SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P56817

- BACE1_HUMAN

UniProt

P56817 - BACE1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Beta-secretase 1
Gene
BACE1, BACE, KIAA1149
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves 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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by RTN3 and RTN4.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931 By similarity
Active sitei289 – 2891 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB
  2. beta-amyloid binding Source: Alzheimers_University_of_Toronto
  3. beta-aspartyl-peptidase activity Source: ProtInc
  4. enzyme binding Source: UniProtKB
  5. protein binding Source: IntAct

GO - Biological processi

  1. beta-amyloid metabolic process Source: UniProtKB
  2. membrane protein ectodomain proteolysis Source: UniProtKB
  3. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000160610-MONOMER.
BRENDAi3.4.23.46. 2681.
SABIO-RKP56817.

Protein family/group databases

MEROPSiA01.004.
TCDBi8.A.32.1.1. the -amyloid cleaving enzyme (bace1) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:BACE1
Synonyms:BACE, KIAA1149
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:933. BACE1.

Subcellular locationi

Membrane; Single-pass type I membrane protein. Golgi apparatustrans-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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 457436Extracellular Reviewed prediction
Add
BLAST
Transmembranei458 – 47821Helical; Reviewed prediction
Add
BLAST
Topological domaini479 – 50123Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. axon Source: Ensembl
  3. cell surface Source: UniProtKB-SubCell
  4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  5. endoplasmic reticulum Source: UniProtKB-SubCell
  6. endosome Source: UniProtKB
  7. integral component of membrane Source: UniProtKB
  8. integral component of plasma membrane Source: UniProtKB
  9. trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed prediction
Add
BLAST
Propeptidei22 – 4524
PRO_0000025939Add
BLAST
Chaini46 – 501456Beta-secretase 1
PRO_0000025940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi153 – 1531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi172 – 1721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi216 ↔ 4201 Publication
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi278 ↔ 4431 Publication
Disulfide bondi330 ↔ 3801 Publication
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP56817.
PRIDEiP56817.

PTM databases

PhosphoSiteiP56817.

Miscellaneous databases

PMAP-CutDBP56817.

Expressioni

Tissue specificityi

Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata.2 Publications

Gene expression databases

ArrayExpressiP56817.
BgeeiP56817.
CleanExiHS_BACE1.
GenevestigatoriP56817.

Organism-specific databases

HPAiCAB016358.

Interactioni

Subunit structurei

Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Interacts with SNX6. Interacts with PCSK9.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FLOT2Q142542EBI-2433139,EBI-348613

Protein-protein interaction databases

BioGridi117154. 7 interactions.
IntActiP56817. 4 interactions.
MINTiMINT-242532.
STRINGi9606.ENSP00000318585.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi61 – 633
Beta strandi67 – 704
Turni71 – 733
Beta strandi75 – 817
Turni82 – 854
Beta strandi86 – 938
Beta strandi99 – 1024
Beta strandi109 – 1113
Helixi115 – 1173
Beta strandi122 – 13110
Beta strandi132 – 1343
Beta strandi136 – 14712
Beta strandi151 – 1533
Beta strandi155 – 16814
Turni172 – 1743
Beta strandi178 – 1814
Helixi185 – 1873
Beta strandi188 – 1903
Helixi197 – 2048
Beta strandi211 – 2155
Helixi224 – 2296
Beta strandi230 – 23910
Helixi242 – 2443
Beta strandi245 – 2539
Turni257 – 2604
Beta strandi264 – 2696
Helixi278 – 2825
Beta strandi286 – 2883
Beta strandi294 – 2985
Helixi299 – 31214
Turni313 – 3153
Helixi320 – 3234
Beta strandi329 – 3324
Turni333 – 3353
Helixi338 – 3403
Beta strandi344 – 3496
Beta strandi355 – 3617
Helixi363 – 3664
Beta strandi367 – 3693
Helixi373 – 3753
Beta strandi378 – 3836
Beta strandi385 – 3906
Beta strandi392 – 3943
Helixi396 – 3994
Beta strandi402 – 4076
Turni408 – 4114
Beta strandi412 – 4187
Beta strandi430 – 4367
Helixi440 – 4434

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/C46-453[»]
3HW1X-ray2.48A/B/C46-453[»]
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-ray2.30A57-453[»]
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[»]
3WB4X-ray2.25A43-454[»]
3WB5X-ray2.50A43-454[»]
3ZMGX-ray1.74A46-454[»]
3ZOVX-ray2.10A46-454[»]
4ACUX-ray1.75A43-453[»]
4ACXX-ray2.00A43-453[»]
4AZYX-ray1.79A43-453[»]
4B00X-ray1.83A43-453[»]
4B05X-ray1.80A43-453[»]
4B0QX-ray1.87A62-445[»]
4B1CX-ray1.95A58-445[»]
4B1DX-ray1.95A58-445[»]
4B1EX-ray1.95A58-445[»]
4B70X-ray1.60A61-445[»]
4B72X-ray1.60A58-445[»]
4B77X-ray1.80A58-445[»]
4B78X-ray1.50A62-445[»]
4BEKX-ray2.39A46-454[»]
4BFDX-ray2.30A46-454[»]
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[»]
4FCOX-ray1.76A43-454[»]
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/E43-453[»]
4GIDX-ray2.00A/B/C/D59-446[»]
4GMIX-ray1.80A57-446[»]
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[»]
4I0DX-ray1.91A57-453[»]
4I0EX-ray1.70A57-453[»]
4I0FX-ray1.80A57-453[»]
4I0GX-ray1.78A57-453[»]
4I0HX-ray2.20A/B/C57-453[»]
4I0IX-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[»]
4IVSX-ray2.64A43-454[»]
4IVTX-ray1.60A43-454[»]
4J0PX-ray1.97A46-454[»]
4J0TX-ray2.05A46-454[»]
4J0VX-ray1.94A46-454[»]
4J0YX-ray1.77A46-454[»]
4J0ZX-ray2.13A46-454[»]
4J17X-ray1.81A46-454[»]
4J1CX-ray2.01A46-454[»]
4J1EX-ray1.78A46-454[»]
4J1FX-ray2.25A46-454[»]
4J1HX-ray2.20A46-454[»]
4J1IX-ray2.05A46-454[»]
4J1KX-ray2.18A46-454[»]
4JOOX-ray1.80A57-453[»]
4JP9X-ray1.80A57-453[»]
4JPCX-ray1.80A57-453[»]
4JPEX-ray1.80A57-453[»]
4K8SX-ray2.39A/B/C59-446[»]
4K9HX-ray2.29A/B/C59-446[»]
4KE0X-ray2.30A/B/C43-453[»]
4KE1X-ray1.91A43-453[»]
4L7GX-ray1.38A57-453[»]
4L7HX-ray1.85A57-453[»]
4L7JX-ray1.65A57-453[»]
4LC7X-ray1.70A57-453[»]
4LXAX-ray1.95A/B/C48-447[»]
4LXKX-ray2.05A/B/C48-447[»]
4LXMX-ray2.30A/B/C48-447[»]
4N00X-ray1.80A57-453[»]
4PZWX-ray1.80A57-453[»]
4PZXX-ray1.80A57-453[»]
ProteinModelPortaliP56817.
SMRiP56817. Positions 58-447.

Miscellaneous databases

EvolutionaryTraceiP56817.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni479 – 50123Interaction with RTN3
Add
BLAST

Domaini

The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP.1 Publication

Sequence similaritiesi

Belongs to the peptidase A1 family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71700.
HOVERGENiHBG059578.
KOiK04521.
OMAiPDMEDCG.
OrthoDBiEOG7DNNVW.
PhylomeDBiP56817.
TreeFamiTF329595.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform A (identifier: P56817-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE    50
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA 100
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH 150
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS 200
LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW 250
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK 300
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG 350
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME 400
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT 450
DESTLMTIAY VMAAICALFM LPLCLMVCQW CCLRCLRQQH DDFADDISLL 500
K 501
Length:501
Mass (Da):55,711
Last modified:May 18, 2010 - v2
Checksum:i377CE4C838C09F05
GO
Isoform B (identifier: P56817-2) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:476
Mass (Da):52,855
Checksum:i6C8C87F8B53FDF66
GO
Isoform C (identifier: P56817-3) [UniParc]FASTAAdd to Basket

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

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

Show »
Length:457
Mass (Da):51,015
Checksum:iC794C9A9F43397A2
GO
Isoform D (identifier: P56817-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:432
Mass (Da):48,159
Checksum:i96FC81E6EC82A01B
GO
Isoform 5 (identifier: P56817-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
     21-120: Missing.

Note: Gene prediction based on EST data.

Show »
Length:401
Mass (Da):44,964
Checksum:iA8D5B1112614B521
GO
Isoform 6 (identifier: P56817-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
     21-120: Missing.
     190-214: Missing.

Note: Gene prediction based on EST data.

Show »
Length:376
Mass (Da):42,107
Checksum:i93E4D8C54F8E4716
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti265 – 2651V → A.1 Publication
Corresponds to variant rs28989503 [ dbSNP | Ensembl ].
VAR_060692
Natural varianti481 – 4811C → R.12 Publications
Corresponds to variant rs539765 [ dbSNP | Ensembl ].
VAR_051509

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MAQAL…VLPAH → MVPFIYLQAHFTLCSGWSST in isoform 5 and isoform 6.
VSP_047092Add
BLAST
Alternative sequencei21 – 120100Missing in isoform 5 and isoform 6.
VSP_047093Add
BLAST
Alternative sequencei146 – 18944Missing in isoform C and isoform D.
VSP_005222Add
BLAST
Alternative sequencei190 – 21425Missing in isoform B, isoform D and isoform 6.
VSP_005223Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS44739.1. [P56817-2]
CCDS44740.1. [P56817-3]
CCDS44741.1. [P56817-4]
CCDS55786.1. [P56817-6]
CCDS55787.1. [P56817-5]
CCDS8383.1. [P56817-1]
PIRiA59090.
RefSeqiNP_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.
UniGeneiHs.504003.

Genome annotation databases

EnsembliENST00000313005; ENSP00000318585; ENSG00000186318. [P56817-1]
ENST00000392937; ENSP00000475405; ENSG00000186318. [P56817-5]
ENST00000428381; ENSP00000402228; ENSG00000186318. [P56817-4]
ENST00000445823; ENSP00000403685; ENSG00000186318. [P56817-3]
ENST00000510630; ENSP00000422461; ENSG00000186318. [P56817-6]
ENST00000513780; ENSP00000424536; ENSG00000186318. [P56817-2]
GeneIDi23621.
KEGGihsa:23621.
UCSCiuc001pqw.3. human. [P56817-2]
uc001pqx.3. human. [P56817-4]
uc001pqy.3. human. [P56817-3]
uc001pqz.3. human. [P56817-1]

Polymorphism databases

DMDMi296434407.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS44739.1. [P56817-2 ]
CCDS44740.1. [P56817-3 ]
CCDS44741.1. [P56817-4 ]
CCDS55786.1. [P56817-6 ]
CCDS55787.1. [P56817-5 ]
CCDS8383.1. [P56817-1 ]
PIRi A59090.
RefSeqi NP_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.
UniGenei Hs.504003.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2WEZ X-ray 1.70 A 61-452 [» ]
2WF0 X-ray 1.60 A 61-452 [» ]
2WF1 X-ray 1.60 A 61-452 [» ]
2WF2 X-ray 1.80 A 61-452 [» ]
2WF3 X-ray 2.08 A 61-452 [» ]
2WF4 X-ray 1.80 A 61-452 [» ]
2WJO X-ray 2.50 A 58-460 [» ]
2XFI X-ray 1.73 A 61-452 [» ]
2XFJ X-ray 1.80 A 61-452 [» ]
2XFK X-ray 1.80 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 [» ]
3H0B X-ray 2.70 A/B/C 43-446 [» ]
3HVG X-ray 2.26 A/B/C 46-453 [» ]
3HW1 X-ray 2.48 A/B/C 46-453 [» ]
3I25 X-ray 2.10 A/B/C 42-446 [» ]
3IGB X-ray 2.24 A 46-454 [» ]
3IN3 X-ray 2.00 A 46-454 [» ]
3IN4 X-ray 2.30 A 46-454 [» ]
3IND X-ray 2.25 A 46-454 [» ]
3INE X-ray 2.00 A 46-454 [» ]
3INF X-ray 1.85 A 46-454 [» ]
3INH X-ray 1.80 A 46-454 [» ]
3IVH X-ray 1.80 A 57-453 [» ]
3IVI X-ray 2.20 A/B/C 57-453 [» ]
3IXJ X-ray 2.20 A/B/C 59-446 [» ]
3IXK X-ray 2.50 A/B/C 42-446 [» ]
3K5C X-ray 2.12 A/B/C 48-447 [» ]
3K5D X-ray 2.90 A/B/C 48-453 [» ]
3K5F X-ray 2.25 A/B/C 48-447 [» ]
3K5G X-ray 2.00 A/B/C 48-447 [» ]
3KMX X-ray 1.70 A/B 53-447 [» ]
3KMY X-ray 1.90 A/B 53-447 [» ]
3KN0 X-ray 1.90 A/B 53-447 [» ]
3KYR X-ray 2.60 A/B/C 42-446 [» ]
3L38 X-ray 2.10 A 46-454 [» ]
3L3A X-ray 2.36 A 46-454 [» ]
3L58 X-ray 1.80 A/B 41-454 [» ]
3L59 X-ray 2.00 A/B 41-454 [» ]
3L5B X-ray 1.80 A/B 41-454 [» ]
3L5C X-ray 1.80 A/B 41-454 [» ]
3L5D X-ray 1.75 A/B 41-454 [» ]
3L5E X-ray 1.53 A/B 41-454 [» ]
3L5F X-ray 1.70 A/B 41-454 [» ]
3LHG X-ray 2.10 A 46-454 [» ]
3LNK X-ray 1.80 A/B 53-447 [» ]
3LPI X-ray 2.05 A/B 14-454 [» ]
3LPJ X-ray 1.79 A/B 14-454 [» ]
3LPK X-ray 1.93 A/B 14-454 [» ]
3MSJ X-ray 1.80 A/B/C 43-453 [» ]
3MSK X-ray 2.00 A 48-453 [» ]
3MSL X-ray 2.40 A 48-453 [» ]
3N4L X-ray 2.70 A/B/C 57-453 [» ]
3NSH X-ray 2.20 A/B/C 57-453 [» ]
3OHF X-ray 2.10 A/B 14-454 [» ]
3OHH X-ray 2.01 A/B 14-454 [» ]
3OOZ X-ray 1.80 A 46-454 [» ]
3PI5 X-ray 2.40 A/B/C 48-447 [» ]
3QBH X-ray 2.24 A/B/C 48-447 [» ]
3QI1 X-ray 2.30 A 57-453 [» ]
3R1G X-ray 2.80 B 57-453 [» ]
3R2F X-ray 2.53 A/B/D/E 14-454 [» ]
3RSV X-ray 2.50 A 43-453 [» ]
3RSX X-ray 2.48 A 43-453 [» ]
3RTH X-ray 2.70 A 43-453 [» ]
3RTM X-ray 2.76 A 43-453 [» ]
3RTN X-ray 2.70 A 43-453 [» ]
3RU1 X-ray 2.30 A 43-453 [» ]
3RVI X-ray 2.65 A 43-453 [» ]
3S2O X-ray 2.60 A 48-453 [» ]
3S7L X-ray 2.16 A 46-454 [» ]
3S7M X-ray 2.20 A 46-454 [» ]
3SKF X-ray 3.00 A/B 14-454 [» ]
3SKG X-ray 2.88 A/B/D/E 14-454 [» ]
3TPJ X-ray 1.61 A 43-454 [» ]
3TPL X-ray 2.50 A/B/C 43-454 [» ]
3TPP X-ray 1.60 A 43-454 [» ]
3TPR X-ray 2.55 A 43-454 [» ]
3U6A X-ray 2.20 A/B/C 58-446 [» ]
3UDH X-ray 1.70 A 58-453 [» ]
3UDJ X-ray 1.80 A 58-453 [» ]
3UDK X-ray 2.51 A 58-453 [» ]
3UDM X-ray 1.94 A 58-453 [» ]
3UDN X-ray 2.19 A 58-453 [» ]
3UDP X-ray 1.95 A 58-453 [» ]
3UDQ X-ray 2.73 A 58-453 [» ]
3UDR X-ray 1.95 A 58-453 [» ]
3UDY X-ray 2.00 A 58-453 [» ]
3UFL X-ray 1.90 A 58-446 [» ]
3UQP X-ray 1.77 A 43-454 [» ]
3UQR X-ray 3.06 A/B/C 43-454 [» ]
3UQU X-ray 1.70 A 43-454 [» ]
3UQW X-ray 2.20 A 43-454 [» ]
3UQX X-ray 1.70 A 43-454 [» ]
3VEU X-ray 1.52 A 48-447 [» ]
3VF3 X-ray 1.48 A 48-447 [» ]
3VG1 X-ray 1.77 A 48-447 [» ]
3VV6 X-ray 2.05 A 43-454 [» ]
3VV7 X-ray 2.10 A 43-454 [» ]
3VV8 X-ray 2.50 A 43-454 [» ]
3WB4 X-ray 2.25 A 43-454 [» ]
3WB5 X-ray 2.50 A 43-454 [» ]
3ZMG X-ray 1.74 A 46-454 [» ]
3ZOV X-ray 2.10 A 46-454 [» ]
4ACU X-ray 1.75 A 43-453 [» ]
4ACX X-ray 2.00 A 43-453 [» ]
4AZY X-ray 1.79 A 43-453 [» ]
4B00 X-ray 1.83 A 43-453 [» ]
4B05 X-ray 1.80 A 43-453 [» ]
4B0Q X-ray 1.87 A 62-445 [» ]
4B1C X-ray 1.95 A 58-445 [» ]
4B1D X-ray 1.95 A 58-445 [» ]
4B1E X-ray 1.95 A 58-445 [» ]
4B70 X-ray 1.60 A 61-445 [» ]
4B72 X-ray 1.60 A 58-445 [» ]
4B77 X-ray 1.80 A 58-445 [» ]
4B78 X-ray 1.50 A 62-445 [» ]
4BEK X-ray 2.39 A 46-454 [» ]
4BFD X-ray 2.30 A 46-454 [» ]
4D83 X-ray 2.40 A/B/C 48-447 [» ]
4D85 X-ray 2.65 A 48-453 [» ]
4D88 X-ray 1.70 A 48-447 [» ]
4D89 X-ray 1.65 A 48-447 [» ]
4D8C X-ray 2.07 A/B/C 48-447 [» ]
4DH6 X-ray 2.50 A 43-453 [» ]
4DI2 X-ray 2.00 A/B/C 43-453 [» ]
4DJU X-ray 1.80 A/B 41-454 [» ]
4DJV X-ray 1.73 A/B 41-454 [» ]
4DJW X-ray 1.90 A/B 41-454 [» ]
4DJX X-ray 1.50 A/B 41-454 [» ]
4DJY X-ray 1.86 A/B 41-454 [» ]
4DPF X-ray 1.80 A 57-446 [» ]
4DPI X-ray 1.90 A 57-446 [» ]
4DUS X-ray 2.50 A 43-453 [» ]
4DV9 X-ray 2.08 A 43-454 [» ]
4DVF X-ray 1.80 A/B 43-454 [» ]
4EWO X-ray 1.80 A 61-446 [» ]
4EXG X-ray 1.80 A 61-446 [» ]
4FCO X-ray 1.76 A 43-454 [» ]
4FGX X-ray 1.59 A 43-454 [» ]
4FM7 X-ray 1.56 A 58-453 [» ]
4FM8 X-ray 1.90 A 58-453 [» ]
4FRI X-ray 2.30 A 43-453 [» ]
4FRJ X-ray 1.95 A 43-453 [» ]
4FRK X-ray 2.10 A 43-453 [» ]
4FRS X-ray 1.70 A/B 53-447 [» ]
4FS4 X-ray 1.74 A/B 58-447 [» ]
4FSE X-ray 2.65 A/B/D/E 14-454 [» ]
4FSL X-ray 2.50 A/B/D/E 43-453 [» ]
4GID X-ray 2.00 A/B/C/D 59-446 [» ]
4GMI X-ray 1.80 A 57-446 [» ]
4H1E X-ray 1.90 A/B 41-454 [» ]
4H3F X-ray 1.70 A/B 41-454 [» ]
4H3G X-ray 1.85 A/B 41-454 [» ]
4H3I X-ray 1.96 A/B 41-454 [» ]
4H3J X-ray 1.60 A/B 41-454 [» ]
4HA5 X-ray 1.83 A/B 41-454 [» ]
4HZT X-ray 1.80 A 57-453 [» ]
4I0D X-ray 1.91 A 57-453 [» ]
4I0E X-ray 1.70 A 57-453 [» ]
4I0F X-ray 1.80 A 57-453 [» ]
4I0G X-ray 1.78 A 57-453 [» ]
4I0H X-ray 2.20 A/B/C 57-453 [» ]
4I0I X-ray 2.20 A/B/C 57-453 [» ]
4I0J X-ray 1.99 A 57-453 [» ]
4I0Z X-ray 1.80 A 57-453 [» ]
4I10 X-ray 2.07 A 57-453 [» ]
4I11 X-ray 1.89 A 57-453 [» ]
4I12 X-ray 1.78 A 57-453 [» ]
4I1C X-ray 2.00 A 57-453 [» ]
4IVS X-ray 2.64 A 43-454 [» ]
4IVT X-ray 1.60 A 43-454 [» ]
4J0P X-ray 1.97 A 46-454 [» ]
4J0T X-ray 2.05 A 46-454 [» ]
4J0V X-ray 1.94 A 46-454 [» ]
4J0Y X-ray 1.77 A 46-454 [» ]
4J0Z X-ray 2.13 A 46-454 [» ]
4J17 X-ray 1.81 A 46-454 [» ]
4J1C X-ray 2.01 A 46-454 [» ]
4J1E X-ray 1.78 A 46-454 [» ]
4J1F X-ray 2.25 A 46-454 [» ]
4J1H X-ray 2.20 A 46-454 [» ]
4J1I X-ray 2.05 A 46-454 [» ]
4J1K X-ray 2.18 A 46-454 [» ]
4JOO X-ray 1.80 A 57-453 [» ]
4JP9 X-ray 1.80 A 57-453 [» ]
4JPC X-ray 1.80 A 57-453 [» ]
4JPE X-ray 1.80 A 57-453 [» ]
4K8S X-ray 2.39 A/B/C 59-446 [» ]
4K9H X-ray 2.29 A/B/C 59-446 [» ]
4KE0 X-ray 2.30 A/B/C 43-453 [» ]
4KE1 X-ray 1.91 A 43-453 [» ]
4L7G X-ray 1.38 A 57-453 [» ]
4L7H X-ray 1.85 A 57-453 [» ]
4L7J X-ray 1.65 A 57-453 [» ]
4LC7 X-ray 1.70 A 57-453 [» ]
4LXA X-ray 1.95 A/B/C 48-447 [» ]
4LXK X-ray 2.05 A/B/C 48-447 [» ]
4LXM X-ray 2.30 A/B/C 48-447 [» ]
4N00 X-ray 1.80 A 57-453 [» ]
4PZW X-ray 1.80 A 57-453 [» ]
4PZX X-ray 1.80 A 57-453 [» ]
ProteinModelPortali P56817.
SMRi P56817. Positions 58-447.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117154. 7 interactions.
IntActi P56817. 4 interactions.
MINTi MINT-242532.
STRINGi 9606.ENSP00000318585.

Chemistry

BindingDBi P56817.
ChEMBLi CHEMBL4822.
GuidetoPHARMACOLOGYi 2330.

Protein family/group databases

MEROPSi A01.004.
TCDBi 8.A.32.1.1. the -amyloid cleaving enzyme (bace1) family.

PTM databases

PhosphoSitei P56817.

Polymorphism databases

DMDMi 296434407.

Proteomic databases

PaxDbi P56817.
PRIDEi P56817.

Protocols and materials databases

DNASUi 23621.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313005 ; ENSP00000318585 ; ENSG00000186318 . [P56817-1 ]
ENST00000392937 ; ENSP00000475405 ; ENSG00000186318 . [P56817-5 ]
ENST00000428381 ; ENSP00000402228 ; ENSG00000186318 . [P56817-4 ]
ENST00000445823 ; ENSP00000403685 ; ENSG00000186318 . [P56817-3 ]
ENST00000510630 ; ENSP00000422461 ; ENSG00000186318 . [P56817-6 ]
ENST00000513780 ; ENSP00000424536 ; ENSG00000186318 . [P56817-2 ]
GeneIDi 23621.
KEGGi hsa:23621.
UCSCi uc001pqw.3. human. [P56817-2 ]
uc001pqx.3. human. [P56817-4 ]
uc001pqy.3. human. [P56817-3 ]
uc001pqz.3. human. [P56817-1 ]

Organism-specific databases

CTDi 23621.
GeneCardsi GC11M117156.
HGNCi HGNC:933. BACE1.
HPAi CAB016358.
MIMi 604252. gene.
neXtProti NX_P56817.
PharmGKBi PA25232.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71700.
HOVERGENi HBG059578.
KOi K04521.
OMAi PDMEDCG.
OrthoDBi EOG7DNNVW.
PhylomeDBi P56817.
TreeFami TF329595.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000160610-MONOMER.
BRENDAi 3.4.23.46. 2681.
SABIO-RK P56817.

Miscellaneous databases

EvolutionaryTracei P56817.
GeneWikii Beta-secretase_1.
GenomeRNAii 23621.
NextBioi 35501710.
PMAP-CutDB P56817.
PROi P56817.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56817.
Bgeei P56817.
CleanExi HS_BACE1.
Genevestigatori P56817.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, CHARACTERIZATION, VARIANT ARG-481.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), VARIANT ARG-481.
  4. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. 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. 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.

Entry informationi

Entry nameiBACE1_HUMAN
AccessioniPrimary (citable) accession number: P56817
Secondary accession number(s): A0M8W7
, B0YIU9, E9PE65, H7BXJ9, Q9BYB9, Q9BYC0, Q9BYC1, Q9UJT5, Q9ULS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi