:533-537(1999) [PubMed] [Europe PMC] [Abstract]
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]"Expression analysis of BACE2 in brain and peripheral tissues."
Bennett B.D., Babu-Khan S., Loeloff R., Louis J.-C., Curran E., Citron M., Vassar R.
J. Biol. Chem. 275:20647-20651(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[6]"ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-secretase site."
Hussain I., Powell D.J., Howlett D.R., Chapman G.A., Gilmour L., Murdock P.R., Tew D.G., Meek T.D., Chapman C., Schneider K., Ratcliffe S.J., Tattersall D., Testa T.T., Southan C., Ryan D.M., Simmons D.L., Walsh F.S., Dingwall C., Christie G.
Mol. Cell. Neurosci. 16:609-619(2000) [PubMed] [Europe PMC] [Abstract]
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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Prodomain processing of Asp1 (BACE2) is autocatalytic."
Hussain I., Christie G., Schneider K., Moore S., Dingwall C.
J. Biol. Chem. 276:23322-23328(2001) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13668.1. [Q9Y5Z0-1]
CCDS13669.1. [Q9Y5Z0-2]
CCDS13670.1. [Q9Y5Z0-3]
RefSeqNP_036237.2. NM_012105.4. [Q9Y5Z0-1]
NP_620476.1. NM_138991.2. [Q9Y5Z0-2]
NP_620477.1. NM_138992.2. [Q9Y5Z0-3]
UniGeneHs.43047.
Hs.529408.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9Y5Z0.
SMRQ9Y5Z0. Positions 76-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117353. 3 interactions.
STRING9606.ENSP00000332979.

Chemistry

BindingDBQ9Y5Z0.
ChEMBLCHEMBL2111390.
GuidetoPHARMACOLOGY2331.

Protein family/group databases

MEROPSA01.041.

PTM databases

PhosphoSiteQ9Y5Z0.

Polymorphism databases

DMDM6685260.

Proteomic databases

MaxQBQ9Y5Z0.
PaxDbQ9Y5Z0.
PRIDEQ9Y5Z0.

Protocols and materials databases

DNASU25825.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328735; ENSP00000333854; ENSG00000182240. [Q9Y5Z0-3]
ENST00000330333; ENSP00000332979; ENSG00000182240. [Q9Y5Z0-1]
ENST00000347667; ENSP00000327528; ENSG00000182240. [Q9Y5Z0-2]
GeneID25825.
KEGGhsa:25825.
UCSCuc002yyw.3. human. [Q9Y5Z0-1]
uc002yyx.3. human. [Q9Y5Z0-2]
uc002yyy.3. human. [Q9Y5Z0-3]

Organism-specific databases

CTD25825.
GeneCardsGC21P042539.
HGNCHGNC:934. BACE2.
HPACAB008975.
MIM605668. gene.
neXtProtNX_Q9Y5Z0.
PharmGKBPA25233.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267436.
HOVERGENHBG059578.
InParanoidQ9Y5Z0.
KOK07747.
OMAMEGFYVI.
OrthoDBEOG7DNNVW.
PhylomeDBQ9Y5Z0.
TreeFamTF329595.

Enzyme and pathway databases

BioCycMetaCyc:G66-33964-MONOMER.
BRENDA3.4.23.45. 2681.

Gene expression databases

BgeeQ9Y5Z0.
CleanExHS_BACE2.
GenevestigatorQ9Y5Z0.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009121. Pept_A1_BACE2.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR01817. BACE2.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBACE2. human.
EvolutionaryTraceQ9Y5Z0.
GeneWikiBeta-secretase_2.
GenomeRNAi25825.
NextBio47099.
PMAP-CutDBQ9Y5Z0.
PROQ9Y5Z0.
SOURCESearch...

Entry information

Entry nameBACE2_HUMAN
AccessionPrimary (citable) accession number: Q9Y5Z0
Secondary accession number(s): A8K7P1 expand/collapse secondary AC list , Q5DIH8, Q8N2D4, Q9H2V8, Q9NZL1, Q9NZL2, Q9UJT6
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM