Reviewed, UniProtKB/Swiss-Prot P56817 (BACE1_HUMAN)

Names and origin

Protein names

Recommended name:
    Beta-secretase 1
    EC=3.4.23.46
Alternative name(s):
    Beta-site amyloid precursor protein cleaving enzyme 1
      Short name=Beta-site APP cleaving enzyme 1
    Membrane-associated aspartic protease 2
    Memapsin-2
    Aspartyl protease 2
      Short name=Asp 2
      Short name=ASP2

Gene names

Name:	BACE1
Synonyms:	BACE, KIAA1149

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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. Ref.15 Ref.16
Subunit structure	Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Ref.15 Ref.16 Ref.14 Ref.17
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Brain.
Sequence similarities	Belongs to the peptidase A1 family.
Sequence caution	The sequence BAA86463.2 differs from that shown. Reason: Frameshift at position 34.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	beta-amyloid metabolic process Inferred from direct assay. Source: UniProtKB membrane protein ectodomain proteolysis Traceable author statement. Source: UniProtKB
Cellular component	Golgi apparatus Ref.1 Inferred from direct assay. Source: UniProtKB endosome Ref.1 Inferred from direct assay. Source: UniProtKB integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	aspartic-type endopeptidase activity Ref.1 Inferred from direct assay. Source: UniProtKB beta-aspartyl-peptidase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 45

24

Ref.2

PRO_0000025939

Chain

46 – 501

456

Beta-secretase 1

PRO_0000025940

Regions

Topological domain

22 – 457

436

Extracellular Potential

Transmembrane

458 – 478

21

Potential

Topological domain

479 – 501

23

Cytoplasmic Potential

Region

479 – 501

23

Interaction with RTN3

Sites

Active site

93

1

By similarity

Active site

289

1

By similarity

Amino acid modifications

Glycosylation

153

1

N-linked (GlcNAc...) Potential

Glycosylation

172

1

N-linked (GlcNAc...) Potential

Glycosylation

223

1

N-linked (GlcNAc...) Potential

Glycosylation

354

1

N-linked (GlcNAc...) Potential

Disulfide bond

216 ↔ 420

Ref.13

Disulfide bond

278 ↔ 443

Ref.13

Disulfide bond

330 ↔ 380

Ref.13

Natural variations

Alternative sequence

146 – 189

44

Missing in isoform C and isoform D.

VSP_005222

Alternative sequence

190 – 214

25

Missing in isoform B and isoform D.

VSP_005223

Natural variant

481

1

R → C: dbSNP rs539765. Ref.10

VAR_051509

Secondary structure

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501

Helix Strand Turn

Details...

Beta strand

67 – 70

4

Turn

71 – 73

3

Beta strand

74 – 81

8

Turn

82 – 85

4

Beta strand

86 – 93

8

Beta strand

99 – 102

4

Helix

115 – 117

3

Beta strand

122 – 131

10

Beta strand

136 – 147

12

Beta strand

155 – 168

14

Beta strand

178 – 181

4

Helix

185 – 187

3

Helix

197 – 204

8

Beta strand

211 – 215

5

Helix

224 – 229

6

Beta strand

233 – 239

7

Helix

242 – 244

3

Beta strand

245 – 253

9

Turn

257 – 260

4

Beta strand

264 – 269

6

Helix

278 – 282

5

Beta strand

286 – 288

3

Beta strand

294 – 298

5

Helix

299 – 312

14

Turn

313 – 315

3

Helix

320 – 323

4

Beta strand

329 – 332

4

Helix

338 – 340

3

Beta strand

344 – 349

6

Beta strand

355 – 361

7

Helix

363 – 366

4

Beta strand

367 – 370

4

Beta strand

377 – 383

7

Beta strand

385 – 390

6

Beta strand

392 – 394

3

Helix

396 – 399

4

Beta strand

402 – 407

6

Turn

408 – 411

4

Beta strand

412 – 418

7

Beta strand

430 – 436

7

Helix

440 – 443

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (BACE-1A) (BAC-501) [UniParc]. Last modified May 30, 2000. Version 1. Checksum: 377CE4C824ACEF05	FASTA	501	55,764
	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
	Isoform B (BACE-1B) (BACE-I-476). Checksum: 6C8C87F8A953AF66	FASTA	476	52,908
	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 GLAYAEIARL CGAGFPLNQS EVLASVGGSM IIGGIDHSLY TGSLWYTPIR REWYYEVIIV 250 260 270 280 290 300 RVEINGQDLK MDCKEYNYDK SIVDSGTTNL RLPKKVFEAA VKSIKAASST EKFPDGFWLG 310 320 330 340 350 360 EQLVCWQAGT TPWNIFPVIS LYLMGEVTNQ SFRITILPQQ YLRPVEDVAT SQDDCYKFAI 370 380 390 400 410 420 SQSSTGTVMG AVIMEGFYVV FDRARKRIGF AVSACHVHDE FRTAAVEGPF VTLDMEDCGY 430 440 450 460 470 NIPQTDESTL MTIAYVMAAI CALFMLPLCL MVCQWRCLRC LRQQHDDFAD DISLLK
	Isoform C (BACE-1C) (BACE-I-457). Checksum: C794C9A9E85FE7A2	FASTA	457	51,068
	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 LGTDLPDDSL EPFFDSLVKQ THVPNLFSLQ LCGAGFPLNQ 190 200 210 220 230 240 SEVLASVGGS MIIGGIDHSL YTGSLWYTPI RREWYYEVII VRVEINGQDL KMDCKEYNYD 250 260 270 280 290 300 KSIVDSGTTN LRLPKKVFEA AVKSIKAASS TEKFPDGFWL GEQLVCWQAG TTPWNIFPVI 310 320 330 340 350 360 SLYLMGEVTN QSFRITILPQ QYLRPVEDVA TSQDDCYKFA ISQSSTGTVM GAVIMEGFYV 370 380 390 400 410 420 VFDRARKRIG FAVSACHVHD EFRTAAVEGP FVTLDMEDCG YNIPQTDEST LMTIAYVMAA 430 440 450 ICALFMLPLC LMVCQWRCLR CLRQQHDDFA DDISLLK
	Isoform D (BACE-1D) (BACE-I-432). Checksum: 96FC81E6F0EED01B	FASTA	432	48,212
	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 LGTDLLCGAG FPLNQSEVLA SVGGSMIIGG IDHSLYTGSL 190 200 210 220 230 240 WYTPIRREWY YEVIIVRVEI NGQDLKMDCK EYNYDKSIVD SGTTNLRLPK KVFEAAVKSI 250 260 270 280 290 300 KAASSTEKFP DGFWLGEQLV CWQAGTTPWN IFPVISLYLM GEVTNQSFRI TILPQQYLRP 310 320 330 340 350 360 VEDVATSQDD CYKFAISQSS TGTVMGAVIM EGFYVVFDRA RKRIGFAVSA CHVHDEFRTA 370 380 390 400 410 420 AVEGPFVTLD MEDCGYNIPQ TDESTLMTIA YVMAAICALF MLPLCLMVCQ WRCLRCLRQQ 430 HDDFADDISL LK

References

	« Hide 'large scale' referencesShow '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. , Burgess T., Louis J.-C., Collins F., Treanor J., Rogers G., Citron M. Science 286:735-741(1999) [PubMed: 10531052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). 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. , 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: 10591214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, CHARACTERIZATION. 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: 10591213] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[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: 10656250] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[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). 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). 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: 11516562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D). 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: 10574461] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). 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: 12168954] [Abstract] Cited for: SEQUENCE REVISION.
[10]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-481.
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Tissue: Lung.
[12]	"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: 10677483] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-501 (ISOFORM A), CHARACTERIZATION.
[13]	"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: 11953458] [Abstract] Cited for: DISULFIDE BONDS.
[14]	"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: 14567678] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2 AND GGA3.
[15]	"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: 15286784] [Abstract] Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
[16]	"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: 16965550] [Abstract] Cited for: INTERACTION WITH RTN3 AND RTN4, ENZYME REGULATION.
[17]	"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: 16979658] [Abstract] Cited for: INTERACTION WITH RTN3.
[18]	"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: 11021803] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
[19]	"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: 12206667] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 56-446 IN COMPLEX WITH SUBSTRATE ANALOG.
[20]	"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: 15096037] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
[21]	"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: 15451669] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-453 IN COMPLEX WITH SUBSTRATE ANALOG.
[22]	"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: 15628850] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
EF444940 Genomic DNA. Translation: ACA05927.1.
BC065492 mRNA. Translation: AAH65492.1.
AF200193 mRNA. Translation: AAF13715.1.

IPI

IPI00011518.
IPI00216209.
IPI00216210.
IPI00216211.

PIR

A59090.

RefSeq

NP_036236.1.
NP_620427.1.
NP_620428.1.
NP_620429.1.

UniGene

Hs.504003

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FKN	X-ray	1.90	A/B	56-446	[»]
1M4H	X-ray	2.10	A/B	56-446	[»]
1PY1	X-ray	2.60	E/F/G/H	494-501	[»]
1SGZ	X-ray	2.00	A/B/C/D	58-446	[»]
1TQF	X-ray	1.80	A	43-446	[»]
1UJJ	X-ray	2.60	C	490-501	[»]
1UJK	X-ray	1.90	C/D	490-501	[»]
1W50	X-ray	1.75	A	43-453	[»]
1W51	X-ray	2.55	A	43-453	[»]
1XN2	X-ray	1.90	A/B/C/D	58-446	[»]
1XN3	X-ray	2.00	A/B/C/D	58-446	[»]
1XS7	X-ray	2.80	D	58-446	[»]
1YM2	X-ray	2.05	A/B/C	48-447	[»]
1YM4	X-ray	2.25	A/B/C	48-453	[»]
2B8L	X-ray	1.70	A	43-446	[»]
2B8V	X-ray	1.80	A	43-446	[»]
2F3E	X-ray	2.11	A/B/C	48-447	[»]
2F3F	X-ray	2.30	A/B/C	48-447	[»]
2FDP	X-ray	2.50	A/B/C	59-446	[»]
2G94	X-ray	1.86	A/B/C/D	58-446	[»]
2HIZ	X-ray	2.50	A/B/C	14-453	[»]
2HM1	X-ray	2.20	A	57-453	[»]
2IQG	X-ray	1.70	A	57-453	[»]
2IRZ	X-ray	1.80	A	43-446	[»]
2IS0	X-ray	2.20	A	43-446	[»]
2NTR	X-ray	1.80	A	43-446	[»]
2OAH	X-ray	1.80	A	43-446	[»]
2OF0	X-ray	2.25	A	45-446	[»]
2OHK	X-ray	2.20	A	45-446	[»]
2OHL	X-ray	2.65	A	45-446	[»]
2OHM	X-ray	2.70	A	45-446	[»]
2OHN	X-ray	2.15	A	45-446	[»]
2OHP	X-ray	2.25	A	45-446	[»]
2OHQ	X-ray	2.10	A	45-446	[»]
2OHR	X-ray	2.25	A	45-446	[»]
2OHS	X-ray	2.45	A	45-446	[»]
2OHT	X-ray	2.30	A	45-446	[»]
2OHU	X-ray	2.35	A	45-446	[»]
2P4J	X-ray	2.50	A/B/C/D	58-446	[»]
2P83	X-ray	2.50	A/B/C	14-446	[»]
2P8H	X-ray	1.80	A	43-446	[»]
2PH6	X-ray	2.00	A	43-446	[»]
2PH8	X-ray	1.70	A	43-446	[»]
2Q11	X-ray	2.40	A/B/C	59-446	[»]
2Q15	X-ray	2.40	A	62-446	[»]
2QK5	X-ray	2.20	A/B	55-447	[»]
2QMD	X-ray	1.65	A/B	55-447	[»]
2QMF	X-ray	1.75	A/B	55-447	[»]
2QMG	X-ray	1.89	A/B	55-447	[»]
2QP8	X-ray	1.50	A/B	55-447	[»]
2QU2	X-ray	2.60	A	46-454	[»]
2QU3	X-ray	2.00	A	46-454	[»]
2QZK	X-ray	1.80	A	43-446	[»]
2QZL	X-ray	1.80	A	43-446	[»]
2VA5	X-ray	2.75	A	14-453	[»]
2VA6	X-ray	2.50	A	14-453	[»]
2VA7	X-ray	2.20	A	14-453	[»]
2VIE	X-ray	1.90	A	61-452	[»]
2VIJ	X-ray	1.60	A	61-452	[»]
2VIY	X-ray	1.82	A	61-452	[»]
2VIZ	X-ray	1.60	A	61-452	[»]
2VJ6	X-ray	1.80	A	61-452	[»]
2VJ7	X-ray	1.60	A	61-452	[»]
2VJ9	X-ray	1.60	A	61-452	[»]
2VKM	X-ray	2.05	A/B/C/D	58-446	[»]
2VNM	X-ray	1.79	A	61-452	[»]
2VNN	X-ray	1.87	A	61-452	[»]
2ZDZ	X-ray	2.00	A	46-454	[»]
2ZE1	X-ray	2.20	A	46-454	[»]
2ZHR	X-ray	2.50	A/B	45-454	[»]
2ZHS	X-ray	2.70	A	45-454	[»]
2ZHT	X-ray	2.35	A	45-454	[»]
2ZHU	X-ray	2.40	A	45-454	[»]
2ZHV	X-ray	1.85	A	45-454	[»]
2ZJH	X-ray	2.60	A	43-446	[»]
2ZJI	X-ray	2.30	A	43-446	[»]
2ZJJ	X-ray	2.20	A	43-446	[»]
2ZJK	X-ray	3.00	A/B/C	43-446	[»]
2ZJL	X-ray	2.10	A	43-446	[»]
2ZJM	X-ray	1.90	A	43-446	[»]
2ZJN	X-ray	2.70	A	43-446	[»]
3BRA	X-ray	2.30	A	46-454	[»]
3BUF	X-ray	2.30	A	46-454	[»]
3BUG	X-ray	2.50	A	46-454	[»]
3BUH	X-ray	2.30	A	46-454	[»]
3CIB	X-ray	1.72	A/B	58-447	[»]
3CIC	X-ray	1.75	A/B	58-447	[»]
3CID	X-ray	1.80	A/B	58-447	[»]
3CKP	X-ray	2.30	A/B/C	43-454	[»]
3CKR	X-ray	2.70	A/B/C	43-454	[»]
3DM6	X-ray	2.60	A/B/C	42-446	[»]
3DUY	X-ray	1.97	A/B/C	48-447	[»]
3DV1	X-ray	2.10	A/B/C	48-447	[»]
3DV5	X-ray	2.10	A/B/C	48-447	[»]
3EXO	X-ray	2.10	A	43-454	[»]
3FKT	X-ray	1.90	A	43-446	[»]

ModBase

Search...

Protein family/group databases

TCDB

8.A.32.1.1. beta-amyloid cleaving enzyme (BACE1) family.

PTM databases

PhosphoSite

P56817.

Proteomic databases

PRIDE

P56817.

Genome annotation databases

Ensembl

ENSG00000186318. Homo sapiens. [Contig view]

GeneID

23621.

KEGG

hsa:23621.

Organism-specific databases

GeneCards

GC11M116661.

H-InvDB

HIX0010165.

HGNC

HGNC:933. BACE1.

HPA

CAB016358.

MIM

604252. gene.

PharmGKB

PA25232.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P56817.

Enzyme and pathway databases

BRENDA

3.4.23.46. 247.

Gene expression databases

ArrayExpress

P56817.

Bgee

P56817.

CleanEx

HS_BACE1.

GermOnline

ENSG00000186318. Homo sapiens.

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]

Gene3D

G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.

PANTHER

PTHR13683. Peptidase_A1. 1 hit.

Pfam

PF00026. Asp. 1 hit.
[Graphical view]

PRINTS

PR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.

PROSITE

PS00141. ASP_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

46358.

PMAP-CutDB

P56817.

SOURCE

Search...

Entry information

Entry name

BACE1_HUMAN

Accession

Primary (citable) accession number: P56817
Secondary accession number(s): B0YIU9 , Q9BYB9, Q9BYC0, Q9BYC1, Q9UJT5, Q9ULS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	June 16, 2009
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)