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 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.
30-AUG-2017, entry version 263.
RecName: Full=Amyloid beta A4 protein;
AltName: Full=ABPP;
AltName: Full=APPI;
Short=APP;
AltName: Full=Alzheimer disease amyloid protein;
AltName: Full=Amyloid precursor protein {ECO:0000305};
AltName: Full=Beta-amyloid precursor protein {ECO:0000305};
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;
Short=S-APP-alpha;
Contains:
RecName: Full=Soluble APP-beta;
Short=S-APP-beta;
Contains:
RecName: Full=C99;
Contains:
RecName: Full=Beta-amyloid protein 42;
AltName: Full=Beta-APP42;
Contains:
RecName: Full=Beta-amyloid protein 40;
AltName: Full=Beta-APP40;
Contains:
RecName: Full=C83;
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; 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.
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, 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 672-713.
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).
[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 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).
[29]
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).
[30]
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).
[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 CLEAVAGE 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]
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).
[38]
FUNCTION OF BETA-AMYLOID 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).
[39]
REVIEW ON FUNCTION OF BETA-AMYLOID 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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[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;
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]
MUTAGENESIS OF VAL-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).
[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 beta-amyloid precursor protein.";
Proc. Natl. Acad. Sci. U.S.A. 93:10832-10837(1996).
[50]
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).
[51]
INTERACTION OF BETA-AMYLOID 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).
[52]
INTERACTION WITH APPBP2, AND MUTAGENESIS OF TYR-728.
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).
[53]
BETA-AMYLOID 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).
[54]
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).
[55]
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).
[56]
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).
[57]
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).
[58]
INTERACTION OF BETA-AMYLOID 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).
[59]
INTERACTION OF BETA-APP42 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).
[60]
IDENTIFICATION OF GAMMA-CTFS BY MASS SPECTROMETRY, AND MUTAGENESIS OF
ASP-739.
PubMed=12214090;
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).
[61]
INTERACTION WITH FPRL1.
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).
[62]
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).
[63]
BETA-AMYLOID COPPER AND ZINC-BINDING.
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).
[64]
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).
[65]
INTERACTION WITH APBB1, FUNCTION, AND SUBCELLULAR LOCATION.
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).
[66]
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).
[67]
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).
[68]
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).
[69]
COPPER-MEDIATED LIPID PEROXIDATION, AND MUTAGENESIS OF HIS-147 AND
HIS-151.
PubMed=11784781;
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).
[70]
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).
[71]
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).
[72]
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).
[73]
PHOSPHORYLATION AT THR-743.
PubMed=8131745;
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).
[74]
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).
[75]
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).
[76]
CLEAVAGE 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).
[77]
PHOSPHORYLATION, AND MUTAGENESIS OF THR-743.
PubMed=10341243;
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).
[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]
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]
CLEAVAGE AT 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]
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).
[85]
SIGNAL SEQUENCE CLEAVAGE SITE, AND TOPOLOGY.
PubMed=2900137;
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).
[86]
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).
[87]
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).
[88]
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).
[89]
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).
[90]
FUNCTION, 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).
[91]
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).
[92]
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).
[93]
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).
[94]
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).
[95]
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).
[96]
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).
[97]
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).
[98]
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).
[99]
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).
[100]
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).
[101]
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).
[102]
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).
[103]
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).
[104]
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).
[105]
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).
[106]
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).
[107]
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).
[108]
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).
[109]
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).
[110]
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).
[111]
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).
[112]
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).
[113]
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).
[114]
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).
[115]
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).
[116]
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).
[117]
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).
[118]
REVIEW ON VARIANTS.
PubMed=1363811; DOI=10.1038/ng0792-233;
Hardy J.;
"Framing beta-amyloid.";
Nat. Genet. 1:233-234(1992).
[119]
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).
[120]
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).
[121]
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).
[122]
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).
[123]
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).
[124]
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).
[125]
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).
[126]
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).
[127]
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).
[128]
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).
[129]
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).
[130]
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).
[131]
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).
[132]
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).
[133]
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).
[134]
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).
[135]
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).
[136]
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).
[137]
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).
[138]
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).
[139]
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).
[140]
VARIANT AD1 ILE-714, CHARACTERIZATION OF VARIANT AD1 ILE-714, AND
MUTAGENESIS OF VAL-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).
[141]
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).
[142]
CHARACTERIZATION OF VARIANT AD1 GLY-692.
PubMed=11311152;
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).
[143]
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).
[144]
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).
[145]
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).
[146]
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).
[147]
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).
[148]
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).
[149]
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. 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. 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}.
-!- FUNCTION: Beta-amyloid 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. Beta-amyloid 42 is a more
effective reductant than beta-amyloid 40. Beta-amyloid peptides
bind to lipoproteins and apolipoproteins E and J in the CSF and to
HDL particles in plasma, inhibiting metal-catalyzed oxidation of
lipoproteins. Beta-APP42 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, FPRL1, APPBP1,
IB1, KNS2 (via its TPR domains) (By similarity), 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-42 binds
CHRNA7 in hippocampal neurons. Beta-amyloid 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; this is promoted by heparin
binding. Beta-amyloid protein 40 interacts with S100A9. CTF-alpha
product of APP interacts with GSAP. Interacts with SORL1.
Interacts with PLD3. Interacts with VDAC1 (PubMed:25168729).
{ECO:0000250, 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:17051221, 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:24336208,
ECO:0000269|PubMed:25168729, 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:
Self; NbExp=104; IntAct=EBI-77613, EBI-77613;
Q306T3:- (xeno); NbExp=3; IntAct=EBI-77613, EBI-8294101;
P31696:AGRN (xeno); NbExp=3; IntAct=EBI-2431589, EBI-457650;
Q02410:APBA1; NbExp=3; IntAct=EBI-77613, EBI-368690;
O00213:APBB1; NbExp=5; IntAct=EBI-77613, EBI-81694;
Q92870:APBB2; NbExp=2; IntAct=EBI-77613, EBI-79277;
P51693:APLP1; NbExp=2; IntAct=EBI-302641, EBI-74648;
Q06481:APLP2; NbExp=2; IntAct=EBI-302641, EBI-79306;
P02647:APOA1; NbExp=5; IntAct=EBI-77613, EBI-701692;
Q13867:BLMH; NbExp=2; IntAct=EBI-302641, EBI-718504;
P15253:CALR (xeno); NbExp=3; IntAct=EBI-77613, EBI-9005200;
P27797:CALR; NbExp=2; IntAct=EBI-77613, EBI-1049597;
Q8K3H7:CALR (xeno); NbExp=2; IntAct=EBI-3894543, EBI-9005068;
P39060:COL18A1; NbExp=2; IntAct=EBI-821758, EBI-2566375;
P07339:CTSD; NbExp=2; IntAct=EBI-77613, EBI-2115097;
O75955:FLOT1; NbExp=5; IntAct=EBI-77613, EBI-603643;
P01100:FOS; NbExp=3; IntAct=EBI-77613, EBI-852851;
P46089:GPR3; NbExp=2; IntAct=EBI-302641, EBI-3909653;
Q9NSC5:HOMER3; NbExp=3; IntAct=EBI-302661, EBI-748420;
Q99714:HSD17B10; NbExp=4; IntAct=EBI-77613, EBI-79964;
O43736:ITM2A; NbExp=3; IntAct=EBI-302641, EBI-2431769;
P05412:JUN; NbExp=2; IntAct=EBI-77613, EBI-852823;
Q99683:MAP3K5; NbExp=2; IntAct=EBI-77613, EBI-476263;
P10636:MAPT; NbExp=9; IntAct=EBI-77613, EBI-366182;
Q93074:MED12; NbExp=2; IntAct=EBI-77613, EBI-394357;
P03897:MT-ND3; NbExp=2; IntAct=EBI-821758, EBI-1246249;
P07196:NEFL; NbExp=2; IntAct=EBI-77613, EBI-475646;
P21359:NF1; NbExp=3; IntAct=EBI-77613, EBI-1172917;
P08138:NGFR; NbExp=2; IntAct=EBI-77613, EBI-1387782;
P07174:Ngfr (xeno); NbExp=2; IntAct=EBI-2431589, EBI-1038810;
P61457:PCBD1; NbExp=2; IntAct=EBI-77613, EBI-740475;
Q15113:PCOLCE; NbExp=3; IntAct=EBI-821758, EBI-8869614;
P30101:PDIA3; NbExp=3; IntAct=EBI-77613, EBI-979862;
Q13526:PIN1; NbExp=2; IntAct=EBI-302641, EBI-714158;
P04156:PRNP; NbExp=3; IntAct=EBI-77613, EBI-977302;
P49768:PSEN1; NbExp=6; IntAct=EBI-77613, EBI-297277;
P29353:SHC1; NbExp=5; IntAct=EBI-77613, EBI-78835;
Q92529:SHC3; NbExp=2; IntAct=EBI-77613, EBI-79084;
Q9NP59:SLC40A1; NbExp=5; IntAct=EBI-77613, EBI-725153;
Q8BGY9:Slc5a7 (xeno); NbExp=2; IntAct=EBI-77613, EBI-2010752;
Q9HCB6:SPON1; NbExp=3; IntAct=EBI-302641, EBI-2431846;
P01137:TGFB1; NbExp=3; IntAct=EBI-77613, EBI-779636;
P61812:TGFB2; NbExp=7; IntAct=EBI-77613, EBI-779581;
O75509:TNFRSF21; NbExp=3; IntAct=EBI-77613, EBI-2313231;
Q13625:TP53BP2; NbExp=3; IntAct=EBI-77613, EBI-77642;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein. Membrane, clathrin-coated pit. Note=Cell surface protein
that rapidly becomes internalized via clathrin-coated pits. 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. Gamma-CTF(59)
peptide is located to both the cytoplasm and nuclei of neurons. It
can be translocated to the nucleus through association with APBB1
(Fe65). Beta-APP42 associates with FRPL1 at the cell surface and
the complex is then rapidly internalized. 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. 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.
-!- 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;
Note=A major isoform.;
Name=APP305;
IsoId=P05067-2; Sequence=VSP_000005, VSP_000006;
Name=L-APP677;
IsoId=P05067-3; Sequence=VSP_000002, VSP_000004, VSP_000009;
Note=The L-isoforms are referred to as appicans.;
Name=APP695; Synonyms=PreA4 695;
IsoId=P05067-4; Sequence=VSP_000002, VSP_000004;
Note=A major isoform.;
Name=L-APP696;
IsoId=P05067-5; Sequence=VSP_000002, VSP_000003, VSP_000009;
Note=The L-isoforms are referred to as appicans.;
Name=APP714;
IsoId=P05067-6; Sequence=VSP_000002, VSP_000003;
Name=L-APP733;
IsoId=P05067-7; Sequence=VSP_000007, VSP_000008, VSP_000009;
Note=The L-isoforms are referred to as appicans.;
Name=APP751; Synonyms=PreA4 751;
IsoId=P05067-8; Sequence=VSP_000007, VSP_000008;
Note=A major isoform.;
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 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}.
-!- INDUCTION: Increased levels during neuronal differentiation.
-!- DOMAIN: The basolateral sorting signal (BaSS) is required for
sorting of membrane proteins to the basolateral surface of
epithelial cells. {ECO:0000269|PubMed:8576160}.
-!- 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 NPXY site is also involved in clathrin-mediated
endocytosis. {ECO:0000269|PubMed:8576160}.
-!- 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 40 (Abeta40) and amyloid-beta 42 (Abeta42),
major components of amyloid plaques, and the cytotoxic C-terminal
fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many
other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are
found in cerebral spinal fluid (CSF) including the beta-amyloid X-
15 peptides, produced from the cleavage by alpha-secretase and all
terminating at Gln-686.
-!- PTM: Proteolytically cleaved by caspases during neuronal
apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9
results in the production of the neurotoxic C31 peptide and the
increased production of beta-amyloid peptides.
-!- PTM: N- and O-glycosylated. 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 beta-amyloid
peptides (beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but
not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid
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}.
-!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
serine residues is neuron-specific. Phosphorylation can affect APP
processing, neuronal differentiation and interaction with other
proteins. 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. The Thr-743 phosphorylated form causes a
conformational change which reduces binding of Fe65 family
members. Phosphorylation on Tyr-757 is required for SHC binding.
Phosphorylated in the extracellular domain by casein kinases on
both soluble and membrane-bound APP. This phosphorylation is
inhibited by heparin. {ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006, ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420, 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 beta-amyloid-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: Beta-amyloid peptides are degraded by IDE.
-!- MASS SPECTROMETRY: Mass=6461.6; Method=MALDI; Range=712-767;
Evidence={ECO:0000269|PubMed:12214090};
-!- MASS SPECTROMETRY: Mass=6451.6; Method=MALDI; Range=714-770;
Evidence={ECO:0000269|PubMed:12214090};
-!- MASS SPECTROMETRY: Mass=6436.8; Method=MALDI; Range=715-769;
Evidence={ECO:0000269|PubMed:12214090};
-!- MASS SPECTROMETRY: Mass=5752.5; Method=MALDI; Range=719-767;
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
constituent of these plaques is the neurotoxic amyloid-beta-APP
40-42 peptide (s), derived proteolytically from the transmembrane
precursor protein APP by sequential secretase processing. The
cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved
products such as C31 derived from APP, are also implicated in
neuronal death. {ECO:0000269|PubMed:10097173,
ECO:0000269|PubMed:10631141, ECO:0000269|PubMed:10665499,
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: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: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 beta-amyloid molecules
resulting in beta-amyloid-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.
-!- SIMILARITY: Belongs to the APP family. {ECO:0000305}.
-!- 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="http://www.alzforum.org/mutations/search?genes%255B%255D=348";
-!- WEB RESOURCE: Name=AD mutations;
URL="http://www.molgen.ua.ac.be/ADmutations/";
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
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]
UniGene; Hs.434980; -.
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; 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; 5KNA; X-ray; 2.32 A; A=682-696.
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; 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; 5KNA; -.
ProteinModelPortal; P05067; -.
SMR; P05067; -.
BioGrid; 106848; 2112.
DIP; DIP-574N; -.
ELM; P05067; -.
IntAct; P05067; 126.
MINT; MINT-150767; -.
STRING; 9606.ENSP00000284981; -.
BindingDB; P05067; -.
ChEMBL; CHEMBL2487; -.
DrugBank; DB05150; CAD106.
DrugBank; DB09148; Florbetaben (18F).
DrugBank; DB09149; Florbetapir (18F).
DrugBank; DB09151; Flutemetamol (18F).
DrugBank; DB02235; L-methionine (R)-S-oxide.
DrugBank; DB05846; Mito-4509.
MEROPS; I02.015; -.
TCDB; 1.C.50.1.2; the amyloid Beta-protein peptide (aBetapp) family.
iPTMnet; P05067; -.
PhosphoSitePlus; P05067; -.
SwissPalm; P05067; -.
UniCarbKB; P05067; -.
BioMuta; APP; -.
DMDM; 112927; -.
SWISS-2DPAGE; P05067; -.
EPD; P05067; -.
MaxQB; P05067; -.
PaxDb; P05067; -.
PeptideAtlas; P05067; -.
PRIDE; P05067; -.
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; -.
GeneReviews; APP; -.
HGNC; HGNC:620; APP.
HPA; CAB000157; -.
HPA; HPA001462; -.
MalaCards; APP; -.
MIM; 104300; phenotype.
MIM; 104760; gene.
MIM; 605714; phenotype.
neXtProt; NX_P05067; -.
OpenTargets; ENSG00000142192; -.
Orphanet; 1020; Early-onset autosomal dominant Alzheimer disease.
Orphanet; 324723; Hereditary cerebral hemorrhage with amyloidosis, Arctic type.
Orphanet; 100006; Hereditary cerebral hemorrhage with amyloidosis, Dutch type.
Orphanet; 324718; Hereditary cerebral hemorrhage with amyloidosis, Flemish type.
Orphanet; 324708; Hereditary cerebral hemorrhage with amyloidosis, Iowa type.
Orphanet; 324713; Hereditary cerebral hemorrhage with amyloidosis, Italian type.
Orphanet; 324703; Hereditary cerebral hemorrhage with amyloidosis, Piedmont type.
PharmGKB; PA24910; -.
eggNOG; KOG3540; Eukaryota.
eggNOG; ENOG410ZW2A; LUCA.
GeneTree; ENSGT00530000063252; -.
HOGENOM; HOG000232190; -.
HOVERGEN; HBG000051; -.
InParanoid; P05067; -.
KO; K04520; -.
OMA; REVCSEQ; -.
OrthoDB; EOG091G0UW4; -.
PhylomeDB; P05067; -.
TreeFam; TF317274; -.
BioCyc; MetaCyc:ENSG00000142192-MONOMER; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
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-977225; Amyloid fiber formation.
SABIO-RK; P05067; -.
SIGNOR; P05067; -.
ChiTaRS; APP; human.
EvolutionaryTrace; P05067; -.
GeneWiki; Amyloid_precursor_protein; -.
GenomeRNAi; 351; -.
PMAP-CutDB; P05067; -.
PRO; PR:P05067; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000142192; -.
ExpressionAtlas; P05067; baseline and differential.
Genevisible; P05067; HS.
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: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:0005737; C:cytoplasm; IDA:UniProtKB.
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:Reactome.
GO; GO:0070381; C:endosome to plasma membrane transport vesicle; IDA:ARUK-UCL.
GO; GO:0030134; C:ER to Golgi transport vesicle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA: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: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:0005622; C:intracellular; 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:0031594; C:neuromuscular junction; IEA:Ensembl.
GO; GO:0005641; C:nuclear envelope lumen; IDA:Alzheimers_University_of_Toronto.
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:0043234; C:protein complex; IDA:ARUK-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
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:0043195; C:terminal bouton; 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:0005109; F:frizzled 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: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:0030546; F:receptor activator activity; IDA:ARUK-UCL.
GO; GO:0005102; F:receptor binding; IPI:ARUK-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
GO; GO:0000187; P:activation of MAPK activity; ISS: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; IDA: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: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: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:0007611; P:learning or memory; IGI: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; IDA:ARUK-UCL.
GO; GO:0014005; P:microglia development; IGI:ARUK-UCL.
GO; GO:0090647; P:modulation of age-related behavioral decline; IGI:ARUK-UCL.
GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IGI:ARUK-UCL.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IGI:ARUK-UCL.
GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; 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 proliferation; IDA:UniProtKB.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IMP:ARUK-UCL.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:ARUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-UCL.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IDA: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:1900181; P:negative regulation of protein localization to nucleus; IGI:ARUK-UCL.
GO; GO:0051826; P:negative regulation of synapse structural plasticity; IMP:ARUK-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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: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:0043065; P:positive regulation of apoptotic process; TAS:ARUK-UCL.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; 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: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: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:0045745; P:positive regulation of G-protein coupled receptor protein 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; IMP:ARUK-UCL.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:ARUK-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; NAS: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:1901216; P:positive regulation of neuron death; IDA:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IGI: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:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ARUK-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:ARUK-UCL.
GO; GO:1904591; P:positive regulation of protein import; ISS: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:1902949; P:positive regulation of tau-protein kinase activity; ISS:ARUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
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:1903048; P:regulation of acetylcholine-gated cation channel activity; IGI:ARUK-UCL.
GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:1902938; P:regulation of intracellular calcium activated chloride channel activity; 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:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IGI:ARUK-UCL.
GO; GO:1905945; P:regulation of response to calcium ion; ISS:ARUK-UCL.
GO; GO:0050803; P:regulation of synapse structure or activity; ISS:UniProtKB.
GO; GO:0060025; P:regulation of synaptic activity; IMP:ARUK-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; IGI:ARUK-UCL.
GO; GO:0034121; P:regulation of toll-like receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0006448; P:regulation of translational elongation; IGI: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.
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; IPR008155; Amyloid_glyco.
InterPro; IPR013803; Amyloid_glyco_Abeta.
InterPro; IPR011178; Amyloid_glyco_Cu-bd.
InterPro; IPR024329; Amyloid_glyco_E2_domain.
InterPro; IPR008154; Amyloid_glyco_extra.
InterPro; IPR019744; Amyloid_glyco_extracell_CS.
InterPro; IPR015849; Amyloid_glyco_heparin-bd.
InterPro; IPR019745; Amyloid_glyco_intracell_CS.
InterPro; IPR028866; APP.
InterPro; IPR019543; APP_amyloid_C.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR23103:SF17; PTHR23103:SF17; 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; A4_EXTRA; 1.
PROSITE; PS00320; A4_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; Coated pit; Complete proteome;
Copper; Direct protein sequencing; Disease mutation; Disulfide bond;
Endocytosis; Glycoprotein; Heparin-binding; Iron; Isopeptide bond;
Membrane; Metal-binding; Neurodegeneration; Notch signaling pathway;
Oxidation; Phosphoprotein; Polymorphism; Protease inhibitor;
Proteoglycan; Reference proteome; Serine protease inhibitor; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation; Zinc.
SIGNAL 1 17 {ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:2900137,
ECO:0000269|PubMed:3597385}.
CHAIN 18 770 Amyloid beta A4 protein.
/FTId=PRO_0000000088.
CHAIN 18 687 Soluble APP-alpha.
/FTId=PRO_0000000089.
CHAIN 18 671 Soluble APP-beta.
/FTId=PRO_0000000090.
CHAIN 18 286 N-APP.
/FTId=PRO_0000381966.
CHAIN 672 770 C99.
/FTId=PRO_0000000091.
CHAIN 672 713 Beta-amyloid protein 42.
/FTId=PRO_0000000092.
CHAIN 672 711 Beta-amyloid protein 40.
/FTId=PRO_0000000093.
CHAIN 688 770 C83.
/FTId=PRO_0000000094.
PEPTIDE 688 713 P3(42).
/FTId=PRO_0000000095.
PEPTIDE 688 711 P3(40).
/FTId=PRO_0000000096.
CHAIN 691 770 C80.
/FTId=PRO_0000384574.
CHAIN 712 770 Gamma-secretase C-terminal fragment 59.
/FTId=PRO_0000000097.
CHAIN 714 770 Gamma-secretase C-terminal fragment 57.
/FTId=PRO_0000000098.
CHAIN 721 770 Gamma-secretase C-terminal fragment 50.
{ECO:0000250}.
/FTId=PRO_0000000099.
CHAIN 740 770 C31.
/FTId=PRO_0000000100.
TOPO_DOM 18 699 Extracellular. {ECO:0000255}.
TRANSMEM 700 723 Helical. {ECO:0000255}.
TOPO_DOM 724 770 Cytoplasmic. {ECO:0000255}.
DOMAIN 291 341 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 96 110 Heparin-binding.
REGION 181 188 Zinc-binding.
REGION 391 423 Heparin-binding.
REGION 491 522 Heparin-binding.
REGION 523 540 Collagen-binding.
REGION 732 751 Interaction with G(o)-alpha.
MOTIF 724 734 Basolateral sorting signal.
MOTIF 759 762 NPXY motif; contains endocytosis signal.
COMPBIAS 230 260 Asp/Glu-rich (acidic).
COMPBIAS 274 280 Poly-Thr.
METAL 147 147 Copper 1.
METAL 151 151 Copper 1.
METAL 168 168 Copper 1.
METAL 677 677 Copper or zinc 2.
METAL 681 681 Copper or zinc 2. {ECO:0000305}.
METAL 684 684 Copper or zinc 2.
METAL 685 685 Copper or zinc 2.
SITE 144 144 Required for Cu(2+) reduction.
SITE 301 302 Reactive bond.
SITE 671 672 Cleavage; by beta-secretase.
SITE 672 673 Cleavage; by caspase-6; when associated
with variant 670-N-L-671.
SITE 687 688 Cleavage; by alpha-secretase.
SITE 690 691 Cleavage; by theta-secretase.
{ECO:0000269|PubMed:16816112}.
SITE 704 704 Implicated in free radical propagation.
{ECO:0000250}.
SITE 706 706 Susceptible to oxidation.
{ECO:0000269|PubMed:10535332}.
SITE 711 712 Cleavage; by gamma-secretase; site 1.
SITE 713 714 Cleavage; by gamma-secretase; site 2.
SITE 720 721 Cleavage; by gamma-secretase; site 3.
SITE 739 740 Cleavage; by caspase-6, caspase-8 or
caspase-9.
MOD_RES 198 198 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8999878}.
MOD_RES 206 206 Phosphoserine; by CK1.
{ECO:0000269|PubMed:8999878}.
MOD_RES 441 441 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000269|PubMed:26091039}.
MOD_RES 729 729 Phosphothreonine.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 730 730 Phosphoserine; by APP-kinase I.
{ECO:0000250|UniProtKB:P08592}.
MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:8131745}.
MOD_RES 757 757 Phosphotyrosine.
{ECO:0000269|PubMed:11877420}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 633 633 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872}.
CARBOHYD 651 651 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872}.
CARBOHYD 652 652 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:21712440,
ECO:0000269|PubMed:22576872}.
CARBOHYD 656 656 O-linked (Xyl...) (chondroitin sulfate)
serine; in L-APP isoforms.
{ECO:0000269|PubMed:21712440}.
CARBOHYD 659 659 O-linked (HexNAc...) threonine; partial.
{ECO:0000269|PubMed:22576872}.
CARBOHYD 663 663 O-linked (GalNAc...) threonine; partial.
{ECO:0000269|PubMed:22576872,
ECO:0000305|PubMed:21712440}.
CARBOHYD 667 667 O-linked (GalNAc...) serine; partial.
{ECO:0000269|PubMed:22576872,
ECO:0000305|PubMed:21712440}.
CARBOHYD 681 681 O-linked (HexNAc...) tyrosine; partial.
{ECO:0000269|PubMed:22576872}.
DISULFID 38 62
DISULFID 73 117
DISULFID 98 105
DISULFID 133 187
DISULFID 144 174
DISULFID 158 186
DISULFID 291 341
DISULFID 300 324
DISULFID 316 337
CROSSLNK 763 763 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P08592}.
VAR_SEQ 1 19 MLPGLALLLLAAWTARALE -> MDQLEDLLVLFINY (in
isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045446.
VAR_SEQ 19 74 Missing (in isoform APP639).
{ECO:0000303|PubMed:12859342}.
/FTId=VSP_009116.
VAR_SEQ 289 363 Missing (in isoform APP639).
{ECO:0000303|PubMed:12859342}.
/FTId=VSP_009117.
VAR_SEQ 289 289 E -> V (in isoform APP695, isoform L-
APP696, isoform L-APP677 and isoform
APP714). {ECO:0000303|PubMed:2881207}.
/FTId=VSP_000002.
VAR_SEQ 290 364 Missing (in isoform APP695 and isoform L-
APP677). {ECO:0000303|PubMed:2881207}.
/FTId=VSP_000004.
VAR_SEQ 290 345 Missing (in isoform L-APP696 and isoform
APP714). {ECO:0000305}.
/FTId=VSP_000003.
VAR_SEQ 290 305 VCSEQAETGPCRAMIS -> KWYKEVHSGQARWLML (in
isoform APP305).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000005.
VAR_SEQ 306 770 Missing (in isoform APP305).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_000006.
VAR_SEQ 345 364 MSQSLLKTTQEPLARDPVKL -> I (in isoform
11). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_045447.
VAR_SEQ 345 345 M -> I (in isoform L-APP733 and isoform
APP751). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1587857,
ECO:0000303|PubMed:2893289}.
/FTId=VSP_000007.
VAR_SEQ 346 364 Missing (in isoform L-APP733 and isoform
APP751). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1587857,
ECO:0000303|PubMed:2893289}.
/FTId=VSP_000008.
VAR_SEQ 364 364 L -> V (in isoform APP639).
{ECO:0000303|PubMed:12859342}.
/FTId=VSP_009118.
VAR_SEQ 637 654 Missing (in isoform L-APP677, isoform L-
APP696, isoform L-APP733 and isoform L-
APP752). {ECO:0000303|PubMed:1587857}.
/FTId=VSP_000009.
VARIANT 501 501 E -> K (in dbSNP:rs45588932).
{ECO:0000269|Ref.10}.
/FTId=VAR_022315.
VARIANT 665 665 E -> D (in a patient with late onset
Alzheimer disease; dbSNP:rs63750363).
{ECO:0000269|PubMed:8154870}.
/FTId=VAR_010107.
VARIANT 670 671 KM -> NL (in AD1; dbSNP:rs281865161).
/FTId=VAR_000015.
VARIANT 678 678 D -> N (in AD1; dbSNP:rs63750064).
{ECO:0000269|PubMed:15201367}.
/FTId=VAR_044424.
VARIANT 692 692 A -> G (in AD1; Flemish mutation;
increases the solubility of processed
beta-amyloid peptides and increases the
stability of peptide oligomers;
dbSNP:rs63750671).
{ECO:0000269|PubMed:11311152,
ECO:0000269|PubMed:1303239,
ECO:0000269|PubMed:9754958}.
/FTId=VAR_000016.
VARIANT 693 693 E -> G (in AD1; dbSNP:rs63751039).
{ECO:0000269|PubMed:11528419,
ECO:0000269|PubMed:1415269}.
/FTId=VAR_014215.
VARIANT 693 693 E -> K (in CAA-APP; Italian type;
dbSNP:rs63750579).
{ECO:0000269|PubMed:20697050}.
/FTId=VAR_014216.
VARIANT 693 693 E -> Q (in CAA-APP; Dutch type;
dbSNP:rs63750579).
{ECO:0000269|PubMed:2111584}.
/FTId=VAR_000017.
VARIANT 694 694 D -> N (in CAA-APP; Iowa type;
dbSNP:rs63749810).
{ECO:0000269|PubMed:11409420,
ECO:0000269|PubMed:12654973}.
/FTId=VAR_014217.
VARIANT 705 705 L -> V (in CAA-APP; Italian type;
dbSNP:rs63750921).
{ECO:0000269|PubMed:16178030}.
/FTId=VAR_032276.
VARIANT 713 713 A -> T (in AD1; dbSNP:rs63750066).
{ECO:0000269|PubMed:1303275,
ECO:0000269|PubMed:15365148}.
/FTId=VAR_000019.
VARIANT 713 713 A -> V (in one chronic schizophrenia
patient; unknown pathological
significance; dbSNP:rs1800557).
{ECO:0000269|PubMed:1307241}.
/FTId=VAR_000018.
VARIANT 714 714 T -> A (in AD1; dbSNP:rs63750643).
{ECO:0000269|PubMed:12034808}.
/FTId=VAR_032277.
VARIANT 714 714 T -> I (in AD1; increased beta-APP42/
beta-APP40 ratio; dbSNP:rs63750973).
{ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:15668448}.
/FTId=VAR_014218.
VARIANT 715 715 V -> M (in AD1; decreased beta-APP40/
total APP-beta; dbSNP:rs63750734).
{ECO:0000269|PubMed:10097173}.
/FTId=VAR_010108.
VARIANT 716 716 I -> V (in AD1; dbSNP:rs63750399).
{ECO:0000269|PubMed:9328472}.
/FTId=VAR_000020.
VARIANT 717 717 V -> F (in AD1; dbSNP:rs63750264).
{ECO:0000269|PubMed:1925564,
ECO:0000269|PubMed:8267572,
ECO:0000269|PubMed:8290042,
ECO:0000269|PubMed:8476439}.
/FTId=VAR_000023.
VARIANT 717 717 V -> G (in AD1; dbSNP:rs63749964).
{ECO:0000269|PubMed:1944558,
ECO:0000269|PubMed:8476439}.
/FTId=VAR_000022.
VARIANT 717 717 V -> I (in AD1; dbSNP:rs63750264).
{ECO:0000269|PubMed:10631141,
ECO:0000269|PubMed:1671712,
ECO:0000269|PubMed:1678058,
ECO:0000269|PubMed:1908231,
ECO:0000269|PubMed:8267572,
ECO:0000269|PubMed:8476439,
ECO:0000269|PubMed:8577393}.
/FTId=VAR_000021.
VARIANT 717 717 V -> L (in AD1; dbSNP:rs63750264).
{ECO:0000269|PubMed:10867787}.
/FTId=VAR_014219.
VARIANT 723 723 L -> P (in AD1; dbSNP:rs63751122).
{ECO:0000269|PubMed:10665499}.
/FTId=VAR_010109.
MUTAGEN 99 102 KRGR->NQGG: Reduced heparin-binding.
{ECO:0000269|PubMed:8158260}.
MUTAGEN 137 137 H->N: Binds copper. Forms dimer.
{ECO:0000269|PubMed:7913895}.
MUTAGEN 141 141 M->T: Binds copper. Forms dimer.
{ECO:0000269|PubMed:7913895}.
MUTAGEN 144 144 C->S: Binds copper. No dimer formation.
No copper reducing activity.
{ECO:0000269|PubMed:10461923,
ECO:0000269|PubMed:7913895}.
MUTAGEN 147 149 HLH->ALA: 50% decrease in copper reducing
activity. {ECO:0000269|PubMed:10461923}.
MUTAGEN 147 147 H->A: Some decrease in copper reducing
activity. {ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895}.
MUTAGEN 147 147 H->N: Binds copper. Forms dimer.
{ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895}.
MUTAGEN 147 147 H->Y: Greatly reduced copper-mediated
low-density lipoprotein oxidation.
{ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895}.
MUTAGEN 151 151 H->K: Greatly reduced copper-mediated
low-density lipoprotein oxidation.
{ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895}.
MUTAGEN 151 151 H->N: Binds copper. Forms dimer.
{ECO:0000269|PubMed:11784781,
ECO:0000269|PubMed:7913895}.
MUTAGEN 198 198 S->A: Greatly reduced casein kinase
phosphorylation.
{ECO:0000269|PubMed:10806211,
ECO:0000269|PubMed:8999878}.
MUTAGEN 206 206 S->A: Reduced casein kinase
phosphorylation.
{ECO:0000269|PubMed:10806211,
ECO:0000269|PubMed:8999878}.
MUTAGEN 499 499 R->A: Reduced affinity for heparin; when
associated with A-503.
{ECO:0000269|PubMed:15304215}.
MUTAGEN 503 503 K->A: Reduced affinity for heparin; when
associated with A-499.
{ECO:0000269|PubMed:15304215}.
MUTAGEN 656 656 S->A: Abolishes chondroitin sulfate
binding in L-APP733 isoform.
{ECO:0000269|PubMed:7737970}.
MUTAGEN 676 676 R->G: 60-70% zinc-induced beta-APP (28)
peptide aggregation.
{ECO:0000269|PubMed:10413512}.
MUTAGEN 681 681 Y->F: 60-70% zinc-induced beta-APP (28)
peptide aggregation.
{ECO:0000269|PubMed:10413512}.
MUTAGEN 684 684 H->R: Only 23% zinc-induced beta-APP (28)
peptide aggregation.
{ECO:0000269|PubMed:10413512}.
MUTAGEN 704 704 G->V: Reduced protein oxidation. No
hippocampal neuron toxicity.
MUTAGEN 706 706 M->L: Reduced lipid peroxidation
inhibition. {ECO:0000269|PubMed:10535332,
ECO:0000269|PubMed:9168929}.
MUTAGEN 706 706 M->V: No free radical production. No
hippocampal neuron toxicity.
{ECO:0000269|PubMed:10535332,
ECO:0000269|PubMed:9168929}.
MUTAGEN 717 717 V->C,S: Unchanged beta-APP42/total APP-
beta ratio. {ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002}.
MUTAGEN 717 717 V->F,G,I: Increased beta-APP42/beta-APP40
ratio. {ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002}.
MUTAGEN 717 717 V->K: Decreased beta-APP42/total APP-beta
ratio. {ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002}.
MUTAGEN 717 717 V->M: Increased beta-APP42/beta-APP40
ratio. No change in apoptosis after
caspase cleavage.
{ECO:0000269|PubMed:11063718,
ECO:0000269|PubMed:8886002}.
MUTAGEN 728 728 Y->A: No effect on APBA1 nor APBB1
binding. Greatly reduces the binding to
APPBP2. APP internalization unchanged. No
change in beta-APP42 secretion.
{ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653,
ECO:0000269|PubMed:9843960}.
MUTAGEN 739 739 D->A: No cleavage by caspases during
apoptosis. {ECO:0000269|PubMed:10319819,
ECO:0000269|PubMed:10742146,
ECO:0000269|PubMed:12214090}.
MUTAGEN 739 739 D->N: No effect on FADD-induced
apoptosis. {ECO:0000269|PubMed:10319819,
ECO:0000269|PubMed:10742146,
ECO:0000269|PubMed:12214090}.
MUTAGEN 743 743 T->A: Greatly reduces the binding to SHC1
and APBB family members; no effect on
NGF-stimulated neurite extension.
{ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006,
ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420}.
MUTAGEN 743 743 T->E: Reduced NGF-stimulated neurite
extension. No effect on APP maturation.
{ECO:0000269|PubMed:10341243,
ECO:0000269|PubMed:11146006,
ECO:0000269|PubMed:11517218,
ECO:0000269|PubMed:11877420}.
MUTAGEN 756 756 G->A: APP internalization unchanged. No
change in beta-APP42 secretion.
{ECO:0000269|PubMed:10383380}.
MUTAGEN 757 757 Y->A: Little APP internalization. Reduced
beta-APP42 secretion.
{ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:11724784,
ECO:0000269|PubMed:11877420,
ECO:0000269|PubMed:8887653}.
MUTAGEN 757 757 Y->G: Loss of binding to MAPK8IP1, APBA1,
APBB1, APPBP2 and SHC1.
{ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:11724784,
ECO:0000269|PubMed:11877420,
ECO:0000269|PubMed:8887653}.
MUTAGEN 759 759 N->A: No binding to APBA1, no effect on
APBB1 binding. Little APP
internalization. Reduced beta-APP42
secretion. {ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653}.
MUTAGEN 760 760 P->A: Little APP internalization. Reduced
beta-APP42 secretion.
{ECO:0000269|PubMed:10383380}.
MUTAGEN 762 762 Y->A: Loss of binding to APBA1 and APBB1.
APP internalization unchanged. No change
in beta-APP42 secretion.
{ECO:0000269|PubMed:10383380,
ECO:0000269|PubMed:8887653}.
CONFLICT 15 16 AR -> VW (in Ref. 3; CAA31830).
{ECO:0000305}.
CONFLICT 647 647 D -> E (in Ref. 36; AAA51722).
{ECO:0000305}.
CONFLICT 724 724 Missing (in Ref. 23; AAB26263/AAB26264).
{ECO:0000305}.
CONFLICT 731 731 I -> N (in Ref. 23; AAB26263/AAB26264/
AAB26265). {ECO:0000305}.
CONFLICT 757 757 Y -> S (in Ref. 31; AAA35540).
{ECO:0000305}.
HELIX 26 28 {ECO:0000244|PDB:4PQD}.
STRAND 33 35 {ECO:0000244|PDB:4PQD}.
STRAND 43 45 {ECO:0000244|PDB:4PQD}.
TURN 47 49 {ECO:0000244|PDB:4PQD}.
STRAND 52 54 {ECO:0000244|PDB:4PQD}.
STRAND 56 58 {ECO:0000244|PDB:4PWQ}.
HELIX 66 76 {ECO:0000244|PDB:4PQD}.
STRAND 82 87 {ECO:0000244|PDB:4PQD}.
STRAND 92 94 {ECO:0000244|PDB:4PQD}.
STRAND 97 99 {ECO:0000244|PDB:4PQD}.
TURN 100 102 {ECO:0000244|PDB:4PQD}.
STRAND 103 106 {ECO:0000244|PDB:4PQD}.
STRAND 110 112 {ECO:0000244|PDB:4PQD}.
STRAND 115 119 {ECO:0000244|PDB:4PQD}.
STRAND 134 139 {ECO:0000244|PDB:2FMA}.
HELIX 147 160 {ECO:0000244|PDB:2FMA}.
STRAND 163 174 {ECO:0000244|PDB:2FMA}.
TURN 175 177 {ECO:0000244|PDB:2FMA}.
STRAND 178 188 {ECO:0000244|PDB:2FMA}.
HELIX 288 292 {ECO:0000244|PDB:1AAP}.
STRAND 299 301 {ECO:0000244|PDB:1AAP}.
STRAND 304 310 {ECO:0000244|PDB:1AAP}.
TURN 311 314 {ECO:0000244|PDB:1AAP}.
STRAND 315 321 {ECO:0000244|PDB:1AAP}.
STRAND 323 325 {ECO:0000244|PDB:1AAP}.
STRAND 331 333 {ECO:0000244|PDB:1AAP}.
HELIX 334 341 {ECO:0000244|PDB:1AAP}.
HELIX 374 380 {ECO:0000244|PDB:3NYL}.
HELIX 389 418 {ECO:0000244|PDB:3UMH}.
STRAND 421 423 {ECO:0000244|PDB:3UMH}.
HELIX 425 480 {ECO:0000244|PDB:3UMH}.
STRAND 482 484 {ECO:0000244|PDB:3NYJ}.
HELIX 487 518 {ECO:0000244|PDB:3UMH}.
HELIX 520 546 {ECO:0000244|PDB:3UMH}.
HELIX 547 550 {ECO:0000244|PDB:3UMH}.
HELIX 552 566 {ECO:0000244|PDB:3UMH}.
HELIX 615 618 {ECO:0000244|PDB:5BUO}.
STRAND 620 622 {ECO:0000244|PDB:5BUO}.
HELIX 673 675 {ECO:0000244|PDB:4OJF}.
STRAND 676 678 {ECO:0000244|PDB:2MVX}.
STRAND 679 682 {ECO:0000244|PDB:1BA6}.
STRAND 683 685 {ECO:0000244|PDB:1BA4}.
STRAND 688 691 {ECO:0000244|PDB:3OVJ}.
STRAND 692 694 {ECO:0000244|PDB:4MVI}.
TURN 695 698 {ECO:0000244|PDB:4MVI}.
STRAND 702 705 {ECO:0000244|PDB:2Y3J}.
STRAND 707 712 {ECO:0000244|PDB:2Y3K}.
HELIX 744 754 {ECO:0000244|PDB:3DXE}.
STRAND 755 758 {ECO:0000244|PDB:1X11}.
STRAND 763 765 {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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