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UniProtKB/Swiss-Prot entry P56817


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BACE1_HUMAN
Primary accession number P56817
Secondary accession numbers B0YIU9 Q9BYB9 Q9BYC0 Q9BYC1 Q9UJT5 Q9ULS1
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 106)
Name and origin of the protein
Protein name Beta-secretase 1 [Precursor]
Synonyms EC 3.4.23.46
Beta-site amyloid precursor protein cleaving enzyme 1
Beta-site APP cleaving enzyme 1
Membrane-associated aspartic protease 2
Memapsin-2
Aspartyl protease 2
Asp 2
ASP2
Gene name
Name: BACE1
Synonyms: BACE, KIAA1149
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Brain;
DOI=10.1126/science.286.5440.735; PubMed=10531052 [NCBI, ExPASy, EBI, Israel, Japan]
Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A., Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y., Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A., Biere A.L., Curran E., Burgess T., Louis J.-C., Collins F., Treanor J., Rogers G., Citron M.;
"Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE.";
Science 286:735-741(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, AND CHARACTERIZATION.
TISSUE=Brain;
DOI=10.1038/990114; PubMed=10591214 [NCBI, ExPASy, EBI, Israel, Japan]
Sinha S., Anderson J.P., Barbour R., Basi G.S., Caccavello R., Davis D., Doan M., Dovey H.F., Frigon N., Hong J., Jacobson-Croak K., Jewett N., Keim P., Knops J., Lieberburg I., Power M., Tan H., Tatsuno G., Tung J., Schenk D., Seubert P., Suomensaari S.M., Wang S., Walker D., Zhao J., McConlogue L., Varghese J.;
"Purification and cloning of amyloid precursor protein beta-secretase from human brain.";
Nature 402:537-540(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
DOI=10.1038/990107; PubMed=10591213 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity.";
Nature 402:533-537(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
DOI=10.1006/mcne.1999.0811; PubMed=10656250 [NCBI, ExPASy, EBI, Israel, Japan]
Hussain I., Powell D.J., Howlett D.R., Tew D.G., Meek T.D., Chapman C., Gloger I.S., Murphy K.E., Southan C.D., Ryan D.M., Smith T.S., Simmons D.L., Walsh F.S., Dingwall C., Christie G.;
"Identification of a novel aspartic proteinase (Asp 2) as beta-secretase.";
Mol. Cell. Neurosci. 14:419-427(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Brain, and Pancreas;
Michel B., De Pietri Tonelli D., Zacchetti D., Keller P.;
"New beta-site APP cleaving enzyme isoform (BACE-1B) obtained from human brain and pancreas.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
TISSUE=Pancreas;
Zacchetti D., De Pietri Tonelli D., Schnurbus R.;
"New beta-site APP cleaving enzyme isoform (BACE-1C) obtained from human pancreas.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D).
TISSUE=Brain;
DOI=10.1016/S0304-3940(01)01912-7; PubMed=11516562 [NCBI, ExPASy, EBI, Israel, Japan]
Tanahashi H., Tabira T.;
"Three novel alternatively spliced isoforms of the human beta-site amyloid precursor protein cleaving enzyme (BACE) and their effect on amyloid beta-peptide production.";
Neurosci. Lett. 307:9-12(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Brain;
DOI=10.1093/dnares/6.5.329; PubMed=10574461 [NCBI, ExPASy, EBI, Israel, Japan]
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[9]
SEQUENCE REVISION.
DOI=10.1093/dnares/9.3.99; PubMed=12168954 [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT CYS-481.
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-501 (ISOFORM A), AND CHARACTERIZATION.
DOI=10.1073/pnas.97.4.1456; PubMed=10677483 [NCBI, ExPASy, EBI, Israel, Japan]
Lin X., Koelsch G., Wu S., Downs D., Dashti A., Tang J.;
"Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:1456-1460(2000).
[13]
DISULFIDE BONDS.
DOI=10.1046/j.0022-3042.2002.00806.x; PubMed=11953458 [NCBI, ExPASy, EBI, Israel, Japan]
Fischer F., Molinari M., Bodendorf U., Paganetti P.;
"The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity.";
J. Neurochem. 80:1079-1088(2002).
[14]
INTERACTION WITH GGA1; GGA2 AND GGA3.
DOI=10.1021/bi035199h; PubMed=14567678 [NCBI, ExPASy, EBI, Israel, Japan]
He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.;
"Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins.";
Biochemistry 42:12174-12180(2003).
[15]
INTERACTION WITH RTN3 AND RTN4, AND ENZYME REGULATION.
DOI=10.1038/nm1088; PubMed=15286784 [NCBI, ExPASy, EBI, Israel, Japan]
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
"Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation.";
Nat. Med. 10:959-965(2004).
[16]
INTERACTION WITH RTN3 AND RTN4, AND ENZYME REGULATION.
DOI=10.1111/j.1460-9568.2006.05005.x; PubMed=16965550 [NCBI, ExPASy, EBI, Israel, Japan]
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein.";
Eur. J. Neurosci. 24:1237-1244(2006).
[17]
INTERACTION WITH RTN3.
DOI=10.1016/j.jmb.2006.07.094; PubMed=16979658 [NCBI, ExPASy, EBI, Israel, Japan]
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
"Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins.";
J. Mol. Biol. 363:625-634(2006).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
DOI=10.1126/science.290.5489.150; PubMed=11021803 [NCBI, ExPASy, EBI, Israel, Japan]
Hong L., Koelsch G., Lin X., Wu S., Terzyan S., Ghosh A.K., Zhang X.C., Tang J.;
"Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.";
Science 290:150-153(2000).
[19]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
DOI=10.1021/bi026232n; PubMed=12206667 [NCBI, ExPASy, EBI, Israel, Japan]
Hong L., Turner R.T. III, Koelsch G., Shin D., Ghosh A.K., Tang J.;
"Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3.";
Biochemistry 41:10963-10967(2002).
[20]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
DOI=10.1021/bi0498252; PubMed=15096037 [NCBI, ExPASy, EBI, Israel, Japan]
Hong L., Tang J.;
"Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis.";
Biochemistry 43:4689-4695(2004).
[21]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-453 IN COMPLEX WITH SUBSTRATE ANALOG.
DOI=10.1016/j.jmb.2004.08.018; PubMed=15451669 [NCBI, ExPASy, EBI, Israel, Japan]
Patel S., Vuillard L., Cleasby A., Murray C.W., Yon J.;
"Apo and inhibitor complex structures of BACE (beta-secretase).";
J. Mol. Biol. 343:407-416(2004).
[22]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
DOI=10.1021/bi048106k; PubMed=15628850 [NCBI, ExPASy, EBI, Israel, Japan]
Turner R.T. III, Hong L., Koelsch G., Ghosh A.K., Tang J.;
"Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase).";
Biochemistry 44:105-112(2005).
Comments
  • FUNCTION: 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.
  • CATALYTIC ACTIVITY: Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.
  • ENZYME REGULATION: Inhibited by RTN3 and RTN4.
  • SUBUNIT: Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4.
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • ALTERNATIVE PRODUCTS: 4 named isoforms [FASTA] produced by alternative splicing.
    NameA
    SynonymsBACE-1A, BAC-501
    Isoform IDP56817-1
    This is the isoform sequence displayed in this entry.
    NameB
    SynonymsBACE-1B, BACE-I-476
    Isoform IDP56817-2
    Features which should be applied to build the isoform sequence: VSP_005223.
    NameC
    SynonymsBACE-1C, BACE-I-457
    Isoform IDP56817-3
    Features which should be applied to build the isoform sequence: VSP_005222.
    NameD
    SynonymsBACE-1D, BACE-I-432
    Isoform IDP56817-4
    Features which should be applied to build the isoform sequence: VSP_005222, VSP_005223.
  • TISSUE SPECIFICITY: Brain.
  • SIMILARITY: Belongs to the peptidase A1 family [view classification].
  • SEQUENCE CAUTION:
    • Sequence=BAA86463.2; Type=Frameshift; Positions=34;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF190725; AAF04142.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF201468; AAF18982.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200343; AAF17079.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF204943; AAF26367.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF338816; AAK38374.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF338817; AAK38375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050436; BAB40931.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050437; BAB40932.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050438; BAB40933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB032975; BAA86463.2; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF444940; ACA05927.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065492; AAH65492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200193; AAF13715.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00011518; -.
IPI00216209; -.
IPI00216210; -.
IPI00216211; -.
PIR A59090; A59090.
RefSeq NP_036236.1; -.
NP_620427.1; -.
NP_620428.1; -.
NP_620429.1; -.
UniGene Hs.504003
3D structure databases
PDB
1FKN; X-ray; 1.90 A; A/B=56-446.[ExPASy / RCSB / EBI]
1M4H; X-ray; 2.10 A; A/B=56-446.[ExPASy / RCSB / EBI]
1PY1; X-ray; 2.60 A; E/F/G/H=494-501.[ExPASy / RCSB / EBI]
1SGZ; X-ray; 2.00 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
1TQF; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
1UJJ; X-ray; 2.60 A; C=490-501.[ExPASy / RCSB / EBI]
1UJK; X-ray; 1.90 A; C/D=490-501.[ExPASy / RCSB / EBI]
1W50; X-ray; 1.75 A; A=43-453.[ExPASy / RCSB / EBI]
1W51; X-ray; 2.55 A; A=43-453.[ExPASy / RCSB / EBI]
1XN2; X-ray; 1.90 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
1XN3; X-ray; 2.00 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
1XS7; X-ray; 2.80 A; D=58-446.[ExPASy / RCSB / EBI]
1YM2; X-ray; 2.05 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
1YM4; X-ray; 2.25 A; A/B/C=48-453.[ExPASy / RCSB / EBI]
2B8L; X-ray; 1.70 A; A=43-446.[ExPASy / RCSB / EBI]
2B8V; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2F3E; X-ray; 2.11 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
2F3F; X-ray; 2.30 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
2FDP; X-ray; 2.50 A; A/B/C=59-446.[ExPASy / RCSB / EBI]
2G94; X-ray; 1.86 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
2HIZ; X-ray; 2.50 A; A/B/C=14-453.[ExPASy / RCSB / EBI]
2HM1; X-ray; 2.20 A; A=57-453.[ExPASy / RCSB / EBI]
2IQG; X-ray; 1.70 A; A=57-453.[ExPASy / RCSB / EBI]
2IRZ; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2IS0; X-ray; 2.20 A; A=43-446.[ExPASy / RCSB / EBI]
2NTR; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2OAH; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2OF0; X-ray; 2.25 A; A=45-446.[ExPASy / RCSB / EBI]
2OHK; X-ray; 2.20 A; A=45-446.[ExPASy / RCSB / EBI]
2OHL; X-ray; 2.65 A; A=45-446.[ExPASy / RCSB / EBI]
2OHM; X-ray; 2.70 A; A=45-446.[ExPASy / RCSB / EBI]
2OHN; X-ray; 2.15 A; A=45-446.[ExPASy / RCSB / EBI]
2OHP; X-ray; 2.25 A; A=45-446.[ExPASy / RCSB / EBI]
2OHQ; X-ray; 2.10 A; A=45-446.[ExPASy / RCSB / EBI]
2OHR; X-ray; 2.25 A; A=45-446.[ExPASy / RCSB / EBI]
2OHS; X-ray; 2.45 A; A=45-446.[ExPASy / RCSB / EBI]
2OHT; X-ray; 2.30 A; A=45-446.[ExPASy / RCSB / EBI]
2OHU; X-ray; 2.35 A; A=45-446.[ExPASy / RCSB / EBI]
2P4J; X-ray; 2.50 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
2P83; X-ray; 2.50 A; A/B/C=14-446.[ExPASy / RCSB / EBI]
2P8H; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2PH6; X-ray; 2.00 A; A=43-446.[ExPASy / RCSB / EBI]
2PH8; X-ray; 1.70 A; A=43-446.[ExPASy / RCSB / EBI]
2Q11; X-ray; 2.40 A; A/B/C=59-446.[ExPASy / RCSB / EBI]
2Q15; X-ray; 2.40 A; A=62-446.[ExPASy / RCSB / EBI]
2QK5; X-ray; 2.20 A; A/B=55-447.[ExPASy / RCSB / EBI]
2QMD; X-ray; 1.65 A; A/B=55-447.[ExPASy / RCSB / EBI]
2QMF; X-ray; 1.75 A; A/B=55-447.[ExPASy / RCSB / EBI]
2QMG; X-ray; 1.89 A; A/B=55-447.[ExPASy / RCSB / EBI]
2QP8; X-ray; 1.50 A; A/B=55-447.[ExPASy / RCSB / EBI]
2QU2; X-ray; 2.60 A; A=46-454.[ExPASy / RCSB / EBI]
2QU3; X-ray; 2.00 A; A=46-454.[ExPASy / RCSB / EBI]
2QZK; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2QZL; X-ray; 1.80 A; A=43-446.[ExPASy / RCSB / EBI]
2VA5; X-ray; 2.75 A; A=14-453.[ExPASy / RCSB / EBI]
2VA6; X-ray; 2.50 A; A=14-453.[ExPASy / RCSB / EBI]
2VA7; X-ray; 2.20 A; A=14-453.[ExPASy / RCSB / EBI]
2VIE; X-ray; 1.90 A; A=61-452.[ExPASy / RCSB / EBI]
2VIJ; X-ray; 1.60 A; A=61-452.[ExPASy / RCSB / EBI]
2VIY; X-ray; 1.82 A; A=61-452.[ExPASy / RCSB / EBI]
2VIZ; X-ray; 1.60 A; A=61-452.[ExPASy / RCSB / EBI]
2VJ6; X-ray; 1.80 A; A=61-452.[ExPASy / RCSB / EBI]
2VJ7; X-ray; 1.60 A; A=61-452.[ExPASy / RCSB / EBI]
2VJ9; X-ray; 1.60 A; A=61-452.[ExPASy / RCSB / EBI]
2VKM; X-ray; 2.05 A; A/B/C/D=58-446.[ExPASy / RCSB / EBI]
2VNM; X-ray; 1.79 A; A=61-452.[ExPASy / RCSB / EBI]
2VNN; X-ray; 1.87 A; A=61-452.[ExPASy / RCSB / EBI]
2ZDZ; X-ray; 2.00 A; A=46-454.[ExPASy / RCSB / EBI]
2ZE1; X-ray; 2.20 A; A=46-454.[ExPASy / RCSB / EBI]
2ZHR; X-ray; 2.50 A; A/B=45-454.[ExPASy / RCSB / EBI]
2ZHS; X-ray; 2.70 A; A=45-454.[ExPASy / RCSB / EBI]
2ZHT; X-ray; 2.35 A; A=45-454.[ExPASy / RCSB / EBI]
2ZHU; X-ray; 2.40 A; A=45-454.[ExPASy / RCSB / EBI]
2ZHV; X-ray; 1.85 A; A=45-454.[ExPASy / RCSB / EBI]
2ZJH; X-ray; 2.60 A; A=43-446.[ExPASy / RCSB / EBI]
2ZJI; X-ray; 2.30 A; A=43-446.[ExPASy / RCSB / EBI]
2ZJJ; X-ray; 2.20 A; A=43-446.[ExPASy / RCSB / EBI]
2ZJK; X-ray; 3.00 A; A/B/C=43-446.[ExPASy / RCSB / EBI]
2ZJL; X-ray; 2.10 A; A=43-446.[ExPASy / RCSB / EBI]
2ZJM; X-ray; 1.90 A; A=43-446.[ExPASy / RCSB / EBI]
2ZJN; X-ray; 2.70 A; A=43-446.[ExPASy / RCSB / EBI]
3BRA; X-ray; 2.30 A; A=46-454.[ExPASy / RCSB / EBI]
3BUF; X-ray; 2.30 A; A=46-454.[ExPASy / RCSB / EBI]
3BUG; X-ray; 2.50 A; A=46-454.[ExPASy / RCSB / EBI]
3BUH; X-ray; 2.30 A; A=46-454.[ExPASy / RCSB / EBI]
3CIB; X-ray; 1.72 A; A/B=58-447.[ExPASy / RCSB / EBI]
3CIC; X-ray; 1.75 A; A/B=58-447.[ExPASy / RCSB / EBI]
3CID; X-ray; 1.80 A; A/B=58-447.[ExPASy / RCSB / EBI]
3CKP; X-ray; 2.30 A; A/B/C=43-454.[ExPASy / RCSB / EBI]
3CKR; X-ray; 2.70 A; A/B/C=43-454.[ExPASy / RCSB / EBI]
3DM6; X-ray; 2.60 A; A/B/C=42-446.[ExPASy / RCSB / EBI]
3DUY; X-ray; 1.97 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
3DV1; X-ray; 2.10 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
3DV5; X-ray; 2.10 A; A/B/C=48-447.[ExPASy / RCSB / EBI]
3EXO; X-ray; 2.10 A; A=43-454.[ExPASy / RCSB / EBI]
3FKT; X-ray; 1.90 A; A=43-446.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FKN; -.
1M4H; -.
1PY1; -.
1SGZ; -.
1TQF; -.
1UJJ; -.
1UJK; -.
1W50; -.
1W51; -.
1XN2; -.
1XN3; -.
1XS7; -.
1YM2; -.
1YM4; -.
2B8L; -.
2B8V; -.
2F3E; -.
2F3F; -.
2FDP; -.
2G94; -.
2HIZ; -.
2HM1; -.
2IQG; -.
2IRZ; -.
2IS0; -.
2NTR; -.
2OAH; -.
2OF0; -.
2OHK; -.
2OHL; -.
2OHM; -.
2OHN; -.
2OHP; -.
2OHQ; -.
2OHR; -.
2OHS; -.
2OHT; -.
2OHU; -.
2P4J; -.
2P83; -.
2P8H; -.
2PH6; -.
2PH8; -.
2Q11; -.
2Q15; -.
2QK5; -.
2QMD; -.
2QMF; -.
2QMG; -.
2QP8; -.
2QU2; -.
2QU3; -.
2QZK; -.
2QZL; -.
2VA5; -.
2VA6; -.
2VA7; -.
2VIE; -.
2VIJ; -.
2VIY; -.
2VIZ; -.
2VJ6; -.
2VJ7; -.
2VJ9; -.
2VKM; -.
2VNM; -.
2VNN; -.
2ZDZ; -.
2ZE1; -.
2ZHR; -.
2ZHS; -.
2ZHT; -.
2ZHU; -.
2ZHV; -.
2ZJH; -.
2ZJI; -.
2ZJJ; -.
2ZJK; -.
2ZJL; -.
2ZJM; -.
2ZJN; -.
3BRA; -.
3BUF; -.
3BUG; -.
3BUH; -.
3CIB; -.
3CIC; -.
3CID; -.
3CKP; -.
3CKR; -.
3DM6; -.
3DUY; -.
3DV1; -.
3DV5; -.
3EXO; -.
3FKT; -.
ModBase P56817.
Protein family/group databases
TCDB 8.A.32.1.1; beta-amyloid cleaving enzyme (BACE1) family.
PTM databases
PhosphoSite P56817; -.
Enzyme and pathway databases
BRENDA 3.4.23.46; 247.
Organism-specific databases
GeneCards GC11M116661; -.
H-InvDB HIX0010165; -.
HGNC HGNC:933; BACE1.
GenAtlas BACE1.
HPA CAB016358; -.
MIM 604252; gene. [NCBI / EBI]
PharmGKB PA25232; -.
HUGE KIAA1149.
Gene expression databases
ArrayExpress P56817; -.
Bgee P56817; -.
CleanEx HS_BACE1; -.
GermOnline ENSG00000186318; Homo sapiens.
Ontologies
GO
GO:0005768; Cellular component: endosome (inferred from direct assay from UniProtKB).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from UniProtKB).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0004190; Molecular function: aspartic-type endopeptidase activity (inferred from direct assay from UniProtKB).
GO:0008798; Molecular function: beta-aspartyl-peptidase activity (traceable author statement from ProtInc).
GO:0050435; Biological process: beta-amyloid metabolic process (inferred from direct assay from UniProtKB).
GO:0006509; Biological process: membrane protein ectodomain proteolysis (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR009119; Pept_A1_BACE.
IPR009120; Pept_A1_BACE1.
IPR001461; Peptidase_A1.
IPR001969; Peptidase_aspartic_AS.
IPR009007; Peptidase_aspartic_catalytic.
Graphical view of domain structure.
Gene3D G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
PANTHER PTHR13683; Peptidase_A1; 1.
Pfam PF00026; Asp; 1.
Pfam graphical view of domain structure.
PRINTS PR01816; BACE1.
PR01815; BACEFAMILY.
PR00792; PEPSIN.
PROSITE PS00141; ASP_PROTEASE; 1.
Proteomic databases
PRIDE P56817; -.
Genome annotation databases
Ensembl ENSG00000186318; Homo sapiens. [Contig view]
GeneID 23621; -.
KEGG hsa:23621; -.
Phylogenomic databases
HOVERGEN P56817; -.
Other
NextBio 46358; -.
PMAP-CutDB P56817; -.
SOURCE BACE1; Homo sapiens.
ProtoNet P56817.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Aspartyl protease; Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase; Membrane; Polymorphism; Protease; Signal; Transmembrane; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
PROPEP   22    45  24      PRO_0000025939
CHAIN   46   501  456     Beta-secretase 1. PRO_0000025940
TOPO_DOM   22   457  436     Extracellular (Potential). 
TRANSMEM   458   478  21     Potential. 
TOPO_DOM   479   501  23     Cytoplasmic (Potential). 
REGION   479   501  23     Interaction with RTN3. 
ACT_SITE   93    93        By similarity. 
ACT_SITE   289   289        By similarity. 
CARBOHYD   153   153        N-linked (GlcNAc...) (Potential). 
CARBOHYD   172   172        N-linked (GlcNAc...) (Potential). 
CARBOHYD   223   223        N-linked (GlcNAc...) (Potential). 
CARBOHYD   354   354        N-linked (GlcNAc...) (Potential). 
DISULFID   216   420         
DISULFID   278   443         
DISULFID   330   380         
VAR_SEQ   146   189        Missing (in isoform C and isoform D). VSP_005222
VAR_SEQ   190   214        Missing (in isoform B and isoform D). VSP_005223
VARIANT   481   481  1     R -> C (in dbSNP:rs539765 [NCBI]). VAR_051509 
STRAND   67    70  4      
TURN   71    73  3      
STRAND   74    81  8      
TURN   82    85  4      
STRAND   86    93  8      
STRAND   99   102  4      
HELIX   115   117  3      
STRAND   122   131  10      
STRAND   136   147  12      
STRAND   155   168  14      
STRAND   178   181  4      
HELIX   185   187  3      
HELIX   197   204  8      
STRAND   211   215  5      
HELIX   224   229  6      
STRAND   233   239  7      
HELIX   242   244  3      
STRAND   245   253  9      
TURN   257   260  4      
STRAND   264   269  6      
HELIX   278   282  5      
STRAND   286   288  3      
STRAND   294   298  5      
HELIX   299   312  14      
TURN   313   315  3      
HELIX   320   323  4      
STRAND   329   332  4      
HELIX   338   340  3      
STRAND   344   349  6      
STRAND   355   361  7      
HELIX   363   366  4      
STRAND   367   370  4      
STRAND   377   383  7      
STRAND   385   390  6      
STRAND   392   394  3      
HELIX   396   399  4      
STRAND   402   407  6      
TURN   408   411  4      
STRAND   412   418  7      
STRAND   430   436  7      
HELIX   440   443  4      
Sequence information
Length: 501 AA [This is the length of the unprocessed precursor] Molecular weight: 55764 Da [This is the MW of the unprocessed precursor] CRC64: 377CE4C824ACEF05 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE PEEPGRRGSF 

        70         80         90        100        110        120 
VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA VGAAPHPFLH RYYQRQLSST 

       130        140        150        160        170        180 
YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH GPNVTVRANI AAITESDKFF INGSNWEGIL 

       190        200        210        220        230        240 
GLAYAEIARP DDSLEPFFDS LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI 

       250        260        270        280        290        300 
DHSLYTGSLW YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK 

       310        320        330        340        350        360 
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG EVTNQSFRIT 

       370        380        390        400        410        420 
ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME GFYVVFDRAR KRIGFAVSAC 

       430        440        450        460        470        480 
HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT DESTLMTIAY VMAAICALFM LPLCLMVCQW 

       490        500 
RCLRCLRQQH DDFADDISLL K 

P56817 in FASTA format

View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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NPSA logo NPSA Sequence analysis tools

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