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Amyloid-beta precursor protein (APP) (ABPP) (APPI) (Alzheimer disease amyloid protein) (Amyloid precursor protein) (Amyloid-beta A4 protein) (Cerebral vascular amyloid peptide) (CVAP) (PreA4) (Protease nexin-II) (PN-II) [Cleaved into: N-APP; Soluble APP-alpha (S-APP-alpha); Soluble APP-beta (S-APP-beta); C99 (Beta-secretase C-terminal fragment) (Beta-CTF); Amyloid-beta protein 42 (Abeta42) (Beta-APP42); Amyloid-beta protein 40 (Abeta40) (Beta-APP40); C83 (Alpha-secretase C-terminal fragment) (Alpha-CTF); P3(42); P3(40); C80; Gamma-secretase C-terminal fragment 59 (Amyloid intracellular domain 59) (AICD-59) (AID(59)) (Gamma-CTF(59)); Gamma-secretase C-terminal fragment 57 (Amyloid intracellular domain 57) (AICD-57) (AID(57)) (Gamma-CTF(57)); Gamma-secretase C-terminal fragment 50 (Amyloid intracellular domain 50) (AICD-50) (AID(50)) (Gamma-CTF(50)); C31]

 A4_HUMAN                Reviewed;         770 AA.
P05067; B2R5V1; B4DII8; D3DSD1; D3DSD2; D3DSD3; P09000; P78438; Q13764;
Q13778; Q13793; Q16011; Q16014; Q16019; Q16020; Q6GSC0; Q8WZ99; Q9BT38;
Q9UC33; Q9UCA9; Q9UCB6; Q9UCC8; Q9UCD1; Q9UQ58;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 3.
22-APR-2020, entry version 290.
RecName: Full=Amyloid-beta precursor protein {ECO:0000305};
Short=APP {ECO:0000305};
AltName: Full=ABPP;
AltName: Full=APPI;
AltName: Full=Alzheimer disease amyloid protein;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Amyloid-beta A4 protein;
AltName: Full=Cerebral vascular amyloid peptide;
Short=CVAP;
AltName: Full=PreA4;
AltName: Full=Protease nexin-II;
Short=PN-II;
Contains:
RecName: Full=N-APP;
Contains:
RecName: Full=Soluble APP-alpha {ECO:0000303|PubMed:10656250};
Short=S-APP-alpha {ECO:0000303|PubMed:10656250};
Contains:
RecName: Full=Soluble APP-beta {ECO:0000303|PubMed:10656250};
Short=S-APP-beta {ECO:0000303|PubMed:10656250};
Contains:
RecName: Full=C99;
AltName: Full=Beta-secretase C-terminal fragment {ECO:0000303|PubMed:10656250};
Short=Beta-CTF {ECO:0000303|PubMed:10656250};
Contains:
RecName: Full=Amyloid-beta protein 42 {ECO:0000303|PubMed:8886002};
Short=Abeta42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Amyloid-beta protein 40 {ECO:0000303|PubMed:8886002};
Short=Abeta40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
AltName: Full=Alpha-secretase C-terminal fragment {ECO:0000303|PubMed:10656250};
Short=Alpha-CTF {ECO:0000303|PubMed:10656250};
Contains:
RecName: Full=P3(42);
Contains:
RecName: Full=P3(40);
Contains:
RecName: Full=C80;
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 59;
AltName: Full=Amyloid intracellular domain 59;
Short=AICD-59;
Short=AID(59);
AltName: Full=Gamma-CTF(59);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 57;
AltName: Full=Amyloid intracellular domain 57;
Short=AICD-57;
Short=AID(57);
AltName: Full=Gamma-CTF(57);
Contains:
RecName: Full=Gamma-secretase C-terminal fragment 50;
AltName: Full=Amyloid intracellular domain 50;
Short=AICD-50;
Short=AID(50);
AltName: Full=Gamma-CTF(50);
Contains:
RecName: Full=C31;
Flags: Precursor;
Name=APP {ECO:0000312|HGNC:HGNC:620}; Synonyms=A4, AD1;
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 APP695).
TISSUE=Brain;
PubMed=2881207; DOI=10.1038/325733a0;
Kang J., Lemaire H.-G., Unterbeck A., Salbaum J.M., Masters C.L.,
Grzeschik K.-H., Multhaup G., Beyreuther K., Mueller-Hill B.;
"The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-
surface receptor.";
Nature 325:733-736(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751).
TISSUE=Brain;
PubMed=2893289; DOI=10.1038/331525a0;
Ponte P., Gonzalez-Dewhitt P., Schilling J., Miller J., Hsu D.,
Greenberg B., Davis K., Wallace W., Lieberburg I., Fuller F., Cordell B.;
"A new A4 amyloid mRNA contains a domain homologous to serine proteinase
inhibitors.";
Nature 331:525-527(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP695).
PubMed=2783775; DOI=10.1093/nar/17.2.517;
Lemaire H.-G., Salbaum J.M., Multhaup G., Kang J., Bayney R.M.,
Unterbeck A., Beyreuther K., Mueller-Hill B.;
"The PreA4(695) precursor protein of Alzheimer's disease A4 amyloid is
encoded by 16 exons.";
Nucleic Acids Res. 17:517-522(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770).
PubMed=2110105; DOI=10.1016/0378-1119(90)90310-n;
Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y.;
"Genomic organization of the human amyloid beta-protein precursor gene.";
Gene 87:257-263(1990).
[5]
ERRATUM OF PUBMED:2110105.
PubMed=1908403; DOI=10.1016/0378-1119(91)90093-q;
Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y.;
Gene 102:291-292(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-APP733).
TISSUE=Leukocyte;
PubMed=1587857;
Koenig G., Moenning U., Czech C., Prior R., Banati R., Schreiter-Gasser U.,
Bauer J., Masters C.L., Beyreuther K.;
"Identification and differential expression of a novel alternative splice
isoform of the beta A4 amyloid precursor protein (APP) mRNA in leukocytes
and brain microglial cells.";
J. Biol. Chem. 267:10804-10809(1992).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770).
PubMed=9108164; DOI=10.1093/nar/25.9.1802;
Hattori M., Tsukahara F., Furuhata Y., Tanahashi H., Hirose M., Saito M.,
Tsukuni S., Sakaki Y.;
"A novel method for making nested deletions and its application for
sequencing of a 300 kb region of human APP locus.";
Nucleic Acids Res. 25:1802-1808(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP639), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12859342; DOI=10.1046/j.1460-9568.2003.02731.x;
Tang K., Wang C., Shen C., Sheng S., Ravid R., Jing N.;
"Identification of a novel alternative splicing isoform of human amyloid
precursor protein gene, APP639.";
Eur. J. Neurosci. 18:102-108(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP770 AND 11).
TISSUE=Cerebellum, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-501.
NIEHS SNPs program;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[12]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP305 AND APP751).
TISSUE=Eye, and Pancreas;
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).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-10.
TISSUE=Liver;
PubMed=3140222; DOI=10.1093/nar/16.19.9351;
Schon E.A., Mita S., Sadlock J., Herbert J.;
"A cDNA specifying the human amyloid beta precursor protein (ABPP) encodes
a 95-kDa polypeptide.";
Nucleic Acids Res. 16:9351-9351(1988).
[15]
ERRATUM OF PUBMED:3140222, AND SEQUENCE REVISION.
Schon E.A., Mita S., Sadlock J., Herbert J.;
Nucleic Acids Res. 16:11402-11402(1988).
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
PubMed=2538123; DOI=10.1016/0006-291x(89)92437-6;
La Fauci G., Lahiri D.K., Salton S.R., Robakis N.K.;
"Characterization of the 5'-end region and the first two exons of the beta-
protein precursor gene.";
Biochem. Biophys. Res. Commun. 159:297-304(1989).
[17]
PROTEIN SEQUENCE OF 18-50.
TISSUE=Fibroblast;
PubMed=3597385;
van Nostrand W.E., Cunningham D.D.;
"Purification of protease nexin II from human fibroblasts.";
J. Biol. Chem. 262:8508-8514(1987).
[18]
PROTEIN SEQUENCE OF 18-40.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric
identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 286-366.
PubMed=2893290; DOI=10.1038/331528a0;
Tanzi R.E., McClatchey A.I., Lamperti E.D., Villa-Komaroff L.,
Gusella J.F., Neve R.L.;
"Protease inhibitor domain encoded by an amyloid protein precursor mRNA
associated with Alzheimer's disease.";
Nature 331:528-530(1988).
[20]
NUCLEOTIDE SEQUENCE [MRNA] OF 287-367.
PubMed=2893291; DOI=10.1038/331530a0;
Kitaguchi N., Takahashi Y., Tokushima Y., Shiojiri S., Ito H.;
"Novel precursor of Alzheimer's disease amyloid protein shows protease
inhibitory activity.";
Nature 331:530-532(1988).
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 507-770.
TISSUE=Brain cortex;
PubMed=2893379; DOI=10.1073/pnas.85.3.929;
Zain S.B., Salim M., Chou W.G., Sajdel-Sulkowska E.M., Majocha R.E.,
Marotta C.A.;
"Molecular cloning of amyloid cDNA derived from mRNA of the Alzheimer
disease brain: coding and noncoding regions of the fetal precursor mRNA are
expressed in the cortex.";
Proc. Natl. Acad. Sci. U.S.A. 85:929-933(1988).
[22]
PROTEIN SEQUENCE OF 523-555, AND DOMAIN COLLAGEN-BINDING.
PubMed=8576160; DOI=10.1074/jbc.271.3.1613;
Beher D., Hesse L., Masters C.L., Multhaup G.;
"Regulation of amyloid protein precursor (APP) binding to collagen and
mapping of the binding sites on APP and collagen type I.";
J. Biol. Chem. 271:1613-1620(1996).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 655-737, AND VARIANTS AD1 GLY-717; ILE-717
AND PHE-717.
PubMed=8476439; DOI=10.1006/bbrc.1993.1386;
Denman R.B., Rosenzcwaig R., Miller D.L.;
"A system for studying the effect(s) of familial Alzheimer disease
mutations on the processing of the beta-amyloid peptide precursor.";
Biochem. Biophys. Res. Commun. 192:96-103(1993).
[24]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737.
PubMed=2675837; DOI=10.1016/0006-291x(89)91112-1;
Johnstone E.M., Chaney M.O., Moore R.E., Ward K.E., Norris F.H.,
Little S.P.;
"Alzheimer's disease amyloid peptide is encoded by two exons and shows
similarity to soybean trypsin inhibitor.";
Biochem. Biophys. Res. Commun. 163:1248-1255(1989).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 672-723, AND VARIANT AD1 ASN-678.
PubMed=15201367; DOI=10.1136/jnnp.2003.010611;
Wakutani Y., Watanabe K., Adachi Y., Wada-Isoe K., Urakami K., Ninomiya H.,
Saido T.C., Hashimoto T., Iwatsubo T., Nakashima K.;
"Novel amyloid precursor protein gene missense mutation (D678N) in probable
familial Alzheimer's disease.";
J. Neurol. Neurosurg. Psych. 75:1039-1042(2004).
[26]
PROTEIN SEQUENCE OF 672-681.
TISSUE=Brain cortex;
PubMed=3312495; DOI=10.1111/j.1471-4159.1987.tb01005.x;
Pardridge W.M., Vinters H.V., Yang J., Eisenberg J., Choi T.B.,
Tourtellotte W.W., Huebner V., Shively J.E.;
"Amyloid angiopathy of Alzheimer's disease: amino acid composition and
partial sequence of a 4,200-dalton peptide isolated from cortical
microvessels.";
J. Neurochem. 49:1394-1401(1987).
[27]
PROTEIN SEQUENCE OF 672-704, AND TISSUE SPECIFICITY.
PubMed=1406936; DOI=10.1038/359325a0;
Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., Sinha S.,
Schlossmacher M., Whaley J., Swindlehurst C.;
"Isolation and quantification of soluble Alzheimer's beta-peptide from
biological fluids.";
Nature 359:325-327(1992).
[28]
PROTEIN SEQUENCE OF 672-701.
TISSUE=Cerebrospinal fluid;
PubMed=8229004; DOI=10.1111/j.1471-4159.1993.tb09841.x;
Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B.;
"Characterization of beta-amyloid peptide from human cerebrospinal fluid.";
J. Neurochem. 61:1965-1968(1993).
[29]
PROTEIN SEQUENCE OF 672-713.
TISSUE=Blood vessel;
PubMed=8248178; DOI=10.1073/pnas.90.22.10836;
Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E.,
Ball M.J.;
"Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid
deposits: implications for the pathology of Alzheimer disease.";
Proc. Natl. Acad. Sci. U.S.A. 90:10836-10840(1993).
[30]
PROTEIN SEQUENCE OF 672-701 AND 707-713.
PubMed=8109908; DOI=10.1002/ana.410350223;
Wisniewski T., Lalowski M., Levy E., Marques M.R.F., Frangione B.;
"The amino acid sequence of neuritic plaque amyloid from a familial
Alzheimer's disease patient.";
Ann. Neurol. 35:245-246(1994).
[31]
NUCLEOTIDE SEQUENCE [MRNA] OF 674-770.
TISSUE=Brain;
PubMed=3810169; DOI=10.1126/science.3810169;
Goldgaber D., Lerman M.I., McBride O.W., Saffiotti U., Gajdusek D.C.;
"Characterization and chromosomal localization of a cDNA encoding brain
amyloid of Alzheimer's disease.";
Science 235:877-880(1987).
[32]
NUCLEOTIDE SEQUENCE [MRNA] OF 674-703.
TISSUE=Fetal brain;
PubMed=2949367; DOI=10.1126/science.2949367;
Tanzi R.E., Gusella J.F., Watkins P.C., Bruns G.A., St George-Hyslop P.H.,
Van Keuren M.L., Patterson D., Pagan S., Kurnit D.M., Neve R.L.;
"Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage
near the Alzheimer locus.";
Science 235:880-884(1987).
[33]
PROTEIN SEQUENCE OF 609-713, AND GLYCOSYLATION AT THR-633; THR-651;
THR-652; THR-659; THR-663; SER-667 AND TYR-681.
TISSUE=Cerebrospinal fluid;
PubMed=22576872; DOI=10.1002/jms.2987;
Brinkmalm G., Portelius E., Ohrfelt A., Mattsson N., Persson R.,
Gustavsson M.K., Vite C.H., Gobom J., Mansson J.E., Nilsson J., Halim A.,
Larson G., Ruetschi U., Zetterberg H., Blennow K., Brinkmalm A.;
"An online nano-LC-ESI-FTICR-MS method for comprehensive characterization
of endogenous fragments from amyloid beta and amyloid precursor protein in
human and cat cerebrospinal fluid.";
J. Mass Spectrom. 47:591-603(2012).
[34]
PROTEIN SEQUENCE OF 691-698, AND PROTEOLYTIC CLEAVAGE AT PHE-690 BY
THETA-SECRETASE.
PubMed=16816112; DOI=10.1096/fj.05-5632com;
Sun X., He G., Song W.;
"BACE2, as a novel APP theta-secretase, is not responsible for the
pathogenesis of Alzheimer's disease in Down syndrome.";
FASEB J. 20:1369-1376(2006).
[35]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751).
TISSUE=Brain;
PubMed=2569763; DOI=10.1126/science.2569763;
de Sauvage F., Octave J.-N.;
"A novel mRNA of the A4 amyloid precursor gene coding for a possibly
secreted protein.";
Science 245:651-653(1989).
[36]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
TISSUE=Brain;
PubMed=3035574; DOI=10.1073/pnas.84.12.4190;
Robakis N.K., Ramakrishna N., Wolfe G., Wisniewski H.M.;
"Molecular cloning and characterization of a cDNA encoding the
cerebrovascular and the neuritic plaque amyloid peptides.";
Proc. Natl. Acad. Sci. U.S.A. 84:4190-4194(1987).
[37]
SUBCELLULAR LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE, AND TOPOLOGY.
PubMed=2900137; DOI=10.1002/j.1460-2075.1988.tb02900.x;
Dyrks T., Weidemann A., Multhaup G., Salbaum J.M., Lemaire H.-G., Kang J.,
Mueller-Hill B., Masters C.L., Beyreuther K.;
"Identification, transmembrane orientation and biogenesis of the amyloid A4
precursor of Alzheimer's disease.";
EMBO J. 7:949-957(1988).
[38]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, SULFATION, AND
OX-2 MOTIF.
PubMed=2649245; DOI=10.1016/0092-8674(89)90177-3;
Weidemann A., Koenig G., Bunke D., Fischer P., Salbaum J.M., Masters C.L.,
Beyreuther K.;
"Identification, biogenesis, and localization of precursors of Alzheimer's
disease A4 amyloid protein.";
Cell 57:115-126(1989).
[39]
IDENTITY OF APP WITH NEXIN-II.
PubMed=2506449; DOI=10.1038/341144a0;
Oltersdorf T., Fritz L.C., Schenk D.B., Lieberburg I., Johnson-Wood K.L.,
Beattie E.C., Ward P.J., Blacher R.W., Dovey H.F., Sinha S.;
"The secreted form of the Alzheimer's amyloid precursor protein with the
Kunitz domain is protease nexin-II.";
Nature 341:144-147(1989).
[40]
PROTEASE-SPECIFICITY OF INHIBITOR DOMAIN.
PubMed=1969731; DOI=10.1016/0006-291x(90)92084-d;
Kido H., Fukutomi A., Schilling J., Wang Y., Cordell B., Katunuma N.;
"Protease-specificity of Kunitz inhibitor domain of Alzheimer's disease
amyloid protein precursor.";
Biochem. Biophys. Res. Commun. 167:716-721(1990).
[41]
EXTRACELLULAR ZINC-BINDING DOMAIN.
PubMed=8344894;
Bush A.I., Multhaup G., Moir R.D., Williamson T.G., Small D.H., Rumble B.,
Pollwein P., Beyreuther K., Masters C.L.;
"A novel zinc(II) binding site modulates the function of the beta A4
amyloid protein precursor of Alzheimer's disease.";
J. Biol. Chem. 268:16109-16112(1993).
[42]
INTERACTION WITH G(O).
PubMed=8446172; DOI=10.1038/362075a0;
Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Okamoto T.,
Murayama Y., Ogata E.;
"Alzheimer amyloid protein precursor complexes with brain GTP-binding
protein G(o).";
Nature 362:75-79(1993).
[43]
PHOSPHORYLATION AT THR-743.
PubMed=8131745; DOI=10.1002/j.1460-2075.1994.tb06360.x;
Suzuki T., Oishi M., Marshak D.R., Czernik A.J., Nairn A.C., Greengard P.;
"Cell cycle-dependent regulation of the phosphorylation and metabolism of
the Alzheimer amyloid precursor protein.";
EMBO J. 13:1114-1122(1994).
[44]
EXTRACELLULAR COPPER-BINDING DOMAIN, AND MUTAGENESIS OF HIS-137; MET-141;
CYS-144; HIS-147 AND HIS-151.
PubMed=7913895; DOI=10.1016/0014-5793(94)00658-x;
Hesse L., Beher D., Masters C.L., Multhaup G.;
"The beta A4 amyloid precursor protein binding to copper.";
FEBS Lett. 349:109-116(1994).
[45]
N-TERMINAL HEPARIN-BINDING DOMAIN, AND MUTAGENESIS OF 99-LYS--ARG-102.
PubMed=8158260; DOI=10.1523/jneurosci.14-04-02117.1994;
Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K.,
Masters C.L.;
"A heparin-binding domain in the amyloid protein precursor of Alzheimer's
disease is involved in the regulation of neurite outgrowth.";
J. Neurosci. 14:2117-2127(1994).
[46]
CHARACTERIZATION OF L-APP733, AND MUTAGENESIS OF SER-656.
PubMed=7737970; DOI=10.1074/jbc.270.18.10388;
Pangalos M.N., Efthimiopoulos S., Shioi J., Robakis N.K.;
"The chondroitin sulfate attachment site of appican is formed by splicing
out exon 15 of the amyloid precursor gene.";
J. Biol. Chem. 270:10388-10391(1995).
[47]
INTERACTION WITH APP-BP1.
PubMed=8626687; DOI=10.1074/jbc.271.19.11339;
Chow N., Korenberg J.R., Chen X.-N., Neve R.L.;
"APP-BP1, a novel protein that binds to the carboxyl-terminal region of the
amyloid precursor protein.";
J. Biol. Chem. 271:11339-11346(1996).
[48]
INTERACTION WITH APBA1 AND APBB1, AND MUTAGENESIS OF TYR-728; TYR-757;
ASN-759 AND TYR-762.
PubMed=8887653; DOI=10.1128/mcb.16.11.6229;
Borg J.-P., Ooi J., Levy E., Margolis B.;
"The phosphotyrosine interaction domains of X11 and FE65 bind to distinct
sites on the YENPTY motif of amyloid precursor protein.";
Mol. Cell. Biol. 16:6229-6241(1996).
[49]
INTERACTION WITH APBB2.
PubMed=8855266; DOI=10.1073/pnas.93.20.10832;
Guenette S.Y., Chen J., Jondro P.D., Tanzi R.E.;
"Association of a novel human FE65-like protein with the cytoplasmic domain
of the amyloid-beta precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 93:10832-10837(1996).
[50]
FUNCTION OF AMYLOID-BETA PEPTIDE AS LIPID PEROXIDATION INHIBITOR, AND
MUTAGENESIS OF MET-706.
PubMed=9168929; DOI=10.1006/bbrc.1997.6547;
Walter M.F., Mason P.E., Mason R.P.;
"Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation
as a result of its membrane interactions.";
Biochem. Biophys. Res. Commun. 233:760-764(1997).
[51]
HEPARIN-BINDING DOMAINS.
PubMed=9357988; DOI=10.1016/s0014-5793(97)01146-0;
Mok S.S., Sberna G., Heffernan D., Cappai R., Galatis D., Clarris H.J.,
Sawyer W.H., Beyreuther K., Masters C.L., Small D.H.;
"Expression and analysis of heparin-binding regions of the amyloid
precursor protein of Alzheimer's disease.";
FEBS Lett. 415:303-307(1997).
[52]
INTERACTION OF AMYLOID-BETA PEPTIDE WITH HADH2.
TISSUE=Brain;
PubMed=9338779; DOI=10.1038/39522;
Yan S.D., Fu J., Soto C., Chen X., Zhu H., Al-Mohanna F., Collinson K.,
Zhu A., Stern E., Saido T., Tohyama M., Ogawa S., Roher A., Stern D.;
"An intracellular protein that binds amyloid-beta peptide and mediates
neurotoxicity in Alzheimer's disease.";
Nature 389:689-695(1997).
[53]
COPPER-BINDING, AND DISULFIDE BOND FORMATION.
PubMed=9585534; DOI=10.1021/bi980022m;
Multhaup G., Ruppert T., Schlicksupp A., Hesse L., Bill E., Pipkorn R.,
Masters C.L., Beyreuther K.;
"Copper-binding amyloid precursor protein undergoes a site-specific
fragmentation in the reduction of hydrogen peroxide.";
Biochemistry 37:7224-7230(1998).
[54]
INTERACTION WITH APPBP2, MUTAGENESIS OF TYR-728, AND DOMAIN.
PubMed=9843960; DOI=10.1073/pnas.95.25.14745;
Zheng P., Eastman J., Vande Pol S., Pimplikar S.W.;
"PAT1, a microtubule-interacting protein, recognizes the basolateral
sorting signal of amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 95:14745-14750(1998).
[55]
AMYLOID-BETA ZINC-BINDING, AND MUTAGENESIS OF ARG-676; TYR-681 AND HIS-684.
PubMed=10413512; DOI=10.1021/bi990205o;
Liu S.T., Howlett G., Barrow C.J.;
"Histidine-13 is a crucial residue in the zinc ion-induced aggregation of
the A beta peptide of Alzheimer's disease.";
Biochemistry 38:9373-9378(1999).
[56]
PROTEOLYTIC CLEAVAGE AT ASP-197; ASP-219 AND ASP-739 BY CASPASES, AND
MUTAGENESIS OF ASP-739.
PubMed=10319819; DOI=10.1016/s0092-8674(00)80748-5;
Gervais F.G., Xu D., Robertson G.S., Vaillancourt J.P., Zhu Y., Huang J.,
LeBlanc A., Smith D., Rigby M., Shearman M.S., Clarke E.E., Zheng H.,
van der Ploeg L.H.T., Ruffolo S.C., Thornberry N.A., Xanthoudakis S.,
Zamboni R.J., Roy S., Nicholson D.W.;
"Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-
beta precursor protein and amyloidogenic A beta peptide formation.";
Cell 97:395-406(1999).
[57]
IMPORTANCE OF MET-706 IN FREE RADICAL OXIDATIVE STRESS, AND MUTAGENESIS OF
MET-706.
PubMed=10535332; DOI=10.1016/s0361-9230(99)00093-3;
Varadarajan S., Yatin S., Kanski J., Jahanshahi F., Butterfield D.A.;
"Methionine residue 35 is important in amyloid beta-peptide-associated free
radical oxidative stress.";
Brain Res. Bull. 50:133-141(1999).
[58]
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND MUTAGENESIS OF THR-743.
PubMed=10341243; DOI=10.1523/jneurosci.19-11-04421.1999;
Ando K., Oishi M., Takeda S., Iijima K., Isohara T., Nairn A.C., Kirino Y.,
Greengard P., Suzuki T.;
"Role of phosphorylation of Alzheimer's amyloid precursor protein during
neuronal differentiation.";
J. Neurosci. 19:4421-4427(1999).
[59]
INTERACTION WITH APBA2.
PubMed=9890987; DOI=10.1074/jbc.274.4.2243;
Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S.,
Kirino Y., Suzuki T.;
"Interaction of a neuron-specific protein containing PDZ domains with
Alzheimer's amyloid precursor protein.";
J. Biol. Chem. 274:2243-2254(1999).
[60]
SUBCELLULAR LOCATION, ENDOCYTOSIS SIGNAL, AND MUTAGENESIS OF TYR-728;
GLY-756; TYR-757; ASN-759; PRO-760 AND TYR-762.
PubMed=10383380; DOI=10.1074/jbc.274.27.18851;
Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W., Selkoe D.J.,
Chen X., Stokin G.B., Koo E.H.;
"Mutagenesis identifies new signals for beta-amyloid precursor protein
endocytosis, turnover, and the generation of secreted fragments, including
Abeta42.";
J. Biol. Chem. 274:18851-18856(1999).
[61]
IMPORTANCE OF CYS-144 IN COPPER REDUCTION, AND MUTAGENESIS OF CYS-144 AND
147-HIS--HIS-149.
PubMed=10461923; DOI=10.1046/j.1471-4159.1999.0731288.x;
Ruiz F.H., Gonzalez M., Bodini M., Opazo C., Inestrosa N.C.;
"Cysteine 144 is a key residue in the copper reduction by the beta-amyloid
precursor protein.";
J. Neurochem. 73:1288-1292(1999).
[62]
CLEAVAGE BY BACE1, SUBCELLULAR LOCATION (SOLUBLE APP-BETA), AND
CHARACTERIZATION OF VARIANT AD1 670-ASN-LEU-671.
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).
[63]
INTERACTION OF AMYLOID-BETA WITH APOE.
PubMed=10816430; DOI=10.1042/bj3480359;
Tokuda T., Calero M., Matsubara E., Vidal R., Kumar A., Permanne B.,
Zlokovic B., Smith J.D., Ladu M.J., Rostagno A., Frangione B., Ghiso J.;
"Lipidation of apolipoprotein E influences its isoform-specific interaction
with Alzheimer's amyloid beta peptides.";
Biochem. J. 348:359-365(2000).
[64]
INTERACTION OF APP42-BETA WITH CHRNA7.
PubMed=10681545; DOI=10.1074/jbc.275.8.5626;
Wang H.-Y., Lee D.H.S., D'Andrea M.R., Peterson P.A., Shank R.P.,
Reitz A.B.;
"Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with
high affinity. Implications for Alzheimer's disease pathology.";
J. Biol. Chem. 275:5626-5632(2000).
[65]
IDENTIFICATION OF GAMMA-CTFS BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-739,
AND PROTEOLYTIC CLEAVAGE.
PubMed=12214090; DOI=10.3233/jad-2000-23-408;
Passer B., Pellegrini L., Russo C., Siegel R.M., Lenardo M.J.,
Schettini G., Bachmann M., Tabaton M., D'Adamio L.;
"Generation of an apoptotic intracellular peptide by gamma-secretase
cleavage of Alzheimer's amyloid beta protein precursor.";
J. Alzheimers Dis. 2:289-301(2000).
[66]
REVIEW ON FUNCTION OF AMYLOID-BETA AS ANTIOXIDANT.
PubMed=11775062; DOI=10.1023/a:1012629603390;
Kontush A.;
"Alzheimer's amyloid-beta as a preventive antioxidant for brain
lipoproteins.";
Cell. Mol. Neurobiol. 21:299-315(2001).
[67]
INTERACTION WITH FPR2 (AMYLOID-BETA PROTEIN 42), AND SUBCELLULAR LOCATION
(AMYLOID-BETA PROTEIN 42).
PubMed=11689470; DOI=10.1096/fj.01-0251com;
Yazawa H., Yu Z.-X., Takeda K., Le Y., Gong W., Ferrans V.J.,
Oppenheim J.J., Li C.C.H., Wang J.M.;
"Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled
receptor FPRL1 and forms fibrillar aggregates in macrophages.";
FASEB J. 15:2454-2462(2001).
[68]
INTERACTION WITH BBP.
PubMed=11278849; DOI=10.1074/jbc.m011161200;
Kajkowski E.M., Lo C.F., Ning X., Walker S., Sofia H.J., Wang W., Edris W.,
Chanda P., Wagner E., Vile S., Ryan K., McHendry-Rinde B., Smith S.C.,
Wood A., Rhodes K.J., Kennedy J.D., Bard J., Jacobsen J.S.,
Ozenberger B.A.;
"Beta-amyloid peptide-induced apoptosis regulated by a novel protein
containing a G protein activation module.";
J. Biol. Chem. 276:18748-18756(2001).
[69]
AMYLOID-BETA COPPER AND ZINC-BINDING SITES.
PubMed=11274207; DOI=10.1074/jbc.m100175200;
Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S.,
Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., Barnham K.J.;
"Alzheimer's disease amyloid-beta binds copper and zinc to generate an
allosterically ordered structure containing superoxide dismutase-like
subunits.";
J. Biol. Chem. 276:20466-20473(2001).
[70]
SUBUNIT.
PubMed=11438549; DOI=10.1074/jbc.m105410200;
Scheuermann S., Hambsch B., Hesse L., Stumm J., Schmidt C., Beher D.,
Bayer T.A., Beyreuther K., Multhaup G.;
"Homodimerization of amyloid precursor protein and its implication in the
amyloidogenic pathway of Alzheimer's disease.";
J. Biol. Chem. 276:33923-33929(2001).
[71]
INTERACTION WITH APBB1, FUNCTION, AND SUBCELLULAR LOCATION (GAMMA-SECRETASE
C-TERMINAL FRAGMENT 59).
PubMed=11544248; DOI=10.1074/jbc.c100447200;
Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J.;
"The intracellular domain of the beta-amyloid precursor protein is
stabilized by Fe65 and translocates to the nucleus in a notch-like
manner.";
J. Biol. Chem. 276:40288-40292(2001).
[72]
INTERACTION WITH FBLN1.
PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x;
Ohsawa I., Takamura C., Kohsaka S.;
"Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein
and modulates its physiological function.";
J. Neurochem. 76:1411-1420(2001).
[73]
INTERACTION WITH MAPT, AND FUNCTION.
PubMed=11943163; DOI=10.1016/s0014-5793(02)02376-1;
Rank K.B., Pauley A.M., Bhattacharya K., Wang Z., Evans D.B., Fleck T.J.,
Johnston J.A., Sharma S.K.;
"Direct interaction of soluble human recombinant tau protein with Abeta 1-
42 results in tau aggregation and hyperphosphorylation by tau protein
kinase II.";
FEBS Lett. 514:263-268(2002).
[74]
INTERACTION WITH MAPK8IP1, AND MUTAGENESIS OF TYR-757.
PubMed=11724784; DOI=10.1074/jbc.m108357200;
Scheinfeld M.H., Roncarati R., Vito P., Lopez P.A., Abdallah M.,
D'Adamio L.;
"Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the
cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein
(APP).";
J. Biol. Chem. 277:3767-3775(2002).
[75]
COPPER-MEDIATED LIPID PEROXIDATION, AND MUTAGENESIS OF HIS-147 AND HIS-151.
PubMed=11784781; DOI=10.1523/jneurosci.22-02-00365.2002;
White A.R., Multhaup G., Galatis D., McKinstry W.J., Parker M.W.,
Pipkorn R., Beyreuther K., Masters C.L., Cappai R.;
"Contrasting species-dependent modulation of copper-mediated neurotoxicity
by the Alzheimer's disease amyloid precursor protein.";
J. Neurosci. 22:365-376(2002).
[76]
REVIEW ON ZINC-BINDING.
PubMed=12032279; DOI=10.1073/pnas.122249699;
Bush A.I., Tanzi R.E.;
"The galvanization of beta-amyloid in Alzheimer's disease.";
Proc. Natl. Acad. Sci. U.S.A. 99:7317-7319(2002).
[77]
PHOSPHORYLATION AT SER-198 AND SER-206 BY CASEIN KINASES, AND MUTAGENESIS
OF SER-198 AND SER-206.
PubMed=8999878; DOI=10.1074/jbc.272.3.1896;
Walter J., Capell A., Hung A.Y., Langen H., Schnoelzer M., Thinakaran G.,
Sisodia S.S., Selkoe D.J., Haass C.;
"Ectodomain phosphorylation of beta-amyloid precursor protein at two
distinct cellular locations.";
J. Biol. Chem. 272:1896-1903(1997).
[78]
CHARACTERIZATION OF CASEIN KINASE PHOSPHORYLATION, AND MUTAGENESIS OF
SER-198 AND SER-206.
PubMed=10806211; DOI=10.1074/jbc.m002850200;
Walter J., Schindzielorz A., Hartung B., Haass C.;
"Phosphorylation of the beta-amyloid precursor protein at the cell surface
by ectocasein kinases 1 and 2.";
J. Biol. Chem. 275:23523-23529(2000).
[79]
PROTEOLYTIC CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-739.
PubMed=10742146; DOI=10.1038/74656;
Lu D.C., Rabizadeh S., Chandra S., Shayya R.F., Ellerby L.M., Ye X.,
Salvesen G.S., Koo E.H., Bredesen D.E.;
"A second cytotoxic proteolytic peptide derived from amyloid beta-protein
precursor.";
Nat. Med. 6:397-404(2000).
[80]
PHOSPHORYLATION, INTERACTION WITH APBB1, AND MUTAGENESIS OF THR-743.
PubMed=11517218; DOI=10.1074/jbc.m104059200;
Ando K., Iijima K., Elliott J.I., Kirino Y., Suzuki T.;
"Phosphorylation-dependent regulation of the interaction of amyloid
precursor protein with Fe65 affects the production of beta-amyloid.";
J. Biol. Chem. 276:40353-40361(2001).
[81]
PHOSPHORYLATION BY MAPK10, AND MUTAGENESIS OF THR-743.
PubMed=11146006; DOI=10.1046/j.1471-4159.2001.00102.x;
Standen C.L., Brownlees J., Grierson A.J., Kesavapany S., Lau K.-F.,
McLoughlin D.M., Miller C.C.J.;
"Phosphorylation of thr(668) in the cytoplasmic domain of the Alzheimer's
disease amyloid precursor protein by stress-activated protein kinase 1b
(Jun N-terminal kinase-3).";
J. Neurochem. 76:316-320(2001).
[82]
PROTEOLYTIC CLEAVAGE AT MET-671; LYS-687; VAL-711; ALA-713 AND LEU-720.
PubMed=11851430; DOI=10.1021/bi015794o;
Weidemann A., Eggert S., Reinhard F.B.M., Vogel M., Paliga K., Baier G.,
Masters C.L., Beyreuther K., Evin G.;
"A novel epsilon-cleavage within the transmembrane domain of the Alzheimer
amyloid precursor protein demonstrates homology with Notch processing.";
Biochemistry 41:2825-2835(2002).
[83]
PHOSPHORYLATION AT TYR-757, INTERACTION WITH SHC1, AND MUTAGENESIS OF
THR-743 AND TYR-757.
PubMed=11877420; DOI=10.1074/jbc.m110286200;
Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., D'Adamio L.;
"Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic
tail promotes interaction with Shc.";
J. Biol. Chem. 277:16798-16804(2002).
[84]
REVIEW.
PubMed=12142279; DOI=10.1146/annurev.cellbio.18.020402.142302;
Annaert W., De Strooper B.;
"A cell biological perspective on Alzheimer's disease.";
Annu. Rev. Cell Dev. Biol. 18:25-51(2002).
[85]
SUBCELLULAR LOCATION, AND ASSOCIATION OF AMYLOID FIBRILS WITH GCP1.
PubMed=15084524; DOI=10.1096/fj.03-1040fje;
Watanabe N., Araki W., Chui D.H., Makifuchi T., Ihara Y., Tabira T.;
"Glypican-1 as an Abeta binding HSPG in the human brain: its localization
in DIG domains and possible roles in the pathogenesis of Alzheimer's
disease.";
FASEB J. 18:1013-1015(2004).
[86]
INTERACTION WITH ANKS1B.
PubMed=15347684; DOI=10.1074/jbc.m405329200;
Ghersi E., Noviello C., D'Adamio L.;
"Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated
protein-1 proteins bind to AbetaPP and modulate its processing in an
isoform-specific manner.";
J. Biol. Chem. 279:49105-49112(2004).
[87]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-542.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[88]
INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION.
PubMed=16174740; DOI=10.1073/pnas.0503689102;
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., Behlke J.,
von Arnim C.A., Breiderhoff T., Jansen P., Wu X., Bales K.R., Cappai R.,
Masters C.L., Gliemann J., Mufson E.J., Hyman B.T., Paul S.M., Nykjaer A.,
Willnow T.E.;
"Neuronal sorting protein-related receptor sorLA/LR11 regulates processing
of the amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005).
[89]
INTERACTION WITH SORL1, AND MUTAGENESIS OF 757-TYR--TYR-762.
PubMed=16407538; DOI=10.1523/jneurosci.3882-05.2006;
Spoelgen R., von Arnim C.A., Thomas A.V., Peltan I.D., Koker M., Deng A.,
Irizarry M.C., Andersen O.M., Willnow T.E., Hyman B.T.;
"Interaction of the cytosolic domains of sorLA/LR11 with the amyloid
precursor protein (APP) and beta-secretase beta-site APP-cleaving enzyme.";
J. Neurosci. 26:418-428(2006).
[90]
FUNCTION.
PubMed=17062754; DOI=10.1073/pnas.0607527103;
Satpute-Krishnan P., DeGiorgis J.A., Conley M.P., Jang M., Bearer E.L.;
"A peptide zipcode sufficient for anterograde transport within amyloid
precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 103:16532-16537(2006).
[91]
INTERACTION WITH SORL1.
PubMed=17855360; DOI=10.1074/jbc.m705073200;
Schmidt V., Sporbert A., Rohe M., Reimer T., Rehm A., Andersen O.M.,
Willnow T.E.;
"SorLA/LR11 regulates processing of amyloid precursor protein via
interaction with adaptors GGA and PACS-1.";
J. Biol. Chem. 282:32956-32964(2007).
[92]
INTERACTION WITH APBB1.
PubMed=18468999; DOI=10.1074/jbc.m801827200;
Nakaya T., Kawai T., Suzuki T.;
"Regulation of FE65 nuclear translocation and function by amyloid beta-
protein precursor in osmotically stressed cells.";
J. Biol. Chem. 283:19119-19131(2008).
[93]
INTERACTION WITH ITM2C.
PubMed=19366692; DOI=10.1074/jbc.m109.006403;
Matsuda S., Matsuda Y., D'Adamio L.;
"BRI3 inhibits amyloid precursor protein processing in a mechanistically
distinct manner from its homologue dementia gene BRI2.";
J. Biol. Chem. 284:15815-15825(2009).
[94]
FUNCTION, PROTEOLYTIC CLEAVAGE, AND INTERACTION WITH TNFRSF21.
PubMed=19225519; DOI=10.1038/nature07767;
Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.;
"APP binds DR6 to trigger axon pruning and neuron death via distinct
caspases.";
Nature 457:981-989(2009).
[95]
FUNCTION, AND INTERACTION WITH AGER.
PubMed=19901339; DOI=10.1073/pnas.0905686106;
Takuma K., Fang F., Zhang W., Yan S., Fukuzaki E., Du H., Sosunov A.,
McKhann G., Funatsu Y., Nakamichi N., Nagai T., Mizoguchi H., Ibi D.,
Hori O., Ogawa S., Stern D.M., Yamada K., Yan S.S.;
"RAGE-mediated signaling contributes to intraneuronal transport of
amyloid-{beta} and neuronal dysfunction.";
Proc. Natl. Acad. Sci. U.S.A. 106:20021-20026(2009).
[96]
SUBCELLULAR LOCATION.
PubMed=20580937; DOI=10.1016/j.bbalip.2010.05.010;
Cossec J.C., Simon A., Marquer C., Moldrich R.X., Leterrier C., Rossier J.,
Duyckaerts C., Lenkei Z., Potier M.C.;
"Clathrin-dependent APP endocytosis and Abeta secretion are highly
sensitive to the level of plasma membrane cholesterol.";
Biochim. Biophys. Acta 1801:846-852(2010).
[97]
INTERACTION WITH GSAP.
PubMed=20811458; DOI=10.1038/nature09325;
He G., Luo W., Li P., Remmers C., Netzer W.J., Hendrick J., Bettayeb K.,
Flajolet M., Gorelick F., Wennogle L.P., Greengard P.;
"Gamma-secretase activating protein is a therapeutic target for Alzheimer's
disease.";
Nature 467:95-98(2010).
[98]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[99]
GLYCOSYLATION AT THR-633; THR-651; THR-652; SER-656; THR-663 AND SER-667
PROTEOLYTIC PROCESSING, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=21712440; DOI=10.1073/pnas.1102664108;
Halim A., Brinkmalm G., Ruetschi U., Westman-Brinkmalm A., Portelius E.,
Zetterberg H., Blennow K., Larson G., Nilsson J.;
"Site-specific characterization of threonine, serine, and tyrosine
glycosylations of amyloid precursor protein/amyloid beta-peptides in human
cerebrospinal fluid.";
Proc. Natl. Acad. Sci. U.S.A. 108:11848-11853(2011).
[100]
FUNCTION, AND INTERACTION WITH KIF5B.
PubMed=23011729; DOI=10.1088/1478-3975/9/5/055005;
Seamster P.E., Loewenberg M., Pascal J., Chauviere A., Gonzales A.,
Cristini V., Bearer E.L.;
"Quantitative measurements and modeling of cargo-motor interactions during
fast transport in the living axon.";
Phys. Biol. 9:055005-055005(2012).
[101]
INTERACTION WITH S100A9.
PubMed=22457725; DOI=10.1371/journal.pone.0032953;
Zhang C., Liu Y., Gilthorpe J., van der Maarel J.R.;
"MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide and
induces its fibrillization.";
PLoS ONE 7:E32953-E32953(2012).
[102]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-743, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[103]
INTERACTION WITH PLD3.
PubMed=24336208; DOI=10.1038/nature12825;
UK Brain Expression Consortium;
Cruchaga C., Karch C.M., Jin S.C., Benitez B.A., Cai Y., Guerreiro R.,
Harari O., Norton J., Budde J., Bertelsen S., Jeng A.T., Cooper B.,
Skorupa T., Carrell D., Levitch D., Hsu S., Choi J., Ryten M., Hardy J.,
Ryten M., Trabzuni D., Weale M.E., Ramasamy A., Smith C., Sassi C.,
Bras J., Gibbs J.R., Hernandez D.G., Lupton M.K., Powell J., Forabosco P.,
Ridge P.G., Corcoran C.D., Tschanz J.T., Norton M.C., Munger R.G.,
Schmutz C., Leary M., Demirci F.Y., Bamne M.N., Wang X., Lopez O.L.,
Ganguli M., Medway C., Turton J., Lord J., Braae A., Barber I., Brown K.,
Passmore P., Craig D., Johnston J., McGuinness B., Todd S., Heun R.,
Kolsch H., Kehoe P.G., Hooper N.M., Vardy E.R., Mann D.M.,
Pickering-Brown S., Brown K., Kalsheker N., Lowe J., Morgan K.,
David Smith A., Wilcock G., Warden D., Holmes C., Pastor P.,
Lorenzo-Betancor O., Brkanac Z., Scott E., Topol E., Morgan K., Rogaeva E.,
Singleton A.B., Hardy J., Kamboh M.I., St George-Hyslop P., Cairns N.,
Morris J.C., Kauwe J.S., Goate A.M.;
"Rare coding variants in the phospholipase D3 gene confer risk for
Alzheimer's disease.";
Nature 505:550-554(2014).
[104]
INTERACTION WITH VDAC1.
PubMed=25168729; DOI=10.1016/j.neuroscience.2014.07.079;
Fernandez-Echevarria C., Diaz M., Ferrer I., Canerina-Amaro A., Marin R.;
"Abeta promotes VDAC1 channel dephosphorylation in neuronal lipid rafts.
Relevance to the mechanisms of neurotoxicity in Alzheimer's disease.";
Neuroscience 278:354-366(2014).
[105]
INTERACTION WITH SORL1.
PubMed=24523320; DOI=10.1126/scitranslmed.3007747;
Caglayan S., Takagi-Niidome S., Liao F., Carlo A.S., Schmidt V.,
Burgert T., Kitago Y., Fuechtbauer E.M., Fuechtbauer A., Holtzman D.M.,
Takagi J., Willnow T.E.;
"Lysosomal sorting of amyloid-beta by the SORLA receptor is impaired by a
familial Alzheimer's disease mutation.";
Sci. Transl. Med. 6:223RA20-223RA20(2014).
[106]
PHOSPHORYLATION AT SER-441 AND TYR-497.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted phosphoproteome.";
Cell 161:1619-1632(2015).
[107]
INTERACTION WITH LRRK2, PHOSPHORYLATION AT THR-743, AND MUTAGENESIS OF
THR-743.
PubMed=28720718; DOI=10.1126/scisignal.aam6790;
Chen Z.C., Zhang W., Chua L.L., Chai C., Li R., Lin L., Cao Z.,
Angeles D.C., Stanton L.W., Peng J.H., Zhou Z.D., Lim K.L., Zeng L.,
Tan E.K.;
"Phosphorylation of amyloid precursor protein by mutant LRRK2 promotes AICD
activity and neurotoxicity in Parkinson's disease.";
Sci. Signal. 10:0-0(2017).
[108]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 287-344.
PubMed=2125487; DOI=10.1021/bi00495a002;
Hynes T.R., Randal M., Kennedy L.A., Eigenbrot C., Kossiakof A.A.;
"X-ray crystal structure of the protease inhibitor domain of Alzheimer's
amyloid beta-protein precursor.";
Biochemistry 29:10018-10022(1990).
[109]
STRUCTURE BY NMR OF 289-344.
PubMed=1718421; DOI=10.1021/bi00107a015;
Heald S.L., Tilton R.F. Jr., Hammond L.S., Lee A., Bayney R.M.,
Kamarck M.E., Ramabhadran T.V., Dreyer R.N., Davis G., Unterbeck A.,
Tamburini P.P.;
"Sequential NMR resonance assignment and structure determination of the
Kunitz-type inhibitor domain of the Alzheimer's beta-amyloid precursor
protein.";
Biochemistry 30:10467-10478(1991).
[110]
STRUCTURE BY NMR OF 672-699.
PubMed=7516706; DOI=10.1021/bi00191a006;
Talafous J., Marcinowski K.J., Klopman G., Zagorski M.G.;
"Solution structure of residues 1-28 of the amyloid beta-peptide.";
Biochemistry 33:7788-7796(1994).
[111]
STRUCTURE BY NMR OF 672-711.
PubMed=7588758; DOI=10.1111/j.1432-1033.1995.293_1.x;
Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K.,
Frank R.W., Rosch P.;
"Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease.";
Eur. J. Biochem. 233:293-298(1995).
[112]
STRUCTURE BY NMR OF 696-706.
PubMed=8973180; DOI=10.1021/bi961598j;
Kohno T., Kobayashi K., Maeda T., Sato K., Takashima A.;
"Three-dimensional structures of the amyloid beta peptide (25-35) in
membrane-mimicking environment.";
Biochemistry 35:16094-16104(1996).
[113]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF KUNITZ DOMAIN IN COMPLEX WITH
CHYMOTRYPSIN; TRYPSIN AND BASIC PANCREATIC TRYPSIN INHIBITOR.
PubMed=9300481; DOI=10.1002/pro.5560060902;
Scheidig A.J., Hynes T.R., Pelletier L.A., Wells J.A., Kossiakoff A.A.;
"Crystal structures of bovine chymotrypsin and trypsin complexed to the
inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and
basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with
altered specificities.";
Protein Sci. 6:1806-1824(1997).
[114]
STRUCTURE BY NMR OF 672-711.
PubMed=9693002; DOI=10.1021/bi972979f;
Coles M., Bicknell W., Watson A.A., Fairlie D.P., Craik D.J.;
"Solution structure of amyloid beta-peptide(1-40) in a water-micelle
environment. Is the membrane-spanning domain where we think it is?";
Biochemistry 37:11064-11077(1998).
[115]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-123.
PubMed=10201399; DOI=10.1038/7562;
Rossjohn J., Cappai R., Feil S.C., Henry A., McKinstry W.J., Galatis D.,
Hesse L., Multhaup G., Beyreuther K., Masters C.L., Parker M.W.;
"Crystal structure of the N-terminal, growth factor-like domain of
Alzheimer amyloid precursor protein.";
Nat. Struct. Biol. 6:327-331(1999).
[116]
STRUCTURE OF CAA-APP VARIANTS.
PubMed=10821838; DOI=10.1074/jbc.m003154200;
Miravalle L., Tokuda T., Chiarle R., Giaccone G., Bugiani O.,
Tagliavini F., Frangione B., Ghiso J.;
"Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse
conformational changes and apoptotic effects in human cerebral endothelial
cells.";
J. Biol. Chem. 275:27110-27116(2000).
[117]
STRUCTURE BY NMR OF 681-706.
PubMed=10940221; DOI=10.1006/jsbi.2000.4288;
Zhang S., Iwata K., Lachenmann M.J., Peng J.W., Li S., Stimson E.R., Lu Y.,
Felix A.M., Maggio J.E., Lee J.P.;
"The Alzheimer's peptide a beta adopts a collapsed coil structure in
water.";
J. Struct. Biol. 130:130-141(2000).
[118]
STRUCTURE BY NMR OF 672-699.
PubMed=10940222; DOI=10.1006/jsbi.2000.4267;
Poulsen S.-A., Watson A.A., Craik D.J.;
"Solution structures in aqueous SDS micelles of two amyloid beta peptides
of Abeta(1-28) mutated at the alpha-secretase cleavage site.";
J. Struct. Biol. 130:142-152(2000).
[119] {ECO:0000244|PDB:1OWT}
STRUCTURE BY NMR OF 124-189, DISULFIDE BONDS, AND COPPER-BINDING SITES.
PubMed=12611883; DOI=10.1074/jbc.m300629200;
Barnham K.J., McKinstry W.J., Multhaup G., Galatis D., Morton C.J.,
Curtain C.C., Williamson N.A., White A.R., Hinds M.G., Norton R.S.,
Beyreuther K., Masters C.L., Parker M.W., Cappai R.;
"Structure of the Alzheimer's disease amyloid precursor protein copper
binding domain. A regulator of neuronal copper homeostasis.";
J. Biol. Chem. 278:17401-17407(2003).
[120]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 346-551, PARTIAL PROTEIN SEQUENCE,
MUTAGENESIS OF ARG-499 AND LYS-503, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=15304215; DOI=10.1016/j.molcel.2004.06.037;
Wang Y., Ha Y.;
"The X-ray structure of an antiparallel dimer of the human amyloid
precursor protein E2 domain.";
Mol. Cell 15:343-353(2004).
[121]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-711 IN COMPLEX WITH IDE.
PubMed=17051221; DOI=10.1038/nature05143;
Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.;
"Structures of human insulin-degrading enzyme reveal a new substrate
recognition mechanism.";
Nature 443:870-874(2006).
[122]
X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 133-189, AND DISULFIDE BONDS.
PubMed=17909280; DOI=10.1107/s1744309107041139;
Kong G.K., Adams J.J., Cappai R., Parker M.W.;
"Structure of Alzheimer's disease amyloid precursor protein copper-binding
domain at atomic resolution.";
Acta Crystallogr. F 63:819-824(2007).
[123] {ECO:0000244|PDB:2FJZ, ECO:0000244|PDB:2FK1, ECO:0000244|PDB:2FK2, ECO:0000244|PDB:2FK3, ECO:0000244|PDB:2FKL}
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 133-189 IN COMPLEXES WITH COPPER
IONS, AND DISULFIDE BONDS.
PubMed=17239395; DOI=10.1016/j.jmb.2006.12.041;
Kong G.K., Adams J.J., Harris H.H., Boas J.F., Curtain C.C., Galatis D.,
Masters C.L., Barnham K.J., McKinstry W.J., Cappai R., Parker M.W.;
"Structural studies of the Alzheimer's amyloid precursor protein copper-
binding domain reveal how it binds copper ions.";
J. Mol. Biol. 367:148-161(2007).
[124]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 672-679 IN COMPLEX WITH IGG.
PubMed=17895381; DOI=10.1073/pnas.0705888104;
Gardberg A.S., Dice L.T., Ou S., Rich R.L., Helmbrecht E., Ko J.,
Wetzel R., Myszka D.G., Patterson P.H., Dealwis C.;
"Molecular basis for passive immunotherapy of Alzheimer's disease.";
Proc. Natl. Acad. Sci. U.S.A. 104:15659-15664(2007).
[125]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 672-678 IN COMPLEXES WITH
ANTIBODY FAB FRAGMENTS.
PubMed=19923222; DOI=10.1074/jbc.m109.045187;
Basi G.S., Feinberg H., Oshidari F., Anderson J., Barbour R., Baker J.,
Comery T.A., Diep L., Gill D., Johnson-Wood K., Goel A., Grantcharova K.,
Lee M., Li J., Partridge A., Griswold-Prenner I., Piot N., Walker D.,
Widom A., Pangalos M.N., Seubert P., Jacobsen J.S., Schenk D., Weis W.I.;
"Structural correlates of antibodies associated with acute reversal of
amyloid beta-related behavioral deficits in a mouse model of Alzheimer
disease.";
J. Biol. Chem. 285:3417-3427(2010).
[126]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 18-190, PARTIAL PROTEIN SEQUENCE,
SUBUNIT, DISULFIDE BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20212142; DOI=10.1073/pnas.0911326107;
Dahms S.O., Hoefgen S., Roeser D., Schlott B., Guhrs K.H., Than M.E.;
"Structure and biochemical analysis of the heparin-induced E1 dimer of the
amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 107:5381-5386(2010).
[127] {ECO:0000244|PDB:2LOH}
STRUCTURE BY NMR OF 686-726, AND SUBCELLULAR LOCATION.
PubMed=22584060; DOI=10.1016/j.febslet.2012.04.062;
Nadezhdin K.D., Bocharova O.V., Bocharov E.V., Arseniev A.S.;
"Dimeric structure of transmembrane domain of amyloid precursor protein in
micellar environment.";
FEBS Lett. 586:1687-1692(2012).
[128] {ECO:0000244|PDB:2LP1}
STRUCTURE BY NMR OF 671-770, AND SUBCELLULAR LOCATION.
PubMed=22654059; DOI=10.1126/science.1219988;
Barrett P.J., Song Y., Van Horn W.D., Hustedt E.J., Schafer J.M.,
Hadziselimovic A., Beel A.J., Sanders C.R.;
"The amyloid precursor protein has a flexible transmembrane domain and
binds cholesterol.";
Science 336:1168-1171(2012).
[129] {ECO:0000244|PDB:4JFN}
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-185 IN COMPLEX WITH COPPER,
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISULFIDE BONDS, AND
MUTAGENESIS OF HIS-108; HIS-110; HIS-147 AND HIS-151.
PubMed=25122912; DOI=10.1523/jneurosci.0180-14.2014;
Baumkotter F., Schmidt N., Vargas C., Schilling S., Weber R., Wagner K.,
Fiedler S., Klug W., Radzimanowski J., Nickolaus S., Keller S., Eggert S.,
Wild K., Kins S.;
"Amyloid precursor protein dimerization and synaptogenic function depend on
copper binding to the growth factor-like domain.";
J. Neurosci. 34:11159-11172(2014).
[130] {ECO:0000244|PDB:2MGT}
STRUCTURE BY NMR OF 672-687, ZINC-BINDING SITES, AND DOMAIN.
PubMed=26898943; DOI=10.1038/srep21734;
Istrate A.N., Kozin S.A., Zhokhov S.S., Mantsyzov A.B., Kechko O.I.,
Pastore A., Makarov A.A., Polshakov V.I.;
"Interplay of histidine residues of the Alzheimer's disease Abeta peptide
governs its Zn-induced oligomerization.";
Sci. Rep. 6:21734-21734(2016).
[131] {ECO:0000244|PDB:5LFY}
STRUCTURE BY NMR OF 672-681, AND DOMAIN.
PubMed=28570778; DOI=10.1002/anie.201704615;
Polshakov V.I., Mantsyzov A.B., Kozin S.A., Adzhubei A.A., Zhokhov S.S.,
van Beek W., Kulikova A.A., Indeykina M.I., Mitkevich V.A., Makarov A.A.;
"A Binuclear Zinc Interaction Fold Discovered in the Homodimer of
Alzheimer's Amyloid-beta Fragment with Taiwanese Mutation D7H.";
Angew. Chem. Int. Ed. Engl. 56:11734-11739(2017).
[132] {ECO:0000244|PDB:5OQV}
STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) OF 672-713.
PubMed=28882996; DOI=10.1126/science.aao2825;
Gremer L., Scholzel D., Schenk C., Reinartz E., Labahn J., Ravelli R.B.G.,
Tusche M., Lopez-Iglesias C., Hoyer W., Heise H., Willbold D.,
Schroder G.F.;
"Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy.";
Science 358:116-119(2017).
[133] {ECO:0000244|PDB:5VOS}
STRUCTURE BY ELECTRON MICROSCOPY (1.42 ANGSTROMS) OF 695-705.
PubMed=29282295; DOI=10.1074/jbc.m117.806109;
Krotee P., Griner S.L., Sawaya M.R., Cascio D., Rodriguez J.A., Shi D.,
Philipp S., Murray K., Saelices L., Lee J., Seidler P., Glabe C.G.,
Jiang L., Gonen T., Eisenberg D.S.;
"Common fibrillar spines of amyloid-beta and human islet amyloid
polypeptide revealed by microelectron diffraction and structure-based
inhibitors.";
J. Biol. Chem. 293:2888-2902(2018).
[134]
STRUCTURE BY ELECTRON MICROSCOPY (2.60 ANGSTROMS) OF 688-770 IN COMPLEX
WITH GAMMA-SECRETASE, INTERACTION WITH PSEN1, SUBUNIT, PROTEOLYTIC CLEAVAGE
BY PSEN1, TOPOLOGY, AND MUTAGENESIS OF VAL-695.
PubMed=30630874; DOI=10.1126/science.aaw0930;
Zhou R., Yang G., Guo X., Zhou Q., Lei J., Shi Y.;
"Recognition of the amyloid precursor protein by human gamma-secretase.";
Science 0:0-0(2019).
[135]
REVIEW ON VARIANTS.
PubMed=1363811; DOI=10.1038/ng0792-233;
Hardy J.;
"Framing beta-amyloid.";
Nat. Genet. 1:233-234(1992).
[136]
VARIANT CAA-APP GLN-693.
PubMed=2111584; DOI=10.1126/science.2111584;
Levy E., Carman M.D., Fernandez-Madrid I.J., Power M.D., Lieberburg I.,
van Duinen S.G., Bots G.T.A.M., Luyendijk W., Frangione B.;
"Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral
hemorrhage, Dutch type.";
Science 248:1124-1126(1990).
[137]
VARIANT AD1 ILE-717.
PubMed=1671712; DOI=10.1038/349704a0;
Goate A., Chartier-Harlin M.-C., Mullan M., Brown J., Crawford F.,
Fidani L., Giuffra L., Haynes A., Irving N., James L., Mant R., Newton P.,
Rooke K., Roques P., Talbot C., Pericak-Vance M., Roses A.D.,
Williamson R., Rossor M., Owen M., Hardy J.;
"Segregation of a missense mutation in the amyloid precursor protein gene
with familial Alzheimer's disease.";
Nature 349:704-706(1991).
[138]
VARIANT AD1 ILE-717.
PubMed=1908231; DOI=10.1016/0006-291x(91)91011-z;
Yoshioka K., Miki T., Katsuya T., Ogihara T., Sakaki Y.;
"The 717Val-->Ile substitution in amyloid precursor protein is associated
with familial Alzheimer's disease regardless of ethnic groups.";
Biochem. Biophys. Res. Commun. 178:1141-1146(1991).
[139]
VARIANT AD1 ILE-717.
PubMed=1678058; DOI=10.1016/0140-6736(91)91612-x;
Naruse S., Igarashi S., Kobayashi H., Aoki K., Inuzuka T., Kaneko K.,
Shimizu T., Iihara K., Kojima T., Miyatake T., Tsuji S.;
"Mis-sense mutation Val->Ile in exon 17 of amyloid precursor protein gene
in Japanese familial Alzheimer's disease.";
Lancet 337:978-979(1991).
[140]
VARIANT AD1 GLY-717.
PubMed=1944558; DOI=10.1038/353844a0;
Chartier-Harlin M.-C., Crawford F., Houlden H., Warren A., Hughes D.,
Fidani L., Goate A., Rossor M., Roques P., Hardy J., Mullan M.;
"Early-onset Alzheimer's disease caused by mutations at codon 717 of the
beta-amyloid precursor protein gene.";
Nature 353:844-846(1991).
[141]
VARIANT AD1 PHE-717.
PubMed=1925564; DOI=10.1126/science.1925564;
Murrell J.R., Farlow M., Ghetti B., Benson M.D.;
"A mutation in the amyloid precursor protein associated with hereditary
Alzheimer's disease.";
Science 254:97-99(1991).
[142]
VARIANT AD1 GLY-693.
PubMed=1415269;
Kamino K., Orr H.T., Payami H., Wijsman E.M., Alonso M.E., Pulst S.M.,
Anderson L., O'Dahl S., Nemens E., White J.A., Sadovnick A.D., Ball M.J.,
Kaye J., Warren A., McInnis M.G., Antonarakis S.E., Korenberg J.R.,
Sharma V., Kukull W., Larson E., Heston L.L., Martin G.M., Bird T.D.,
Schellenberg G.D.;
"Linkage and mutational analysis of familial Alzheimer disease kindreds for
the APP gene region.";
Am. J. Hum. Genet. 51:998-1014(1992).
[143]
VARIANT AD1 GLY-692.
PubMed=1303239; DOI=10.1038/ng0692-218;
Hendriks L., van Duijn C.M., Cras P., Cruts M., Van Hul W.,
van Harskamp F., Warren A., McInnis M.G., Antonarakis S.E., Martin J.J.,
Hofman A., Van Broeckhoven C.;
"Presenile dementia and cerebral haemorrhage linked to a mutation at codon
692 of the beta-amyloid precursor protein gene.";
Nat. Genet. 1:218-221(1992).
[144]
VARIANT AD1 670-ASN-LEU-671.
PubMed=1302033; DOI=10.1038/ng0892-345;
Mullan M., Crawford F., Axelman K., Houlden H., Lilius L., Winblad B.,
Lannfelt L.;
"A pathogenic mutation for probable Alzheimer's disease in the APP gene at
the N-terminus of beta-amyloid.";
Nat. Genet. 1:345-347(1992).
[145]
CHARACTERIZATION OF VARIANT AD1 670-ASN-LEU-671.
PubMed=1465129; DOI=10.1038/360672a0;
Citron M., Oltersdorf T., Haass C., McConlogue L., Hung A.Y., Seubert P.,
Vigo-Pelfrey C., Lieberburg I., Selkoe D.J.;
"Mutation of the beta-amyloid precursor protein in familial Alzheimer's
disease increases beta-protein production.";
Nature 360:672-674(1992).
[146]
VARIANT VAL-713.
PubMed=1307241; DOI=10.1038/ng0792-306;
Jones C.T., Morris S., Yates C.M., Moffoot A., Sharpe C., Brock D.J.H.,
St Clair D.;
"Mutation in codon 713 of the beta amyloid precursor protein gene
presenting with schizophrenia.";
Nat. Genet. 1:306-309(1992).
[147]
VARIANT AD1 THR-713.
PubMed=1303275; DOI=10.1038/ng1292-255;
Carter D.A., Desmarais E., Bellis M., Campion D., Clerget-Darpoux F.,
Brice A., Agid Y., Jaillard-Serradt A., Mallet J.;
"More missense in amyloid gene.";
Nat. Genet. 2:255-256(1992).
[148]
VARIANTS AD1 ILE-717 AND PHE-717.
PubMed=8267572; DOI=10.1006/bbrc.1993.2491;
Liepnieks J.J., Ghetti B., Farlow M., Roses A.D., Benson M.D.;
"Characterization of amyloid fibril beta-peptide in familial Alzheimer's
disease with APP717 mutations.";
Biochem. Biophys. Res. Commun. 197:386-392(1993).
[149]
VARIANT ASP-665.
PubMed=8154870; DOI=10.1002/ana.410350410;
Peacock M.L., Murman D.L., Sima A.A.F., Warren J.T. Jr., Roses A.D.,
Fink J.K.;
"Novel amyloid precursor protein gene mutation (codon 665Asp) in a patient
with late-onset Alzheimer's disease.";
Ann. Neurol. 35:432-438(1994).
[150]
VARIANT AD1 PHE-717.
PubMed=8290042; DOI=10.1212/wnl.44.1.105;
Farlow M., Murrell J., Ghetti B., Unverzagt F., Zeldenrust S., Benson M.D.;
"Clinical characteristics in a kindred with early-onset Alzheimer's disease
and their linkage to a G-->T change at position 2149 of the amyloid
precursor protein gene.";
Neurology 44:105-111(1994).
[151]
VARIANT AD1 ILE-717.
PubMed=8577393; DOI=10.1016/0304-3940(95)12046-7;
Brooks W.S., Martins R.N., De Voecht J., Nicholson G.A., Schofield P.R.,
Kwok J.B.J., Fisher C., Yeung L.U., Van Broeckhoven C.;
"A mutation in codon 717 of the amyloid precursor protein gene in an
Australian family with Alzheimer's disease.";
Neurosci. Lett. 199:183-186(1995).
[152]
CHARACTERIZATION OF VARIANTS AD1 GLY-717; ILE-717 AND PHE-717.
PubMed=8886002; DOI=10.1006/bbrc.1996.1577;
Maruyama K., Tomita T., Shinozaki K., Kume H., Asada H., Saido T.C.,
Ishiura S., Iwatsubo T., Obata K.;
"Familial Alzheimer's disease-linked mutations at Val717 of amyloid
precursor protein are specific for the increased secretion of A beta
42(43).";
Biochem. Biophys. Res. Commun. 227:730-735(1996).
[153]
VARIANT AD1 VAL-716.
PubMed=9328472; DOI=10.1093/hmg/6.12.2087;
Eckman C.B., Mehta N.D., Crook R., Perez-Tur J., Prihar G., Pfeiffer E.,
Graff-Radford N., Hinder P., Yager D., Zenk B., Refolo L.M., Prada C.M.,
Younkin S.G., Hutton M., Hardy J.;
"A new pathogenic mutation in the APP gene (I716V) increases the relative
proportion of A beta 42(43).";
Hum. Mol. Genet. 6:2087-2089(1997).
[154]
VARIANT AD1 GLY-692, AND CHARACTERIZATION OF PHENOTYPE.
PubMed=9754958; DOI=10.1007/s004010050892;
Cras P., van Harskamp F., Hendriks L., Ceuterick C., van Duijn C.M.,
Stefanko S.Z., Hofman A., Kros J.M., Van Broeckhoven C., Martin J.J.;
"Presenile Alzheimer dementia characterized by amyloid angiopathy and large
amyloid core type senile plaques in the APP 692Ala-->Gly mutation.";
Acta Neuropathol. 96:253-260(1998).
[155]
VARIANT AD1 MET-715, AND CHARACTERIZATION OF VARIANT AD1 MET-715.
PubMed=10097173; DOI=10.1073/pnas.96.7.4119;
Ancolio K., Dumanchin C., Barelli H., Warter J.-M., Brice A., Campion D.,
Frebourg T., Checler F.;
"Unusual phenotypic alteration of beta amyloid precursor protein (betaAPP)
maturation by a new Val-715 --> Met betaAPP-770 mutation responsible for
probable early-onset Alzheimer's disease.";
Proc. Natl. Acad. Sci. U.S.A. 96:4119-4124(1999).
[156]
VARIANT AD1 ILE-717.
PubMed=10631141; DOI=10.1086/302702;
Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J.,
Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A.;
"High prevalence of pathogenic mutations in patients with early-onset
dementia detected by sequence analyses of four different genes.";
Am. J. Hum. Genet. 66:110-117(2000).
[157]
VARIANT AD1 PRO-723.
PubMed=10665499;
DOI=10.1002/1531-8249(200002)47:2<249::aid-ana18>3.0.co;2-8;
Kwok J.B.J., Li Q.X., Hallupp M., Whyte S., Ames D., Beyreuther K.,
Masters C.L., Schofield P.R.;
"Novel Leu723Pro amyloid precursor protein mutation increases amyloid
beta42(43) peptide levels and induces apoptosis.";
Ann. Neurol. 47:249-253(2000).
[158]
VARIANT AD1 LEU-717.
PubMed=10867787; DOI=10.1001/archneur.57.6.885;
Murrell J.R., Hake A.M., Quaid K.A., Farlow M.R., Ghetti B.;
"Early-onset Alzheimer disease caused by a new mutation (V717L) in the
amyloid precursor protein gene.";
Arch. Neurol. 57:885-887(2000).
[159]
VARIANT AD1 ILE-714, AND CHARACTERIZATION OF VARIANTS AD1 ILE-714 AND
ILE-717.
PubMed=11063718; DOI=10.1093/hmg/9.18.2589;
Kumar-Singh S., De Jonghe C., Cruts M., Kleinert R., Wang R., Mercken M.,
De Strooper B., Vanderstichele H., Loefgren A., Vanderhoeven I.,
Backhovens H., Vanmechelen E., Kroisel P.M., Van Broeckhoven C.;
"Nonfibrillar diffuse amyloid deposition due to a gamma(42)-secretase site
mutation points to an essential role for N-truncated A beta(42) in
Alzheimer's disease.";
Hum. Mol. Genet. 9:2589-2598(2000).
[160]
CHARACTERIZATION OF VARIANT AD1 670-ASN-LEU-671.
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).
[161]
VARIANT CAA-APP ASN-694.
PubMed=11409420; DOI=10.1002/ana.1009;
Grabowski T.J., Cho H.S., Vonsattel J.P.G., Rebeck G.W., Greenberg S.M.;
"Novel amyloid precursor protein mutation in an Iowa family with dementia
and severe cerebral amyloid angiopathy.";
Ann. Neurol. 49:697-705(2001).
[162]
CHARACTERIZATION OF VARIANT AD1 GLY-692.
PubMed=11311152; DOI=10.1042/bj3550869;
Walsh D.M., Hartley D.M., Condron M.M., Selkoe D.J., Teplow D.B.;
"In vitro studies of amyloid beta-protein fibril assembly and toxicity
provide clues to the aetiology of Flemish variant (Ala692-->Gly)
Alzheimer's disease.";
Biochem. J. 355:869-877(2001).
[163]
VARIANT AD1 GLY-693.
PubMed=11528419; DOI=10.1038/nn0901-887;
Nilsberth C., Westlind-Danielsson A., Eckman C.B., Condron M.M.,
Axelman K., Forsell C., Stenh C., Luthman J., Teplow D.B., Younkin S.G.,
Naeslund J., Lannfelt L.;
"The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced
Abeta protofibril formation.";
Nat. Neurosci. 4:887-893(2001).
[164]
VARIANT AD1 ALA-714.
PubMed=12034808; DOI=10.1212/wnl.58.10.1574;
Pasalar P., Najmabadi H., Noorian A.R., Moghimi B., Jannati A.,
Soltanzadeh A., Krefft T., Crook R., Hardy J.;
"An Iranian family with Alzheimer's disease caused by a novel APP mutation
(Thr714Ala).";
Neurology 58:1574-1575(2002).
[165]
VARIANT CAA-APP ASN-694.
PubMed=12654973; DOI=10.1212/01.wnl.0000050140.10044.a8;
Greenberg S.M., Shin Y., Grabowski T.J., Cooper G.E., Rebeck G.W.,
Iglesias S., Chapon F., Tournier-Lasserve E., Baron J.-C.;
"Hemorrhagic stroke associated with the Iowa amyloid precursor protein
mutation.";
Neurology 60:1020-1022(2003).
[166]
VARIANT AD1 THR-713.
PubMed=15365148; DOI=10.1212/01.wnl.0000137048.80666.86;
Rossi G., Giaccone G., Maletta R., Morbin M., Capobianco R., Mangieri M.,
Giovagnoli A.R., Bizzi A., Tomaino C., Perri M., Di Natale M.,
Tagliavini F., Bugiani O., Bruni A.C.;
"A family with Alzheimer disease and strokes associated with A713T mutation
of the APP gene.";
Neurology 63:910-912(2004).
[167]
VARIANT CAA-APP VAL-705.
PubMed=16178030; DOI=10.1002/ana.20571;
Obici L., Demarchi A., de Rosa G., Bellotti V., Marciano S., Donadei S.,
Arbustini E., Palladini G., Diegoli M., Genovese E., Ferrari G.,
Coverlizza S., Merlini G.;
"A novel AbetaPP mutation exclusively associated with cerebral amyloid
angiopathy.";
Ann. Neurol. 58:639-644(2005).
[168]
VARIANT AD1 ILE-714.
PubMed=15668448; DOI=10.1212/01.wnl.0000149761.70566.3e;
Edwards-Lee T., Ringman J.M., Chung J., Werner J., Morgan A.,
St George-Hyslop P.H., Thompson P., Dutton R., Mlikotic A., Rogaeva E.,
Hardy J.;
"An African American family with early-onset Alzheimer disease and an APP
(T714I) mutation.";
Neurology 64:377-379(2005).
[169]
VARIANT CAA-APP LYS-693.
PubMed=20697050; DOI=10.1001/archneurol.2010.178;
Bugiani O., Giaccone G., Rossi G., Mangieri M., Capobianco R., Morbin M.,
Mazzoleni G., Cupidi C., Marcon G., Giovagnoli A., Bizzi A., Di Fede G.,
Puoti G., Carella F., Salmaggi A., Romorini A., Patruno G.M., Magoni M.,
Padovani A., Tagliavini F.;
"Hereditary cerebral hemorrhage with amyloidosis associated with the E693K
mutation of APP.";
Arch. Neurol. 67:987-995(2010).
-!- FUNCTION: Functions as a cell surface receptor and performs
physiological functions on the surface of neurons relevant to neurite
growth, neuronal adhesion and axonogenesis. Interaction between APP
molecules on neighboring cells promotes synaptogenesis
(PubMed:25122912). Involved in cell mobility and transcription
regulation through protein-protein interactions. Can promote
transcription activation through binding to APBB1-KAT5 and inhibits
Notch signaling through interaction with Numb. Couples to apoptosis-
inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o)
alpha ATPase activity (By similarity). Acts as a kinesin I membrane
receptor, mediating the axonal transport of beta-secretase and
presenilin 1 (By similarity). By acting as a kinesin I membrane
receptor, plays a role in axonal anterograde transport of cargo towards
synapes in axons (PubMed:17062754, PubMed:23011729). Involved in copper
homeostasis/oxidative stress through copper ion reduction. In vitro,
copper-metallated APP induces neuronal death directly or is potentiated
through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate
neurite outgrowth through binding to components of the extracellular
matrix such as heparin and collagen I and IV. The splice isoforms that
contain the BPTI domain possess protease inhibitor activity. Induces a
AGER-dependent pathway that involves activation of p38 MAPK, resulting
in internalization of amyloid-beta peptide and leading to mitochondrial
dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1
which are required for release of nitric oxide (NO) and subsequent
degradation of the heparan sulfate chains on GPC1. {ECO:0000250,
ECO:0000250|UniProtKB:P12023, ECO:0000269|PubMed:17062754,
ECO:0000269|PubMed:23011729, ECO:0000269|PubMed:25122912}.
-!- FUNCTION: Amyloid-beta peptides are lipophilic metal chelators with
metal-reducing activity. Bind transient metals such as copper, zinc and
iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+),
respectively. Amyloid-beta protein 42 is a more effective reductant
than amyloid-beta protein 40. Amyloid-beta peptides bind to
lipoproteins and apolipoproteins E and J in the CSF and to HDL
particles in plasma, inhibiting metal-catalyzed oxidation of
lipoproteins. APP42-beta may activate mononuclear phagocytes in the
brain and elicit inflammatory responses. Promotes both tau aggregation
and TPK II-mediated phosphorylation. Interaction with overexpressed
HADH2 leads to oxidative stress and neurotoxicity. Also binds GPC1 in
lipid rafts.
-!- FUNCTION: Appicans elicit adhesion of neural cells to the extracellular
matrix and may regulate neurite outgrowth in the brain. {ECO:0000250}.
-!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved
peptides, including C31, are potent enhancers of neuronal apoptosis.
-!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and
degeneration of both neuronal cell bodies (via caspase-3) and axons
(via caspase-6).
-!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several
cytoplasmic proteins, including APBB family members, the APBA family,
MAPK8IP1, SHC1 and, NUMB and DAB1 (By similarity). Binding to DAB1
inhibits its serine phosphorylation (By similarity). Interacts (via
NPXY motif) with DAB2 (via PID domain); the interaction is impaired by
tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-
like protein BPP, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via
BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By
similarity). Associates with microtubules in the presence of ATP and in
a kinesin-dependent manner (By similarity). Interacts, through a C-
terminal domain, with GNAO1. Amyloid-beta protein 42 binds CHRNA7 in
hippocampal neurons. Amyloid-beta associates with HADH2. Soluble APP
binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER
(By similarity). Interacts with ANKS1B and TNFRSF21. Interacts with
ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers;
dimerization is enhanced in the presence of Cu(2+) ions
(PubMed:25122912). Can form homodimers; this is promoted by heparin
binding. Amyloid-beta protein 40 interacts with S100A9. CTF-alpha
product of APP interacts with GSAP. Isoform APP695 interacts with SORL1
(via N-terminal ectodomain); this interaction retains APP in the trans-
Golgi network and reduces processing into soluble APP-alpha and
amyloid-beta peptides (PubMed:16174740, PubMed:16407538,
PubMed:17855360, PubMed:24523320). The C99 fragment also interacts with
SORL1 (PubMed:16407538). Isoform APP751 interacts with SORL1
(PubMed:16174740). Isoform APP770 interacts with SORL1
(PubMed:16174740). Interacts with PLD3. Interacts with VDAC1
(PubMed:25168729). Interacts with NSG1; could regulate APP processing
(By similarity). Amyloid-beta protein 42 interacts with FPR2
(PubMed:11689470). Interacts with SYT7 (By similarity). Interacts (via
transmembrane region) with PSEN1; the interaction is direct
(PubMed:30630874). Interacts with LRRK2 (PubMed:28720718). Interacts
(via cytoplasmic domain) with KIF5B (PubMed:23011729).
{ECO:0000250|UniProtKB:P08592, ECO:0000250|UniProtKB:P12023,
ECO:0000269|PubMed:10681545, ECO:0000269|PubMed:10816430,
ECO:0000269|PubMed:11238726, ECO:0000269|PubMed:11278849,
ECO:0000269|PubMed:11438549, ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11544248, ECO:0000269|PubMed:11689470,
ECO:0000269|PubMed:11724784, ECO:0000269|PubMed:11877420,
ECO:0000269|PubMed:11943163, ECO:0000269|PubMed:15347684,
ECO:0000269|PubMed:16174740, ECO:0000269|PubMed:16407538,
ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17855360,
ECO:0000269|PubMed:17895381, ECO:0000269|PubMed:18468999,
ECO:0000269|PubMed:19225519, ECO:0000269|PubMed:19366692,
ECO:0000269|PubMed:19901339, ECO:0000269|PubMed:20212142,
ECO:0000269|PubMed:20811458, ECO:0000269|PubMed:22457725,
ECO:0000269|PubMed:23011729, ECO:0000269|PubMed:24336208,
ECO:0000269|PubMed:24523320, ECO:0000269|PubMed:25122912,
ECO:0000269|PubMed:25168729, ECO:0000269|PubMed:28720718,
ECO:0000269|PubMed:30630874, ECO:0000269|PubMed:8446172,
ECO:0000269|PubMed:8626687, ECO:0000269|PubMed:8855266,
ECO:0000269|PubMed:8887653, ECO:0000269|PubMed:9300481,
ECO:0000269|PubMed:9338779, ECO:0000269|PubMed:9843960,
ECO:0000269|PubMed:9890987}.
-!- INTERACTION:
P05067; P05067; NbExp=106; IntAct=EBI-77613, EBI-77613;
P05067-4; P05067-4; NbExp=8; IntAct=EBI-302641, EBI-302641;
PRO_0000000092; PRO_0000000092 [P05067]; NbExp=42; IntAct=EBI-821758, EBI-821758;
PRO_0000000093; PRO_0000000093 [P05067]; NbExp=29; IntAct=EBI-2431589, EBI-2431589;
P05067; Q306T3; Xeno; NbExp=3; IntAct=EBI-77613, EBI-8294101;
P05067; O14672: ADAM10; NbExp=4; IntAct=EBI-77613, EBI-1536151;
PRO_0000000093; P31696: AGRN; Xeno; NbExp=3; IntAct=EBI-2431589, EBI-457650;
P05067; Q02410: APBA1; NbExp=4; IntAct=EBI-77613, EBI-368690;
P05067; Q99767: APBA2; NbExp=2; IntAct=EBI-77613, EBI-81711;
P05067; O35431: Apba2; Xeno; NbExp=5; IntAct=EBI-77613, EBI-2028211;
P05067; O00213: APBB1; NbExp=7; IntAct=EBI-77613, EBI-81694;
P05067-4; O00213: APBB1; NbExp=5; IntAct=EBI-302641, EBI-81694;
P05067; Q92870: APBB2; NbExp=3; IntAct=EBI-77613, EBI-79277;
P05067-4; P51693: APLP1; NbExp=2; IntAct=EBI-302641, EBI-74648;
P05067-4; Q06481: APLP2; NbExp=2; IntAct=EBI-302641, EBI-79306;
P05067; P02647: APOA1; NbExp=5; IntAct=EBI-77613, EBI-701692;
PRO_0000000093; P02649: APOE; NbExp=4; IntAct=EBI-2431589, EBI-1222467;
PRO_0000000092; P48047: ATP5PO; NbExp=2; IntAct=EBI-821758, EBI-355815;
P05067; P56817: BACE1; NbExp=8; IntAct=EBI-77613, EBI-2433139;
P05067-4; Q13867: BLMH; NbExp=2; IntAct=EBI-302641, EBI-718504;
P05067; P35613: BSG; NbExp=2; IntAct=EBI-77613, EBI-750709;
P05067; P15253: CALR; Xeno; NbExp=3; IntAct=EBI-77613, EBI-9005200;
PRO_0000000092; P15253: CALR; Xeno; NbExp=2; IntAct=EBI-821758, EBI-9005200;
PRO_0000000093; P15253: CALR; Xeno; NbExp=2; IntAct=EBI-2431589, EBI-9005200;
P05067; P27797: CALR; NbExp=2; IntAct=EBI-77613, EBI-1049597;
PRO_0000000091; Q8K3H7: CALR; Xeno; NbExp=2; IntAct=EBI-3894543, EBI-9005068;
PRO_0000000092; P36544: CHRNA7; NbExp=7; IntAct=EBI-821758, EBI-79333;
PRO_0000000092; Q05941: Chrna7; Xeno; NbExp=3; IntAct=EBI-821758, EBI-79422;
PRO_0000000093; P10909: CLU; NbExp=4; IntAct=EBI-2431589, EBI-1104674;
PRO_0000000092; P10909-5: CLU; NbExp=2; IntAct=EBI-821758, EBI-10961636;
PRO_0000000092; PRO_0000005794 [P39060]: COL18A1; NbExp=2; IntAct=EBI-821758, EBI-2566375;
PRO_0000000092; PRO_0000033156 [O00230]: CORT; NbExp=4; IntAct=EBI-821758, EBI-20824092;
P05067; P07339: CTSD; NbExp=2; IntAct=EBI-77613, EBI-2115097;
P05067; O75955: FLOT1; NbExp=5; IntAct=EBI-77613, EBI-603643;
P05067-4; Q9NZU0: FLRT3; NbExp=3; IntAct=EBI-302641, EBI-1057092;
P05067; P01100: FOS; NbExp=3; IntAct=EBI-77613, EBI-852851;
P05067-8; P17677: GAP43; NbExp=3; IntAct=EBI-302661, EBI-1267511;
P05067-4; P46089: GPR3; NbExp=2; IntAct=EBI-302641, EBI-3909653;
P05067; A4D1B5: GSAP; NbExp=3; IntAct=EBI-77613, EBI-15875313;
PRO_0000000093; P49840: GSK3A; NbExp=3; IntAct=EBI-2431589, EBI-1044067;
PRO_0000000093; P49841: GSK3B; NbExp=2; IntAct=EBI-2431589, EBI-373586;
P05067-8; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-302661, EBI-748420;
P05067; Q99714: HSD17B10; NbExp=4; IntAct=EBI-77613, EBI-79964;
PRO_0000000093; P14735-1: IDE; NbExp=3; IntAct=EBI-2431589, EBI-15607031;
P05067-4; O43736: ITM2A; NbExp=3; IntAct=EBI-302641, EBI-2431769;
P05067-8; Q9Y287: ITM2B; NbExp=4; IntAct=EBI-302661, EBI-2866431;
P05067; P05412: JUN; NbExp=2; IntAct=EBI-77613, EBI-852823;
P05067-4; Q68DU8: KCTD16; NbExp=3; IntAct=EBI-302641, EBI-20768174;
PRO_0000000092; Q8N423: LILRB2; NbExp=7; IntAct=EBI-821758, EBI-2816428;
PRO_0000000092; P97484: Lilrb3; Xeno; NbExp=8; IntAct=EBI-821758, EBI-15728641;
P05067-4; Q96FE5: LINGO1; NbExp=2; IntAct=EBI-302641, EBI-719955;
P05067; P42704: LRPPRC; NbExp=8; IntAct=EBI-77613, EBI-1050853;
P05067; Q99683: MAP3K5; NbExp=2; IntAct=EBI-77613, EBI-476263;
P05067; P10636: MAPT; NbExp=5; IntAct=EBI-77613, EBI-366182;
PRO_0000000092; P10636: MAPT; NbExp=5; IntAct=EBI-821758, EBI-366182;
P05067; Q93074: MED12; NbExp=2; IntAct=EBI-77613, EBI-394357;
PRO_0000000092; P08253: MMP2; NbExp=4; IntAct=EBI-821758, EBI-1033518;
PRO_0000000093; P08253: MMP2; NbExp=2; IntAct=EBI-2431589, EBI-1033518;
PRO_0000000092; Q9NZV6: MSRB1; NbExp=4; IntAct=EBI-821758, EBI-12330065;
PRO_0000000092; P03897: MT-ND3; NbExp=2; IntAct=EBI-821758, EBI-1246249;
PRO_0000000092; Q8IVG9: MT-RNR2; NbExp=4; IntAct=EBI-821758, EBI-8643752;
P05067-2; P15941-11: MUC1; NbExp=3; IntAct=EBI-17264467, EBI-17263240;
P05067; P07196: NEFL; NbExp=2; IntAct=EBI-77613, EBI-475646;
P05067; P21359: NF1; NbExp=3; IntAct=EBI-77613, EBI-1172917;
P05067; P08138: NGFR; NbExp=2; IntAct=EBI-77613, EBI-1387782;
PRO_0000000093; P08138: NGFR; NbExp=2; IntAct=EBI-2431589, EBI-1387782;
PRO_0000000093; P07174: Ngfr; Xeno; NbExp=2; IntAct=EBI-2431589, EBI-1038810;
PRO_0000000089; O95631: NTN1; NbExp=3; IntAct=EBI-20829246, EBI-2678626;
PRO_0000000092; O95631: NTN1; NbExp=6; IntAct=EBI-821758, EBI-2678626;
P05067-4; P04629: NTRK1; NbExp=7; IntAct=EBI-302641, EBI-1028226;
P05067; P61457: PCBD1; NbExp=2; IntAct=EBI-77613, EBI-740475;
PRO_0000000092; Q15113: PCOLCE; NbExp=4; IntAct=EBI-821758, EBI-8869614;
P05067; P30101: PDIA3; NbExp=3; IntAct=EBI-77613, EBI-979862;
P05067-4; Q13526: PIN1; NbExp=2; IntAct=EBI-302641, EBI-714158;
PRO_0000000093; Q5JRX3-1: PITRM1; NbExp=3; IntAct=EBI-2431589, EBI-16109799;
P05067-4; P60201: PLP1; NbExp=5; IntAct=EBI-302641, EBI-8653150;
PRO_0000000092; Q08752: PPID; NbExp=4; IntAct=EBI-821758, EBI-716596;
PRO_0000000093; Q08752: PPID; NbExp=2; IntAct=EBI-2431589, EBI-716596;
P05067; P04156: PRNP; NbExp=3; IntAct=EBI-77613, EBI-977302;
P05067-4; P04156: PRNP; NbExp=2; IntAct=EBI-302641, EBI-977302;
PRO_0000000092; P04156: PRNP; NbExp=3; IntAct=EBI-821758, EBI-977302;
P05067; P49768: PSEN1; NbExp=6; IntAct=EBI-77613, EBI-297277;
P05067-4; P49768: PSEN1; NbExp=4; IntAct=EBI-302641, EBI-297277;
PRO_0000000092; P11686-1: SFTPC; NbExp=4; IntAct=EBI-821758, EBI-16143688;
P05067; P29353: SHC1; NbExp=5; IntAct=EBI-77613, EBI-78835;
P05067; Q92529: SHC3; NbExp=2; IntAct=EBI-77613, EBI-79084;
P05067; Q9NP59: SLC40A1; NbExp=5; IntAct=EBI-77613, EBI-725153;
P05067; Q8BGY9: Slc5a7; Xeno; NbExp=2; IntAct=EBI-77613, EBI-2010752;
P05067-4; Q92673: SORL1; NbExp=8; IntAct=EBI-302641, EBI-1171329;
PRO_0000000091; Q92673: SORL1; NbExp=4; IntAct=EBI-3894543, EBI-1171329;
PRO_0000000093; Q92673: SORL1; NbExp=3; IntAct=EBI-2431589, EBI-1171329;
P05067-4; PRO_0000033163 [Q99523]: SORT1; NbExp=4; IntAct=EBI-302641, EBI-21467118;
P05067-4; Q9HCB6: SPON1; NbExp=3; IntAct=EBI-302641, EBI-2431846;
PRO_0000000092; PRO_0000033088 [P61278]: SST; NbExp=4; IntAct=EBI-821758, EBI-20824010;
P05067-4; O95793: STAU1; NbExp=2; IntAct=EBI-302641, EBI-358174;
P05067; P01137: TGFB1; NbExp=3; IntAct=EBI-77613, EBI-779636;
P05067; P61812: TGFB2; NbExp=7; IntAct=EBI-77613, EBI-779581;
PRO_0000000092; P21980: TGM2; NbExp=2; IntAct=EBI-821758, EBI-727668;
PRO_0000000092; O95411: TIAF1; NbExp=3; IntAct=EBI-821758, EBI-302378;
PRO_0000000092; O60602: TLR5; NbExp=3; IntAct=EBI-821758, EBI-3505951;
PRO_0000000093; O60602: TLR5; NbExp=3; IntAct=EBI-2431589, EBI-3505951;
PRO_0000000090; Q9UIK5: TMEFF2; NbExp=3; IntAct=EBI-21194918, EBI-11423693;
P05067-4; Q8VEK0: Tmem30a; Xeno; NbExp=6; IntAct=EBI-302641, EBI-8381028;
PRO_0000000091; Q8VEK0: Tmem30a; Xeno; NbExp=3; IntAct=EBI-3894543, EBI-8381028;
P05067; Q13625: TP53BP2; NbExp=3; IntAct=EBI-77613, EBI-77642;
PRO_0000000092; Q9NZC2: TREM2; NbExp=4; IntAct=EBI-821758, EBI-14036387;
PRO_0000000092; Q99NH8: Trem2; Xeno; NbExp=2; IntAct=EBI-821758, EBI-15982016;
PRO_0000000092; P02766: TTR; NbExp=2; IntAct=EBI-821758, EBI-711909;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:20580937, ECO:0000269|PubMed:2649245,
ECO:0000305|PubMed:25122912}; Single-pass type I membrane protein
{ECO:0000269|PubMed:30630874, ECO:0000305|PubMed:10383380,
ECO:0000305|PubMed:25122912}. Membrane {ECO:0000269|PubMed:2900137,
ECO:0000305|PubMed:22584060}; Single-pass type I membrane protein
{ECO:0000269|PubMed:2900137, ECO:0000269|PubMed:30630874,
ECO:0000305|PubMed:22584060}. Perikaryon {ECO:0000269|PubMed:10341243}.
Cell projection, growth cone {ECO:0000269|PubMed:10341243}. Membrane,
clathrin-coated pit {ECO:0000269|PubMed:20580937}. Early endosome
{ECO:0000269|PubMed:20580937}. Cytoplasmic vesicle
{ECO:0000269|PubMed:20580937, ECO:0000269|PubMed:25122912}. Note=Cell
surface protein that rapidly becomes internalized via clathrin-coated
pits. Only a minor proportion is present at the cell membrane; most of
the protein is present in intracellular vesicles (PubMed:20580937).
During maturation, the immature APP (N-glycosylated in the endoplasmic
reticulum) moves to the Golgi complex where complete maturation occurs
(O-glycosylated and sulfated). After alpha-secretase cleavage, soluble
APP is released into the extracellular space and the C-terminal is
internalized to endosomes and lysosomes. Some APP accumulates in
secretory transport vesicles leaving the late Golgi compartment and
returns to the cell surface. APP sorts to the basolateral surface in
epithelial cells. During neuronal differentiation, the Thr-743
phosphorylated form is located mainly in growth cones, moderately in
neurites and sparingly in the cell body (PubMed:10341243). Casein
kinase phosphorylation can occur either at the cell surface or within a
post-Golgi compartment. Associates with GPC1 in perinuclear
compartments. Colocalizes with SORL1 in a vesicular pattern in
cytoplasm and perinuclear regions. {ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:20580937}.
-!- SUBCELLULAR LOCATION: [Soluble APP-beta]: Secreted
{ECO:0000269|PubMed:10656250, ECO:0000269|PubMed:2649245}.
-!- SUBCELLULAR LOCATION: [Amyloid-beta protein 42]: Cell surface.
Note=Associates with FPR2 at the cell surface and the complex is then
rapidly internalized. {ECO:0000269|PubMed:11689470}.
-!- SUBCELLULAR LOCATION: [Gamma-secretase C-terminal fragment 59]: Nucleus
{ECO:0000269|PubMed:11544248}. Cytoplasm {ECO:0000269|PubMed:11544248}.
Note=Located to both the cytoplasm and nuclei of neurons. It can be
translocated to the nucleus through association with APBB1 (Fe65)
(PubMed:11544248). In dopaminergic neurons, the phosphorylated Thr-743
form is localized to the nucleus (By similarity).
{ECO:0000250|UniProtKB:P12023, ECO:0000269|PubMed:11544248}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist. Experimental confirmation
may be lacking for some isoforms.;
Name=APP770; Synonyms=PreA4 770;
IsoId=P05067-1; Sequence=Displayed;
Name=APP305;
IsoId=P05067-2; Sequence=VSP_000005, VSP_000006;
Name=L-APP677;
IsoId=P05067-3; Sequence=VSP_000002, VSP_000004, VSP_000009;
Name=APP695; Synonyms=PreA4 695;
IsoId=P05067-4; Sequence=VSP_000002, VSP_000004;
Name=L-APP696;
IsoId=P05067-5; Sequence=VSP_000002, VSP_000003, VSP_000009;
Name=APP714;
IsoId=P05067-6; Sequence=VSP_000002, VSP_000003;
Name=L-APP733;
IsoId=P05067-7; Sequence=VSP_000007, VSP_000008, VSP_000009;
Name=APP751; Synonyms=PreA4 751;
IsoId=P05067-8; Sequence=VSP_000007, VSP_000008;
Name=L-APP752;
IsoId=P05067-9; Sequence=VSP_000009;
Name=APP639;
IsoId=P05067-10; Sequence=VSP_009116, VSP_009117, VSP_009118;
Name=11;
IsoId=P05067-11; Sequence=VSP_045446, VSP_045447;
-!- TISSUE SPECIFICITY: Expressed in the brain and in cerebrospinal fluid
(at protein level) (PubMed:2649245). Expressed in all fetal tissues
examined with highest levels in brain, kidney, heart and spleen. Weak
expression in liver. In adult brain, highest expression found in the
frontal lobe of the cortex and in the anterior perisylvian cortex-
opercular gyri. Moderate expression in the cerebellar cortex, the
posterior perisylvian cortex-opercular gyri and the temporal associated
cortex. Weak expression found in the striate, extra-striate and motor
cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695
is the predominant form in neuronal tissue, isoform APP751 and isoform
APP770 are widely expressed in non-neuronal cells. Isoform APP751 is
the most abundant form in T-lymphocytes. Appican is expressed in
astrocytes. {ECO:0000269|PubMed:12859342, ECO:0000269|PubMed:1406936,
ECO:0000269|PubMed:2649245}.
-!- INDUCTION: Increased levels during neuronal differentiation.
-!- DOMAIN: The transmembrane helix undergoes a conformation change and
unravels partially when bound to PSEN1, facilitating cleavage by PSEN1.
{ECO:0000269|PubMed:30630874}.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for sorting
of membrane proteins to the basolateral surface of epithelial cells.
{ECO:0000269|PubMed:9843960}.
-!- DOMAIN: The GFLD subdomain binds Cu(2+) ions; this promotes
homodimerization. {ECO:0000269|PubMed:25122912}.
-!- DOMAIN: The NPXY sequence motif found in many tyrosine-phosphorylated
proteins is required for the specific binding of the PID domain.
However, additional amino acids either N- or C-terminal to the NPXY
motif are often required for complete interaction. The PID domain-
containing proteins which bind APP require the YENPTY motif for full
interaction. These interactions are independent of phosphorylation on
the terminal tyrosine residue. The YENPXY site is also involved in
clathrin-mediated endocytosis. {ECO:0000269|PubMed:10383380}.
-!- DOMAIN: The C-terminal region can bind zinc ions; this favors
dimerization and formation of higher oligomers.
{ECO:0000269|PubMed:26898943, ECO:0000269|PubMed:28570778}.
-!- DOMAIN: The OX-2 motif shows some similarity to a region in the N-
terminus of CD200/MOX2. {ECO:0000269|PubMed:2649245}.
-!- PTM: Proteolytically processed under normal cellular conditions.
Cleavage either by alpha-secretase, beta-secretase or theta-secretase
leads to generation and extracellular release of soluble APP peptides,
S-APP-alpha and S-APP-beta, and the retention of corresponding
membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent
processing of C80 and C83 by gamma-secretase yields P3 peptides. This
is the major secretory pathway and is non-amyloidogenic. Alternatively,
presenilin/nicastrin-mediated gamma-secretase processing of C99
releases the amyloid-beta proteins, amyloid-beta protein 40 and
amyloid-beta protein 42, major components of amyloid plaques, and the
cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-
CTF(59). PSEN1 cleavage is more efficient with C83 than with C99 as
substrate (in vitro) (PubMed:30630874). Many other minor amyloid-beta
peptides, amyloid-beta 1-X peptides, are found in cerebral spinal fluid
(CSF) including the amyloid-beta X-15 peptides, produced from the
cleavage by alpha-secretase and all terminating at Gln-686.
{ECO:0000269|PubMed:10656250, ECO:0000269|PubMed:30630874}.
-!- PTM: Proteolytically cleaved by caspases during neuronal apoptosis.
Cleavage at Asp-739 by either CASP6, CASP8 or CASP9 results in the
production of the neurotoxic C31 peptide and the increased production
of amyloid-beta peptides. {ECO:0000269|PubMed:10319819}.
-!- PTM: N-glycosylated (PubMed:2900137). N- and O-glycosylated
(PubMed:2649245). O-glycosylation on Ser and Thr residues with core 1
or possibly core 8 glycans. Partial tyrosine glycosylation (Tyr-681) is
found on some minor, short amyloid-beta peptides (amyloid-beta 1-15, 1-
16, 1-17, 1-18, 1-19 and 1-20) but not found on amyloid-beta protein
38, amyloid-beta protein 40 nor on amyloid-beta protein 42.
Modification on a tyrosine is unusual and is more prevelant in AD
patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr,
Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O-
AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O-
acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac 2,8Neu5Ac
linked. O-glycosylations in the vicinity of the cleavage sites may
influence the proteolytic processing. Appicans are L-APP isoforms with
O-linked chondroitin sulfate. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:21712440, ECO:0000269|PubMed:22576872,
ECO:0000269|PubMed:2649245, ECO:0000269|PubMed:2900137}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific (PubMed:10341243). Phosphorylation
can affect APP processing, neuronal differentiation and interaction
with other proteins (PubMed:10341243). Phosphorylated on Thr-743 in
neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2
kinase in a cell-cycle dependent manner with maximal levels at the G2/M
phase and, in vitro, by GSK-3-beta (PubMed:8131745, PubMed:11146006).
The Thr-743 phosphorylated form causes a conformational change which
reduces binding of Fe65 family members (PubMed:11517218). In
dopaminergic (DA) neurons, phosphorylation on Thr-743 by LRKK2 promotes
the production and the nuclear translocation of the APP intracellular
domain (AICD) which induces DA neuron apoptosis (PubMed:28720718).
Phosphorylation on Tyr-757 is required for SHC binding
(PubMed:11877420). Phosphorylated in the extracellular domain by casein
kinases on both soluble and membrane-bound APP. This phosphorylation is
inhibited by heparin (PubMed:8999878). {ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006, ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420, ECO:0000269|PubMed:28720718,
ECO:0000269|PubMed:8131745, ECO:0000269|PubMed:8999878}.
-!- PTM: Extracellular binding and reduction of copper, results in a
corresponding oxidation of Cys-144 and Cys-158, and the formation of a
disulfide bond. In vitro, the APP-Cu(+) complex in the presence of
hydrogen peroxide results in an increased production of amyloid-beta-
containing peptides.
-!- PTM: Trophic-factor deprivation triggers the cleavage of surface APP by
beta-secretase to release sAPP-beta which is further cleaved to release
an N-terminal fragment of APP (N-APP).
-!- PTM: Amyloid-beta peptides are degraded by IDE.
{ECO:0000250|UniProtKB:P12023}.
-!- PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:2649245}.
-!- MASS SPECTROMETRY: [Gamma-secretase C-terminal fragment 59]:
Mass=6461.6; Method=MALDI; Evidence={ECO:0000269|PubMed:12214090};
-!- MASS SPECTROMETRY: [Gamma-secretase C-terminal fragment 57]:
Mass=6451.6; Method=MALDI; Evidence={ECO:0000269|PubMed:12214090};
-!- DISEASE: Alzheimer disease 1 (AD1) [MIM:104300]: A familial early-onset
form of Alzheimer disease. It can be associated with cerebral amyloid
angiopathy. Alzheimer disease is a neurodegenerative disorder
characterized by progressive dementia, loss of cognitive abilities, and
deposition of fibrillar amyloid proteins as intraneuronal
neurofibrillary tangles, extracellular amyloid plaques and vascular
amyloid deposits. The major constituents of these plaques are
neurotoxic amyloid-beta protein 40 and amyloid-beta protein 42, that
are produced by the proteolysis of the transmembrane APP protein. The
cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products,
such as C31, are also implicated in neuronal death.
{ECO:0000269|PubMed:10097173, ECO:0000269|PubMed:10631141,
ECO:0000269|PubMed:10656250, ECO:0000269|PubMed:10665499,
ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:10867787,
ECO:0000269|PubMed:11063718, ECO:0000269|PubMed:11311152,
ECO:0000269|PubMed:11528419, ECO:0000269|PubMed:12034808,
ECO:0000269|PubMed:1302033, ECO:0000269|PubMed:1303239,
ECO:0000269|PubMed:1303275, ECO:0000269|PubMed:1415269,
ECO:0000269|PubMed:1465129, ECO:0000269|PubMed:15201367,
ECO:0000269|PubMed:15365148, ECO:0000269|PubMed:15668448,
ECO:0000269|PubMed:1671712, ECO:0000269|PubMed:1678058,
ECO:0000269|PubMed:1908231, ECO:0000269|PubMed:1925564,
ECO:0000269|PubMed:1944558, ECO:0000269|PubMed:8267572,
ECO:0000269|PubMed:8290042, ECO:0000269|PubMed:8476439,
ECO:0000269|PubMed:8577393, ECO:0000269|PubMed:8886002,
ECO:0000269|PubMed:9328472, ECO:0000269|PubMed:9754958}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Cerebral amyloid angiopathy, APP-related (CAA-APP)
[MIM:605714]: A hereditary localized amyloidosis due to amyloid-beta A4
peptide(s) deposition in the cerebral vessels. The principal clinical
characteristics are recurrent cerebral and cerebellar hemorrhages,
recurrent strokes, cerebral ischemia, cerebral infarction, and
progressive mental deterioration. Patients develop cerebral hemorrhage
because of the severe cerebral amyloid angiopathy. Parenchymal amyloid
deposits are rare and largely in the form of pre-amyloid lesions or
diffuse plaque-like structures. They are Congo red negative and lack
the dense amyloid cores commonly present in Alzheimer disease. Some
affected individuals manifest progressive aphasic dementia,
leukoencephalopathy, and occipital calcifications.
{ECO:0000269|PubMed:11409420, ECO:0000269|PubMed:12654973,
ECO:0000269|PubMed:16178030, ECO:0000269|PubMed:20697050,
ECO:0000269|PubMed:2111584}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and zinc,
can induce histidine-bridging between amyloid-beta molecules resulting
in amyloid-beta-metal aggregates. The affinity for copper is much
higher than for other transient metals and is increased under acidic
conditions. Extracellular zinc-binding increases binding of heparin to
APP and inhibits collagen-binding. {ECO:0000269|PubMed:26898943,
ECO:0000269|PubMed:28570778}.
-!- MISCELLANEOUS: [Isoform APP770]: A major isoform.
-!- MISCELLANEOUS: [Isoform L-APP677]: The L-isoforms are referred to as
appicans. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform APP695]: A major isoform. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform L-APP696]: The L-isoforms are referred to as
appicans. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform L-APP733]: The L-isoforms are referred to as
appicans. {ECO:0000305}.
-!- MISCELLANEOUS: [Isoform APP751]: A major isoform. {ECO:0000305}.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
ProRule:PRU01217}.
-!- SEQUENCE CAUTION:
Sequence=AAA58727.1; Type=Miscellaneous discrepancy; Note=Contamination by an Alu repeat.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Alzforum; Note=APP mutations;
URL="https://www.alzforum.org/mutations/search?genes%255B%255D=348";
-!- WEB RESOURCE: Name=AD mutations;
URL="https://uantwerpen.vib.be/CMTMutations";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/app/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Amyloid beta entry;
URL="https://en.wikipedia.org/wiki/Amyloid_beta";
---------------------------------------------------------------------------
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EMBL; Y00264; CAA68374.1; -; mRNA.
EMBL; X13466; CAA31830.1; -; Genomic_DNA.
EMBL; X13467; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13468; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13469; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13470; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13471; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13472; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13473; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13474; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13475; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13476; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13477; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13478; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13479; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13487; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X13488; CAA31830.1; JOINED; Genomic_DNA.
EMBL; X06989; CAA30050.1; -; mRNA.
EMBL; M33112; AAB59502.1; -; Genomic_DNA.
EMBL; M34862; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34863; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34864; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34865; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34866; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34867; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34868; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34869; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34870; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34871; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34872; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34873; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34874; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34876; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34877; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34878; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34879; AAB59502.1; JOINED; Genomic_DNA.
EMBL; M34875; AAB59501.1; ALT_TERM; Genomic_DNA.
EMBL; M34862; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34863; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34864; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34865; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34866; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34867; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34868; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34869; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34870; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34871; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34872; AAB59501.1; JOINED; Genomic_DNA.
EMBL; M34873; AAB59501.1; JOINED; Genomic_DNA.
EMBL; D87675; BAA22264.1; -; Genomic_DNA.
EMBL; AK312326; BAG35248.1; -; mRNA.
EMBL; AK295621; BAG58500.1; -; mRNA.
EMBL; AY919674; AAW82435.1; -; Genomic_DNA.
EMBL; AP001439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09958.1; -; Genomic_DNA.
EMBL; CH471079; EAX09959.1; -; Genomic_DNA.
EMBL; CH471079; EAX09960.1; -; Genomic_DNA.
EMBL; CH471079; EAX09961.1; -; Genomic_DNA.
EMBL; CH471079; EAX09963.1; -; Genomic_DNA.
EMBL; CH471079; EAX09965.1; -; Genomic_DNA.
EMBL; BC004369; AAH04369.1; -; mRNA.
EMBL; BC065529; AAH65529.1; -; mRNA.
EMBL; M35675; AAA60163.1; ALT_SEQ; mRNA.
EMBL; M24547; AAC13654.1; -; Genomic_DNA.
EMBL; M24546; AAC13654.1; JOINED; Genomic_DNA.
EMBL; M28373; AAA58727.1; ALT_SEQ; mRNA.
EMBL; X06982; CAA30042.1; -; mRNA.
EMBL; X06981; CAA30041.1; -; mRNA.
EMBL; M18734; AAA51726.1; -; mRNA.
EMBL; M29270; AAA51768.1; -; Genomic_DNA.
EMBL; M29269; AAA51768.1; JOINED; Genomic_DNA.
EMBL; AB066441; BAB71958.2; -; mRNA.
EMBL; M15533; AAA35540.1; -; mRNA.
EMBL; M15532; AAA51564.1; -; mRNA.
EMBL; M37896; AAA51727.1; -; Genomic_DNA.
EMBL; M37895; AAA51727.1; JOINED; Genomic_DNA.
EMBL; S45136; AAB23646.1; -; Genomic_DNA.
EMBL; S60317; AAC60601.2; -; Genomic_DNA.
EMBL; AF282245; AAQ14327.1; -; mRNA.
EMBL; S60721; AAB26263.2; -; mRNA.
EMBL; S61380; AAB26264.2; -; mRNA.
EMBL; S61383; AAB26265.2; -; mRNA.
EMBL; M16765; AAA51722.1; -; mRNA.
CCDS; CCDS13576.1; -. [P05067-1]
CCDS; CCDS13577.1; -. [P05067-4]
CCDS; CCDS33523.1; -. [P05067-8]
CCDS; CCDS46638.1; -. [P05067-10]
CCDS; CCDS56212.1; -. [P05067-11]
CCDS; CCDS56213.1; -. [P05067-9]
PIR; S01442; S01442.
PIR; S02260; QRHUA4.
RefSeq; NP_000475.1; NM_000484.3. [P05067-1]
RefSeq; NP_001129488.1; NM_001136016.3. [P05067-11]
RefSeq; NP_001129601.1; NM_001136129.2. [P05067-10]
RefSeq; NP_001129602.1; NM_001136130.2.
RefSeq; NP_001129603.1; NM_001136131.2.
RefSeq; NP_001191230.1; NM_001204301.1. [P05067-9]
RefSeq; NP_001191231.1; NM_001204302.1. [P05067-7]
RefSeq; NP_001191232.1; NM_001204303.1. [P05067-3]
RefSeq; NP_958816.1; NM_201413.2. [P05067-8]
RefSeq; NP_958817.1; NM_201414.2. [P05067-4]
PDB; 1AAP; X-ray; 1.50 A; A/B=287-344.
PDB; 1AMB; NMR; -; A=672-699.
PDB; 1AMC; NMR; -; A=672-699.
PDB; 1AML; NMR; -; A=672-711.
PDB; 1BA4; NMR; -; A=672-711.
PDB; 1BA6; NMR; -; A=672-711.
PDB; 1BJB; NMR; -; A=672-699.
PDB; 1BJC; NMR; -; A=672-699.
PDB; 1BRC; X-ray; 2.50 A; I=287-342.
PDB; 1CA0; X-ray; 2.10 A; D/I=289-342.
PDB; 1HZ3; NMR; -; A=681-706.
PDB; 1IYT; NMR; -; A=672-713.
PDB; 1MWP; X-ray; 1.80 A; A=28-123.
PDB; 1OWT; NMR; -; A=124-189.
PDB; 1QCM; NMR; -; A=696-706.
PDB; 1QWP; NMR; -; A=696-706.
PDB; 1QXC; NMR; -; A=696-706.
PDB; 1QYT; NMR; -; A=696-706.
PDB; 1TAW; X-ray; 1.80 A; B=287-344.
PDB; 1TKN; NMR; -; A=460-569.
PDB; 1UO7; Model; -; A=672-713.
PDB; 1UO8; Model; -; A=672-713.
PDB; 1UOA; Model; -; A=672-713.
PDB; 1UOI; Model; -; A=672-713.
PDB; 1X11; X-ray; 2.50 A; C/D=754-766.
PDB; 1Z0Q; NMR; -; A=672-713.
PDB; 1ZE7; NMR; -; A=672-687.
PDB; 1ZE9; NMR; -; A=672-687.
PDB; 1ZJD; X-ray; 2.60 A; B=289-344.
PDB; 2BEG; NMR; -; A/B/C/D/E=672-713.
PDB; 2BOM; Model; -; A/B=681-713.
PDB; 2BP4; NMR; -; A=672-687.
PDB; 2FJZ; X-ray; 1.61 A; A=133-189.
PDB; 2FK1; X-ray; 1.60 A; A=133-189.
PDB; 2FK2; X-ray; 1.65 A; A=133-189.
PDB; 2FK3; X-ray; 2.40 A; A/B/C/D/E/F/G/H=133-189.
PDB; 2FKL; X-ray; 2.50 A; A/B=124-189.
PDB; 2FMA; X-ray; 0.85 A; A=133-189.
PDB; 2G47; X-ray; 2.10 A; C/D=672-711.
PDB; 2IPU; X-ray; 1.65 A; P/Q=672-679.
PDB; 2LFM; NMR; -; A=672-711.
PDB; 2LLM; NMR; -; A=686-726.
PDB; 2LMN; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=672-711.
PDB; 2LMO; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=672-711.
PDB; 2LMP; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=672-711.
PDB; 2LMQ; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=672-711.
PDB; 2LNQ; NMR; -; A/B/C/D/E/F/G/H=672-711.
PDB; 2LOH; NMR; -; A/B=686-726.
PDB; 2LP1; NMR; -; A=671-770.
PDB; 2LZ3; NMR; -; A/B=699-726.
PDB; 2LZ4; NMR; -; A/B=699-726.
PDB; 2M4J; NMR; -; A/B/C/D/E/F/G/H/I=672-711.
PDB; 2M9R; NMR; -; A=672-711.
PDB; 2M9S; NMR; -; A=672-711.
PDB; 2MGT; NMR; -; A/B=672-687.
PDB; 2MJ1; NMR; -; A=688-705.
PDB; 2MPZ; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a=686-711.
PDB; 2MVX; NMR; -; A/B/C/D/E/F/G/H/I/J=672-711.
PDB; 2MXU; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=672-713.
PDB; 2NAO; NMR; -; A/B/C/D/E/F=672-713.
PDB; 2OTK; NMR; -; C=672-711.
PDB; 2R0W; X-ray; 2.50 A; Q=672-679.
PDB; 2WK3; X-ray; 2.59 A; C/D=672-713.
PDB; 2Y29; X-ray; 2.30 A; A=687-692.
PDB; 2Y2A; X-ray; 1.91 A; A=687-692.
PDB; 2Y3J; X-ray; 1.99 A; A/B/C/D/E/F/G/H=701-706.
PDB; 2Y3K; X-ray; 1.90 A; A/B/C/D/E/F/G/H=706-713.
PDB; 2Y3L; X-ray; 2.10 A; A/B/C/G=706-713.
PDB; 3AYU; X-ray; 2.00 A; B=586-595.
PDB; 3BAE; X-ray; 1.59 A; A=672-699.
PDB; 3BKJ; X-ray; 1.59 A; A=672-687.
PDB; 3DXC; X-ray; 2.10 A; B/D=739-770.
PDB; 3DXD; X-ray; 2.20 A; B/D=739-770.
PDB; 3DXE; X-ray; 2.00 A; B/D=739-770.
PDB; 3GCI; X-ray; 2.04 A; P=707-713.
PDB; 3IFL; X-ray; 1.50 A; P=672-678.
PDB; 3IFN; X-ray; 1.50 A; P=672-711.
PDB; 3IFO; X-ray; 2.15 A; P/Q=672-678.
PDB; 3IFP; X-ray; 2.95 A; P/Q/R/S=672-678.
PDB; 3JQ5; X-ray; 2.03 A; B=672-679.
PDB; 3JQL; X-ray; 1.20 A; B=687-692.
PDB; 3JTI; X-ray; 1.80 A; B=699-706.
PDB; 3KTM; X-ray; 2.70 A; A/B/C/D/E/F/G/H=18-190.
PDB; 3L33; X-ray; 2.48 A; E/F/G/H=290-341.
PDB; 3L81; X-ray; 1.60 A; B=761-767.
PDB; 3MOQ; X-ray; 2.05 A; A/B/C/D=689-712.
PDB; 3MXC; X-ray; 2.00 A; L=754-762.
PDB; 3MXY; X-ray; 2.30 A; L=754-762.
PDB; 3NYJ; X-ray; 3.20 A; A=365-567.
PDB; 3NYL; X-ray; 2.80 A; A=365-570.
PDB; 3OVJ; X-ray; 1.80 A; A/B/C/D=687-692.
PDB; 3OW9; X-ray; 1.80 A; A/B=687-692.
PDB; 3PZZ; X-ray; 1.29 A; A/B=700-705.
PDB; 3Q2X; X-ray; 1.45 A; A=698-703.
PDB; 3SV1; X-ray; 3.30 A; D/E/F=754-767.
PDB; 3U0T; X-ray; 2.50 A; E/F=701-711.
PDB; 3UMH; X-ray; 2.00 A; A=370-575.
PDB; 3UMI; X-ray; 2.40 A; A=370-575.
PDB; 3UMK; X-ray; 2.60 A; A=370-575.
PDB; 4HIX; X-ray; 2.20 A; A=672-699.
PDB; 4JFN; X-ray; 1.75 A; A=23-185.
PDB; 4M1C; X-ray; 3.50 A; G/H=672-711.
PDB; 4MDR; X-ray; 1.85 A; B=758-767.
PDB; 4MVI; X-ray; 1.70 A; B=672-711.
PDB; 4MVK; X-ray; 1.50 A; B=689-694.
PDB; 4MVL; X-ray; 2.30 A; E/F/G/H=672-711.
PDB; 4NGE; X-ray; 2.70 A; B/E=672-711.
PDB; 4OJF; X-ray; 2.00 A; A=672-679.
PDB; 4ONF; X-ray; 2.00 A; P=672-678.
PDB; 4ONG; X-ray; 2.20 A; P=672-711.
PDB; 4PQD; X-ray; 1.33 A; A=22-126.
PDB; 4PWQ; X-ray; 1.40 A; A/B=18-190.
PDB; 4XXD; X-ray; 2.41 A; C/F=683-699.
PDB; 5AEF; EM; 5.00 A; A/B=686-713.
PDB; 5AM8; X-ray; 1.90 A; P/Q/R/S=675-681.
PDB; 5AMB; X-ray; 1.55 A; P/Q=706-713.
PDB; 5BUO; X-ray; 2.31 A; A/B=370-710.
PDB; 5C67; X-ray; 1.83 A; C/E=294-344.
PDB; 5CSZ; X-ray; 1.80 A; D/E=672-682.
PDB; 5HOW; X-ray; 2.29 A; A/B/C/D/E/F=688-705.
PDB; 5HOX; X-ray; 1.90 A; A/B/C/D/E/F=688-707.
PDB; 5HOY; X-ray; 2.29 A; A/B/C/D/E/F=688-707.
PDB; 5KK3; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=672-713.
PDB; 5LFY; NMR; -; A/B=672-681.
PDB; 5LV0; X-ray; 2.70 A; C/D=706-711.
PDB; 5MY4; X-ray; 2.21 A; C=674-683.
PDB; 5MYO; X-ray; 1.59 A; E=674-683.
PDB; 5MYX; X-ray; 1.49 A; E/F=674-689.
PDB; 5ONP; X-ray; 1.34 A; B=700-704.
PDB; 5ONQ; X-ray; 1.17 A; B=700-704.
PDB; 5OQV; EM; 4.00 A; A/B/C/D/E/F/G/H/I=672-713.
PDB; 5TXD; X-ray; 1.45 A; Z=698-703.
PDB; 5VOS; EM; 1.42 A; A=695-705.
PDB; 5VZY; X-ray; 2.32 A; A=682-696.
PDB; 5W3P; X-ray; 1.92 A; P=672-687.
PDB; 6CO3; X-ray; 2.38 A; Q=672-682.
PDB; 6GFI; X-ray; 2.30 A; C/E=294-346.
PDB; 6ITU; X-ray; 2.17 A; B=755-766.
PDB; 6IYC; EM; 2.60 A; E=688-770.
PDB; 6NB9; EM; 1.05 A; A=691-705.
PDB; 6O4J; EM; 1.40 A; A/B=687-697.
PDB; 6OC9; NMR; -; A/B/C/D/E/F/G/H/I/J=672-711.
PDB; 6RHY; NMR; -; A/B/C/D=672-713.
PDB; 6SHS; EM; 4.40 A; A/B/C/D/E/F/G/H/I/J/K/L=672-711.
PDBsum; 1AAP; -.
PDBsum; 1AMB; -.
PDBsum; 1AMC; -.
PDBsum; 1AML; -.
PDBsum; 1BA4; -.
PDBsum; 1BA6; -.
PDBsum; 1BJB; -.
PDBsum; 1BJC; -.
PDBsum; 1BRC; -.
PDBsum; 1CA0; -.
PDBsum; 1HZ3; -.
PDBsum; 1IYT; -.
PDBsum; 1MWP; -.
PDBsum; 1OWT; -.
PDBsum; 1QCM; -.
PDBsum; 1QWP; -.
PDBsum; 1QXC; -.
PDBsum; 1QYT; -.
PDBsum; 1TAW; -.
PDBsum; 1TKN; -.
PDBsum; 1UO7; -.
PDBsum; 1UO8; -.
PDBsum; 1UOA; -.
PDBsum; 1UOI; -.
PDBsum; 1X11; -.
PDBsum; 1Z0Q; -.
PDBsum; 1ZE7; -.
PDBsum; 1ZE9; -.
PDBsum; 1ZJD; -.
PDBsum; 2BEG; -.
PDBsum; 2BOM; -.
PDBsum; 2BP4; -.
PDBsum; 2FJZ; -.
PDBsum; 2FK1; -.
PDBsum; 2FK2; -.
PDBsum; 2FK3; -.
PDBsum; 2FKL; -.
PDBsum; 2FMA; -.
PDBsum; 2G47; -.
PDBsum; 2IPU; -.
PDBsum; 2LFM; -.
PDBsum; 2LLM; -.
PDBsum; 2LMN; -.
PDBsum; 2LMO; -.
PDBsum; 2LMP; -.
PDBsum; 2LMQ; -.
PDBsum; 2LNQ; -.
PDBsum; 2LOH; -.
PDBsum; 2LP1; -.
PDBsum; 2LZ3; -.
PDBsum; 2LZ4; -.
PDBsum; 2M4J; -.
PDBsum; 2M9R; -.
PDBsum; 2M9S; -.
PDBsum; 2MGT; -.
PDBsum; 2MJ1; -.
PDBsum; 2MPZ; -.
PDBsum; 2MVX; -.
PDBsum; 2MXU; -.
PDBsum; 2NAO; -.
PDBsum; 2OTK; -.
PDBsum; 2R0W; -.
PDBsum; 2WK3; -.
PDBsum; 2Y29; -.
PDBsum; 2Y2A; -.
PDBsum; 2Y3J; -.
PDBsum; 2Y3K; -.
PDBsum; 2Y3L; -.
PDBsum; 3AYU; -.
PDBsum; 3BAE; -.
PDBsum; 3BKJ; -.
PDBsum; 3DXC; -.
PDBsum; 3DXD; -.
PDBsum; 3DXE; -.
PDBsum; 3GCI; -.
PDBsum; 3IFL; -.
PDBsum; 3IFN; -.
PDBsum; 3IFO; -.
PDBsum; 3IFP; -.
PDBsum; 3JQ5; -.
PDBsum; 3JQL; -.
PDBsum; 3JTI; -.
PDBsum; 3KTM; -.
PDBsum; 3L33; -.
PDBsum; 3L81; -.
PDBsum; 3MOQ; -.
PDBsum; 3MXC; -.
PDBsum; 3MXY; -.
PDBsum; 3NYJ; -.
PDBsum; 3NYL; -.
PDBsum; 3OVJ; -.
PDBsum; 3OW9; -.
PDBsum; 3PZZ; -.
PDBsum; 3Q2X; -.
PDBsum; 3SV1; -.
PDBsum; 3U0T; -.
PDBsum; 3UMH; -.
PDBsum; 3UMI; -.
PDBsum; 3UMK; -.
PDBsum; 4HIX; -.
PDBsum; 4JFN; -.
PDBsum; 4M1C; -.
PDBsum; 4MDR; -.
PDBsum; 4MVI; -.
PDBsum; 4MVK; -.
PDBsum; 4MVL; -.
PDBsum; 4NGE; -.
PDBsum; 4OJF; -.
PDBsum; 4ONF; -.
PDBsum; 4ONG; -.
PDBsum; 4PQD; -.
PDBsum; 4PWQ; -.
PDBsum; 4XXD; -.
PDBsum; 5AEF; -.
PDBsum; 5AM8; -.
PDBsum; 5AMB; -.
PDBsum; 5BUO; -.
PDBsum; 5C67; -.
PDBsum; 5CSZ; -.
PDBsum; 5HOW; -.
PDBsum; 5HOX; -.
PDBsum; 5HOY; -.
PDBsum; 5KK3; -.
PDBsum; 5LFY; -.
PDBsum; 5LV0; -.
PDBsum; 5MY4; -.
PDBsum; 5MYO; -.
PDBsum; 5MYX; -.
PDBsum; 5ONP; -.
PDBsum; 5ONQ; -.
PDBsum; 5OQV; -.
PDBsum; 5TXD; -.
PDBsum; 5VOS; -.
PDBsum; 5VZY; -.
PDBsum; 5W3P; -.
PDBsum; 6CO3; -.
PDBsum; 6GFI; -.
PDBsum; 6ITU; -.
PDBsum; 6IYC; -.
PDBsum; 6NB9; -.
PDBsum; 6O4J; -.
PDBsum; 6OC9; -.
PDBsum; 6RHY; -.
PDBsum; 6SHS; -.
SMR; P05067; -.
BioGrid; 106848; 2157.
ComplexPortal; CPX-1062; Amyloid-beta protein 40/42 complex.
ComplexPortal; CPX-1069; Amyloid-beta protein 40 complex.
ComplexPortal; CPX-1070; Amyloid-beta protein 42 complex.
ComplexPortal; CPX-1120; Amyloid-beta protein 40/42 oligomeric complex.
ComplexPortal; CPX-1134; Amyloid-beta protein 42 oligomeric complex.
ComplexPortal; CPX-1180; Amyloid-beta protein 40 oligomeric complex.
CORUM; P05067; -.
DIP; DIP-574N; -.
ELM; P05067; -.
IntAct; P05067; 575.
MINT; P05067; -.
STRING; 9606.ENSP00000284981; -.
BindingDB; P05067; -.
ChEMBL; CHEMBL2487; -.
DrugBank; DB01370; Aluminium.
DrugBank; DB14517; Aluminium phosphate.
DrugBank; DB14518; Aluminum acetate.
DrugBank; DB05150; CAD106.
DrugBank; DB09130; Copper.
DrugBank; DB00746; Deferoxamine.
DrugBank; DB06782; Dimercaprol.
DrugBank; DB05938; Edonerpic.
DrugBank; DB09148; Florbetaben (18F).
DrugBank; DB09149; Florbetapir (18F).
DrugBank; DB09151; Flutemetamol (18F).
DrugBank; DB02235; L-methionine (R)-S-oxide.
DrugBank; DB05846; Mito-4509.
DrugBank; DB04892; Phenserine.
DrugBank; DB02709; Resveratrol.
DrugBank; DB05088; Tetrathiomolybdate.
DrugBank; DB01593; Zinc.
DrugBank; DB14487; Zinc acetate.
DrugBank; DB14533; Zinc chloride.
DrugCentral; P05067; -.
MEROPS; I02.015; -.
TCDB; 1.C.50.1.2; the amyloid Beta-protein peptide (aBetapp) family.
GlyConnect; 49; -.
iPTMnet; P05067; -.
MetOSite; P05067; -.
PhosphoSitePlus; P05067; -.
SwissPalm; P05067; -.
UniCarbKB; P05067; -.
BioMuta; APP; -.
DMDM; 112927; -.
SWISS-2DPAGE; P05067; -.
EPD; P05067; -.
jPOST; P05067; -.
MassIVE; P05067; -.
MaxQB; P05067; -.
PaxDb; P05067; -.
PeptideAtlas; P05067; -.
PRIDE; P05067; -.
ProteomicsDB; 4307; -.
ProteomicsDB; 51774; -. [P05067-1]
ProteomicsDB; 51775; -. [P05067-10]
ProteomicsDB; 51776; -. [P05067-2]
ProteomicsDB; 51777; -. [P05067-3]
ProteomicsDB; 51778; -. [P05067-4]
ProteomicsDB; 51779; -. [P05067-5]
ProteomicsDB; 51780; -. [P05067-6]
ProteomicsDB; 51781; -. [P05067-7]
ProteomicsDB; 51782; -. [P05067-8]
ProteomicsDB; 51783; -. [P05067-9]
ABCD; P05067; -.
Antibodypedia; 668; 3948 antibodies.
DNASU; 351; -.
Ensembl; ENST00000346798; ENSP00000284981; ENSG00000142192. [P05067-1]
Ensembl; ENST00000348990; ENSP00000345463; ENSG00000142192. [P05067-4]
Ensembl; ENST00000354192; ENSP00000346129; ENSG00000142192. [P05067-10]
Ensembl; ENST00000357903; ENSP00000350578; ENSG00000142192. [P05067-8]
Ensembl; ENST00000358918; ENSP00000351796; ENSG00000142192. [P05067-9]
Ensembl; ENST00000440126; ENSP00000387483; ENSG00000142192. [P05067-11]
GeneID; 351; -.
KEGG; hsa:351; -.
UCSC; uc002ylz.4; human. [P05067-1]
CTD; 351; -.
DisGeNET; 351; -.
GeneCards; APP; -.
HGNC; HGNC:620; APP.
HPA; ENSG00000142192; Low tissue specificity.
MalaCards; APP; -.
MIM; 104300; phenotype.
MIM; 104760; gene.
MIM; 605714; phenotype.
neXtProt; NX_P05067; -.
NIAGADS; ENSG00000142192; -.
OpenTargets; ENSG00000142192; -.
Orphanet; 324723; ABeta amyloidosis, Arctic type.
Orphanet; 100006; ABeta amyloidosis, Dutch type.
Orphanet; 324708; ABeta amyloidosis, Iowa type.
Orphanet; 324713; ABeta amyloidosis, Italian type.
Orphanet; 324718; ABetaA21G amyloidosis.
Orphanet; 324703; ABetaL34V amyloidosis.
Orphanet; 1020; Early-onset autosomal dominant Alzheimer disease.
PharmGKB; PA24910; -.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZW2A; LUCA.
GeneTree; ENSGT00530000063252; -.
InParanoid; P05067; -.
KO; K04520; -.
OMA; EGRCVQF; -.
PhylomeDB; P05067; -.
TreeFam; TF317274; -.
BioCyc; MetaCyc:ENSG00000142192-MONOMER; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
Reactome; R-HSA-977225; Amyloid fiber formation.
SABIO-RK; P05067; -.
SIGNOR; P05067; -.
ChiTaRS; APP; human.
EvolutionaryTrace; P05067; -.
GeneWiki; Amyloid_precursor_protein; -.
GenomeRNAi; 351; -.
Pharos; P05067; Tchem.
PRO; PR:P05067; -.
Proteomes; UP000005640; Chromosome 21.
RNAct; P05067; protein.
Bgee; ENSG00000142192; Expressed in frontal cortex and 241 other tissues.
ExpressionAtlas; P05067; baseline and differential.
Genevisible; P05067; HS.
GO; GO:0106003; C:amyloid-beta complex; IMP:ARUK-UCL.
GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
GO; GO:0097449; C:astrocyte projection; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0005623; C:cell; IDA:ARUK-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043198; C:dendritic shaft; IDA:MGI.
GO; GO:0043197; C:dendritic spine; IDA:MGI.
GO; GO:0005769; C:early endosome; IDA:ARUK-UCL.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0031904; C:endosome lumen; TAS:ARUK-UCL.
GO; GO:0070381; C:endosome to plasma membrane transport vesicle; IDA:ARUK-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:ARUK-UCL.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
GO; GO:1990812; C:growth cone filopodium; IEA:Ensembl.
GO; GO:1990761; C:growth cone lamellipodium; IEA:Ensembl.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:ARUK-UCL.
GO; GO:1990777; C:lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0044304; C:main axon; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
GO; GO:0045121; C:membrane raft; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:ARUK-UCL.
GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; IGI:ARUK-UCL.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:ARUK-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:GOC.
GO; GO:0051233; C:spindle midzone; IEA:Ensembl.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030549; F:acetylcholine receptor activator activity; TAS:ARUK-UCL.
GO; GO:0033130; F:acetylcholine receptor binding; IPI:UniProtKB.
GO; GO:0097645; F:amylin binding; TAS:ARUK-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:ARUK-UCL.
GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
GO; GO:0042056; F:chemoattractant activity; IGI:ARUK-UCL.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:0046875; F:ephrin receptor binding; IPI:ARUK-UCL.
GO; GO:0005109; F:frizzled binding; IPI:ARUK-UCL.
GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ARUK-UCL.
GO; GO:0070851; F:growth factor receptor binding; IEA:Ensembl.
GO; GO:1904399; F:heparan sulfate binding; TAS:ARUK-UCL.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IMP:ARUK-UCL.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; IPI:ARUK-UCL.
GO; GO:0005178; F:integrin binding; IDA:ARUK-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISS:ARUK-UCL.
GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
GO; GO:0046983; F:protein dimerization activity; IDA:ARUK-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IPI:ARUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0051425; F:PTB domain binding; IPI:BHF-UCL.
GO; GO:0050786; F:RAGE receptor binding; IPI:ARUK-UCL.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IGI:ARUK-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0030546; F:signaling receptor activator activity; IDA:ARUK-UCL.
GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0000187; P:activation of MAPK activity; ISS:ARUK-UCL.
GO; GO:0000185; P:activation of MAPKKK activity; IGI:ARUK-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB.
GO; GO:1990000; P:amyloid fibril formation; IMP:ParkinsonsUK-UCL.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019732; P:antifungal humoral response; IMP:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IMP:UniProtKB.
GO; GO:0008306; P:associative learning; IGI:ARUK-UCL.
GO; GO:0048143; P:astrocyte activation; IGI:ARUK-UCL.
GO; GO:0002265; P:astrocyte activation involved in immune response; IGI:ARUK-UCL.
GO; GO:0008088; P:axo-dendritic transport; ISS:UniProtKB.
GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB.
GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
GO; GO:0019722; P:calcium-mediated signaling; IDA:ARUK-UCL.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB.
GO; GO:0009987; P:cellular process; IMP:ParkinsonsUK-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:1904646; P:cellular response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0071320; P:cellular response to cAMP; 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:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071874; P:cellular response to norepinephrine stimulus; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0050890; P:cognition; ISS:UniProtKB.
GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0016358; P:dendrite development; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:ARUK-UCL.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007612; P:learning; IMP:ARUK-UCL.
GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL.
GO; GO:0042157; P:lipoprotein metabolic process; IC:ARUK-UCL.
GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB.
GO; GO:0007617; P:mating behavior; ISS:UniProtKB.
GO; GO:0007613; P:memory; IGI:ARUK-UCL.
GO; GO:0014005; P:microglia development; IGI:ARUK-UCL.
GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
GO; GO:0090647; P:modulation of age-related behavioral decline; IMP:ARUK-UCL.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IGI:ARUK-UCL.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:1903523; P:negative regulation of blood circulation; IGI:ARUK-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ARUK-UCL.
GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-UCL.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0010823; P:negative regulation of mitochondrion organization; TAS:ARUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IDA:ARUK-UCL.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; IDA:ARUK-UCL.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IGI:ARUK-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:ARUK-UCL.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0061903; P:positive regulation of 1-phosphatidylinositol-3-kinase activity; IGI:ARUK-UCL.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; IMP:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IGI:ARUK-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ARUK-UCL.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IGI:ARUK-UCL.
GO; GO:0050867; P:positive regulation of cell activation; NAS:ARUK-UCL.
GO; GO:1905893; P:positive regulation of cellular response to thapsigargin; IDA:ARUK-UCL.
GO; GO:1905896; P:positive regulation of cellular response to tunicamycin; IDA:ARUK-UCL.
GO; GO:0045080; P:positive regulation of chemokine biosynthetic process; IGI:ARUK-UCL.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:ARUK-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; NAS:ARUK-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IGI:ARUK-UCL.
GO; GO:1904472; P:positive regulation of endothelin secretion; IGI:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ARUK-UCL.
GO; GO:1904022; P:positive regulation of G protein-coupled receptor internalization; IDA:ARUK-UCL.
GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:ARUK-UCL.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
GO; GO:0045821; P:positive regulation of glycolytic process; IGI:ARUK-UCL.
GO; GO:0035066; P:positive regulation of histone acetylation; IGI:ARUK-UCL.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IGI:ARUK-UCL.
GO; GO:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IGI:ARUK-UCL.
GO; GO:0045410; P:positive regulation of interleukin-6 biosynthetic process; IGI:ARUK-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; IGI:ARUK-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:ARUK-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:ARUK-UCL.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:ARUK-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:ARUK-UCL.
GO; GO:1901216; P:positive regulation of neuron death; IDA:ARUK-UCL.
GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI:ARUK-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IGI:ARUK-UCL.
GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IGI:ARUK-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ARUK-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:ARUK-UCL.
GO; GO:0042327; P:positive regulation of phosphorylation; IGI:ARUK-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:ARUK-UCL.
GO; GO:1904591; P:positive regulation of protein import; IDA:ARUK-UCL.
GO; GO:0010739; P:positive regulation of protein kinase A signaling; NAS:ARUK-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; NAS:ARUK-UCL.
GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ARUK-UCL.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
GO; GO:1900122; P:positive regulation of receptor binding; IDA:ARUK-UCL.
GO; GO:1905898; P:positive regulation of response to endoplasmic reticulum stress; IDA:ARUK-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IGI:ARUK-UCL.
GO; GO:2000406; P:positive regulation of T cell migration; IMP:ARUK-UCL.
GO; GO:1902949; P:positive regulation of tau-protein kinase activity; IGI:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:ARUK-UCL.
GO; GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; IGI:ARUK-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0051260; P:protein homooligomerization; IDA:ARUK-UCL.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IMP:ARUK-UCL.
GO; GO:0070206; P:protein trimerization; IMP:ARUK-UCL.
GO; GO:1903048; P:regulation of acetylcholine-gated cation channel activity; IGI:ARUK-UCL.
GO; GO:1905906; P:regulation of amyloid fibril formation; IGI:ARUK-UCL.
GO; GO:1900221; P:regulation of amyloid-beta clearance; IC:ARUK-UCL.
GO; GO:1902950; P:regulation of dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IGI:ARUK-UCL.
GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:2000310; P:regulation of NMDA receptor activity; TAS:ARUK-UCL.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IGI:ARUK-UCL.
GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
GO; GO:1905945; P:regulation of response to calcium ion; ISS:ARUK-UCL.
GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IGI:ARUK-UCL.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:ARUK-UCL.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; IC:ARUK-UCL.
GO; GO:0070555; P:response to interleukin-1; ISS:ARUK-UCL.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0001878; P:response to yeast; IMP:UniProtKB.
GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
GO; GO:0050808; P:synapse organization; IGI:ARUK-UCL.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Ensembl.
GO; GO:0032640; P:tumor necrosis factor production; IGI:ARUK-UCL.
GO; GO:0008542; P:visual learning; ISS:UniProtKB.
CDD; cd00109; KU; 1.
DisProt; DP01280; -.
Gene3D; 1.20.120.770; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.1490.140; -; 1.
Gene3D; 3.90.570.10; -; 1.
Gene3D; 4.10.230.10; -; 1.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR036669; Amyloid_Cu-bd_sf.
InterPro; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR037071; Amyloid_glyco_Abeta_sf.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR019744; APP_CUBD_CS.
InterPro; IPR036176; E2_sf.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103; PTHR23103; 1.
PANTHER; PTHR23103:SF7; PTHR23103:SF7; 1.
Pfam; PF10515; APP_amyloid; 1.
Pfam; PF12924; APP_Cu_bd; 1.
Pfam; PF12925; APP_E2; 1.
Pfam; PF02177; APP_N; 1.
Pfam; PF03494; Beta-APP; 1.
Pfam; PF00014; Kunitz_BPTI; 1.
PRINTS; PR00203; AMYLOIDA4.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00204; BETAAMYLOID.
SMART; SM00006; A4_EXTRA; 1.
SMART; SM00131; KU; 1.
SUPFAM; SSF109843; SSF109843; 1.
SUPFAM; SSF56491; SSF56491; 1.
SUPFAM; SSF57362; SSF57362; 1.
SUPFAM; SSF89811; SSF89811; 1.
PROSITE; PS00319; APP_CUBD; 1.
PROSITE; PS51869; APP_E1; 1.
PROSITE; PS51870; APP_E2; 1.
PROSITE; PS00320; APP_INTRA; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Alzheimer disease; Amyloid;
Amyloidosis; Apoptosis; Cell adhesion; Cell membrane; Cell projection;
Coated pit; Copper; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Disease mutation; Disulfide bond; Endocytosis;
Endosome; Glycoprotein; Heparin-binding; Iron; Isopeptide bond; Membrane;
Metal-binding; Neurodegeneration; Notch signaling pathway; Nucleus;
Oxidation; Phosphoprotein; Polymorphism; Protease inhibitor; Proteoglycan;
Reference proteome; Secreted; Serine protease inhibitor; Signal; Sulfation;
Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
SIGNAL 1..17
/evidence="ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:2900137, ECO:0000269|PubMed:3597385"
CHAIN 18..770
/note="Amyloid-beta precursor protein"
/id="PRO_0000000088"
CHAIN 18..687
/note="Soluble APP-alpha"
/id="PRO_0000000089"
CHAIN 18..671
/note="Soluble APP-beta"
/id="PRO_0000000090"
CHAIN 18..286
/note="N-APP"
/id="PRO_0000381966"
CHAIN 672..770
/note="C99"
/id="PRO_0000000091"
CHAIN 672..713
/note="Amyloid-beta protein 42"
/id="PRO_0000000092"
CHAIN 672..711
/note="Amyloid-beta protein 40"
/id="PRO_0000000093"
CHAIN 688..770
/note="C83"
/id="PRO_0000000094"
PEPTIDE 688..713
/note="P3(42)"
/id="PRO_0000000095"
PEPTIDE 688..711
/note="P3(40)"
/id="PRO_0000000096"
CHAIN 691..770
/note="C80"
/id="PRO_0000384574"
CHAIN 712..770
/note="Gamma-secretase C-terminal fragment 59"
/id="PRO_0000000097"
CHAIN 714..770
/note="Gamma-secretase C-terminal fragment 57"
/id="PRO_0000000098"
CHAIN 721..770
/note="Gamma-secretase C-terminal fragment 50"
/evidence="ECO:0000250"
/id="PRO_0000000099"
CHAIN 740..770
/note="C31"
/id="PRO_0000000100"
TOPO_DOM 18..701
/note="Extracellular"
/evidence="ECO:0000305"
TRANSMEM 702..722
/note="Helical"
/evidence="ECO:0000305|PubMed:22584060,
ECO:0000305|PubMed:22654059, ECO:0000305|PubMed:30630874"
TOPO_DOM 723..770
/note="Cytoplasmic"
/evidence="ECO:0000305"
DOMAIN 28..189
/note="E1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
DOMAIN 291..341
/note="BPTI/Kunitz inhibitor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
DOMAIN 374..565
/note="E2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
REGION 28..123
/note="GFLD subdomain"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
REGION 96..110
/note="Heparin-binding"
/evidence="ECO:0000269|PubMed:8158260"
REGION 131..189
/note="CuBD subdomain"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
REGION 181..188
/note="Zinc-binding"
REGION 391..423
/note="Heparin-binding"
REGION 491..522
/note="Heparin-binding"
REGION 523..540
/note="Collagen-binding"
/evidence="ECO:0000269|PubMed:8576160"
REGION 695..722
/note="Interaction with PSEN1"
/evidence="ECO:0000269|PubMed:30630874"
REGION 732..751
/note="Interaction with G(o)-alpha"
REGION 756..770
/note="Required for the interaction with KIF5B and for
anterograde transport in axons"
/evidence="ECO:0000269|PubMed:17062754"
MOTIF 344..365
/note="OX-2"
/evidence="ECO:0000269|PubMed:2649245"
MOTIF 724..734
/note="Basolateral sorting signal"
MOTIF 757..762
/note="YENPXY motif; contains endocytosis signal"
/evidence="ECO:0000269|PubMed:10383380"
COMPBIAS 230..260
/note="Asp/Glu-rich (acidic)"
COMPBIAS 274..280
/note="Poly-Thr"
METAL 147
/note="Copper 1"
/evidence="ECO:0000244|PDB:2FK1, ECO:0000255|PROSITE-
ProRule:PRU01217, ECO:0000269|PubMed:17239395,
ECO:0000269|PubMed:25122912"
METAL 151
/note="Copper 1"
/evidence="ECO:0000244|PDB:2FK1, ECO:0000255|PROSITE-
ProRule:PRU01217, ECO:0000269|PubMed:17239395,
ECO:0000269|PubMed:25122912"
METAL 168
/note="Copper 1"
/evidence="ECO:0000244|PDB:2FK1, ECO:0000255|PROSITE-
ProRule:PRU01217, ECO:0000269|PubMed:17239395"
METAL 677
/note="Copper or zinc 2"
/evidence="ECO:0000269|PubMed:11274207,
ECO:0000269|PubMed:26898943"
METAL 681
/note="Copper or zinc 2"
/evidence="ECO:0000305|PubMed:10413512,
ECO:0000305|PubMed:11274207"
METAL 684
/note="Copper or zinc 2"
/evidence="ECO:0000269|PubMed:10413512,
ECO:0000269|PubMed:11274207, ECO:0000269|PubMed:26898943"
METAL 685
/note="Copper or zinc 2"
/evidence="ECO:0000269|PubMed:11274207,
ECO:0000269|PubMed:26898943"
SITE 170
/note="Required for Cu(2+) reduction"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
SITE 197..198
/note="Cleavage; by caspases"
/evidence="ECO:0000269|PubMed:10319819"
SITE 219..220
/note="Cleavage; by caspases"
/evidence="ECO:0000269|PubMed:10319819"
SITE 301..302
/note="Reactive bond"
SITE 671..672
/note="Cleavage; by beta-secretase"
/evidence="ECO:0000305|PubMed:11851430"
SITE 672..673
/note="Cleavage; by caspase-6; when associated with variant
670-N-L-671"
SITE 687..688
/note="Cleavage; by alpha-secretase"
/evidence="ECO:0000305|PubMed:11851430"
SITE 690..691
/note="Cleavage; by theta-secretase"
/evidence="ECO:0000269|PubMed:16816112"
SITE 704
/note="Implicated in free radical propagation"
/evidence="ECO:0000250"
SITE 706
/note="Susceptible to oxidation"
/evidence="ECO:0000269|PubMed:10535332"
SITE 711..712
/note="Cleavage; by gamma-secretase; site 1"
/evidence="ECO:0000305|PubMed:11851430"
SITE 713..714
/note="Cleavage; by gamma-secretase; site 2"
/evidence="ECO:0000305|PubMed:11851430"
SITE 720..721
/note="Cleavage; by gamma-secretase; site 3"
/evidence="ECO:0000269|PubMed:11851430,
ECO:0000305|PubMed:30630874"
SITE 739..740
/note="Cleavage; by caspase-6, caspase-8 or caspase-9"
/evidence="ECO:0000269|PubMed:10319819"
MOD_RES 198
/note="Phosphoserine; by CK2"
/evidence="ECO:0000269|PubMed:8999878"
MOD_RES 206
/note="Phosphoserine; by CK1"
/evidence="ECO:0000269|PubMed:8999878"
MOD_RES 217
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 262
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 336
/note="Sulfotyrosine"
/evidence="ECO:0000255"
MOD_RES 441
/note="Phosphoserine; by FAM20C"
/evidence="ECO:0000269|PubMed:26091039"
MOD_RES 497
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:26091039"
MOD_RES 729
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P08592"
MOD_RES 730
/note="Phosphoserine; by APP-kinase I"
/evidence="ECO:0000250|UniProtKB:P08592"
MOD_RES 743
/note="Phosphothreonine; by CDK5 and MAPK10"
/evidence="ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:28720718, ECO:0000269|PubMed:8131745"
MOD_RES 757
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:11877420"
CARBOHYD 542
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:16335952"
CARBOHYD 571
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000305"
CARBOHYD 633
/note="O-linked (GalNAc...) threonine; partial"
/evidence="ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872"
CARBOHYD 651
/note="O-linked (GalNAc...) threonine; partial"
/evidence="ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872"
CARBOHYD 652
/note="O-linked (GalNAc...) threonine; partial"
/evidence="ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872"
CARBOHYD 656
/note="O-linked (Xyl...) (chondroitin sulfate) serine; in
L-APP isoforms"
/evidence="ECO:0000269|PubMed:21712440"
CARBOHYD 659
/note="O-linked (HexNAc...) threonine; partial"
/evidence="ECO:0000269|PubMed:22576872"
CARBOHYD 663
/note="O-linked (GalNAc...) threonine; partial"
/evidence="ECO:0000269|PubMed:22576872,
ECO:0000305|PubMed:21712440"
CARBOHYD 667
/note="O-linked (GalNAc...) serine; partial"
/evidence="ECO:0000269|PubMed:22576872,
ECO:0000305|PubMed:21712440"
CARBOHYD 681
/note="O-linked (HexNAc...) tyrosine; partial"
/evidence="ECO:0000269|PubMed:22576872"
DISULFID 38..62
/evidence="ECO:0000244|PDB:1MWP, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4JFN, ECO:0000244|PDB:4PQD,
ECO:0000244|PDB:4PWQ, ECO:0000255|PROSITE-ProRule:PRU01217"
DISULFID 73..117
/evidence="ECO:0000244|PDB:1MWP, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4JFN, ECO:0000244|PDB:4PQD,
ECO:0000244|PDB:4PWQ, ECO:0000255|PROSITE-ProRule:PRU01217"
DISULFID 98..105
/evidence="ECO:0000244|PDB:1MWP, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4PQD, ECO:0000244|PDB:4PWQ,
ECO:0000255|PROSITE-ProRule:PRU01217"
DISULFID 133..187
/evidence="ECO:0000244|PDB:1OWT, ECO:0000244|PDB:2FJZ,
ECO:0000244|PDB:2FK1, ECO:0000244|PDB:2FK2,
ECO:0000244|PDB:2FK3, ECO:0000244|PDB:2FKL,
ECO:0000244|PDB:2FMA, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4PWQ, ECO:0000255|PROSITE-ProRule:PRU01217,
ECO:0000269|PubMed:12611883, ECO:0000269|PubMed:17239395,
ECO:0000269|PubMed:17909280"
DISULFID 144..174
/evidence="ECO:0000244|PDB:1OWT, ECO:0000244|PDB:2FJZ,
ECO:0000244|PDB:2FK1, ECO:0000244|PDB:2FK2,
ECO:0000244|PDB:2FK3, ECO:0000244|PDB:2FKL,
ECO:0000244|PDB:2FMA, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4PWQ, ECO:0000255|PROSITE-ProRule:PRU01217,
ECO:0000269|PubMed:12611883, ECO:0000269|PubMed:17239395,
ECO:0000269|PubMed:17909280"
DISULFID 158..186
/evidence="ECO:0000244|PDB:1OWT, ECO:0000244|PDB:2FJZ,
ECO:0000244|PDB:2FK1, ECO:0000244|PDB:2FK2,
ECO:0000244|PDB:2FK3, ECO:0000244|PDB:2FKL,
ECO:0000244|PDB:2FMA, ECO:0000244|PDB:3KTM,
ECO:0000244|PDB:4PWQ, ECO:0000255|PROSITE-ProRule:PRU01217,
ECO:0000269|PubMed:12611883, ECO:0000269|PubMed:17239395,
ECO:0000269|PubMed:17909280"
DISULFID 291..341
/evidence="ECO:0000244|PDB:1AAP, ECO:0000244|PDB:1BRC,
ECO:0000244|PDB:1CA0, ECO:0000244|PDB:1TAW,
ECO:0000244|PDB:1ZJD, ECO:0000244|PDB:3L33"
DISULFID 300..324
/evidence="ECO:0000244|PDB:1AAP, ECO:0000244|PDB:1BRC,
ECO:0000244|PDB:1CA0, ECO:0000244|PDB:1TAW,
ECO:0000244|PDB:1ZJD, ECO:0000244|PDB:3L33,
ECO:0000244|PDB:5C67"
DISULFID 316..337
/evidence="ECO:0000244|PDB:1AAP, ECO:0000244|PDB:1BRC,
ECO:0000244|PDB:1CA0, ECO:0000244|PDB:1TAW,
ECO:0000244|PDB:1ZJD, ECO:0000244|PDB:3L33,
ECO:0000244|PDB:5C67"
CROSSLNK 763
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000250|UniProtKB:P08592"
VAR_SEQ 1..19
/note="MLPGLALLLLAAWTARALE -> MDQLEDLLVLFINY (in isoform
11)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045446"
VAR_SEQ 19..74
/note="Missing (in isoform APP639)"
/evidence="ECO:0000303|PubMed:12859342"
/id="VSP_009116"
VAR_SEQ 289..363
/note="Missing (in isoform APP639)"
/evidence="ECO:0000303|PubMed:12859342"
/id="VSP_009117"
VAR_SEQ 289
/note="E -> V (in isoform APP695, isoform L-APP696, isoform
L-APP677 and isoform APP714)"
/evidence="ECO:0000303|PubMed:2881207"
/id="VSP_000002"
VAR_SEQ 290..364
/note="Missing (in isoform APP695 and isoform L-APP677)"
/evidence="ECO:0000303|PubMed:2881207"
/id="VSP_000004"
VAR_SEQ 290..345
/note="Missing (in isoform L-APP696 and isoform APP714)"
/evidence="ECO:0000305"
/id="VSP_000003"
VAR_SEQ 290..305
/note="VCSEQAETGPCRAMIS -> KWYKEVHSGQARWLML (in isoform
APP305)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_000005"
VAR_SEQ 306..770
/note="Missing (in isoform APP305)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_000006"
VAR_SEQ 345..364
/note="MSQSLLKTTQEPLARDPVKL -> I (in isoform 11)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045447"
VAR_SEQ 345
/note="M -> I (in isoform L-APP733 and isoform APP751)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1587857, ECO:0000303|PubMed:2893289"
/id="VSP_000007"
VAR_SEQ 346..364
/note="Missing (in isoform L-APP733 and isoform APP751)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1587857, ECO:0000303|PubMed:2893289"
/id="VSP_000008"
VAR_SEQ 364
/note="L -> V (in isoform APP639)"
/evidence="ECO:0000303|PubMed:12859342"
/id="VSP_009118"
VAR_SEQ 637..654
/note="Missing (in isoform L-APP677, isoform L-APP696,
isoform L-APP733 and isoform L-APP752)"
/evidence="ECO:0000303|PubMed:1587857"
/id="VSP_000009"
VARIANT 501
/note="E -> K (in dbSNP:rs45588932)"
/evidence="ECO:0000269|Ref.10"
/id="VAR_022315"
VARIANT 665
/note="E -> D (in a patient with late onset Alzheimer
disease; dbSNP:rs63750363)"
/evidence="ECO:0000269|PubMed:8154870"
/id="VAR_010107"
VARIANT 670..671
/note="KM -> NL (in AD1; Swedish mutation; highly increases
hydrolysis by BACE1 and amyloid-beta proteins production;
dbSNP:rs281865161)"
/evidence="ECO:0000269|PubMed:10656250,
ECO:0000269|PubMed:10677483, ECO:0000269|PubMed:1302033,
ECO:0000269|PubMed:1465129"
/id="VAR_000015"
VARIANT 678
/note="D -> N (in AD1; dbSNP:rs63750064)"
/evidence="ECO:0000269|PubMed:15201367"
/id="VAR_044424"
VARIANT 692
/note="A -> G (in AD1; Flemish mutation; increases the
solubility of processed amyloid-beta peptides and increases
the stability of peptide oligomers; dbSNP:rs63750671)"
/evidence="ECO:0000269|PubMed:11311152,
ECO:0000269|PubMed:1303239, ECO:0000269|PubMed:9754958"
/id="VAR_000016"
VARIANT 693
/note="E -> G (in AD1; dbSNP:rs63751039)"
/evidence="ECO:0000269|PubMed:11528419,
ECO:0000269|PubMed:1415269"
/id="VAR_014215"
VARIANT 693
/note="E -> K (in CAA-APP; Italian type; dbSNP:rs63750579)"
/evidence="ECO:0000269|PubMed:20697050"
/id="VAR_014216"
VARIANT 693
/note="E -> Q (in CAA-APP; Dutch type; dbSNP:rs63750579)"
/evidence="ECO:0000269|PubMed:2111584"
/id="VAR_000017"
VARIANT 694
/note="D -> N (in CAA-APP; Iowa type; dbSNP:rs63749810)"
/evidence="ECO:0000269|PubMed:11409420,
ECO:0000269|PubMed:12654973"
/id="VAR_014217"
VARIANT 705
/note="L -> V (in CAA-APP; Italian type; dbSNP:rs63750921)"
/evidence="ECO:0000269|PubMed:16178030"
/id="VAR_032276"
VARIANT 713
/note="A -> T (in AD1; dbSNP:rs63750066)"
/evidence="ECO:0000269|PubMed:1303275,
ECO:0000269|PubMed:15365148"
/id="VAR_000019"
VARIANT 713
/note="A -> V (in one chronic schizophrenia patient;
unknown pathological significance; dbSNP:rs1800557)"
/evidence="ECO:0000269|PubMed:1307241"
/id="VAR_000018"
VARIANT 714
/note="T -> A (in AD1; dbSNP:rs63750643)"
/evidence="ECO:0000269|PubMed:12034808"
/id="VAR_032277"
VARIANT 714
/note="T -> I (in AD1; increased amyloid-beta protein 42/40
ratio; dbSNP:rs63750973)"
/evidence="ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:15668448"
/id="VAR_014218"
VARIANT 715
/note="V -> M (in AD1; decreased amyloid-beta protein 40/
total amyloid-beta; dbSNP:rs63750734)"
/evidence="ECO:0000269|PubMed:10097173"
/id="VAR_010108"
VARIANT 716
/note="I -> V (in AD1; dbSNP:rs63750399)"
/evidence="ECO:0000269|PubMed:9328472"
/id="VAR_000020"
VARIANT 717
/note="V -> F (in AD1; increased amyloid-beta protein 42/40
ratio; dbSNP:rs63750264)"
/evidence="ECO:0000269|PubMed:1925564,
ECO:0000269|PubMed:8267572, ECO:0000269|PubMed:8290042,
ECO:0000269|PubMed:8476439, ECO:0000269|PubMed:8886002"
/id="VAR_000023"
VARIANT 717
/note="V -> G (in AD1; increased amyloid-beta protein 42/40
ratio; dbSNP:rs63749964)"
/evidence="ECO:0000269|PubMed:1944558,
ECO:0000269|PubMed:8476439, ECO:0000269|PubMed:8886002"
/id="VAR_000022"
VARIANT 717
/note="V -> I (in AD1; increased amyloid-beta protein 42/40
ratio; dbSNP:rs63750264)"
/evidence="ECO:0000269|PubMed:10631141,
ECO:0000269|PubMed:11063718, ECO:0000269|PubMed:1671712,
ECO:0000269|PubMed:1678058, ECO:0000269|PubMed:1908231,
ECO:0000269|PubMed:8267572, ECO:0000269|PubMed:8476439,
ECO:0000269|PubMed:8577393, ECO:0000269|PubMed:8886002"
/id="VAR_000021"
VARIANT 717
/note="V -> L (in AD1; dbSNP:rs63750264)"
/evidence="ECO:0000269|PubMed:10867787"
/id="VAR_014219"
VARIANT 723
/note="L -> P (in AD1; dbSNP:rs63751122)"
/evidence="ECO:0000269|PubMed:10665499"
/id="VAR_010109"
MUTAGEN 99..102
/note="KRGR->NQGG: Reduced heparin-binding."
/evidence="ECO:0000269|PubMed:8158260"
MUTAGEN 108
/note="H->A: Loss of the copper binding site in the GFLD
subdomain; when associated with A-110."
/evidence="ECO:0000269|PubMed:25122912"
MUTAGEN 110
/note="H->A: Loss of the copper binding site in the GFLD
subdomain; when associated with A-108."
/evidence="ECO:0000269|PubMed:25122912"
MUTAGEN 137
/note="H->N: Binds copper. Forms dimer."
/evidence="ECO:0000269|PubMed:7913895"
MUTAGEN 141
/note="M->T: Binds copper. Forms dimer."
/evidence="ECO:0000269|PubMed:7913895"
MUTAGEN 144
/note="C->S: Binds copper. No dimer formation. No copper
reducing activity."
/evidence="ECO:0000269|PubMed:10461923,
ECO:0000269|PubMed:7913895"
MUTAGEN 147..149
/note="HLH->ALA: 50% decrease in copper reducing activity."
/evidence="ECO:0000269|PubMed:10461923"
MUTAGEN 147
/note="H->A: Loss of a copper binding site; when associated
with A-151."
/evidence="ECO:0000269|PubMed:25122912"
MUTAGEN 147
/note="H->A: Some decrease in copper reducing activity."
/evidence="ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895"
MUTAGEN 147
/note="H->N: Binds copper. Forms dimer."
/evidence="ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895"
MUTAGEN 147
/note="H->Y: Greatly reduced copper-mediated low-density
lipoprotein oxidation."
/evidence="ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895"
MUTAGEN 151
/note="H->A: Loss of a copper binding site; when associated
with A-147."
/evidence="ECO:0000269|PubMed:25122912"
MUTAGEN 151
/note="H->K: Greatly reduced copper-mediated low-density
lipoprotein oxidation."
/evidence="ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895"
MUTAGEN 151
/note="H->N: Binds copper. Forms dimer."
/evidence="ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895"
MUTAGEN 198
/note="S->A: Greatly reduced casein kinase
phosphorylation."
/evidence="ECO:0000269|PubMed:10806211,
ECO:0000269|PubMed:8999878"
MUTAGEN 206
/note="S->A: Reduced casein kinase phosphorylation."
/evidence="ECO:0000269|PubMed:10806211,
ECO:0000269|PubMed:8999878"
MUTAGEN 499
/note="R->A: Reduced affinity for heparin; when associated
with A-503."
/evidence="ECO:0000269|PubMed:15304215"
MUTAGEN 503
/note="K->A: Reduced affinity for heparin; when associated
with A-499."
/evidence="ECO:0000269|PubMed:15304215"
MUTAGEN 656
/note="S->A: Abolishes chondroitin sulfate binding in L-
APP733 isoform."
/evidence="ECO:0000269|PubMed:7737970"
MUTAGEN 676
/note="R->G: 60-70% zinc-induced amyloid-beta protein 28
aggregation."
/evidence="ECO:0000269|PubMed:10413512"
MUTAGEN 681
/note="Y->F: 60-70% zinc-induced amyloid-beta protein 28
aggregation."
/evidence="ECO:0000269|PubMed:10413512"
MUTAGEN 684
/note="H->R: Only 23% zinc-induced amyloid-beta protein 28
aggregation."
/evidence="ECO:0000269|PubMed:10413512"
MUTAGEN 695
/note="V->C: Causes formation of an artifactual disulfide
bond with PSEN1."
/evidence="ECO:0000269|PubMed:30630874"
MUTAGEN 704
/note="G->V: Reduced protein oxidation. No hippocampal
neuron toxicity."
MUTAGEN 706
/note="M->L: Reduced lipid peroxidation inhibition."
/evidence="ECO:0000269|PubMed:10535332,
ECO:0000269|PubMed:9168929"
MUTAGEN 706
/note="M->V: No free radical production. No hippocampal
neuron toxicity."
/evidence="ECO:0000269|PubMed:10535332,
ECO:0000269|PubMed:9168929"
MUTAGEN 717
/note="V->C,S: Unchanged amyloid-beta protein 42/total
amyloid-beta ratio."
/evidence="ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002"
MUTAGEN 717
/note="V->K: Decreased amyloid-beta protein 42/total
amyloid-beta ratio."
/evidence="ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002"
MUTAGEN 717
/note="V->M: Increased amyloid-beta protein 42/40 ratio. No
change in apoptosis after caspase cleavage."
/evidence="ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002"
MUTAGEN 728
/note="Y->A: No effect on APBA1 nor APBB1 binding. Greatly
reduces the binding to APPBP2. APP internalization
unchanged. No change in amyloid-beta protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653, ECO:0000269|PubMed:9843960"
MUTAGEN 739
/note="D->A: No cleavage by caspases during apoptosis."
/evidence="ECO:0000269|PubMed:10319819,
ECO:0000269|PubMed:10742146, ECO:0000269|PubMed:12214090"
MUTAGEN 739
/note="D->N: No effect on FADD-induced apoptosis."
/evidence="ECO:0000269|PubMed:10319819,
ECO:0000269|PubMed:10742146, ECO:0000269|PubMed:12214090"
MUTAGEN 743
/note="T->A: Greatly reduces the binding to SHC1 and APBB
family members; no effect on NGF-stimulated neurite
extension. Loss of phosphorylation by LRRK2."
/evidence="ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006, ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420, ECO:0000269|PubMed:28720718"
MUTAGEN 743
/note="T->E: Reduced NGF-stimulated neurite extension. No
effect on APP maturation."
/evidence="ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006, ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420"
MUTAGEN 756
/note="G->A: APP internalization unchanged. No change in
amyloid-beta protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380"
MUTAGEN 757..762
/note="YENPTY->AENPTA: No effect on C99 interaction with
SORL1."
/evidence="ECO:0000269|PubMed:16407538"
MUTAGEN 757
/note="Y->A: Little APP internalization. Reduced amyloid-
beta protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:11724784, ECO:0000269|PubMed:11877420,
ECO:0000269|PubMed:8887653"
MUTAGEN 757
/note="Y->G: Loss of binding to MAPK8IP1, APBA1, APBB1,
APPBP2 and SHC1."
/evidence="ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:11724784, ECO:0000269|PubMed:11877420,
ECO:0000269|PubMed:8887653"
MUTAGEN 759
/note="N->A: No binding to APBA1, no effect on APBB1
binding. Little APP internalization. Reduced amyloid-beta
protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653"
MUTAGEN 760
/note="P->A: Little APP internalization. Reduced amyloid-
beta protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380"
MUTAGEN 762
/note="Y->A: Loss of binding to APBA1 and APBB1. APP
internalization unchanged. No change in amyloid-beta
protein 42 secretion."
/evidence="ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653"
CONFLICT 15..16
/note="AR -> VW (in Ref. 3; CAA31830)"
/evidence="ECO:0000305"
CONFLICT 647
/note="D -> E (in Ref. 36; AAA51722)"
/evidence="ECO:0000305"
CONFLICT 724
/note="Missing (in Ref. 23; AAB26263/AAB26264)"
/evidence="ECO:0000305"
CONFLICT 731
/note="I -> N (in Ref. 23; AAB26263/AAB26264/AAB26265)"
/evidence="ECO:0000305"
CONFLICT 757
/note="Y -> S (in Ref. 31; AAA35540)"
/evidence="ECO:0000305"
HELIX 26..28
/evidence="ECO:0000244|PDB:4PQD"
STRAND 33..35
/evidence="ECO:0000244|PDB:4PQD"
STRAND 43..45
/evidence="ECO:0000244|PDB:4PQD"
TURN 47..49
/evidence="ECO:0000244|PDB:4PQD"
STRAND 52..54
/evidence="ECO:0000244|PDB:4PQD"
STRAND 56..58
/evidence="ECO:0000244|PDB:4PWQ"
HELIX 66..76
/evidence="ECO:0000244|PDB:4PQD"
STRAND 82..87
/evidence="ECO:0000244|PDB:4PQD"
STRAND 92..94
/evidence="ECO:0000244|PDB:4PQD"
STRAND 97..99
/evidence="ECO:0000244|PDB:4PQD"
TURN 100..102
/evidence="ECO:0000244|PDB:4PQD"
STRAND 103..106
/evidence="ECO:0000244|PDB:4PQD"
STRAND 110..112
/evidence="ECO:0000244|PDB:4PQD"
STRAND 115..119
/evidence="ECO:0000244|PDB:4PQD"
STRAND 134..139
/evidence="ECO:0000244|PDB:2FMA"
HELIX 147..160
/evidence="ECO:0000244|PDB:2FMA"
STRAND 163..174
/evidence="ECO:0000244|PDB:2FMA"
TURN 175..177
/evidence="ECO:0000244|PDB:2FMA"
STRAND 178..188
/evidence="ECO:0000244|PDB:2FMA"
HELIX 288..292
/evidence="ECO:0000244|PDB:1AAP"
STRAND 299..301
/evidence="ECO:0000244|PDB:1AAP"
STRAND 304..310
/evidence="ECO:0000244|PDB:1AAP"
TURN 311..314
/evidence="ECO:0000244|PDB:1AAP"
STRAND 315..321
/evidence="ECO:0000244|PDB:1AAP"
STRAND 323..325
/evidence="ECO:0000244|PDB:1AAP"
STRAND 331..333
/evidence="ECO:0000244|PDB:1AAP"
HELIX 334..341
/evidence="ECO:0000244|PDB:1AAP"
HELIX 374..380
/evidence="ECO:0000244|PDB:3NYL"
HELIX 389..418
/evidence="ECO:0000244|PDB:3UMH"
STRAND 421..423
/evidence="ECO:0000244|PDB:3UMH"
HELIX 425..480
/evidence="ECO:0000244|PDB:3UMH"
STRAND 482..484
/evidence="ECO:0000244|PDB:3NYJ"
HELIX 487..518
/evidence="ECO:0000244|PDB:3UMH"
HELIX 520..546
/evidence="ECO:0000244|PDB:3UMH"
HELIX 547..550
/evidence="ECO:0000244|PDB:3UMH"
HELIX 552..566
/evidence="ECO:0000244|PDB:3UMH"
HELIX 615..618
/evidence="ECO:0000244|PDB:5BUO"
STRAND 620..622
/evidence="ECO:0000244|PDB:5BUO"
HELIX 673..675
/evidence="ECO:0000244|PDB:4OJF"
TURN 677..680
/evidence="ECO:0000244|PDB:5MYO"
STRAND 683..685
/evidence="ECO:0000244|PDB:1BA4"
STRAND 688..691
/evidence="ECO:0000244|PDB:6O4J"
STRAND 692..694
/evidence="ECO:0000244|PDB:4MVI"
TURN 695..698
/evidence="ECO:0000244|PDB:4MVI"
STRAND 701..703
/evidence="ECO:0000244|PDB:3PZZ"
STRAND 707..712
/evidence="ECO:0000244|PDB:2Y3K"
HELIX 713..715
/evidence="ECO:0000244|PDB:6IYC"
STRAND 721..725
/evidence="ECO:0000244|PDB:6IYC"
HELIX 744..754
/evidence="ECO:0000244|PDB:3DXE"
STRAND 755..758
/evidence="ECO:0000244|PDB:1X11"
STRAND 763..765
/evidence="ECO:0000244|PDB:3L81"
SEQUENCE 770 AA; 86943 MW; A12EE761403740F5 CRC64;
MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK
TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG
EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE
EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC
RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAMSQSLL KTTQEPLARD
PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA
KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL
QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER
MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET
KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN


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