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Beta-secretase 1 (EC 3.4.23.46) (Aspartyl protease 2) (ASP2) (Asp 2) (Beta-site amyloid precursor protein cleaving enzyme 1) (Beta-site APP cleaving enzyme 1) (Memapsin-2) (Membrane-associated aspartic protease 2)

 BACE1_HUMAN             Reviewed;         501 AA.
P56817; A0M8W7; B0YIU9; E9PE65; H7BXJ9; Q9BYB9; Q9BYC0; Q9BYC1;
Q9UJT5; Q9ULS1;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
07-JUN-2017, sequence version 3.
05-DEC-2018, entry version 208.
RecName: Full=Beta-secretase 1 {ECO:0000305};
EC=3.4.23.46 {ECO:0000269|PubMed:10677483};
AltName: Full=Aspartyl protease 2 {ECO:0000303|PubMed:10656250};
Short=ASP2 {ECO:0000303|PubMed:10656250};
Short=Asp 2 {ECO:0000303|PubMed:10656250};
AltName: Full=Beta-site amyloid precursor protein cleaving enzyme 1;
Short=Beta-site APP cleaving enzyme 1;
AltName: Full=Memapsin-2 {ECO:0000303|PubMed:10677483, ECO:0000303|PubMed:14567678};
AltName: Full=Membrane-associated aspartic protease 2;
Flags: Precursor;
Name=BACE1 {ECO:0000312|HGNC:HGNC:933}; Synonyms=BACE, KIAA1149;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Brain;
PubMed=10531052; DOI=10.1126/science.286.5440.735;
Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A.,
Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y.,
Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A.,
Biere A.L., Curran E., Burgess T., Louis J.-C., Collins F.,
Treanor J., Rogers G., Citron M.;
"Beta-secretase cleavage of Alzheimer's amyloid precursor protein by
the transmembrane aspartic protease BACE.";
Science 286:735-741(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 46-68, AND
CHARACTERIZATION.
TISSUE=Brain;
PubMed=10591214; DOI=10.1038/990114;
Sinha S., Anderson J.P., Barbour R., Basi G.S., Caccavello R.,
Davis D., Doan M., Dovey H.F., Frigon N., Hong J., Jacobson-Croak K.,
Jewett N., Keim P., Knops J., Lieberburg I., Power M., Tan H.,
Tatsuno G., Tung J., Schenk D., Seubert P., Suomensaari S.M., Wang S.,
Walker D., Zhao J., McConlogue L., Varghese J.;
"Purification and cloning of amyloid precursor protein beta-secretase
from human brain.";
Nature 402:537-540(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
PubMed=10591213; DOI=10.1038/990107;
Yan R., Bienkowski M.J., Shuck M.E., Miao H., Tory M.C., Pauley A.M.,
Brashier J.R., Stratman N.C., Mathews W.R., Buhl A.E., Carter D.B.,
Tomasselli A.G., Parodi L.A., Heinrikson R.L., Gurney M.E.;
"Membrane-anchored aspartyl protease with Alzheimer's disease beta-
secretase activity.";
Nature 402:533-537(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND MUTAGENESIS OF
ASP-93 AND ASP-284.
PubMed=10656250; DOI=10.1006/mcne.1999.0811;
Hussain I., Powell D.J., Howlett D.R., Tew D.G., Meek T.D.,
Chapman C., Gloger I.S., Murphy K.E., Southan C.D., Ryan D.M.,
Smith T.S., Simmons D.L., Walsh F.S., Dingwall C., Christie G.;
"Identification of a novel aspartic proteinase (Asp 2) as beta-
secretase.";
Mol. Cell. Neurosci. 14:419-427(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Brain, and Pancreas;
Michel B., De Pietri Tonelli D., Zacchetti D., Keller P.;
"New beta-site APP cleaving enzyme isoform (BACE-1B) obtained from
human brain and pancreas.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
TISSUE=Pancreas;
Zacchetti D., De Pietri Tonelli D., Schnurbus R.;
"New beta-site APP cleaving enzyme isoform (BACE-1C) obtained from
human pancreas.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D).
TISSUE=Brain;
PubMed=11516562; DOI=10.1016/S0304-3940(01)01912-7;
Tanahashi H., Tabira T.;
"Three novel alternatively spliced isoforms of the human beta-site
amyloid precursor protein cleaving enzyme (BACE) and their effect on
amyloid beta-peptide production.";
Neurosci. Lett. 307:9-12(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Brain;
PubMed=10574461; DOI=10.1093/dnares/6.5.329;
Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
"Characterization of cDNA clones selected by the GeneMark analysis
from size-fractionated cDNA libraries from human brain.";
DNA Res. 6:329-336(1999).
[9]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-265.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-501 (ISOFORM A), FUNCTION, TISSUE
SPECIFICITY, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10677483; DOI=10.1073/pnas.97.4.1456;
Lin X., Koelsch G., Wu S., Downs D., Dashti A., Tang J.;
"Human aspartic protease memapsin 2 cleaves the beta-secretase site of
beta-amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 97:1456-1460(2000).
[16]
TISSUE SPECIFICITY, AND GLYCOSYLATION.
PubMed=11083922; DOI=10.1006/mcne.2000.0884;
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.;
"ASP1 (BACE2) cleaves the amyloid precursor protein at the beta-
secretase site.";
Mol. Cell. Neurosci. 16:609-619(2000).
[17]
SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=11466313; DOI=10.1074/jbc.M104350200;
Yan R., Han P., Miao H., Greengard P., Xu H.;
"The transmembrane domain of the Alzheimer's beta-secretase (BACE1)
determines its late Golgi localization and access to beta -amyloid
precursor protein (APP) substrate.";
J. Biol. Chem. 276:36788-36796(2001).
[18]
DISULFIDE BONDS.
PubMed=11953458; DOI=10.1046/j.0022-3042.2002.00806.x;
Fischer F., Molinari M., Bodendorf U., Paganetti P.;
"The disulphide bonds in the catalytic domain of BACE are critical but
not essential for amyloid precursor protein processing activity.";
J. Neurochem. 80:1079-1088(2002).
[19]
INTERACTION WITH GGA1; GGA2 AND GGA3.
PubMed=14567678; DOI=10.1021/bi035199h;
He X., Zhu G., Koelsch G., Rodgers K.K., Zhang X.C., Tang J.;
"Biochemical and structural characterization of the interaction of
memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of
GGA proteins.";
Biochemistry 42:12174-12180(2003).
[20]
INTERACTION WITH RTN3 AND RTN4, AND ACTIVITY REGULATION.
PubMed=15286784; DOI=10.1038/nm1088;
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.;
"Reticulon family members modulate BACE1 activity and amyloid-beta
peptide generation.";
Nat. Med. 10:959-965(2004).
[21]
SUBCELLULAR LOCATION, MUTAGENESIS OF 499-LEU-LEU-500, AND LYSOSOMAL
DEGRADATION.
PubMed=16033761; DOI=10.1074/jbc.M506199200;
Koh Y.H., von Arnim C.A., Hyman B.T., Tanzi R.E., Tesco G.;
"BACE is degraded via the lysosomal pathway.";
J. Biol. Chem. 280:32499-32504(2005).
[22]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-498 AND 499-LEU-LEU-500.
PubMed=15615712; DOI=10.1074/jbc.M411296200;
He X., Li F., Chang W.P., Tang J.;
"GGA proteins mediate the recycling pathway of memapsin 2 (BACE).";
J. Biol. Chem. 280:11696-11703(2005).
[23]
SUBCELLULAR LOCATION, MUTAGENESIS OF SER-498, AND PHOSPHORYLATION AT
SER-498.
PubMed=15886016; DOI=10.1016/j.mcn.2005.03.014;
Wahle T., Prager K., Raffler N., Haass C., Famulok M., Walter J.;
"GGA proteins regulate retrograde transport of BACE1 from endosomes to
the trans-Golgi network.";
Mol. Cell. Neurosci. 29:453-461(2005).
[24]
INTERACTION WITH RTN3 AND RTN4, AND ACTIVITY REGULATION.
PubMed=16965550; DOI=10.1111/j.1460-9568.2006.05005.x;
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.;
"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its
ability to produce amyloid beta-protein.";
Eur. J. Neurosci. 24:1237-1244(2006).
[25]
INTERACTION WITH RTN3.
PubMed=16979658; DOI=10.1016/j.jmb.2006.07.094;
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.;
"Mapping of interaction domains mediating binding between BACE1 and
RTN/Nogo proteins.";
J. Mol. Biol. 363:625-634(2006).
[26]
IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION
AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300 AND LYS-307,
AND GLYCOSYLATION.
PubMed=17425515; DOI=10.1042/BJ20070040;
Costantini C., Ko M.H., Jonas M.C., Puglielli L.;
"A reversible form of lysine acetylation in the ER and Golgi lumen
controls the molecular stabilization of BACE1.";
Biochem. J. 407:383-395(2007).
[27]
INTERACTION WITH PCSK9.
PubMed=18660751; DOI=10.1038/embor.2008.132;
Jonas M.C., Costantini C., Puglielli L.;
"PCSK9 is required for the disposal of non-acetylated intermediates of
the nascent membrane protein BACE1.";
EMBO Rep. 9:916-922(2008).
[28]
ACETYLATION AT LYS-126; LYS-275; LYS-279; LYS-285; LYS-299; LYS-300
AND LYS-307 BY NAT8 AND NAT8B, DEACETYLATION, AND INTERACTION WITH
NAT8 AND NAT8B.
PubMed=19011241; DOI=10.1074/jbc.M804901200;
Ko M.H., Puglielli L.;
"Two endoplasmic reticulum (ER)/ER Golgi intermediate compartment-
based lysine acetyltransferases post-translationally regulate BACE1
levels.";
J. Biol. Chem. 284:2482-2492(2009).
[29]
FUNCTION, INTERACTION WITH SNX6, AND SUBCELLULAR LOCATION.
PubMed=20354142; DOI=10.1096/fj.09-146357;
Okada H., Zhang W., Peterhoff C., Hwang J.C., Nixon R.A., Ryu S.H.,
Kim T.W.;
"Proteomic identification of sorting nexin 6 as a negative regulator
of BACE1-mediated APP processing.";
FASEB J. 24:2783-2794(2010).
[30]
UBIQUITINATION AT LYS-501, AND MUTAGENESIS OF 499-LEU-LEU-500 AND
LYS-501.
PubMed=20484053; DOI=10.1074/jbc.M109.092742;
Kang E.L., Cameron A.N., Piazza F., Walker K.R., Tesco G.;
"Ubiquitin regulates GGA3-mediated degradation of BACE1.";
J. Biol. Chem. 285:24108-24119(2010).
[31]
SUBCELLULAR LOCATION, MUTAGENESIS OF 499-LEU-LEU-500 AND LYS-501, AND
DOMAIN.
PubMed=23109336; DOI=10.1074/jbc.M112.407072;
Kang E.L., Biscaro B., Piazza F., Tesco G.;
"BACE1 protein endocytosis and trafficking are differentially
regulated by ubiquitination at lysine 501 and the Di-leucine motif in
the carboxyl terminus.";
J. Biol. Chem. 287:42867-42880(2012).
[32]
DEUBIQUITINATION AT LYS-501, MUTAGENESIS OF LYS-501, AND SUBCELLULAR
LOCATION.
PubMed=27302062; DOI=10.1074/jbc.M116.718023;
Yeates E.F., Tesco G.;
"The Endosome-associated Deubiquitinating Enzyme USP8 Regulates BACE1
Enzyme Ubiquitination and Degradation.";
J. Biol. Chem. 291:15753-15766(2016).
[33]
SUBCELLULAR LOCATION.
PubMed=27084579; DOI=10.1242/jcs.185215;
Kurkinen K.M., Marttinen M., Turner L., Natunen T., Maekinen P.,
Haapalinna F., Sarajaervi T., Gabbouj S., Kurki M., Paananen J.,
Koivisto A.M., Rauramaa T., Leinonen V., Tanila H., Soininen H.,
Lucas F.R., Haapasalo A., Hiltunen M.;
"SEPT8 modulates beta-amyloidogenic processing of APP by affecting the
sorting and accumulation of BACE1.";
J. Cell Sci. 129:2224-2238(2016).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 56-446 IN COMPLEX WITH
SUBSTRATE ANALOG.
PubMed=11021803; DOI=10.1126/science.290.5489.150;
Hong L., Koelsch G., Lin X., Wu S., Terzyan S., Ghosh A.K.,
Zhang X.C., Tang J.;
"Structure of the protease domain of memapsin 2 (beta-secretase)
complexed with inhibitor.";
Science 290:150-153(2000).
[35]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 56-446 IN COMPLEX WITH
SUBSTRATE ANALOG.
PubMed=12206667; DOI=10.1021/bi026232n;
Hong L., Turner R.T. III, Koelsch G., Shin D., Ghosh A.K., Tang J.;
"Crystal structure of memapsin 2 (beta-secretase) in complex with an
inhibitor OM00-3.";
Biochemistry 41:10963-10967(2002).
[36]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
PubMed=15096037; DOI=10.1021/bi0498252;
Hong L., Tang J.;
"Flap position of free memapsin 2 (beta-secretase), a model for flap
opening in aspartic protease catalysis.";
Biochemistry 43:4689-4695(2004).
[37]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 43-453 IN COMPLEX WITH
SUBSTRATE ANALOG.
PubMed=15451669; DOI=10.1016/j.jmb.2004.08.018;
Patel S., Vuillard L., Cleasby A., Murray C.W., Yon J.;
"Apo and inhibitor complex structures of BACE (beta-secretase).";
J. Mol. Biol. 343:407-416(2004).
[38]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-446.
PubMed=15628850; DOI=10.1021/bi048106k;
Turner R.T. III, Hong L., Koelsch G., Ghosh A.K., Tang J.;
"Structural locations and functional roles of new subsites S5, S6, and
S7 in memapsin 2 (beta-secretase).";
Biochemistry 44:105-112(2005).
-!- FUNCTION: Responsible for the proteolytic processing of the
amyloid precursor protein (APP). Cleaves at the N-terminus of the
A-beta peptide sequence, between residues 671 and 672 of APP,
leads to the generation and extracellular release of beta-cleaved
soluble APP, and a corresponding cell-associated C-terminal
fragment which is later released by gamma-secretase. Cleaves APP
with much more catalytic efficiency than for the wild-type.
{ECO:0000269|PubMed:10656250, ECO:0000269|PubMed:10677483,
ECO:0000269|PubMed:20354142}.
-!- CATALYTIC ACTIVITY:
Reaction=Broad endopeptidase specificity. Cleaves Glu-Val-Asn-
Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's
amyloid precursor protein.; EC=3.4.23.46;
Evidence={ECO:0000269|PubMed:10677483};
-!- ACTIVITY REGULATION: Inhibited by RTN3 and RTN4.
{ECO:0000269|PubMed:15286784, ECO:0000269|PubMed:16965550}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15.2 mM for APP cleaved by PSEN1 (at pH4)
{ECO:0000269|PubMed:10677483};
KM=1 mM for APP Swedish variant (at pH4)
{ECO:0000269|PubMed:10677483};
Note=kcat is 0.67 sec(-1) and 2.45 sec(-1) for APP cleaved by
PSEN1 and APP Swedish variant, respectively (PubMed:10677483).
{ECO:0000269|PubMed:10677483};
-!- SUBUNIT: Monomer. Interacts (via DXXLL motif) with GGA1, GGA2 and
GGA3 (via their VHS domain); the interaction highly increases when
BACE1 is phosphorylated at Ser-498 (PubMed:14567678,
PubMed:15886016). Interacts with RTN3 and RTN4 (PubMed:15286784,
PubMed:16965550, PubMed:16979658). Interacts with SNX6
(PubMed:20354142). Interacts with PCSK9 (PubMed:18660751).
Interacts with NAT8 and NAT8B (PubMed:19011241).
{ECO:0000269|PubMed:14567678, ECO:0000269|PubMed:15286784,
ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:16965550,
ECO:0000269|PubMed:16979658, ECO:0000269|PubMed:18660751,
ECO:0000269|PubMed:19011241, ECO:0000269|PubMed:20354142}.
-!- INTERACTION:
Q8BNX1:Clec4g (xeno); NbExp=2; IntAct=EBI-2433139, EBI-11176364;
Q14254:FLOT2; NbExp=2; IntAct=EBI-2433139, EBI-348613;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11466313};
Single-pass type I membrane protein {ECO:0000305|PubMed:11466313}.
Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11466313,
ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016,
ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:20354142,
ECO:0000269|PubMed:23109336}. Endoplasmic reticulum
{ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:17425515}.
Endosome {ECO:0000269|PubMed:11466313,
ECO:0000269|PubMed:15886016}. Cell surface
{ECO:0000269|PubMed:11466313, ECO:0000269|PubMed:15886016,
ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:23109336}.
Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11466313,
ECO:0000269|PubMed:15886016}; Single-pass type I membrane protein
{ECO:0000305|PubMed:11466313}. Membrane raft
{ECO:0000250|UniProtKB:P56818}. Lysosome
{ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:23109336,
ECO:0000269|PubMed:27084579, ECO:0000269|PubMed:27302062}. Late
endosome {ECO:0000269|PubMed:16033761,
ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27084579,
ECO:0000269|PubMed:27302062}. Early endosome
{ECO:0000269|PubMed:15615712, ECO:0000269|PubMed:15886016,
ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27084579,
ECO:0000269|PubMed:27302062}. Recycling endosome
{ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:27084579,
ECO:0000269|PubMed:27302062}. 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
(PubMed:17425515, PubMed:11466313). Colocalization with APP in
early endosomes is due to addition of bisecting N-
acetylglucosamine wich blocks targeting to late endosomes and
lysosomes (By similarity). Retrogradly transported from endosomal
compartments to the trans-Golgi network in a phosphorylation- and
GGA1- dependent manner (PubMed:15886016).
{ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:11466313,
ECO:0000269|PubMed:15886016, ECO:0000269|PubMed:17425515}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=A; Synonyms=BACE-1A, BAC-501;
IsoId=P56817-1; Sequence=Displayed;
Name=B; Synonyms=BACE-1B, BACE-I-476;
IsoId=P56817-2; Sequence=VSP_005223;
Name=C; Synonyms=BACE-1C, BACE-I-457;
IsoId=P56817-3; Sequence=VSP_005222;
Name=D; Synonyms=BACE-1D, BACE-I-432;
IsoId=P56817-4; Sequence=VSP_005222, VSP_005223;
Name=5;
IsoId=P56817-5; Sequence=VSP_047092, VSP_047093;
Note=Gene prediction based on EST data.;
Name=6;
IsoId=P56817-6; Sequence=VSP_047092, VSP_047093, VSP_005223;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed at high levels in the brain and
pancreas. In the brain, expression is highest in the substantia
nigra, locus coruleus and medulla oblongata.
{ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:11083922}.
-!- DOMAIN: DXXLL motif is required for a proper endocytosis and
retrograde transport to the trans-Golgi network, as well as for
regulation of lysosomal degradation.
{ECO:0000269|PubMed:23109336}.
-!- DOMAIN: The transmembrane domain is necessary for its activity. It
determines its late Golgi localization and access to its
substrate, APP. {ECO:0000269|PubMed:11466313}.
-!- PTM: N-Glycosylated (PubMed:11083922, PubMed:17425515). Addition
of a bisecting N-acetylglucosamine by MGAT3 blocks lysosomal
targeting, further degradation and is required for maintaining
stability under stress conditions (By similarity).
{ECO:0000250|UniProtKB:P56818, ECO:0000269|PubMed:11083922,
ECO:0000269|PubMed:17425515}.
-!- PTM: Acetylated in the endoplasmic reticulum at Lys-126, Lys-275,
Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307. Acetylation by
NAT8 and NAT8B is transient and deacetylation probably occurs in
the Golgi. Acetylation regulates the maturation, the transport to
the plasma membrane, the stability and the expression of the
protein. {ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
-!- PTM: Palmitoylation mediates lipid raft localization.
{ECO:0000250|UniProtKB:P56818}.
-!- PTM: Ubiquitinated at Lys-501, ubiquitination leads to lysosomal
degradation (PubMed:27302062, PubMed:16033761, PubMed:20484053,
PubMed:23109336). Monoubiquitinated and 'Lys-63'-linked
polyubitinated (PubMed:20484053). Deubiquitnated by USP8; inhibits
lysosomal degradation (PubMed:27302062).
{ECO:0000269|PubMed:16033761, ECO:0000269|PubMed:20484053,
ECO:0000269|PubMed:23109336, ECO:0000269|PubMed:27302062}.
-!- PTM: Phosphorylation at Ser-498 is required for interaction with
GGA1 and retrograded transport from endosomal compartments to the
trans-Golgi network. Non-phosphorylated BACE1 enters a direct
recycling route to the cell surface.
{ECO:0000269|PubMed:15886016}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA86463.2; Type=Frameshift; Positions=34; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/bace1/";
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EMBL; AF190725; AAF04142.1; -; mRNA.
EMBL; AF201468; AAF18982.1; -; mRNA.
EMBL; AF200343; AAF17079.1; -; mRNA.
EMBL; AF204943; AAF26367.1; -; mRNA.
EMBL; AF338816; AAK38374.1; -; mRNA.
EMBL; AF338817; AAK38375.1; -; mRNA.
EMBL; AB050436; BAB40931.1; -; mRNA.
EMBL; AB050437; BAB40932.1; -; mRNA.
EMBL; AB050438; BAB40933.1; -; mRNA.
EMBL; AB032975; BAA86463.2; ALT_FRAME; mRNA.
EMBL; DQ007053; AAY16982.1; -; Genomic_DNA.
EMBL; EF444940; ACA05927.1; -; Genomic_DNA.
EMBL; AP000892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67313.1; -; Genomic_DNA.
EMBL; BC065492; AAH65492.1; -; mRNA.
EMBL; AF200193; AAF13715.1; -; mRNA.
CCDS; CCDS44739.1; -. [P56817-2]
CCDS; CCDS44740.1; -. [P56817-3]
CCDS; CCDS44741.1; -. [P56817-4]
CCDS; CCDS55786.1; -. [P56817-6]
CCDS; CCDS55787.1; -. [P56817-5]
CCDS; CCDS8383.1; -. [P56817-1]
PIR; A59090; A59090.
RefSeq; NP_001193978.1; NM_001207049.1. [P56817-6]
RefSeq; NP_036236.1; NM_012104.4. [P56817-1]
RefSeq; NP_620427.1; NM_138971.3. [P56817-3]
RefSeq; NP_620428.1; NM_138972.3. [P56817-2]
RefSeq; NP_620429.1; NM_138973.3. [P56817-4]
UniGene; Hs.504003; -.
PDB; 1FKN; X-ray; 1.90 A; A/B=56-446.
PDB; 1M4H; X-ray; 2.10 A; A/B=56-446.
PDB; 1PY1; X-ray; 2.60 A; E/F/G/H=494-501.
PDB; 1SGZ; X-ray; 2.00 A; A/B/C/D=58-446.
PDB; 1TQF; X-ray; 1.80 A; A=43-446.
PDB; 1UJJ; X-ray; 2.60 A; C=490-501.
PDB; 1UJK; X-ray; 1.90 A; C/D=490-501.
PDB; 1W50; X-ray; 1.75 A; A=43-453.
PDB; 1W51; X-ray; 2.55 A; A=43-453.
PDB; 1XN2; X-ray; 1.90 A; A/B/C/D=58-446.
PDB; 1XN3; X-ray; 2.00 A; A/B/C/D=58-446.
PDB; 1XS7; X-ray; 2.80 A; D=58-446.
PDB; 1YM2; X-ray; 2.05 A; A/B/C=48-447.
PDB; 1YM4; X-ray; 2.25 A; A/B/C=48-453.
PDB; 2B8L; X-ray; 1.70 A; A=43-446.
PDB; 2B8V; X-ray; 1.80 A; A=43-446.
PDB; 2F3E; X-ray; 2.11 A; A/B/C=48-447.
PDB; 2F3F; X-ray; 2.30 A; A/B/C=48-447.
PDB; 2FDP; X-ray; 2.50 A; A/B/C=59-446.
PDB; 2G94; X-ray; 1.86 A; A/B/C/D=58-446.
PDB; 2HIZ; X-ray; 2.50 A; A/B/C=14-453.
PDB; 2HM1; X-ray; 2.20 A; A=57-453.
PDB; 2IQG; X-ray; 1.70 A; A=57-453.
PDB; 2IRZ; X-ray; 1.80 A; A=43-446.
PDB; 2IS0; X-ray; 2.20 A; A=43-446.
PDB; 2NTR; X-ray; 1.80 A; A=43-446.
PDB; 2OAH; X-ray; 1.80 A; A=43-446.
PDB; 2OF0; X-ray; 2.25 A; A=45-446.
PDB; 2OHK; X-ray; 2.20 A; A=45-446.
PDB; 2OHL; X-ray; 2.65 A; A=45-446.
PDB; 2OHM; X-ray; 2.70 A; A=45-446.
PDB; 2OHN; X-ray; 2.15 A; A=45-446.
PDB; 2OHP; X-ray; 2.25 A; A=45-446.
PDB; 2OHQ; X-ray; 2.10 A; A=45-446.
PDB; 2OHR; X-ray; 2.25 A; A=45-446.
PDB; 2OHS; X-ray; 2.45 A; A=45-446.
PDB; 2OHT; X-ray; 2.30 A; A=45-446.
PDB; 2OHU; X-ray; 2.35 A; A=45-446.
PDB; 2P4J; X-ray; 2.50 A; A/B/C/D=58-446.
PDB; 2P83; X-ray; 2.50 A; A/B/C=14-446.
PDB; 2P8H; X-ray; 1.80 A; A=43-446.
PDB; 2PH6; X-ray; 2.00 A; A=43-446.
PDB; 2PH8; X-ray; 1.70 A; A=43-446.
PDB; 2Q11; X-ray; 2.40 A; A/B/C=59-446.
PDB; 2Q15; X-ray; 2.40 A; A=62-446.
PDB; 2QK5; X-ray; 2.20 A; A/B=55-447.
PDB; 2QMD; X-ray; 1.65 A; A/B=55-447.
PDB; 2QMF; X-ray; 1.75 A; A/B=55-447.
PDB; 2QMG; X-ray; 1.89 A; A/B=55-447.
PDB; 2QP8; X-ray; 1.50 A; A/B=55-447.
PDB; 2QU2; X-ray; 2.60 A; A=46-454.
PDB; 2QU3; X-ray; 2.00 A; A=46-454.
PDB; 2QZK; X-ray; 1.80 A; A=43-446.
PDB; 2QZL; X-ray; 1.80 A; A=43-446.
PDB; 2VA5; X-ray; 2.75 A; A=14-453.
PDB; 2VA6; X-ray; 2.50 A; A=14-453.
PDB; 2VA7; X-ray; 2.20 A; A=14-453.
PDB; 2VIE; X-ray; 1.90 A; A=61-452.
PDB; 2VIJ; X-ray; 1.60 A; A=61-452.
PDB; 2VIY; X-ray; 1.82 A; A=61-452.
PDB; 2VIZ; X-ray; 1.60 A; A=61-452.
PDB; 2VJ6; X-ray; 1.80 A; A=61-452.
PDB; 2VJ7; X-ray; 1.60 A; A=61-452.
PDB; 2VJ9; X-ray; 1.60 A; A=61-452.
PDB; 2VKM; X-ray; 2.05 A; A/B/C/D=58-446.
PDB; 2VNM; X-ray; 1.79 A; A=61-452.
PDB; 2VNN; X-ray; 1.87 A; A=61-452.
PDB; 2WEZ; X-ray; 1.70 A; A=61-452.
PDB; 2WF0; X-ray; 1.60 A; A=61-452.
PDB; 2WF1; X-ray; 1.60 A; A=61-452.
PDB; 2WF2; X-ray; 1.80 A; A=61-452.
PDB; 2WF3; X-ray; 2.08 A; A=61-452.
PDB; 2WF4; X-ray; 1.80 A; A=61-452.
PDB; 2WJO; X-ray; 2.50 A; A=58-460.
PDB; 2XFI; X-ray; 1.73 A; A=61-452.
PDB; 2XFJ; X-ray; 1.80 A; A=61-452.
PDB; 2XFK; X-ray; 1.80 A; A=61-452.
PDB; 2ZDZ; X-ray; 2.00 A; A=46-454.
PDB; 2ZE1; X-ray; 2.20 A; A=46-454.
PDB; 2ZHR; X-ray; 2.50 A; A/B=45-454.
PDB; 2ZHS; X-ray; 2.70 A; A=45-454.
PDB; 2ZHT; X-ray; 2.35 A; A=45-454.
PDB; 2ZHU; X-ray; 2.40 A; A=45-454.
PDB; 2ZHV; X-ray; 1.85 A; A=45-454.
PDB; 2ZJH; X-ray; 2.60 A; A=43-446.
PDB; 2ZJI; X-ray; 2.30 A; A=43-446.
PDB; 2ZJJ; X-ray; 2.20 A; A=43-446.
PDB; 2ZJK; X-ray; 3.00 A; A/B/C=43-446.
PDB; 2ZJL; X-ray; 2.10 A; A=43-446.
PDB; 2ZJM; X-ray; 1.90 A; A=43-446.
PDB; 2ZJN; X-ray; 2.70 A; A=43-446.
PDB; 3BRA; X-ray; 2.30 A; A=46-454.
PDB; 3BUF; X-ray; 2.30 A; A=46-454.
PDB; 3BUG; X-ray; 2.50 A; A=46-454.
PDB; 3BUH; X-ray; 2.30 A; A=46-454.
PDB; 3CIB; X-ray; 1.72 A; A/B=58-447.
PDB; 3CIC; X-ray; 1.75 A; A/B=58-447.
PDB; 3CID; X-ray; 1.80 A; A/B=58-447.
PDB; 3CKP; X-ray; 2.30 A; A/B/C=43-454.
PDB; 3CKR; X-ray; 2.70 A; A/B/C=43-454.
PDB; 3DM6; X-ray; 2.60 A; A/B/C=42-446.
PDB; 3DUY; X-ray; 1.97 A; A/B/C=48-447.
PDB; 3DV1; X-ray; 2.10 A; A/B/C=48-447.
PDB; 3DV5; X-ray; 2.10 A; A/B/C=48-447.
PDB; 3EXO; X-ray; 2.10 A; A=43-454.
PDB; 3FKT; X-ray; 1.90 A; A=43-446.
PDB; 3H0B; X-ray; 2.70 A; A/B/C=43-446.
PDB; 3HVG; X-ray; 2.26 A; A/B/C=46-453.
PDB; 3HW1; X-ray; 2.48 A; A/B/C=46-453.
PDB; 3I25; X-ray; 2.10 A; A/B/C=42-446.
PDB; 3IGB; X-ray; 2.24 A; A=46-454.
PDB; 3IN3; X-ray; 2.00 A; A=46-454.
PDB; 3IN4; X-ray; 2.30 A; A=46-454.
PDB; 3IND; X-ray; 2.25 A; A=46-454.
PDB; 3INE; X-ray; 2.00 A; A=46-454.
PDB; 3INF; X-ray; 1.85 A; A=46-454.
PDB; 3INH; X-ray; 1.80 A; A=46-454.
PDB; 3IVH; X-ray; 1.80 A; A=57-453.
PDB; 3IVI; X-ray; 2.20 A; A/B/C=57-453.
PDB; 3IXJ; X-ray; 2.20 A; A/B/C=59-446.
PDB; 3IXK; X-ray; 2.50 A; A/B/C=42-446.
PDB; 3K5C; X-ray; 2.12 A; A/B/C=48-447.
PDB; 3K5D; X-ray; 2.90 A; A/B/C=48-453.
PDB; 3K5F; X-ray; 2.25 A; A/B/C=48-447.
PDB; 3K5G; X-ray; 2.00 A; A/B/C=48-447.
PDB; 3KMX; X-ray; 1.70 A; A/B=53-447.
PDB; 3KMY; X-ray; 1.90 A; A/B=53-447.
PDB; 3KN0; X-ray; 1.90 A; A/B=53-447.
PDB; 3KYR; X-ray; 2.60 A; A/B/C=42-446.
PDB; 3L38; X-ray; 2.10 A; A=46-454.
PDB; 3L3A; X-ray; 2.36 A; A=46-454.
PDB; 3L58; X-ray; 1.80 A; A/B=41-454.
PDB; 3L59; X-ray; 2.00 A; A/B=41-454.
PDB; 3L5B; X-ray; 1.80 A; A/B=41-454.
PDB; 3L5C; X-ray; 1.80 A; A/B=41-454.
PDB; 3L5D; X-ray; 1.75 A; A/B=41-454.
PDB; 3L5E; X-ray; 1.53 A; A/B=41-454.
PDB; 3L5F; X-ray; 1.70 A; A/B=41-454.
PDB; 3LHG; X-ray; 2.10 A; A=46-454.
PDB; 3LNK; X-ray; 1.80 A; A/B=53-447.
PDB; 3LPI; X-ray; 2.05 A; A/B=14-454.
PDB; 3LPJ; X-ray; 1.79 A; A/B=14-454.
PDB; 3LPK; X-ray; 1.93 A; A/B=14-454.
PDB; 3MSJ; X-ray; 1.80 A; A/B/C=43-453.
PDB; 3MSK; X-ray; 2.00 A; A=48-453.
PDB; 3MSL; X-ray; 2.40 A; A=48-453.
PDB; 3N4L; X-ray; 2.70 A; A/B/C=57-453.
PDB; 3NSH; X-ray; 2.20 A; A/B/C=57-453.
PDB; 3OHF; X-ray; 2.10 A; A/B=14-454.
PDB; 3OHH; X-ray; 2.01 A; A/B=14-454.
PDB; 3OOZ; X-ray; 1.80 A; A=46-454.
PDB; 3PI5; X-ray; 2.40 A; A/B/C=48-447.
PDB; 3QBH; X-ray; 2.24 A; A/B/C=48-447.
PDB; 3QI1; X-ray; 2.30 A; A=57-453.
PDB; 3R1G; X-ray; 2.80 A; B=57-453.
PDB; 3R2F; X-ray; 2.53 A; A/B/D/E=14-454.
PDB; 3RSV; X-ray; 2.50 A; A=43-453.
PDB; 3RSX; X-ray; 2.48 A; A=43-453.
PDB; 3RTH; X-ray; 2.70 A; A=43-453.
PDB; 3RTM; X-ray; 2.76 A; A=43-453.
PDB; 3RTN; X-ray; 2.70 A; A=43-453.
PDB; 3RU1; X-ray; 2.30 A; A=43-453.
PDB; 3RVI; X-ray; 2.65 A; A=43-453.
PDB; 3S2O; X-ray; 2.60 A; A=48-453.
PDB; 3S7L; X-ray; 2.16 A; A=46-454.
PDB; 3S7M; X-ray; 2.20 A; A=46-454.
PDB; 3SKF; X-ray; 3.00 A; A/B=14-454.
PDB; 3SKG; X-ray; 2.88 A; A/B/D/E=14-454.
PDB; 3TPJ; X-ray; 1.61 A; A=43-454.
PDB; 3TPL; X-ray; 2.50 A; A/B/C=43-454.
PDB; 3TPP; X-ray; 1.60 A; A=43-454.
PDB; 3TPR; X-ray; 2.55 A; A=43-454.
PDB; 3U6A; X-ray; 2.20 A; A/B/C=58-446.
PDB; 3UDH; X-ray; 1.70 A; A=58-453.
PDB; 3UDJ; X-ray; 1.80 A; A=58-453.
PDB; 3UDK; X-ray; 2.51 A; A=58-453.
PDB; 3UDM; X-ray; 1.94 A; A=58-453.
PDB; 3UDN; X-ray; 2.19 A; A=58-453.
PDB; 3UDP; X-ray; 1.95 A; A=58-453.
PDB; 3UDQ; X-ray; 2.73 A; A=58-453.
PDB; 3UDR; X-ray; 1.95 A; A=58-453.
PDB; 3UDY; X-ray; 2.00 A; A=58-453.
PDB; 3UFL; X-ray; 1.90 A; A=58-446.
PDB; 3UQP; X-ray; 1.77 A; A=43-454.
PDB; 3UQR; X-ray; 3.06 A; A/B/C=43-454.
PDB; 3UQU; X-ray; 1.70 A; A=43-454.
PDB; 3UQW; X-ray; 2.20 A; A=43-454.
PDB; 3UQX; X-ray; 1.70 A; A=43-454.
PDB; 3VEU; X-ray; 1.52 A; A=48-447.
PDB; 3VF3; X-ray; 1.48 A; A=48-447.
PDB; 3VG1; X-ray; 1.77 A; A=48-447.
PDB; 3VV6; X-ray; 2.05 A; A=43-454.
PDB; 3VV7; X-ray; 2.10 A; A=43-454.
PDB; 3VV8; X-ray; 2.50 A; A=43-454.
PDB; 3WB4; X-ray; 2.25 A; A=43-454.
PDB; 3WB5; X-ray; 2.50 A; A=43-454.
PDB; 3ZMG; X-ray; 1.74 A; A=46-454.
PDB; 3ZOV; X-ray; 2.10 A; A=46-454.
PDB; 4ACU; X-ray; 1.75 A; A=43-453.
PDB; 4ACX; X-ray; 2.00 A; A=43-453.
PDB; 4AZY; X-ray; 1.79 A; A=43-453.
PDB; 4B00; X-ray; 1.83 A; A=43-453.
PDB; 4B05; X-ray; 1.80 A; A=43-453.
PDB; 4B0Q; X-ray; 1.87 A; A=62-445.
PDB; 4B1C; X-ray; 1.95 A; A=58-445.
PDB; 4B1D; X-ray; 1.95 A; A=58-445.
PDB; 4B1E; X-ray; 1.95 A; A=58-445.
PDB; 4B70; X-ray; 1.60 A; A=61-445.
PDB; 4B72; X-ray; 1.60 A; A=58-445.
PDB; 4B77; X-ray; 1.80 A; A=58-445.
PDB; 4B78; X-ray; 1.50 A; A=62-445.
PDB; 4BEK; X-ray; 2.39 A; A=46-454.
PDB; 4BFD; X-ray; 2.30 A; A=46-454.
PDB; 4D83; X-ray; 2.40 A; A/B/C=48-447.
PDB; 4D85; X-ray; 2.65 A; A=48-453.
PDB; 4D88; X-ray; 1.70 A; A=48-447.
PDB; 4D89; X-ray; 1.65 A; A=48-447.
PDB; 4D8C; X-ray; 2.07 A; A/B/C=48-447.
PDB; 4DH6; X-ray; 2.50 A; A=43-453.
PDB; 4DI2; X-ray; 2.00 A; A/B/C=43-453.
PDB; 4DJU; X-ray; 1.80 A; A/B=41-454.
PDB; 4DJV; X-ray; 1.73 A; A/B=41-454.
PDB; 4DJW; X-ray; 1.90 A; A/B=41-454.
PDB; 4DJX; X-ray; 1.50 A; A/B=41-454.
PDB; 4DJY; X-ray; 1.86 A; A/B=41-454.
PDB; 4DPF; X-ray; 1.80 A; A=57-446.
PDB; 4DPI; X-ray; 1.90 A; A=57-446.
PDB; 4DUS; X-ray; 2.50 A; A=43-453.
PDB; 4DV9; X-ray; 2.08 A; A=43-454.
PDB; 4DVF; X-ray; 1.80 A; A/B=43-454.
PDB; 4EWO; X-ray; 1.80 A; A=61-446.
PDB; 4EXG; X-ray; 1.80 A; A=61-446.
PDB; 4FCO; X-ray; 1.76 A; A=43-454.
PDB; 4FGX; X-ray; 1.59 A; A=43-454.
PDB; 4FM7; X-ray; 1.56 A; A=58-453.
PDB; 4FM8; X-ray; 1.90 A; A=58-453.
PDB; 4FRI; X-ray; 2.30 A; A=43-453.
PDB; 4FRJ; X-ray; 1.95 A; A=43-453.
PDB; 4FRK; X-ray; 2.10 A; A=43-453.
PDB; 4FRS; X-ray; 1.70 A; A/B=53-447.
PDB; 4FS4; X-ray; 1.74 A; A/B=58-447.
PDB; 4FSE; X-ray; 2.65 A; A/B/D/E=14-454.
PDB; 4FSL; X-ray; 2.50 A; A/B/D/E=43-453.
PDB; 4GID; X-ray; 2.00 A; A/B/C/D=59-446.
PDB; 4GMI; X-ray; 1.80 A; A=57-446.
PDB; 4H1E; X-ray; 1.90 A; A/B=41-454.
PDB; 4H3F; X-ray; 1.70 A; A/B=41-454.
PDB; 4H3G; X-ray; 1.85 A; A/B=41-454.
PDB; 4H3I; X-ray; 1.96 A; A/B=41-454.
PDB; 4H3J; X-ray; 1.60 A; A/B=41-454.
PDB; 4HA5; X-ray; 1.83 A; A/B=41-454.
PDB; 4HZT; X-ray; 1.80 A; A=57-453.
PDB; 4I0D; X-ray; 1.91 A; A=57-453.
PDB; 4I0E; X-ray; 1.70 A; A=57-453.
PDB; 4I0F; X-ray; 1.80 A; A=57-453.
PDB; 4I0G; X-ray; 1.78 A; A=57-453.
PDB; 4I0H; X-ray; 2.20 A; A/B/C=57-453.
PDB; 4I0I; X-ray; 2.20 A; A/B/C=57-453.
PDB; 4I0J; X-ray; 1.99 A; A=57-453.
PDB; 4I0Z; X-ray; 1.80 A; A=57-453.
PDB; 4I10; X-ray; 2.07 A; A=57-453.
PDB; 4I11; X-ray; 1.89 A; A=57-453.
PDB; 4I12; X-ray; 1.78 A; A=57-453.
PDB; 4I1C; X-ray; 2.00 A; A=57-453.
PDB; 4IVS; X-ray; 2.64 A; A=43-454.
PDB; 4IVT; X-ray; 1.60 A; A=43-454.
PDB; 4J0P; X-ray; 1.97 A; A=46-454.
PDB; 4J0T; X-ray; 2.05 A; A=46-454.
PDB; 4J0V; X-ray; 1.94 A; A=46-454.
PDB; 4J0Y; X-ray; 1.77 A; A=46-454.
PDB; 4J0Z; X-ray; 2.13 A; A=46-454.
PDB; 4J17; X-ray; 1.81 A; A=46-454.
PDB; 4J1C; X-ray; 2.01 A; A=46-454.
PDB; 4J1E; X-ray; 1.78 A; A=46-454.
PDB; 4J1F; X-ray; 2.25 A; A=46-454.
PDB; 4J1H; X-ray; 2.20 A; A=46-454.
PDB; 4J1I; X-ray; 2.05 A; A=46-454.
PDB; 4J1K; X-ray; 2.18 A; A=46-454.
PDB; 4JOO; X-ray; 1.80 A; A=57-453.
PDB; 4JP9; X-ray; 1.80 A; A=57-453.
PDB; 4JPC; X-ray; 1.80 A; A=57-453.
PDB; 4JPE; X-ray; 1.80 A; A=57-453.
PDB; 4K8S; X-ray; 2.39 A; A/B/C=59-446.
PDB; 4K9H; X-ray; 2.29 A; A/B/C=59-446.
PDB; 4KE0; X-ray; 2.30 A; A/B/C=43-453.
PDB; 4KE1; X-ray; 1.91 A; A=43-453.
PDB; 4L7G; X-ray; 1.38 A; A=57-453.
PDB; 4L7H; X-ray; 1.85 A; A=57-453.
PDB; 4L7J; X-ray; 1.65 A; A=57-453.
PDB; 4LC7; X-ray; 1.70 A; A=57-453.
PDB; 4LXA; X-ray; 1.95 A; A/B/C=48-447.
PDB; 4LXK; X-ray; 2.05 A; A/B/C=48-447.
PDB; 4LXM; X-ray; 2.30 A; A/B/C=48-447.
PDB; 4N00; X-ray; 1.80 A; A=57-453.
PDB; 4PZW; X-ray; 1.80 A; A=57-453.
PDB; 4PZX; X-ray; 1.80 A; A=57-453.
PDB; 4R5N; X-ray; 1.80 A; A=57-453.
PDB; 4R8Y; X-ray; 1.90 A; A/B=41-454.
PDB; 4R91; X-ray; 1.58 A; A/B=41-454.
PDB; 4R92; X-ray; 1.71 A; A/B=41-454.
PDB; 4R93; X-ray; 1.71 A; A/B=41-454.
PDB; 4R95; X-ray; 1.99 A; A/B=41-454.
PDB; 4RCD; X-ray; 1.90 A; A=43-453.
PDB; 4RCE; X-ray; 2.40 A; A=43-453.
PDB; 4RCF; X-ray; 1.78 A; A=43-453.
PDB; 4RRN; X-ray; 1.80 A; A=57-453.
PDB; 4RRO; X-ray; 1.80 A; A=57-453.
PDB; 4RRS; X-ray; 1.80 A; A=57-453.
PDB; 4TRW; X-ray; 2.85 A; A/B/C=58-447.
PDB; 4TRY; X-ray; 2.75 A; A/B/C=60-447.
PDB; 4TRZ; X-ray; 3.25 A; A/B/C=60-447.
PDB; 4WTU; X-ray; 1.85 A; A=43-453.
PDB; 4WY1; X-ray; 1.98 A; A=58-453.
PDB; 4WY6; X-ray; 2.10 A; A=46-454.
PDB; 4X2L; X-ray; 2.55 A; A=46-454.
PDB; 4X7I; X-ray; 1.77 A; A/B=14-454.
PDB; 4XKX; X-ray; 1.80 A; A=43-453.
PDB; 4XXS; X-ray; 1.86 A; A=46-454.
PDB; 4YBI; X-ray; 1.84 A; A/B=14-454.
PDB; 4ZPE; X-ray; 1.70 A; A=43-446.
PDB; 4ZPF; X-ray; 1.80 A; A=43-446.
PDB; 4ZPG; X-ray; 2.00 A; A=43-446.
PDB; 4ZSM; X-ray; 1.96 A; A/B=14-454.
PDB; 4ZSP; X-ray; 1.91 A; A/B=14-454.
PDB; 4ZSQ; X-ray; 2.30 A; A/B=14-454.
PDB; 4ZSR; X-ray; 1.65 A; A/B=14-454.
PDB; 5CLM; X-ray; 2.61 A; A=46-446.
PDB; 5DQC; X-ray; 2.47 A; A/B/C=58-447.
PDB; 5ENK; X-ray; 2.11 A; A=14-454.
PDB; 5ENM; X-ray; 1.98 A; A=14-454.
PDB; 5EZX; X-ray; 1.90 A; A=57-446.
PDB; 5EZZ; X-ray; 2.10 A; A=57-446.
PDB; 5F00; X-ray; 1.95 A; A=57-446.
PDB; 5F01; X-ray; 1.52 A; A=57-446.
PDB; 5HD0; X-ray; 1.65 A; A/B=41-454.
PDB; 5HDU; X-ray; 1.58 A; A/B=41-454.
PDB; 5HDV; X-ray; 1.71 A; A/B=41-454.
PDB; 5HDX; X-ray; 1.60 A; A/B=41-454.
PDB; 5HDZ; X-ray; 1.49 A; A/B=41-454.
PDB; 5HE4; X-ray; 1.53 A; A/B=41-454.
PDB; 5HE5; X-ray; 1.55 A; A/B=41-454.
PDB; 5HE7; X-ray; 1.71 A; A/B=41-454.
PDB; 5HTZ; X-ray; 1.95 A; A/B=43-454.
PDB; 5HU0; X-ray; 1.83 A; A/B=43-454.
PDB; 5HU1; X-ray; 1.50 A; A/B=43-454.
PDB; 5I3V; X-ray; 1.62 A; A=43-453.
PDB; 5I3W; X-ray; 2.15 A; A=43-453.
PDB; 5I3X; X-ray; 1.85 A; A=43-453.
PDB; 5I3Y; X-ray; 2.15 A; A=43-453.
PDB; 5IE1; X-ray; 2.30 A; A=43-453.
PDB; 5KQF; X-ray; 1.98 A; A=14-454.
PDB; 5KR8; X-ray; 2.12 A; A=14-454.
PDB; 5MBW; X-ray; 2.95 A; A=46-454.
PDB; 5MCO; X-ray; 2.49 A; A=46-454.
PDB; 5MCQ; X-ray; 1.82 A; A=46-454.
PDB; 5MXD; X-ray; 2.52 A; A/B/C=22-446.
PDB; 5T1U; X-ray; 1.78 A; A=46-454.
PDB; 5T1W; X-ray; 2.96 A; A=46-454.
PDB; 5TOL; X-ray; 2.51 A; A=43-454.
PDB; 5UYU; X-ray; 1.90 A; A=43-453.
PDB; 5V0N; X-ray; 2.15 A; A/B/C=14-454.
PDB; 5YGX; X-ray; 2.20 A; A=43-454.
PDB; 5YGY; X-ray; 2.30 A; A=43-454.
PDB; 6BFD; X-ray; 1.62 A; A/B=14-454.
PDB; 6BFE; X-ray; 1.51 A; A/B=14-454.
PDB; 6BFW; X-ray; 1.84 A; A/B=14-454.
PDB; 6BFX; X-ray; 1.99 A; A/B=14-454.
PDB; 6C2I; X-ray; 1.95 A; A=43-453.
PDB; 6DHC; X-ray; 2.85 A; A/B/C=14-454.
PDB; 6EJ2; X-ray; 1.46 A; A=1-501.
PDB; 6EJ3; X-ray; 1.94 A; A=1-501.
PDB; 6EQM; X-ray; 1.35 A; A=48-447.
PDB; 6FGY; X-ray; 1.54 A; A=60-453.
PDBsum; 1FKN; -.
PDBsum; 1M4H; -.
PDBsum; 1PY1; -.
PDBsum; 1SGZ; -.
PDBsum; 1TQF; -.
PDBsum; 1UJJ; -.
PDBsum; 1UJK; -.
PDBsum; 1W50; -.
PDBsum; 1W51; -.
PDBsum; 1XN2; -.
PDBsum; 1XN3; -.
PDBsum; 1XS7; -.
PDBsum; 1YM2; -.
PDBsum; 1YM4; -.
PDBsum; 2B8L; -.
PDBsum; 2B8V; -.
PDBsum; 2F3E; -.
PDBsum; 2F3F; -.
PDBsum; 2FDP; -.
PDBsum; 2G94; -.
PDBsum; 2HIZ; -.
PDBsum; 2HM1; -.
PDBsum; 2IQG; -.
PDBsum; 2IRZ; -.
PDBsum; 2IS0; -.
PDBsum; 2NTR; -.
PDBsum; 2OAH; -.
PDBsum; 2OF0; -.
PDBsum; 2OHK; -.
PDBsum; 2OHL; -.
PDBsum; 2OHM; -.
PDBsum; 2OHN; -.
PDBsum; 2OHP; -.
PDBsum; 2OHQ; -.
PDBsum; 2OHR; -.
PDBsum; 2OHS; -.
PDBsum; 2OHT; -.
PDBsum; 2OHU; -.
PDBsum; 2P4J; -.
PDBsum; 2P83; -.
PDBsum; 2P8H; -.
PDBsum; 2PH6; -.
PDBsum; 2PH8; -.
PDBsum; 2Q11; -.
PDBsum; 2Q15; -.
PDBsum; 2QK5; -.
PDBsum; 2QMD; -.
PDBsum; 2QMF; -.
PDBsum; 2QMG; -.
PDBsum; 2QP8; -.
PDBsum; 2QU2; -.
PDBsum; 2QU3; -.
PDBsum; 2QZK; -.
PDBsum; 2QZL; -.
PDBsum; 2VA5; -.
PDBsum; 2VA6; -.
PDBsum; 2VA7; -.
PDBsum; 2VIE; -.
PDBsum; 2VIJ; -.
PDBsum; 2VIY; -.
PDBsum; 2VIZ; -.
PDBsum; 2VJ6; -.
PDBsum; 2VJ7; -.
PDBsum; 2VJ9; -.
PDBsum; 2VKM; -.
PDBsum; 2VNM; -.
PDBsum; 2VNN; -.
PDBsum; 2WEZ; -.
PDBsum; 2WF0; -.
PDBsum; 2WF1; -.
PDBsum; 2WF2; -.
PDBsum; 2WF3; -.
PDBsum; 2WF4; -.
PDBsum; 2WJO; -.
PDBsum; 2XFI; -.
PDBsum; 2XFJ; -.
PDBsum; 2XFK; -.
PDBsum; 2ZDZ; -.
PDBsum; 2ZE1; -.
PDBsum; 2ZHR; -.
PDBsum; 2ZHS; -.
PDBsum; 2ZHT; -.
PDBsum; 2ZHU; -.
PDBsum; 2ZHV; -.
PDBsum; 2ZJH; -.
PDBsum; 2ZJI; -.
PDBsum; 2ZJJ; -.
PDBsum; 2ZJK; -.
PDBsum; 2ZJL; -.
PDBsum; 2ZJM; -.
PDBsum; 2ZJN; -.
PDBsum; 3BRA; -.
PDBsum; 3BUF; -.
PDBsum; 3BUG; -.
PDBsum; 3BUH; -.
PDBsum; 3CIB; -.
PDBsum; 3CIC; -.
PDBsum; 3CID; -.
PDBsum; 3CKP; -.
PDBsum; 3CKR; -.
PDBsum; 3DM6; -.
PDBsum; 3DUY; -.
PDBsum; 3DV1; -.
PDBsum; 3DV5; -.
PDBsum; 3EXO; -.
PDBsum; 3FKT; -.
PDBsum; 3H0B; -.
PDBsum; 3HVG; -.
PDBsum; 3HW1; -.
PDBsum; 3I25; -.
PDBsum; 3IGB; -.
PDBsum; 3IN3; -.
PDBsum; 3IN4; -.
PDBsum; 3IND; -.
PDBsum; 3INE; -.
PDBsum; 3INF; -.
PDBsum; 3INH; -.
PDBsum; 3IVH; -.
PDBsum; 3IVI; -.
PDBsum; 3IXJ; -.
PDBsum; 3IXK; -.
PDBsum; 3K5C; -.
PDBsum; 3K5D; -.
PDBsum; 3K5F; -.
PDBsum; 3K5G; -.
PDBsum; 3KMX; -.
PDBsum; 3KMY; -.
PDBsum; 3KN0; -.
PDBsum; 3KYR; -.
PDBsum; 3L38; -.
PDBsum; 3L3A; -.
PDBsum; 3L58; -.
PDBsum; 3L59; -.
PDBsum; 3L5B; -.
PDBsum; 3L5C; -.
PDBsum; 3L5D; -.
PDBsum; 3L5E; -.
PDBsum; 3L5F; -.
PDBsum; 3LHG; -.
PDBsum; 3LNK; -.
PDBsum; 3LPI; -.
PDBsum; 3LPJ; -.
PDBsum; 3LPK; -.
PDBsum; 3MSJ; -.
PDBsum; 3MSK; -.
PDBsum; 3MSL; -.
PDBsum; 3N4L; -.
PDBsum; 3NSH; -.
PDBsum; 3OHF; -.
PDBsum; 3OHH; -.
PDBsum; 3OOZ; -.
PDBsum; 3PI5; -.
PDBsum; 3QBH; -.
PDBsum; 3QI1; -.
PDBsum; 3R1G; -.
PDBsum; 3R2F; -.
PDBsum; 3RSV; -.
PDBsum; 3RSX; -.
PDBsum; 3RTH; -.
PDBsum; 3RTM; -.
PDBsum; 3RTN; -.
PDBsum; 3RU1; -.
PDBsum; 3RVI; -.
PDBsum; 3S2O; -.
PDBsum; 3S7L; -.
PDBsum; 3S7M; -.
PDBsum; 3SKF; -.
PDBsum; 3SKG; -.
PDBsum; 3TPJ; -.
PDBsum; 3TPL; -.
PDBsum; 3TPP; -.
PDBsum; 3TPR; -.
PDBsum; 3U6A; -.
PDBsum; 3UDH; -.
PDBsum; 3UDJ; -.
PDBsum; 3UDK; -.
PDBsum; 3UDM; -.
PDBsum; 3UDN; -.
PDBsum; 3UDP; -.
PDBsum; 3UDQ; -.
PDBsum; 3UDR; -.
PDBsum; 3UDY; -.
PDBsum; 3UFL; -.
PDBsum; 3UQP; -.
PDBsum; 3UQR; -.
PDBsum; 3UQU; -.
PDBsum; 3UQW; -.
PDBsum; 3UQX; -.
PDBsum; 3VEU; -.
PDBsum; 3VF3; -.
PDBsum; 3VG1; -.
PDBsum; 3VV6; -.
PDBsum; 3VV7; -.
PDBsum; 3VV8; -.
PDBsum; 3WB4; -.
PDBsum; 3WB5; -.
PDBsum; 3ZMG; -.
PDBsum; 3ZOV; -.
PDBsum; 4ACU; -.
PDBsum; 4ACX; -.
PDBsum; 4AZY; -.
PDBsum; 4B00; -.
PDBsum; 4B05; -.
PDBsum; 4B0Q; -.
PDBsum; 4B1C; -.
PDBsum; 4B1D; -.
PDBsum; 4B1E; -.
PDBsum; 4B70; -.
PDBsum; 4B72; -.
PDBsum; 4B77; -.
PDBsum; 4B78; -.
PDBsum; 4BEK; -.
PDBsum; 4BFD; -.
PDBsum; 4D83; -.
PDBsum; 4D85; -.
PDBsum; 4D88; -.
PDBsum; 4D89; -.
PDBsum; 4D8C; -.
PDBsum; 4DH6; -.
PDBsum; 4DI2; -.
PDBsum; 4DJU; -.
PDBsum; 4DJV; -.
PDBsum; 4DJW; -.
PDBsum; 4DJX; -.
PDBsum; 4DJY; -.
PDBsum; 4DPF; -.
PDBsum; 4DPI; -.
PDBsum; 4DUS; -.
PDBsum; 4DV9; -.
PDBsum; 4DVF; -.
PDBsum; 4EWO; -.
PDBsum; 4EXG; -.
PDBsum; 4FCO; -.
PDBsum; 4FGX; -.
PDBsum; 4FM7; -.
PDBsum; 4FM8; -.
PDBsum; 4FRI; -.
PDBsum; 4FRJ; -.
PDBsum; 4FRK; -.
PDBsum; 4FRS; -.
PDBsum; 4FS4; -.
PDBsum; 4FSE; -.
PDBsum; 4FSL; -.
PDBsum; 4GID; -.
PDBsum; 4GMI; -.
PDBsum; 4H1E; -.
PDBsum; 4H3F; -.
PDBsum; 4H3G; -.
PDBsum; 4H3I; -.
PDBsum; 4H3J; -.
PDBsum; 4HA5; -.
PDBsum; 4HZT; -.
PDBsum; 4I0D; -.
PDBsum; 4I0E; -.
PDBsum; 4I0F; -.
PDBsum; 4I0G; -.
PDBsum; 4I0H; -.
PDBsum; 4I0I; -.
PDBsum; 4I0J; -.
PDBsum; 4I0Z; -.
PDBsum; 4I10; -.
PDBsum; 4I11; -.
PDBsum; 4I12; -.
PDBsum; 4I1C; -.
PDBsum; 4IVS; -.
PDBsum; 4IVT; -.
PDBsum; 4J0P; -.
PDBsum; 4J0T; -.
PDBsum; 4J0V; -.
PDBsum; 4J0Y; -.
PDBsum; 4J0Z; -.
PDBsum; 4J17; -.
PDBsum; 4J1C; -.
PDBsum; 4J1E; -.
PDBsum; 4J1F; -.
PDBsum; 4J1H; -.
PDBsum; 4J1I; -.
PDBsum; 4J1K; -.
PDBsum; 4JOO; -.
PDBsum; 4JP9; -.
PDBsum; 4JPC; -.
PDBsum; 4JPE; -.
PDBsum; 4K8S; -.
PDBsum; 4K9H; -.
PDBsum; 4KE0; -.
PDBsum; 4KE1; -.
PDBsum; 4L7G; -.
PDBsum; 4L7H; -.
PDBsum; 4L7J; -.
PDBsum; 4LC7; -.
PDBsum; 4LXA; -.
PDBsum; 4LXK; -.
PDBsum; 4LXM; -.
PDBsum; 4N00; -.
PDBsum; 4PZW; -.
PDBsum; 4PZX; -.
PDBsum; 4R5N; -.
PDBsum; 4R8Y; -.
PDBsum; 4R91; -.
PDBsum; 4R92; -.
PDBsum; 4R93; -.
PDBsum; 4R95; -.
PDBsum; 4RCD; -.
PDBsum; 4RCE; -.
PDBsum; 4RCF; -.
PDBsum; 4RRN; -.
PDBsum; 4RRO; -.
PDBsum; 4RRS; -.
PDBsum; 4TRW; -.
PDBsum; 4TRY; -.
PDBsum; 4TRZ; -.
PDBsum; 4WTU; -.
PDBsum; 4WY1; -.
PDBsum; 4WY6; -.
PDBsum; 4X2L; -.
PDBsum; 4X7I; -.
PDBsum; 4XKX; -.
PDBsum; 4XXS; -.
PDBsum; 4YBI; -.
PDBsum; 4ZPE; -.
PDBsum; 4ZPF; -.
PDBsum; 4ZPG; -.
PDBsum; 4ZSM; -.
PDBsum; 4ZSP; -.
PDBsum; 4ZSQ; -.
PDBsum; 4ZSR; -.
PDBsum; 5CLM; -.
PDBsum; 5DQC; -.
PDBsum; 5ENK; -.
PDBsum; 5ENM; -.
PDBsum; 5EZX; -.
PDBsum; 5EZZ; -.
PDBsum; 5F00; -.
PDBsum; 5F01; -.
PDBsum; 5HD0; -.
PDBsum; 5HDU; -.
PDBsum; 5HDV; -.
PDBsum; 5HDX; -.
PDBsum; 5HDZ; -.
PDBsum; 5HE4; -.
PDBsum; 5HE5; -.
PDBsum; 5HE7; -.
PDBsum; 5HTZ; -.
PDBsum; 5HU0; -.
PDBsum; 5HU1; -.
PDBsum; 5I3V; -.
PDBsum; 5I3W; -.
PDBsum; 5I3X; -.
PDBsum; 5I3Y; -.
PDBsum; 5IE1; -.
PDBsum; 5KQF; -.
PDBsum; 5KR8; -.
PDBsum; 5MBW; -.
PDBsum; 5MCO; -.
PDBsum; 5MCQ; -.
PDBsum; 5MXD; -.
PDBsum; 5T1U; -.
PDBsum; 5T1W; -.
PDBsum; 5TOL; -.
PDBsum; 5UYU; -.
PDBsum; 5V0N; -.
PDBsum; 5YGX; -.
PDBsum; 5YGY; -.
PDBsum; 6BFD; -.
PDBsum; 6BFE; -.
PDBsum; 6BFW; -.
PDBsum; 6BFX; -.
PDBsum; 6C2I; -.
PDBsum; 6DHC; -.
PDBsum; 6EJ2; -.
PDBsum; 6EJ3; -.
PDBsum; 6EQM; -.
PDBsum; 6FGY; -.
ProteinModelPortal; P56817; -.
SMR; P56817; -.
BioGrid; 117154; 19.
CORUM; P56817; -.
DIP; DIP-41388N; -.
IntAct; P56817; 9.
MINT; P56817; -.
STRING; 9606.ENSP00000318585; -.
BindingDB; P56817; -.
ChEMBL; CHEMBL4822; -.
DrugBank; DB07736; (2S)-4-(4-fluorobenzyl)-N-(2-sulfanylethyl)piperazine-2-carboxamide.
DrugBank; DB07737; (2S)-4-(4-fluorobenzyl)-N-(3-sulfanylpropyl)piperazine-2-carboxamide.
DrugBank; DB07535; 2-amino-6-[2-(1H-indol-6-yl)ethyl]pyrimidin-4(3H)-one.
DrugBank; DB08749; 3-(2-AMINO-6-BENZOYLQUINAZOLIN-3(4H)-YL)-N-CYCLOHEXYL-N-METHYLPROPANAMIDE.
DrugBank; DB07345; 4-(2-aminoethyl)-2-cyclohexylphenol.
DrugBank; DB07346; 4-(2-aminoethyl)-2-ethylphenol.
DrugBank; DB07110; 4-(4-FLUOROBENZYL)PIPERIDINE.
DrugBank; DB07415; 4-[(1S)-1-(3-fluoro-4-methoxyphenyl)-2-(2-methoxy-5-nitrophenyl)ethyl]-1H-imidazol-2-amine.
DrugBank; DB07206; 6-[2-(1H-INDOL-6-YL)ETHYL]PYRIDIN-2-AMINE.
DrugBank; DB07245; 6-[2-(3'-METHOXYBIPHENYL-3-YL)ETHYL]PYRIDIN-2-AMINE.
DrugBank; DB06073; CTS-21166.
DrugBank; DB08929; MK-8931.
DrugBank; DB02378; MMI-175.
DrugBank; DB07734; N-(1-benzylpiperidin-4-yl)-4-sulfanylbutanamide.
DrugBank; DB07089; N-[amino(imino)methyl]-2-[2-(2-chlorophenyl)-4-(4-propoxyphenyl)-3-thienyl]acetamide.
DrugBank; DB07175; N-{2-methyl-5-[(6-phenylpyrimidin-4-yl)amino]phenyl}methanesulfonamide.
GuidetoPHARMACOLOGY; 2330; -.
MEROPS; A01.004; -.
TCDB; 8.A.32.1.1; the Beta-amyloid cleaving enzyme (bace1) family.
GlyConnect; 71; -.
GlyConnect; 72; -.
iPTMnet; P56817; -.
PhosphoSitePlus; P56817; -.
SwissPalm; P56817; -.
UniCarbKB; P56817; -.
BioMuta; BACE1; -.
DMDM; 296434407; -.
PaxDb; P56817; -.
PeptideAtlas; P56817; -.
PRIDE; P56817; -.
ProteomicsDB; 56947; -.
ProteomicsDB; 56948; -. [P56817-2]
ProteomicsDB; 56949; -. [P56817-3]
ProteomicsDB; 56950; -. [P56817-4]
DNASU; 23621; -.
Ensembl; ENST00000313005; ENSP00000318585; ENSG00000186318. [P56817-1]
Ensembl; ENST00000392937; ENSP00000475405; ENSG00000186318. [P56817-5]
Ensembl; ENST00000428381; ENSP00000402228; ENSG00000186318. [P56817-4]
Ensembl; ENST00000445823; ENSP00000403685; ENSG00000186318. [P56817-3]
Ensembl; ENST00000510630; ENSP00000422461; ENSG00000186318. [P56817-6]
Ensembl; ENST00000513780; ENSP00000424536; ENSG00000186318. [P56817-2]
GeneID; 23621; -.
KEGG; hsa:23621; -.
UCSC; uc001pqw.4; human. [P56817-1]
CTD; 23621; -.
DisGeNET; 23621; -.
EuPathDB; HostDB:ENSG00000186318.16; -.
GeneCards; BACE1; -.
HGNC; HGNC:933; BACE1.
HPA; CAB016358; -.
MIM; 604252; gene.
neXtProt; NX_P56817; -.
OpenTargets; ENSG00000186318; -.
PharmGKB; PA25232; -.
eggNOG; KOG1339; Eukaryota.
eggNOG; ENOG410XNV7; LUCA.
GeneTree; ENSGT00940000157786; -.
HOVERGEN; HBG059578; -.
InParanoid; P56817; -.
KO; K04521; -.
OMA; NGQDLNM; -.
OrthoDB; EOG091G0CNK; -.
PhylomeDB; P56817; -.
TreeFam; TF329595; -.
BioCyc; MetaCyc:ENSG00000160610-MONOMER; -.
BRENDA; 3.4.23.46; 2681.
Reactome; R-HSA-977225; Amyloid fiber formation.
SABIO-RK; P56817; -.
SIGNOR; P56817; -.
ChiTaRS; BACE1; human.
EvolutionaryTrace; P56817; -.
GeneWiki; Beta-secretase_1; -.
GenomeRNAi; 23621; -.
PMAP-CutDB; P56817; -.
PRO; PR:P56817; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000186318; Expressed in 223 organ(s), highest expression level in C1 segment of cervical spinal cord.
CleanEx; HS_BACE1; -.
ExpressionAtlas; P56817; baseline and differential.
Genevisible; P56817; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0070931; C:Golgi-associated vesicle lumen; TAS:Reactome.
GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005771; C:multivesicular body; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IPI:Alzheimers_University_of_Toronto.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008798; F:beta-aspartyl-peptidase activity; TAS:Reactome.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:CACAO.
GO; GO:0050435; P:amyloid-beta metabolic process; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IGI:ARUK-UCL.
GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
GO; GO:0030163; P:protein catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IEA:Ensembl.
CDD; cd05473; beta_secretase_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR009119; BACE.
InterPro; IPR009120; BACE1.
InterPro; IPR033874; Memapsin-like.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
PANTHER; PTHR13683; PTHR13683; 1.
PANTHER; PTHR13683:SF245; PTHR13683:SF245; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR01816; BACE1.
PRINTS; PR01815; BACEFAMILY.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Aspartyl protease;
Cell membrane; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
Endosome; Glycoprotein; Golgi apparatus; Hydrolase; Isopeptide bond;
Lipoprotein; Lysosome; Membrane; Palmitate; Phosphoprotein;
Polymorphism; Protease; Reference proteome; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 45 {ECO:0000269|PubMed:10591214}.
/FTId=PRO_0000025939.
CHAIN 46 501 Beta-secretase 1.
/FTId=PRO_0000025940.
TOPO_DOM 22 457 Extracellular. {ECO:0000255}.
TRANSMEM 458 478 Helical. {ECO:0000255}.
TOPO_DOM 479 501 Cytoplasmic. {ECO:0000255}.
DOMAIN 75 416 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
REGION 479 501 Interaction with RTN3.
MOTIF 496 500 DXXLL. {ECO:0000269|PubMed:15886016}.
ACT_SITE 93 93 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 289 289 {ECO:0000255|PROSITE-ProRule:PRU10094}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 275 275 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 285 285 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 300 300 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 307 307 N6-acetyllysine.
{ECO:0000269|PubMed:17425515,
ECO:0000269|PubMed:19011241}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000269|PubMed:15886016}.
LIPID 474 474 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P56818}.
LIPID 478 478 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P56818}.
LIPID 482 482 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P56818}.
LIPID 485 485 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:P56818}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 216 420 {ECO:0000269|PubMed:11953458}.
DISULFID 278 443 {ECO:0000269|PubMed:11953458}.
DISULFID 330 380 {ECO:0000269|PubMed:11953458}.
CROSSLNK 501 501 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:20484053,
ECO:0000269|PubMed:27302062}.
VAR_SEQ 1 20 MAQALPWLLLWMGAGVLPAH -> MVPFIYLQAHFTLCSGW
SST (in isoform 5 and isoform 6).
{ECO:0000305}.
/FTId=VSP_047092.
VAR_SEQ 21 120 Missing (in isoform 5 and isoform 6).
{ECO:0000305}.
/FTId=VSP_047093.
VAR_SEQ 146 189 Missing (in isoform C and isoform D).
{ECO:0000303|PubMed:11516562,
ECO:0000303|Ref.6}.
/FTId=VSP_005222.
VAR_SEQ 190 214 Missing (in isoform B, isoform D and
isoform 6). {ECO:0000303|PubMed:11516562,
ECO:0000303|Ref.5}.
/FTId=VSP_005223.
VARIANT 265 265 V -> A (in dbSNP:rs28989503).
{ECO:0000269|Ref.10}.
/FTId=VAR_060692.
VARIANT 481 481 R -> C (in dbSNP:rs539765).
/FTId=VAR_051509.
MUTAGEN 93 93 D->N: Decreases beta-cleaved soluble APP
production.
{ECO:0000269|PubMed:10656250}.
MUTAGEN 284 284 D->N: Almost abolishes beta-cleaved
soluble APP production.
{ECO:0000269|PubMed:10656250}.
MUTAGEN 498 498 S->A: No effect on endocytosis from the
cell surface. Increases recycling from
endosomes to the cell surface.
{ECO:0000269|PubMed:15615712,
ECO:0000269|PubMed:15886016}.
MUTAGEN 498 498 S->D: No effect on endocytosis form the
cell surface. Decreases recycling from
endosomes to the cell surface.
{ECO:0000269|PubMed:15886016}.
MUTAGEN 499 500 LL->AA: Impairs endocytosis and produces
a delayed retrograde transport to the
trans-Golgi network and delivery to the
lysosmes, decreasinf its degradation.
Disrupts location to late endosomes and
lysosomes. Locates mainly at the cell
surface. No effect on degradation
regulated by GGA3. Effects on protein
stability and defective internalization
increases; when associated with R-501.
{ECO:0000269|PubMed:15615712,
ECO:0000269|PubMed:16033761,
ECO:0000269|PubMed:20484053,
ECO:0000269|PubMed:23109336}.
MUTAGEN 501 501 K->R: Inhibits ubiquitination. No effect
on endocytosis rate. Induced protein
stability and acculmulation in early and
late endosomes, lysosomes and cell
membrane. Effects on protein stability
and defective internalization increases;
when associated with A-499-500-A.
{ECO:0000269|PubMed:20484053,
ECO:0000269|PubMed:23109336,
ECO:0000269|PubMed:27302062}.
HELIX 61 63 {ECO:0000244|PDB:4L7G}.
STRAND 67 70 {ECO:0000244|PDB:4L7G}.
TURN 71 73 {ECO:0000244|PDB:3VF3}.
STRAND 75 81 {ECO:0000244|PDB:4L7G}.
TURN 82 85 {ECO:0000244|PDB:4L7G}.
STRAND 86 93 {ECO:0000244|PDB:4L7G}.
STRAND 99 102 {ECO:0000244|PDB:4L7G}.
STRAND 109 111 {ECO:0000244|PDB:3S7L}.
HELIX 115 117 {ECO:0000244|PDB:4L7G}.
STRAND 122 131 {ECO:0000244|PDB:4L7G}.
STRAND 132 134 {ECO:0000244|PDB:2OHN}.
STRAND 136 147 {ECO:0000244|PDB:4L7G}.
TURN 149 152 {ECO:0000244|PDB:5MXD}.
STRAND 155 168 {ECO:0000244|PDB:4L7G}.
TURN 172 174 {ECO:0000244|PDB:1SGZ}.
STRAND 178 181 {ECO:0000244|PDB:4L7G}.
HELIX 185 187 {ECO:0000244|PDB:4L7G}.
STRAND 188 190 {ECO:0000244|PDB:4FSL}.
HELIX 197 204 {ECO:0000244|PDB:4L7G}.
STRAND 211 215 {ECO:0000244|PDB:4L7G}.
HELIX 224 229 {ECO:0000244|PDB:5HDZ}.
STRAND 230 239 {ECO:0000244|PDB:4L7G}.
HELIX 242 244 {ECO:0000244|PDB:4L7G}.
STRAND 245 253 {ECO:0000244|PDB:4L7G}.
TURN 257 260 {ECO:0000244|PDB:4L7G}.
STRAND 264 269 {ECO:0000244|PDB:4L7G}.
HELIX 278 282 {ECO:0000244|PDB:4L7G}.
STRAND 286 288 {ECO:0000244|PDB:4L7G}.
STRAND 294 298 {ECO:0000244|PDB:4L7G}.
HELIX 299 312 {ECO:0000244|PDB:4L7G}.
TURN 313 315 {ECO:0000244|PDB:4L7G}.
HELIX 320 323 {ECO:0000244|PDB:4L7G}.
STRAND 329 332 {ECO:0000244|PDB:4L7G}.
TURN 333 335 {ECO:0000244|PDB:2VA7}.
HELIX 338 340 {ECO:0000244|PDB:4L7G}.
STRAND 344 349 {ECO:0000244|PDB:4L7G}.
STRAND 355 361 {ECO:0000244|PDB:4L7G}.
HELIX 363 366 {ECO:0000244|PDB:4L7G}.
STRAND 367 369 {ECO:0000244|PDB:4L7G}.
HELIX 373 375 {ECO:0000244|PDB:3VF3}.
STRAND 378 383 {ECO:0000244|PDB:4L7G}.
STRAND 385 390 {ECO:0000244|PDB:4L7G}.
STRAND 392 394 {ECO:0000244|PDB:4L7G}.
HELIX 396 399 {ECO:0000244|PDB:4L7G}.
STRAND 402 407 {ECO:0000244|PDB:4L7G}.
TURN 408 411 {ECO:0000244|PDB:4L7G}.
STRAND 412 418 {ECO:0000244|PDB:4L7G}.
STRAND 430 436 {ECO:0000244|PDB:4L7G}.
HELIX 440 443 {ECO:0000244|PDB:6EJ2}.
SEQUENCE 501 AA; 55764 MW; 377CE4C824ACEF05 CRC64;
MAQALPWLLL WMGAGVLPAH GTQHGIRLPL RSGLGGAPLG LRLPRETDEE PEEPGRRGSF
VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA VGAAPHPFLH RYYQRQLSST
YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH GPNVTVRANI AAITESDKFF INGSNWEGIL
GLAYAEIARP DDSLEPFFDS LVKQTHVPNL FSLQLCGAGF PLNQSEVLAS VGGSMIIGGI
DHSLYTGSLW YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG EVTNQSFRIT
ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME GFYVVFDRAR KRIGFAVSAC
HVHDEFRTAA VEGPFVTLDM EDCGYNIPQT DESTLMTIAY VMAAICALFM LPLCLMVCQW
RCLRCLRQQH DDFADDISLL K


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