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P56817 (BACE1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-secretase 1
EC=3.4.23.46
Alternative name(s):
Aspartyl protease 2
Short name=ASP2
Short name=Asp 2
Beta-site amyloid precursor protein cleaving enzyme 1
Short name=Beta-site APP cleaving enzyme 1
Memapsin-2
Membrane-associated aspartic protease 2
Gene names
Name:BACE1
Synonyms:BACE, KIAA1149
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length501 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 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. Ref.15 Ref.24

Catalytic activity

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

Enzyme regulation

Inhibited by RTN3 and RTN4. Ref.20 Ref.21

Subunit structure

Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Interacts with SNX6. Interacts with PCSK9. Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24

Subcellular location

Membrane; Single-pass type I membrane protein. Golgi apparatus › trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Cytoplasmic vesicle membrane. Note: Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface. Ref.17 Ref.24

Tissue specificity

Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata. Ref.15 Ref.16

Domain

The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP. Ref.17

Post-translational modification

Glycosylated. Ref.16

Sequence similarities

Belongs to the peptidase A1 family.

Sequence caution

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P56817-1)

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: P56817-2)

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

The sequence of this isoform differs from the canonical sequence as follows:
     190-214: Missing.
Isoform C (identifier: P56817-3)

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

The sequence of this isoform differs from the canonical sequence as follows:
     146-189: Missing.
Isoform D (identifier: P56817-4)

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 4524
PRO_0000025939
Chain46 – 501456Beta-secretase 1
PRO_0000025940

Regions

Topological domain22 – 457436Extracellular Potential
Transmembrane458 – 47821Helical; Potential
Topological domain479 – 50123Cytoplasmic Potential
Region479 – 50123Interaction with RTN3

Sites

Active site931 By similarity
Active site2891 By similarity

Amino acid modifications

Glycosylation1531N-linked (GlcNAc...) Potential
Glycosylation1721N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Disulfide bond216 ↔ 420 Ref.18
Disulfide bond278 ↔ 443 Ref.18
Disulfide bond330 ↔ 380 Ref.18

Natural variations

Alternative sequence146 – 18944Missing in isoform C and isoform D.
VSP_005222
Alternative sequence190 – 21425Missing in isoform B and isoform D.
VSP_005223
Natural variant2651V → A. Ref.10
VAR_060692
Natural variant4811C → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.13 Ref.14 Ref.15
Corresponds to variant rs539765 [ dbSNP | Ensembl ].
VAR_051509

Secondary structure

1 ....................................................................................... 501
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (BACE-1A) (BAC-501) [UniParc].

Last modified May 18, 2010. Version 2.
Checksum: 377CE4C838C09F05

FASTA50155,711
        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 
CCLRCLRQQH DDFADDISLL K

« Hide

Isoform B (BACE-1B) (BACE-I-476) [UniParc].

Checksum: 6C8C87F8B53FDF66
Show »

FASTA47652,855
Isoform C (BACE-1C) (BACE-I-457) [UniParc].

Checksum: C794C9A9F43397A2
Show »

FASTA45751,015
Isoform D (BACE-1D) (BACE-I-432) [UniParc].

Checksum: 96FC81E6EC82A01B
Show »

FASTA43248,159

References

« Hide 'large scale' references
[1]"Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE."
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. expand/collapse author list , Burgess T., Louis J.-C., Collins F., Treanor J., Rogers G., Citron M.
Science 286:735-741(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
Tissue: Brain.
[2]"Purification and cloning of amyloid precursor protein beta-secretase from human brain."
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. expand/collapse author list , Tung J., Schenk D., Seubert P., Suomensaari S.M., Wang S., Walker D., Zhao J., McConlogue L., Varghese J.
Nature 402:537-540(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, CHARACTERIZATION, VARIANT ARG-481.
Tissue: Brain.
[3]"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 A), VARIANT ARG-481.
[4]"Identification of a novel aspartic proteinase (Asp 2) as beta-secretase."
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.
Mol. Cell. Neurosci. 14:419-427(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
[5]"New beta-site APP cleaving enzyme isoform (BACE-1B) obtained from human brain and pancreas."
Michel B., De Pietri Tonelli D., Zacchetti D., Keller P.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT ARG-481.
Tissue: Brain and Pancreas.
[6]"New beta-site APP cleaving enzyme isoform (BACE-1C) obtained from human pancreas."
Zacchetti D., De Pietri Tonelli D., Schnurbus R.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), VARIANT ARG-481.
Tissue: Pancreas.
[7]"Three novel alternatively spliced isoforms of the human beta-site amyloid precursor protein cleaving enzyme (BACE) and their effect on amyloid beta-peptide production."
Tanahashi H., Tabira T.
Neurosci. Lett. 307:9-12(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D), VARIANT ARG-481.
Tissue: Brain.
[8]"Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ARG-481.
Tissue: Brain.
[9]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[10]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-265 AND ARG-481.
[11]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[12]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-481.
[14]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ARG-481.
Tissue: Lung.
[15]"Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein."
Lin X., Koelsch G., Wu S., Downs D., Dashti A., Tang J.
Proc. Natl. Acad. Sci. U.S.A. 97:1456-1460(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-501 (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, VARIANT ARG-481.
[16]"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: TISSUE SPECIFICITY, GLYCOSYLATION.
[17]"The transmembrane domain of the Alzheimer's beta-secretase (BACE1) determines its late Golgi localization and access to beta -amyloid precursor protein (APP) substrate."
Yan R., Han P., Miao H., Greengard P., Xu H.
J. Biol. Chem. 276:36788-36796(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN.
[18]"The disulphide bonds in the catalytic domain of BACE are critical but not essential for amyloid precursor protein processing activity."
Fischer F., Molinari M., Bodendorf U., Paganetti P.
J. Neurochem. 80:1079-1088(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[19]"Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins."
He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.
Biochemistry 42:12174-12180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GGA1; GGA2 AND GGA3.
[20]"Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
[21]"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
[22]"Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN3.
[23]"PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1."
Jonas M.C., Costantini C., Puglielli L.
EMBO Rep. 9:916-922(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCSK9.
[24]"Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing."
Okada H., Zhang W., Peterhoff C., Hwang J.C., Nixon R.A., Ryu S.H., Kim T.W.
FASEB J. 24:2783-2794(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SNX6, SUBCELLULAR LOCATION.
[25]"Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor."
Hong L., Koelsch G., Lin X., Wu S., Terzyan S., Ghosh A.K., Zhang X.C., Tang J.
Science 290:150-153(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
[26]"Crystal structure of memapsin 2 (beta-secretase) in complex with an inhibitor OM00-3."
Hong L., Turner R.T. III, Koelsch G., Shin D., Ghosh A.K., Tang J.
Biochemistry 41:10963-10967(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
[27]"Flap position of free memapsin 2 (beta-secretase), a model for flap opening in aspartic protease catalysis."
Hong L., Tang J.
Biochemistry 43:4689-4695(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
[28]"Apo and inhibitor complex structures of BACE (beta-secretase)."
Patel S., Vuillard L., Cleasby A., Murray C.W., Yon J.
J. Mol. Biol. 343:407-416(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-453 IN COMPLEX WITH SUBSTRATE ANALOG.
[29]"Structural locations and functional roles of new subsites S5, S6, and S7 in memapsin 2 (beta-secretase)."
Turner R.T. III, Hong L., Koelsch G., Ghosh A.K., Tang J.
Biochemistry 44:105-112(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF190725 mRNA. Translation: AAF04142.1.
AF201468 mRNA. Translation: AAF18982.1.
AF200343 mRNA. Translation: AAF17079.1.
AF204943 mRNA. Translation: AAF26367.1.
AF338816 mRNA. Translation: AAK38374.1.
AF338817 mRNA. Translation: AAK38375.1.
AB050436 mRNA. Translation: BAB40931.1.
AB050437 mRNA. Translation: BAB40932.1.
AB050438 mRNA. Translation: BAB40933.1.
AB032975 mRNA. Translation: BAA86463.2. Frameshift.
DQ007053 Genomic DNA. Translation: AAY16982.1.
EF444940 Genomic DNA. Translation: ACA05927.1.
AP000892 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67313.1.
BC065492 mRNA. Translation: AAH65492.1.
AF200193 mRNA. Translation: AAF13715.1.
IPIIPI00011518.
IPI00216209.
IPI00216210.
IPI00216211.
PIRA59090.
RefSeqNP_001193978.1. NM_001207049.1.
NP_036236.1. NM_012104.4.
NP_620427.1. NM_138971.3.
NP_620428.1. NM_138972.3.
NP_620429.1. NM_138973.3.
UniGeneHs.504003.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FKNX-ray1.90A/B56-446[»]
1M4HX-ray2.10A/B56-446[»]
1PY1X-ray2.60E/F/G/H494-501[»]
1SGZX-ray2.00A/B/C/D58-446[»]
1TQFX-ray1.80A43-446[»]
1UJJX-ray2.60C490-501[»]
1UJKX-ray1.90C/D490-501[»]
1W50X-ray1.75A43-453[»]
1W51X-ray2.55A43-453[»]
1XN2X-ray1.90A/B/C/D58-446[»]
1XN3X-ray2.00A/B/C/D58-446[»]
1XS7X-ray2.80D58-446[»]
1YM2X-ray2.05A/B/C48-447[»]
1YM4X-ray2.25A/B/C48-453[»]
2B8LX-ray1.70A43-446[»]
2B8VX-ray1.80A43-446[»]
2F3EX-ray2.11A/B/C48-447[»]
2F3FX-ray2.30A/B/C48-447[»]
2FDPX-ray2.50A/B/C59-446[»]
2G94X-ray1.86A/B/C/D58-446[»]
2HIZX-ray2.50A/B/C14-453[»]
2HM1X-ray2.20A57-453[»]
2IQGX-ray1.70A57-453[»]
2IRZX-ray1.80A43-446[»]
2IS0X-ray2.20A43-446[»]
2NTRX-ray1.80A43-446[»]
2OAHX-ray1.80A43-446[»]
2OF0X-ray2.25A45-446[»]
2OHKX-ray2.20A45-446[»]
2OHLX-ray2.65A45-446[»]
2OHMX-ray2.70A45-446[»]
2OHNX-ray2.15A45-446[»]
2OHPX-ray2.25A45-446[»]
2OHQX-ray2.10A45-446[»]
2OHRX-ray2.25A45-446[»]
2OHSX-ray2.45A45-446[»]
2OHTX-ray2.30A45-446[»]
2OHUX-ray2.35A45-446[»]
2P4JX-ray2.50A/B/C/D58-446[»]
2P83X-ray2.50A/B/C14-446[»]
2P8HX-ray1.80A43-446[»]
2PH6X-ray2.00A43-446[»]
2PH8X-ray1.70A43-446[»]
2Q11X-ray2.40A/B/C59-446[»]
2Q15X-ray2.40A62-446[»]
2QK5X-ray2.20A/B55-447[»]
2QMDX-ray1.65A/B55-447[»]
2QMFX-ray1.75A/B55-447[»]
2QMGX-ray1.89A/B55-447[»]
2QP8X-ray1.50A/B55-447[»]
2QU2X-ray2.60A46-454[»]
2QU3X-ray2.00A46-454[»]
2QZKX-ray1.80A43-446[»]
2QZLX-ray1.80A43-446[»]
2VA5X-ray2.75A14-453[»]
2VA6X-ray2.50A14-453[»]
2VA7X-ray2.20A14-453[»]
2VIEX-ray1.90A61-452[»]
2VIJX-ray1.60A61-452[»]
2VIYX-ray1.82A61-452[»]
2VIZX-ray1.60A61-452[»]
2VJ6X-ray1.80A61-452[»]
2VJ7X-ray1.60A61-452[»]
2VJ9X-ray1.60A61-452[»]
2VKMX-ray2.05A/B/C/D58-446[»]
2VNMX-ray1.79A61-452[»]
2VNNX-ray1.87A61-452[»]
2WEZX-ray1.70A61-452[»]
2WF0X-ray1.60A61-452[»]
2WF1X-ray1.60A61-452[»]
2WF2X-ray1.80A61-452[»]
2WF3X-ray2.08A61-452[»]
2WF4X-ray1.80A61-452[»]
2WJOX-ray2.50A58-460[»]
2XFIX-ray1.73A61-452[»]
2XFJX-ray1.80A61-452[»]
2XFKX-ray1.80A61-452[»]
2ZDZX-ray2.00A46-454[»]
2ZE1X-ray2.20A46-454[»]
2ZHRX-ray2.50A/B45-454[»]
2ZHSX-ray2.70A45-454[»]
2ZHTX-ray2.35A45-454[»]
2ZHUX-ray2.40A45-454[»]
2ZHVX-ray1.85A45-454[»]
2ZJHX-ray2.60A43-446[»]
2ZJIX-ray2.30A43-446[»]
2ZJJX-ray2.20A43-446[»]
2ZJKX-ray3.00A/B/C43-446[»]
2ZJLX-ray2.10A43-446[»]
2ZJMX-ray1.90A43-446[»]
2ZJNX-ray2.70A43-446[»]
3BRAX-ray2.30A46-454[»]
3BUFX-ray2.30A46-454[»]
3BUGX-ray2.50A46-454[»]
3BUHX-ray2.30A46-454[»]
3CIBX-ray1.72A/B58-447[»]
3CICX-ray1.75A/B58-447[»]
3CIDX-ray1.80A/B58-447[»]
3CKPX-ray2.30A/B/C43-454[»]
3CKRX-ray2.70A/B/C43-454[»]
3DM6X-ray2.60A/B/C42-446[»]
3DUYX-ray1.97A/B/C48-447[»]
3DV1X-ray2.10A/B/C48-447[»]
3DV5X-ray2.10A/B/C48-447[»]
3EXOX-ray2.10A43-454[»]
3FKTX-ray1.90A43-446[»]
3H0BX-ray2.70A/B/C43-446[»]
3HVGX-ray2.26A/B/C43-453[»]
3HW1X-ray2.48A/B/C43-453[»]
3I25X-ray2.10A/B/C42-446[»]
3IGBX-ray2.24A46-454[»]
3IN3X-ray2.00A46-454[»]
3IN4X-ray2.30A46-454[»]
3INDX-ray2.25A46-454[»]
3INEX-ray2.00A46-454[»]
3INFX-ray1.85A46-454[»]
3INHX-ray1.80A46-454[»]
3IVHX-ray1.80A57-453[»]
3IVIX-ray2.20A/B/C57-453[»]
3IXJX-ray2.20A/B/C59-446[»]
3IXKX-ray2.50A/B/C42-446[»]
3K5CX-ray2.12A/B/C48-447[»]
3K5DX-ray2.90A/B/C48-453[»]
3K5FX-ray2.25A/B/C48-447[»]
3K5GX-ray2.00A/B/C48-447[»]
3KMXX-ray1.70A/B53-447[»]
3KMYX-ray1.90A/B53-447[»]
3KN0X-ray1.90A/B53-447[»]
3KYRX-ray2.60A/B/C42-446[»]
3L38X-ray2.10A46-454[»]
3L3AX-ray2.36A46-454[»]
3L58X-ray1.80A/B41-454[»]
3L59X-ray2.00A/B41-454[»]
3L5BX-ray1.80A/B41-454[»]
3L5CX-ray1.80A/B41-454[»]
3L5DX-ray1.75A/B41-454[»]
3L5EX-ray1.53A/B41-454[»]
3L5FX-ray1.70A/B41-454[»]
3LHGX-ray2.10A46-454[»]
3LNKX-ray1.80A/B53-447[»]
3LPIX-ray2.05A/B14-454[»]
3LPJX-ray1.79A/B14-454[»]
3LPKX-ray1.93A/B14-454[»]
3MSJX-ray1.80A/B/C43-453[»]
3MSKX-ray2.00A48-453[»]
3MSLX-ray2.40A48-453[»]
3N4LX-ray2.70A/B/C57-453[»]
3NSHX-ray2.20A/B/C57-453[»]
3OHFX-ray2.10A/B14-454[»]
3OHHX-ray2.01A/B14-454[»]
3OOZX-ray1.80A46-454[»]
3PI5X-ray2.40A/B/C48-447[»]
3QBHX-ray2.24A/B/C48-447[»]
3QI1X-ray2.30A46-453[»]
3R1GX-ray2.80B57-453[»]
3R2FX-ray2.53A/B/D/E14-454[»]
3RSVX-ray2.50A43-453[»]
3RSXX-ray2.48A43-453[»]
3RTHX-ray2.70A43-453[»]
3RTMX-ray2.76A43-453[»]
3RTNX-ray2.70A43-453[»]
3RU1X-ray2.30A43-453[»]
3RVIX-ray2.65A43-453[»]
3S2OX-ray2.60A48-453[»]
3S7LX-ray2.16A46-454[»]
3S7MX-ray2.20A46-454[»]
3SKFX-ray3.00A/B14-454[»]
3SKGX-ray2.88A/B/D/E14-454[»]
3TPJX-ray1.61A43-454[»]
3TPLX-ray2.50A/B/C43-454[»]
3TPPX-ray1.60A43-454[»]
3TPRX-ray2.55A43-454[»]
3U6AX-ray2.20A/B/C58-446[»]
3UDHX-ray1.70A58-453[»]
3UDJX-ray1.80A58-453[»]
3UDKX-ray2.51A58-453[»]
3UDMX-ray1.94A58-453[»]
3UDNX-ray2.19A58-453[»]
3UDPX-ray1.95A58-453[»]
3UDQX-ray2.73A58-453[»]
3UDRX-ray1.95A58-453[»]
3UDYX-ray2.00A58-453[»]
3UFLX-ray1.90A58-446[»]
3UQPX-ray1.77A43-454[»]
3UQRX-ray3.06A/B/C43-454[»]
3UQUX-ray1.70A43-454[»]
3UQWX-ray2.20A43-454[»]
3UQXX-ray1.70A43-454[»]
3VEUX-ray1.52A48-447[»]
3VF3X-ray1.48A48-447[»]
3VG1X-ray1.77A48-447[»]
3VV6X-ray2.05A43-454[»]
3VV7X-ray2.10A43-454[»]
3VV8X-ray2.50A43-454[»]
4ACUX-ray1.75A43-453[»]
4ACXX-ray2.00A43-453[»]
4AZYX-ray1.79A43-453[»]
4B00X-ray1.83A43-453[»]
4B05X-ray1.80A43-453[»]
4B1CX-ray1.95A58-438[»]
4B1DX-ray1.95A58-445[»]
4B1EX-ray1.95A58-445[»]
4D83X-ray2.40A/B/C48-447[»]
4D85X-ray2.65A48-453[»]
4D88X-ray1.70A48-447[»]
4D89X-ray1.65A48-447[»]
4D8CX-ray2.07A/B/C48-447[»]
4DH6X-ray2.50A43-453[»]
4DI2X-ray2.00A/B/C43-453[»]
4DJUX-ray1.80A/B41-454[»]
4DJVX-ray1.73A/B41-454[»]
4DJWX-ray1.90A/B41-454[»]
4DJXX-ray1.50A/B41-454[»]
4DJYX-ray1.86A/B41-454[»]
4DPFX-ray1.80A57-446[»]
4DPIX-ray1.90A57-446[»]
4DUSX-ray2.50A43-453[»]
4DV9X-ray2.08A43-454[»]
4DVFX-ray1.80A/B43-454[»]
4EWOX-ray1.80A61-446[»]
4EXGX-ray1.80A61-446[»]
4FGXX-ray1.59A43-454[»]
4FM7X-ray1.56A58-453[»]
4FM8X-ray1.90A58-453[»]
4FRIX-ray2.30A43-453[»]
4FRJX-ray1.95A43-453[»]
4FRKX-ray2.10A43-453[»]
4FRSX-ray1.70A/B53-447[»]
4FS4X-ray1.74A/B58-447[»]
4FSEX-ray2.65A/B/D/E14-454[»]
4FSLX-ray2.50A/B/D/E43-454[»]
4GIDX-ray2.00A/B/C/D59-446[»]
4H1EX-ray1.90A/B41-454[»]
4H3FX-ray1.70A/B41-454[»]
4H3GX-ray1.85A/B41-454[»]
4H3IX-ray1.96A/B41-454[»]
4H3JX-ray1.60A/B41-454[»]
4HA5X-ray1.83A/B41-454[»]
4HZTX-ray1.80A57-453[»]
4I0EX-ray1.70A57-453[»]
4I0FX-ray1.80A57-453[»]
4I0GX-ray1.78A57-453[»]
4I0HX-ray2.20A/B/C57-453[»]
4I0JX-ray1.99A57-453[»]
4I0ZX-ray1.80A57-453[»]
4I10X-ray2.07A57-453[»]
4I11X-ray1.89A57-453[»]
4I12X-ray1.78A57-453[»]
4I1CX-ray2.00A57-453[»]
ProteinModelPortalP56817.
SMRP56817. Positions 58-447.
ModBaseSearch...

Protein-protein interaction databases

IntActP56817. 1 interaction.
STRING9606.ENSP00000318585.

Protein family/group databases

MEROPSA01.004.
TCDB8.A.32.1.1. beta-amyloid cleaving enzyme (BACE1) family.

PTM databases

PhosphoSiteP56817.

Polymorphism databases

DMDM296434407.

Proteomic databases

PaxDbP56817.
PRIDEP56817.

Protocols and materials databases

DNASU23621.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313005; ENSP00000318585; ENSG00000186318.
ENST00000428381; ENSP00000402228; ENSG00000186318.
ENST00000445823; ENSP00000403685; ENSG00000186318.
ENST00000513780; ENSP00000424536; ENSG00000186318.
GeneID23621.
KEGGhsa:23621.
UCSCuc001pqw.3. human.
uc001pqx.3. human.
uc001pqy.3. human.
uc001pqz.3. human.

Organism-specific databases

CTD23621.
GeneCardsGC11M117156.
HGNCHGNC:933. BACE1.
HPACAB016358.
MIM604252. gene.
neXtProtNX_P56817.
PharmGKBPA25232.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG71700.
HOVERGENHBG059578.
KOK04521.
OMAPDMEDCG.
OrthoDBEOG4SF95Q.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000160610-MONOMER.
BRENDA3.4.23.46. 2681.
SABIO-RKP56817.

Gene expression databases

ArrayExpressP56817.
BgeeP56817.
CleanExHS_BACE1.
GenevestigatorP56817.
GermOnlineENSG00000186318. Homo sapiens.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP56817.
ChEMBLCHEMBL4822.
EvolutionaryTraceP56817.
GenomeRNAi23621.
NextBio46358.
PMAP-CutDBP56817.
SOURCESearch...

Entry information

Entry nameBACE1_HUMAN
AccessionPrimary (citable) accession number: P56817
Secondary accession number(s): A0M8W7 expand/collapse secondary AC list , B0YIU9, Q9BYB9, Q9BYC0, Q9BYC1, Q9UJT5, Q9ULS1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: May 1, 2013
This is version 149 of the entry and version 2 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

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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