UniProtKB - P56817 (BACE1_HUMAN)
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- BLAST>sp|P56817|BACE1_HUMAN Beta-secretase 1 OS=Homo sapiens OX=9606 GN=BACE1 PE=1 SV=3 MAQALPWLLLWMGAGVLPAHGTQHGIRLPLRSGLGGAPLGLRLPRETDEEPEEPGRRGSF VEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSST YRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGIL GLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGI DHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKK VFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRIT ILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSAC HVHDEFRTAAVEGPFVTLDMEDCGYNIPQTDESTLMTIAYVMAAICALFMLPLCLMVCQW RCLRCLRQQHDDFADDISLLK
- Align
Beta-secretase 1
BACE1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.26"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.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 93 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 289 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- amyloid-beta binding Source: Alzheimers_University_of_Toronto <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- aspartic-type endopeptidase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- beta-aspartyl-peptidase activity Source: Reactome
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- peptidase activity Source: CACAO <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- amyloid-beta metabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cellular protein metabolic process Source: Reactome
- membrane protein ectodomain proteolysis Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- modulation of chemical synaptic transmission Source: Ensembl
- protein catabolic process Source: GO_Central
- proteolysis Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Aspartyl protease, Hydrolase, Protease |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000160610-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.23.46 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-977225 Amyloid fiber formation |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P56817 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P56817 |
Protein family/group databases
MEROPS protease database More...MEROPSi | A01.004 |
Transport Classification Database More...TCDBi | 8.A.32.1.1 the Beta-amyloid cleaving enzyme (bace1) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:BACE1 Synonyms:BACE, KIAA1149 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000186318.16 |
Human Gene Nomenclature Database More...HGNCi | HGNC:933 BACE1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604252 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P56817 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endosome
- Endosome By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- Endosome By similarity
Endoplasmic reticulum
Golgi apparatus
- trans-Golgi network By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
- trans-Golgi network By similarity
Other locations
- Membrane ; Single-pass type I membrane protein
- Cell surface
- Cytoplasmic vesicle membrane
- Membrane raft By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
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.
Endoplasmic reticulum
- endoplasmic reticulum lumen Source: Reactome
Endosome
- early endosome Source: ARUK-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endosome membrane Source: Reactome
- late endosome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- multivesicular body Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Golgi apparatus
- Golgi apparatus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- Golgi-associated vesicle lumen Source: Reactome
- trans-Golgi network Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- integral component of plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- plasma membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- axon Source: Ensembl
- cell surface Source: UniProtKB-SubCell
- cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- membrane raft Source: UniProtKB-SubCell
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 22 – 457 | ExtracellularSequence analysisAdd BLAST | 436 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 458 – 478 | HelicalSequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 479 – 501 | CytoplasmicSequence analysisAdd BLAST | 23 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Organism-specific databases
DisGeNET More...DisGeNETi | 23621 |
Open Targets More...OpenTargetsi | ENSG00000186318 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25232 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4822 |
Drug and drug target database More...DrugBanki | DB07736 (2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide DB07737 (2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide DB07535 2-amino-6-[2-(1H-indol-6-yl)ethyl]pyrimidin-4(3H)-one DB08749 3-(2-AMINO-6-BENZOYLQUINAZOLIN-3(4H)-YL)-N-CYCLOHEXYL-N-METHYLPROPANAMIDE DB07345 4-(2-aminoethyl)-2-cyclohexylphenol DB07346 4-(2-aminoethyl)-2-ethylphenol DB07110 4-(4-FLUOROBENZYL)PIPERIDINE DB07415 4-[(1S)-1-(3-fluoro-4-methoxyphenyl)-2-(2-methoxy-5-nitrophenyl)ethyl]-1H-imidazol-2-amine DB07206 6-[2-(1H-INDOL-6-YL)ETHYL]PYRIDIN-2-AMINE DB07245 6-[2-(3'-METHOXYBIPHENYL-3-YL)ETHYL]PYRIDIN-2-AMINE DB06073 CTS-21166 DB08929 MK-8931 DB02378 MMI-175 DB07734 N-(1-benzylpiperidin-4-yl)-4-sulfanylbutanamide DB07089 N-[amino(imino)methyl]-2-[2-(2-chlorophenyl)-4-(4-propoxyphenyl)-3-thienyl]acetamide DB07175 N-{2-methyl-5-[(6-phenylpyrimidin-4-yl)amino]phenyl}methanesulfonamide |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2330 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BACE1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 296434407 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 21 | Sequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000025939 | 22 – 45 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 24 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000025940 | 46 – 501 | Beta-secretase 1Add BLAST | 456 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 126 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 153 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 172 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 216 ↔ 420 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 223 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 275 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 278 ↔ 443 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 279 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 285 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 299 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 300 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 307 | N6-acetyllysine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 330 ↔ 380 | 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 354 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 474 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 478 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 482 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 485 | S-palmitoyl cysteineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 498 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.23"A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1."
Costantini C., Ko M.H., Jonas M.C., Puglielli L.
Biochem. J. 407:383-395(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307, GLYCOSYLATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"A reversible form of lysine acetylation in the ER and Golgi lumen controls the molecular stabilization of BACE1."
Costantini C., Ko M.H., Jonas M.C., Puglielli L.
Biochem. J. 407:383-395(2007) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307, GLYCOSYLATION. - Ref.25"Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels."
Ko M.H., Puglielli L.
J. Biol. Chem. 284:2482-2492(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307 BY NAT8 AND NAT8B, DEACETYLATION, INTERACTION WITH NAT8 AND NAT8B.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, ZymogenProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P56817 |
PeptideAtlas More...PeptideAtlasi | P56817 |
PRoteomics IDEntifications database More...PRIDEi | P56817 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56947 56948 [P56817-2] 56949 [P56817-3] 56950 [P56817-4] |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 71 72 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P56817 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P56817 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P56817 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P56817 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000186318 |
CleanEx database of gene expression profiles More...CleanExi | HS_BACE1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P56817 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P56817 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB016358 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.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. - Ref.24"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. - Ref.25"Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-based lysine acetyltransferases post-translationally regulate BACE1 levels."
Ko M.H., Puglielli L.
J. Biol. Chem. 284:2482-2492(2009) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307 BY NAT8 AND NAT8B, DEACETYLATION, INTERACTION WITH NAT8 AND NAT8B. - Ref.26"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. - Ref.27"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. - Ref.28"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. - Ref.30"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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Clec4g | Q8BNX1 | 2 | EBI-2433139,EBI-11176364 | From Mus musculus. |
| FLOT2 | Q14254 | 2 | EBI-2433139,EBI-348613 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117154, 19 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P56817 |
Database of interacting proteins More...DIPi | DIP-41388N |
Protein interaction database and analysis system More...IntActi | P56817, 9 interactors |
Molecular INTeraction database More...MINTi | P56817 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000318585 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P56817 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 61 – 63 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 67 – 70 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 71 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 75 – 81 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 82 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 86 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 99 – 102 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 109 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 115 – 117 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 122 – 131 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 132 – 134 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 136 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 149 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 155 – 168 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 172 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 178 – 181 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 185 – 187 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 188 – 190 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 197 – 204 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 211 – 215 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 224 – 229 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 230 – 239 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 242 – 244 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 245 – 253 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 257 – 260 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 264 – 269 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 278 – 282 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 286 – 288 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 294 – 298 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 299 – 312 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 313 – 315 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 320 – 323 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 329 – 332 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 333 – 335 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 338 – 340 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 344 – 349 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 355 – 361 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 363 – 366 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 367 – 369 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 373 – 375 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 378 – 383 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 385 – 390 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 392 – 394 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 396 – 399 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 402 – 407 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 408 – 411 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 412 – 418 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 430 – 436 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 440 – 443 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P56817 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P56817 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P56817 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 75 – 416 | Peptidase A1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 342 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 479 – 501 | Interaction with RTN3Add BLAST | 23 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Signal, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1339 Eukaryota ENOG410XNV7 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144168 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG059578 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P56817 |
KEGG Orthology (KO) More...KOi | K04521 |
Identification of Orthologs from Complete Genome Data More...OMAi | PDMEDCG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0CNK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P56817 |
TreeFam database of animal gene trees More...TreeFami | TF329595 |
Family and domain databases
Conserved Domains Database More...CDDi | cd05473 beta_secretase_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.70.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001461 Aspartic_peptidase_A1 IPR001969 Aspartic_peptidase_AS IPR009119 BACE IPR009120 BACE1 IPR033874 Memapsin-like IPR033121 PEPTIDASE_A1 IPR021109 Peptidase_aspartic_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR13683 PTHR13683, 1 hit PTHR13683:SF245 PTHR13683:SF245, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00026 Asp, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01816 BACE1 PR01815 BACEFAMILY PR00792 PEPSIN |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50630 SSF50630, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00141 ASP_PROTEASE, 1 hit PS51767 PEPTIDASE_A1, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
160 170 180 190 200
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS
210 220 230 240 250
LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW
260 270 280 290 300
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
310 320 330 340 350
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG
360 370 380 390 400
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME
410 420 430 440 450
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT
460 470 480 490 500
DESTLMTIAY VMAAICALFM LPLCLMVCQW RCLRCLRQQH DDFADDISLL
K
The sequence of this isoform differs from the canonical sequence as follows:
190-214: Missing.
10 20 30 40 50
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
160 170 180 190 200
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARL CGAGFPLNQS
210 220 230 240 250
EVLASVGGSM IIGGIDHSLY TGSLWYTPIR REWYYEVIIV RVEINGQDLK
260 270 280 290 300
MDCKEYNYDK SIVDSGTTNL RLPKKVFEAA VKSIKAASST EKFPDGFWLG
310 320 330 340 350
EQLVCWQAGT TPWNIFPVIS LYLMGEVTNQ SFRITILPQQ YLRPVEDVAT
360 370 380 390 400
SQDDCYKFAI SQSSTGTVMG AVIMEGFYVV FDRARKRIGF AVSACHVHDE
410 420 430 440 450
FRTAAVEGPF VTLDMEDCGY NIPQTDESTL MTIAYVMAAI CALFMLPLCL
460 470
MVCQWRCLRC LRQQHDDFAD DISLLK
The sequence of this isoform differs from the canonical sequence as follows:
146-189: Missing.
10 20 30 40 50
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLPDDSL
160 170 180 190 200
EPFFDSLVKQ THVPNLFSLQ LCGAGFPLNQ SEVLASVGGS MIIGGIDHSL
210 220 230 240 250
YTGSLWYTPI RREWYYEVII VRVEINGQDL KMDCKEYNYD KSIVDSGTTN
260 270 280 290 300
LRLPKKVFEA AVKSIKAASS TEKFPDGFWL GEQLVCWQAG TTPWNIFPVI
310 320 330 340 350
SLYLMGEVTN QSFRITILPQ QYLRPVEDVA TSQDDCYKFA ISQSSTGTVM
360 370 380 390 400
GAVIMEGFYV VFDRARKRIG FAVSACHVHD EFRTAAVEGP FVTLDMEDCG
410 420 430 440 450
YNIPQTDEST LMTIAYVMAA ICALFMLPLC LMVCQWRCLR CLRQQHDDFA
DDISLLK
The sequence of this isoform differs from the canonical sequence as follows:
146-189: Missing.
190-214: Missing.
10 20 30 40 50
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
PEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLLCGAG
160 170 180 190 200
FPLNQSEVLA SVGGSMIIGG IDHSLYTGSL WYTPIRREWY YEVIIVRVEI
210 220 230 240 250
NGQDLKMDCK EYNYDKSIVD SGTTNLRLPK KVFEAAVKSI KAASSTEKFP
260 270 280 290 300
DGFWLGEQLV CWQAGTTPWN IFPVISLYLM GEVTNQSFRI TILPQQYLRP
310 320 330 340 350
VEDVATSQDD CYKFAISQSS TGTVMGAVIM EGFYVVFDRA RKRIGFAVSA
360 370 380 390 400
CHVHDEFRTA AVEGPFVTLD MEDCGYNIPQ TDESTLMTIA YVMAAICALF
410 420 430
MLPLCLMVCQ WRCLRCLRQQ HDDFADDISL LK
The sequence of this isoform differs from the canonical sequence as follows:
1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
21-120: Missing.
10 20 30 40 50
MVPFIYLQAH FTLCSGWSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
60 70 80 90 100
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS
110 120 130 140 150
LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI DHSLYTGSLW
160 170 180 190 200
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
210 220 230 240 250
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG
260 270 280 290 300
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME
310 320 330 340 350
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT
360 370 380 390 400
DESTLMTIAY VMAAICALFM LPLCLMVCQW RCLRCLRQQH DDFADDISLL
K
The sequence of this isoform differs from the canonical sequence as follows:
1-20: MAQALPWLLLWMGAGVLPAH → MVPFIYLQAHFTLCSGWSST
21-120: Missing.
190-214: Missing.
10 20 30 40 50
MVPFIYLQAH FTLCSGWSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
60 70 80 90 100
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARL CGAGFPLNQS
110 120 130 140 150
EVLASVGGSM IIGGIDHSLY TGSLWYTPIR REWYYEVIIV RVEINGQDLK
160 170 180 190 200
MDCKEYNYDK SIVDSGTTNL RLPKKVFEAA VKSIKAASST EKFPDGFWLG
210 220 230 240 250
EQLVCWQAGT TPWNIFPVIS LYLMGEVTNQ SFRITILPQQ YLRPVEDVAT
260 270 280 290 300
SQDDCYKFAI SQSSTGTVMG AVIMEGFYVV FDRARKRIGF AVSACHVHDE
310 320 330 340 350
FRTAAVEGPF VTLDMEDCGY NIPQTDESTL MTIAYVMAAI CALFMLPLCL
360 370
MVCQWRCLRC LRQQHDDFAD DISLLK
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060692 | 265 | V → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051509 | 481 | R → C. Corresponds to variant dbSNP:rs539765Ensembl. | 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047092 | 1 – 20 | MAQAL…VLPAH → MVPFIYLQAHFTLCSGWSST in isoform 5 and isoform 6. CuratedAdd BLAST | 20 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_047093 | 21 – 120 | Missing in isoform 5 and isoform 6. CuratedAdd BLAST | 100 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005222 | 146 – 189 | Missing in isoform C and isoform D. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 44 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005223 | 190 – 214 | Missing in isoform B, isoform D and isoform 6. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 25 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...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] |
Protein sequence database of the Protein Information Resource More...PIRi | A59090 |
NCBI Reference Sequences More...RefSeqi | NP_001193978.1, NM_001207049.1 [P56817-6] NP_036236.1, NM_012104.4 [P56817-1] NP_620427.1, NM_138971.3 [P56817-3] NP_620428.1, NM_138972.3 [P56817-2] NP_620429.1, NM_138973.3 [P56817-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.504003 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...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] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23621 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23621 |
UCSC genome browser More...UCSCi | uc001pqw.4 human [P56817-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P56817 | Beta-site APP-cleaving enzyme 1, isoform CRA_d | 501 | |||
| BACE1 isoform 1 | 501 | ||||
| UPI0006526458 | 388 | ||||
| UPI000350839D | 385 | ||||
| UPI00006881AC | 388 | ||||
| +12 | |||||
| P56817-2 | Beta-site APP-cleaving enzyme 1, isoform CRA_c | 476 | |||
| BACE1 isoform 3 | 476 | ||||
| P56817-3 | Beta-site APP-cleaving enzyme 1, isoform CRA_b | 457 | |||
| BACE1 isoform 5 | 457 | ||||
| P56817-4 | Beta-site APP-cleaving enzyme 1, isoform CRA_a | 432 | |||
| BACE1 isoform 4 | 432 | ||||
| P56817-5 | Beta-site APP-cleaving enzyme 1, isoform CRA_f | 401 | |||
| KIAA1149 splice variant 1 (Fragment) | 396 | ||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P56817 | Beta-site APP-cleaving enzyme 1, isoform CRA_d | 501 | |||
| BACE1 isoform 1 | 501 | ||||
| UPI000C87BEA4 | 508 | ||||
| UPI000C9DBBE4 | 508 | ||||
| Beta-secretase 1 precursor | 506 | ||||
| +163 | |||||
| P56817-2 | Beta-secretase 1 | 473 | |||
| UPI000C87C3FF | 483 | ||||
| UPI000C9EBB10 | 483 | ||||
| Beta-site APP-cleaving enzyme 1, isoform CRA_c | 476 | ||||
| BACE1 isoform 3 | 476 | ||||
| +30 | |||||
| P56817-3 | Beta-site APP-cleaving enzyme 1, isoform CRA_b | 457 | |||
| BACE1 isoform 5 | 457 | ||||
| UPI00034474CF | 461 | ||||
| Beta-secretase 1 isoform C preproprotein | 457 | ||||
| beta-secretase 1 isoform X3 | 457 | ||||
| +22 | |||||
| P56817-4 | Beta-secretase 1 | 436 | |||
| Beta-secretase 1 | 436 | ||||
| Beta-secretase 1 | 436 | ||||
| Beta-secretase 1 | 436 | ||||
| Beta-secretase 1 | 432 | ||||
| +22 | |||||
| P56817-5 | BACE1 isoform 10 | 401 | |||
| Beta-site APP-cleaving enzyme 1, isoform CRA_f | 401 | ||||
| BACE1 isoform 9 | 401 | ||||
| Beta-secretase 1 | 401 | ||||
| Beta-secretase 1 | 401 | ||||
| +5 | |||||
| P56817-6 | cDNA FLJ54690, highly similar to Beta-secretase 1 (EC 3.4.23.46) | 376 | |||
| BACE1 isoform 10 | 376 | ||||
| BACE1 isoform 11 | 376 | ||||
| UPI0003AB4DFF | 376 | ||||
| UPI0005F3DFC5 | 376 | ||||
| +2 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P56817 | Beta-site APP-cleaving enzyme 1, isoform CRA_d | 501 | |||
| BACE1 isoform 1 | 501 | ||||
| UPI000C87BEA4 | 508 | ||||
| UPI000C9DBBE4 | 508 | ||||
| Beta-secretase 1 precursor | 506 | ||||
| +239 | |||||
| P56817-2 | Beta-secretase 1 | 473 | |||
| UPI000C87C3FF | 483 | ||||
| UPI000C9EBB10 | 483 | ||||
| UPI0003F0A91E | 476 | ||||
| UPI0007883E1D | 476 | ||||
| +34 | |||||
| P56817-3 | Beta-secretase 1 | 507 | |||
| UPI0009B4B8DC | 529 | ||||
| UPI000A1C3C60 | 520 | ||||
| Beta-secretase 1 | 490 | ||||
| UPI0007AC65F4 | 465 | ||||
| +66 | |||||
| P56817-4 | Beta-secretase 1 | 427 | |||
| Beta-secretase 1 | 519 | ||||
| UPI000523B8C9 | 350 | ||||
| UPI0005212208 | 225 | ||||
| UPI0003314543 | 439 | ||||
| +77 | |||||
| P56817-5 | Predicted protein (Fragment) | 421 | |||
| Beta-secretase 1 | 401 | ||||
| Beta-site APP-cleaving enzyme 1, isoform CRA_f | 401 | ||||
| Beta-secretase 1 | 401 | ||||
| UPI0005F4535A | 401 | ||||
| +16 | |||||
| P56817-6 | cDNA FLJ54690, highly similar to Beta-secretase 1 (EC 3.4.23.46) | 376 | |||
| UPI0003AB4DFF | 376 | ||||
| BACE1 isoform 10 | 376 | ||||
| BACE1 isoform 11 | 376 | ||||
| UPI0008F470A4 | 376 | ||||
| +15 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...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] |
Protein sequence database of the Protein Information Resource More...PIRi | A59090 |
NCBI Reference Sequences More...RefSeqi | NP_001193978.1, NM_001207049.1 [P56817-6] NP_036236.1, NM_012104.4 [P56817-1] NP_620427.1, NM_138971.3 [P56817-3] NP_620428.1, NM_138972.3 [P56817-2] NP_620429.1, NM_138973.3 [P56817-4] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.504003 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB 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 | [»] | |
| 4R5N | X-ray | 1.80 | A | 57-453 | [»] | |
| 4R8Y | X-ray | 1.90 | A/B | 41-454 | [»] | |
| 4R91 | X-ray | 1.58 | A/B | 41-454 | [»] | |
| 4R92 | X-ray | 1.71 | A/B | 41-454 | [»] | |
| 4R93 | X-ray | 1.71 | A/B | 41-454 | [»] | |
| 4R95 | X-ray | 1.99 | A/B | 41-454 | [»] | |
| 4RCD | X-ray | 1.90 | A | 43-453 | [»] | |
| 4RCE | X-ray | 2.40 | A | 43-453 | [»] | |
| 4RCF | X-ray | 1.78 | A | 43-453 | [»] | |
| 4RRN | X-ray | 1.80 | A | 57-453 | [»] | |
| 4RRO | X-ray | 1.80 | A | 57-453 | [»] | |
| 4RRS | X-ray | 1.80 | A | 57-453 | [»] | |
| 4TRW | X-ray | 2.85 | A/B/C | 58-447 | [»] | |
| 4TRY | X-ray | 2.75 | A/B/C | 60-447 | [»] | |
| 4TRZ | X-ray | 3.25 | A/B/C | 60-447 | [»] | |
| 4WTU | X-ray | 1.85 | A | 43-453 | [»] | |
| 4WY1 | X-ray | 1.98 | A | 58-453 | [»] | |
| 4WY6 | X-ray | 2.10 | A | 46-454 | [»] | |
| 4X2L | X-ray | 2.55 | A | 46-454 | [»] | |
| 4X7I | X-ray | 1.77 | A/B | 14-454 | [»] | |
| 4XKX | X-ray | 1.80 | A | 43-453 | [»] | |
| 4XXS | X-ray | 1.86 | A | 46-454 | [»] | |
| 4YBI | X-ray | 1.84 | A/B | 14-454 | [»] | |
| 4ZPE | X-ray | 1.70 | A | 43-446 | [»] | |
| 4ZPF | X-ray | 1.80 | A | 43-446 | [»] | |
| 4ZPG | X-ray | 2.00 | A | 43-446 | [»] | |
| 4ZSM | X-ray | 1.96 | A/B | 14-454 | [»] | |
| 4ZSP | X-ray | 1.91 | A/B | 14-454 | [»] | |
| 4ZSQ | X-ray | 2.30 | A/B | 14-454 | [»] | |
| 4ZSR | X-ray | 1.65 | A/B | 14-454 | [»] | |
| 5CLM | X-ray | 2.61 | A | 46-446 | [»] | |
| 5DQC | X-ray | 2.47 | A/B/C | 58-447 | [»] | |
| 5ENK | X-ray | 2.11 | A | 14-454 | [»] | |
| 5ENM | X-ray | 1.98 | A | 14-454 | [»] | |
| 5EZX | X-ray | 1.90 | A | 57-446 | [»] | |
| 5EZZ | X-ray | 2.10 | A | 57-446 | [»] | |
| 5F00 | X-ray | 1.95 | A | 57-446 | [»] | |
| 5F01 | X-ray | 1.52 | A | 57-446 | [»] | |
| 5HD0 | X-ray | 1.65 | A/B | 41-454 | [»] | |
| 5HDU | X-ray | 1.58 | A/B | 41-454 | [»] | |
| 5HDV | X-ray | 1.71 | A/B | 41-454 | [»] | |
| 5HDX | X-ray | 1.60 | A/B | 41-454 | [»] | |
| 5HDZ | X-ray | 1.49 | A/B | 41-454 | [»] | |
| 5HE4 | X-ray | 1.53 | A/B | 41-454 | [»] | |
| 5HE5 | X-ray | 1.55 | A/B | 41-454 | [»] | |
| 5HE7 | X-ray | 1.71 | A/B | 41-454 | [»] | |
| 5HTZ | X-ray | 1.95 | A/B | 43-454 | [»] | |
| 5HU0 | X-ray | 1.83 | A/B | 43-454 | [»] | |
| 5HU1 | X-ray | 1.50 | A/B | 43-454 | [»] | |
| 5I3V | X-ray | 1.62 | A | 43-453 | [»] | |
| 5I3W | X-ray | 2.15 | A | 43-453 | [»] | |
| 5I3X | X-ray | 1.85 | A | 43-453 | [»] | |
| 5I3Y | X-ray | 2.15 | A | 43-453 | [»] | |
| 5IE1 | X-ray | 2.30 | A | 43-453 | [»] | |
| 5KQF | X-ray | 1.98 | A | 14-454 | [»] | |
| 5KR8 | X-ray | 2.12 | A | 14-454 | [»] | |
| 5MBW | X-ray | 2.95 | A | 46-454 | [»] | |
| 5MCO | X-ray | 2.49 | A | 46-454 | [»] | |
| 5MCQ | X-ray | 1.82 | A | 46-454 | [»] | |
| 5MXD | X-ray | 2.52 | A/B/C | 22-446 | [»] | |
| 5T1U | X-ray | 1.78 | A | 46-454 | [»] | |
| 5T1W | X-ray | 2.96 | A | 46-454 | [»] | |
| 5TOL | X-ray | 2.51 | A | 43-454 | [»] | |
| 5UYU | X-ray | 1.90 | A | 43-453 | [»] | |
| 5V0N | X-ray | 2.15 | A/B/C | 14-454 | [»] | |
| 5YGY | X-ray | 2.30 | A | 43-454 | [»] | |
| 6BFD | X-ray | 1.62 | A/B | 14-454 | [»] | |
| 6BFE | X-ray | 1.51 | A/B | 14-454 | [»] | |
| 6BFW | X-ray | 1.84 | A/B | 14-454 | [»] | |
| 6BFX | X-ray | 1.99 | A/B | 14-454 | [»] | |
| 6C2I | X-ray | 1.95 | A | 43-453 | [»] | |
| 6EJ2 | X-ray | 1.46 | A | 1-501 | [»] | |
| 6EJ3 | X-ray | 1.94 | A | 1-501 | [»] | |
| 6FGY | X-ray | 1.54 | A | 60-453 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P56817 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P56817 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 117154, 19 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | P56817 |
Database of interacting proteins More...DIPi | DIP-41388N |
Protein interaction database and analysis system More...IntActi | P56817, 9 interactors |
Molecular INTeraction database More...MINTi | P56817 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000318585 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P56817 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL4822 |
Drug and drug target database More...DrugBanki | DB07736 (2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide DB07737 (2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide DB07535 2-amino-6-[2-(1H-indol-6-yl)ethyl]pyrimidin-4(3H)-one DB08749 3-(2-AMINO-6-BENZOYLQUINAZOLIN-3(4H)-YL)-N-CYCLOHEXYL-N-METHYLPROPANAMIDE DB07345 4-(2-aminoethyl)-2-cyclohexylphenol DB07346 4-(2-aminoethyl)-2-ethylphenol DB07110 4-(4-FLUOROBENZYL)PIPERIDINE DB07415 4-[(1S)-1-(3-fluoro-4-methoxyphenyl)-2-(2-methoxy-5-nitrophenyl)ethyl]-1H-imidazol-2-amine DB07206 6-[2-(1H-INDOL-6-YL)ETHYL]PYRIDIN-2-AMINE DB07245 6-[2-(3'-METHOXYBIPHENYL-3-YL)ETHYL]PYRIDIN-2-AMINE DB06073 CTS-21166 DB08929 MK-8931 DB02378 MMI-175 DB07734 N-(1-benzylpiperidin-4-yl)-4-sulfanylbutanamide DB07089 N-[amino(imino)methyl]-2-[2-(2-chlorophenyl)-4-(4-propoxyphenyl)-3-thienyl]acetamide DB07175 N-{2-methyl-5-[(6-phenylpyrimidin-4-yl)amino]phenyl}methanesulfonamide |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2330 |
Protein family/group databases
MEROPS protease database More...MEROPSi | A01.004 |
Transport Classification Database More...TCDBi | 8.A.32.1.1 the Beta-amyloid cleaving enzyme (bace1) family |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 71 72 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P56817 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P56817 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P56817 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BACE1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 296434407 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P56817 |
PeptideAtlas More...PeptideAtlasi | P56817 |
PRoteomics IDEntifications database More...PRIDEi | P56817 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56947 56948 [P56817-2] 56949 [P56817-3] 56950 [P56817-4] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 23621 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...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] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 23621 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:23621 |
UCSC genome browser More...UCSCi | uc001pqw.4 human [P56817-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 23621 |
DisGeNET More...DisGeNETi | 23621 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000186318.16 |
GeneCards: human genes, protein and diseases More...GeneCardsi | BACE1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:933 BACE1 |
Human Protein Atlas More...HPAi | CAB016358 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604252 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P56817 |
Open Targets More...OpenTargetsi | ENSG00000186318 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA25232 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1339 Eukaryota ENOG410XNV7 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144168 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG059578 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P56817 |
KEGG Orthology (KO) More...KOi | K04521 |
Identification of Orthologs from Complete Genome Data More...OMAi | PDMEDCG |
Database of Orthologous Groups More...OrthoDBi | EOG091G0CNK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P56817 |
TreeFam database of animal gene trees More...TreeFami | TF329595 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:ENSG00000160610-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.23.46 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-977225 Amyloid fiber formation |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P56817 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P56817 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | BACE1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P56817 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Beta-secretase_1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 23621 |
CutDB - Proteolytic event database More...PMAP-CutDBi | P56817 |
Protein Ontology More...PROi | PR:P56817 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000186318 |
CleanEx database of gene expression profiles More...CleanExi | HS_BACE1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P56817 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P56817 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd05473 beta_secretase_like, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 2.40.70.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001461 Aspartic_peptidase_A1 IPR001969 Aspartic_peptidase_AS IPR009119 BACE IPR009120 BACE1 IPR033874 Memapsin-like IPR033121 PEPTIDASE_A1 IPR021109 Peptidase_aspartic_dom_sf |
The PANTHER Classification System More...PANTHERi | PTHR13683 PTHR13683, 1 hit PTHR13683:SF245 PTHR13683:SF245, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF00026 Asp, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01816 BACE1 PR01815 BACEFAMILY PR00792 PEPSIN |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50630 SSF50630, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00141 ASP_PROTEASE, 1 hit PS51767 PEPTIDASE_A1, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | BACE1_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P56817Primary (citable) accession number: P56817 Secondary accession number(s): A0M8W7 , B0YIU9, E9PE65, H7BXJ9, Q9BYB9, Q9BYC0, Q9BYC1, Q9UJT5, Q9ULS1 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
| Last sequence update: | June 7, 2017 | |
| Last modified: | July 18, 2018 | |
| This is version 204 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- 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 - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
