P05067 (A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amyloid beta A4 protein

Alternative name(s):
ABPP
APPI
Short name=APP
Alzheimer disease amyloid protein
Cerebral vascular amyloid peptide
Short name=CVAP
PreA4
Protease nexin-II
Short name=PN-II

Cleaved into the following 14 chains:

1. N-APP
2. Soluble APP-alpha
   Short name=S-APP-alpha
3. Soluble APP-beta
   Short name=S-APP-beta
4. C99
5. Beta-amyloid protein 42
   Alternative name(s):
   Beta-APP42
6. Beta-amyloid protein 40
   Alternative name(s):
   Beta-APP40
7. C83
8. P3(42)
9. P3(40)
10. C80
11. Gamma-secretase C-terminal fragment 59
    Alternative name(s):
    Amyloid intracellular domain 59
    Short name=AICD-59
    Short name=AID(59)
    Gamma-CTF(59)
12. Gamma-secretase C-terminal fragment 57
    Alternative name(s):
    Amyloid intracellular domain 57
    Short name=AICD-57
    Short name=AID(57)
    Gamma-CTF(57)
13. Gamma-secretase C-terminal fragment 50
    Alternative name(s):
    Amyloid intracellular domain 50
    Short name=AICD-50
    Short name=AID(50)
    Gamma-CTF(50)
14. C31

Gene names

Name:	APP
Synonyms:	A4, AD1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	770 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 Cu2+-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 Cu2+ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Ref.38 Ref.65 Ref.67 Ref.89 Ref.90 Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu2+ and Fe3+ to Cu+ and Fe2+, 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 Also bind GPC1 in lipid rafts. Ref.38 Ref.65 Ref.67 Ref.89 Ref.90 Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain By similarity. Ref.38 Ref.65 Ref.67 Ref.89 Ref.90 The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. Ref.38 Ref.65 Ref.67 Ref.89 Ref.90 N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Ref.38 Ref.65 Ref.67 Ref.89 Ref.90
Subunit structure	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. Ref.43 Ref.47 Ref.48 Ref.49 Ref.51 Ref.52 Ref.55 Ref.58 Ref.59 Ref.61 Ref.62 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.72 Ref.80 Ref.83 Ref.87 Ref.88 Ref.89 Ref.90 Ref.94 Ref.112
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-CTF59 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. Ref.65 Ref.71
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. Ref.8 Ref.27
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. Ref.22 Ref.41 Ref.42 Ref.44 Ref.45 Ref.50 Ref.100 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. Ref.22 Ref.41 Ref.42 Ref.44 Ref.45 Ref.50 Ref.100
Post-translational modification	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-CTF50, gamma-CTF57 and gamma-CTF59. 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 terminatiing at Gln-686. 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. Ref.34 Ref.76 Ref.79 Ref.82 Ref.85 Ref.89 Ref.93 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. Ref.33 Ref.93 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. Ref.73 Ref.74 Ref.77 Ref.78 Ref.80 Ref.81 Ref.83 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. 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). Ref.34 Ref.76 Ref.79 Ref.82 Ref.85 Ref.89 Ref.93 Beta-amyloid peptides are degraded by IDE.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.25 Ref.115 Ref.116 Ref.117 Ref.118 Ref.119 Ref.120 Ref.121 Ref.122 Ref.124 Ref.125 Ref.127 Ref.128 Ref.129 Ref.130 Ref.131 Ref.132 Ref.133 Ref.134 Ref.135 Ref.137 Ref.138 Ref.139 Ref.141 Ref.143 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.103 Ref.114 Ref.136 Ref.140 Ref.142
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.
Sequence similarities	Belongs to the APP family. Contains 1 BPTI/Kunitz inhibitor domain.
Mass spectrometry	Molecular mass is 6461.6 Da from positions 712 - 767. Determined by MALDI. Ref.60 Molecular mass is 6451.6 Da from positions 714 - 770. Determined by MALDI. Ref.60 Molecular mass is 6436.8 Da from positions 715 - 769. Determined by MALDI. Ref.60 Molecular mass is 5752.5 Da from positions 719 - 767. Determined by MALDI. Ref.60
Sequence caution	The sequence AAA58727.1 differs from that shown. Reason: Contamination by an Alu repeat.

Ontologies

Keywords
Biological process	Apoptosis Cell adhesion Endocytosis Notch signaling pathway
Cellular component	Amyloid Coated pit Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Alzheimer disease Amyloidosis Disease mutation Neurodegeneration
Domain	Signal Transmembrane Transmembrane helix
Ligand	Copper Heparin-binding Iron Metal-binding Zinc
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2 phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB Notch signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW adult locomotory behavior Inferred from sequence or structural similarity. Source: UniProtKB axon cargo transport Inferred from sequence or structural similarity. Source: UniProtKB axon midline choice point recognition Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cellular copper ion homeostasis Inferred from sequence or structural similarity. Source: UniProtKB cholesterol metabolic process Inferred from electronic annotation. Source: Compara collateral sprouting in absence of injury Inferred from sequence or structural similarity. Source: UniProtKB dendrite development Inferred from sequence or structural similarity. Source: UniProtKB endocytosis Inferred from sequence or structural similarity. Source: UniProtKB extracellular matrix organization Inferred from sequence or structural similarity. Source: UniProtKB forebrain development Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome ionotropic glutamate receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB mRNA polyadenylation Inferred from sequence or structural similarity. Source: UniProtKB mating behavior Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of neuron differentiation Inferred from electronic annotation. Source: Compara neuromuscular process controlling balance Inferred from electronic annotation. Source: Compara neuron apoptotic process Inferred from mutant phenotype Ref.89. Source: UniProtKB neuron remodeling Inferred from sequence or structural similarity. Source: UniProtKB nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of epidermal growth factor-activated receptor activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of multicellular organism growth Inferred from sequence or structural similarity. Source: UniProtKB regulation of protein binding Inferred from electronic annotation. Source: Compara regulation of synapse structure and activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of translation Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from electronic annotation. Source: Compara smooth endoplasmic reticulum calcium ion homeostasis Inferred from electronic annotation. Source: Compara suckling behavior Inferred from electronic annotation. Source: Compara synaptic growth at neuromuscular junction Inferred from electronic annotation. Source: Compara visual learning Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB apical part of cell Inferred from electronic annotation. Source: Compara axon Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from direct assay PubMed 7593229. Source: UniProtKB ciliary rootlet Inferred from electronic annotation. Source: Compara coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome dendritic shaft Inferred from direct assay PubMed 11988176. Source: MGI dendritic spine Inferred from direct assay PubMed 11988176. Source: MGI extracellular region Traceable author statement. Source: Reactome integral to plasma membrane Traceable author statement Ref.78. Source: ProtInc neuromuscular junction Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara platelet alpha granule lumen Traceable author statement. Source: Reactome spindle midzone Inferred from electronic annotation. Source: Compara synapse Inferred from direct assay PubMed 11988176. Source: MGI
Molecular_function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB heparin binding Inferred from electronic annotation. Source: UniProtKB-KW peptidase activator activity Inferred from electronic annotation. Source: Compara serine-type endopeptidase inhibitor activity Inferred from direct assay PubMed 10652580. Source: UniProtKB transition metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-821758,EBI-821758
AGRN	P31696	3	EBI-2431589,EBI-457650	From a different organism.
APBA1	Q02410	3	EBI-77613,EBI-368690
APBB1	O00213	5	EBI-77613,EBI-81694
APBB2	Q92870	2	EBI-77613,EBI-79277
APLP1	P51693	2	EBI-302641,EBI-74648
APLP2	Q06481	2	EBI-302641,EBI-79306
APOA1	P02647	5	EBI-77613,EBI-701692
BLMH	Q13867	2	EBI-302641,EBI-718504
COL18A1	P39060	2	EBI-821758,EBI-2566375
FLOT1	O75955	5	EBI-77613,EBI-603643
FOS	P01100	3	EBI-77613,EBI-852851
HOMER3	Q9NSC5	3	EBI-302661,EBI-748420
HSD17B10	Q99714	4	EBI-77613,EBI-79964
ITM2A	O43736	3	EBI-302641,EBI-2431769
JUN	P05412	2	EBI-77613,EBI-852823
MAPK8IP1	Q9UQF2	4	EBI-77613,EBI-78404
Mapk8ip1	Q9WVI9-1	2	EBI-77613,EBI-288461	From a different organism.
MAPT	P10636	9	EBI-77613,EBI-366182
MT-ND3	P03897	2	EBI-821758,EBI-1246249
NF1	P21359	3	EBI-77613,EBI-1172917
NGFR	P08138	2	EBI-77613,EBI-1387782
Ngfr	P07174	2	EBI-2431589,EBI-1038810	From a different organism.
PCBD1	P61457	2	EBI-77613,EBI-740475
PDIA3	P30101	3	EBI-77613,EBI-979862
PIN1	Q13526	2	EBI-302641,EBI-714158
PSEN1	P49768	6	EBI-77613,EBI-297277
SHC1	P29353	5	EBI-77613,EBI-78835
SHC3	Q92529	2	EBI-77613,EBI-79084
SLC40A1	Q9NP59	4	EBI-77613,EBI-725153
Slc5a7	Q8BGY9	2	EBI-77613,EBI-2010752	From a different organism.
SPON1	Q9HCB6	3	EBI-302641,EBI-2431846
TGFB1	P01137	2	EBI-77613,EBI-779636
TGFB2	P61812	6	EBI-77613,EBI-779581
TNFRSF21	O75509	3	EBI-77613,EBI-2313231
TP53BP2	Q13625	3	EBI-77613,EBI-77642

Alternative products

This entry describes 11 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Experimental confirmation may be lacking for some isoforms.

Isoform APP770 (identifier: P05067-1)

Also known as: PreA4 770;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: A major isoform.

Isoform APP305 (identifier: P05067-2)

The sequence of this isoform differs from the canonical sequence as follows:
     290-305: VCSEQAETGPCRAMIS → KWYKEVHSGQARWLML
     306-770: Missing.

Isoform L-APP677 (identifier: P05067-3)

The sequence of this isoform differs from the canonical sequence as follows:
     289-289: E → V
     290-364: Missing.
     637-654: Missing.

Note: The L-isoforms are referred to as appicans.

Isoform APP695 (identifier: P05067-4)

Also known as: PreA4 695;

The sequence of this isoform differs from the canonical sequence as follows:
     289-289: E → V
     290-364: Missing.

Note: A major isoform.

Isoform L-APP696 (identifier: P05067-5)

The sequence of this isoform differs from the canonical sequence as follows:
     289-289: E → V
     290-345: Missing.
     637-654: Missing.

Note: The L-isoforms are referred to as appicans.

Isoform APP714 (identifier: P05067-6)

The sequence of this isoform differs from the canonical sequence as follows:
     289-289: E → V
     290-345: Missing.

Isoform L-APP733 (identifier: P05067-7)

The sequence of this isoform differs from the canonical sequence as follows:
     345-345: M → I
     346-364: Missing.
     637-654: Missing.

Note: The L-isoforms are referred to as appicans.

Isoform APP751 (identifier: P05067-8)

Also known as: PreA4 751;

The sequence of this isoform differs from the canonical sequence as follows:
     345-345: M → I
     346-364: Missing.

Note: A major isoform.

Isoform L-APP752 (identifier: P05067-9)

The sequence of this isoform differs from the canonical sequence as follows:
     637-654: Missing.

Isoform APP639 (identifier: P05067-10)

The sequence of this isoform differs from the canonical sequence as follows:
     19-74: Missing.
     289-363: Missing.
     364-364: L → V

Isoform 11 (identifier: P05067-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MLPGLALLLLAAWTARALE → MDQLEDLLVLFINY
     345-364: MSQSLLKTTQEPLARDPVKL → I

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.17 Ref.18

Chain

18 – 770

753

Amyloid beta A4 protein

PRO_0000000088

Chain

18 – 687

670

Soluble APP-alpha

PRO_0000000089

Chain

18 – 671

654

Soluble APP-beta

PRO_0000000090

Chain

18 – 286

269

N-APP

PRO_0000381966

Chain

672 – 770

99

C99

PRO_0000000091

Chain

672 – 713

42

Beta-amyloid protein 42

PRO_0000000092

Chain

672 – 711

40

Beta-amyloid protein 40

PRO_0000000093

Chain

688 – 770

83

C83

PRO_0000000094

Peptide

688 – 713

26

P3(42)

PRO_0000000095

Peptide

688 – 711

24

P3(40)

PRO_0000000096

Chain

691 – 770

80

C80

PRO_0000384574

Chain

712 – 770

59

Gamma-secretase C-terminal fragment 59

PRO_0000000097

Chain

714 – 770

57

Gamma-secretase C-terminal fragment 57

PRO_0000000098

Chain

721 – 770

50

Gamma-secretase C-terminal fragment 50 By similarity

PRO_0000000099

Chain

740 – 770

31

C31

PRO_0000000100

Regions

Topological domain

18 – 699

682

Extracellular Potential

Transmembrane

700 – 723

24

Helical; Potential

Topological domain

724 – 770

47

Cytoplasmic Potential

Domain

291 – 341

51

BPTI/Kunitz inhibitor

Region

96 – 110

15

Heparin-binding

Region

181 – 188

8

Zinc-binding

Region

391 – 423

33

Heparin-binding

Region

491 – 522

32

Heparin-binding

Region

523 – 540

18

Collagen-binding

Region

732 – 751

20

Interaction with G(o)-alpha

Motif

724 – 734

11

Basolateral sorting signal

Motif

759 – 762

4

NPXY motif; contains endocytosis signal

Compositional bias

230 – 260

31

Asp/Glu-rich (acidic)

Compositional bias

274 – 280

7

Poly-Thr

Sites

Metal binding

147

1

Copper 1

Metal binding

151

1

Copper 1

Metal binding

168

1

Copper 1

Metal binding

677

1

Copper or zinc 2

Metal binding

681

1

Copper or zinc 2 Probable

Metal binding

684

1

Copper or zinc 2

Metal binding

685

1

Copper or zinc 2

Site

144

1

Required for Cu(2+) reduction

Site

301 – 302

2

Reactive bond

Site

671 – 672

2

Cleavage; by beta-secretase

Site

672 – 673

2

Cleavage; by caspase-6; when associated with variant 670-N-L-671

Site

687 – 688

2

Cleavage; by alpha-secretase

Site

690 – 691

2

Cleavage; by theta-secretase

Site

704

1

Implicated in free radical propagation By similarity

Site

706

1

Susceptible to oxidation

Site

711 – 712

2

Cleavage; by gamma-secretase; site 1

Site

713 – 714

2

Cleavage; by gamma-secretase; site 2

Site

720 – 721

2

Cleavage; by gamma-secretase; site 3

Site

739 – 740

2

Cleavage; by caspase-6, caspase-8 or caspase-9

Amino acid modifications

Modified residue

198

1

Phosphoserine; by CK2 Ref.83

Modified residue

206

1

Phosphoserine; by CK1 Ref.83

Modified residue

729

1

Phosphothreonine By similarity

Modified residue

730

1

Phosphoserine; by APP-kinase I By similarity

Modified residue

743

1

Phosphothreonine; by CDK5 and MAPK10 Ref.73 Ref.83

Modified residue

757

1

Phosphotyrosine; alternate Ref.83

Modified residue

757

1

Phosphotyrosine; by ABL1; alternate By similarity

Glycosylation

542

1

N-linked (GlcNAc...) Ref.84

Glycosylation

571

1

N-linked (GlcNAc...) Probable

Glycosylation

614

1

O-linked (GalNAc...) Ref.33

Glycosylation

623

1

O-linked (GalNAc...) Ref.33

Glycosylation

628

1

O-linked (GalNAc...) Ref.33

Glycosylation

633

1

O-linked (GalNAc...) Ref.93

Glycosylation

651

1

O-linked (GalNAc...) Ref.93

Glycosylation

652

1

O-linked (GalNAc...) Ref.93

Glycosylation

656

1

O-linked (Xyl...) (chondroitin sulfate); in L-APP isoforms Ref.93

Glycosylation

659

1

O-linked (GalNAc...)

Glycosylation

663

1

O-linked (GalNAc...) Probable

Glycosylation

667

1

O-linked (GalNAc...) Probable

Glycosylation

679

1

O-linked (GalNAc...) Ref.33

Glycosylation

697

1

O-linked (GalNAc...) Ref.33

Disulfide bond

38 ↔ 62

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

73 ↔ 117

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

98 ↔ 105

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

133 ↔ 187

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

144 ↔ 174

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

158 ↔ 186

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

291 ↔ 341

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

300 ↔ 324

Ref.75 Ref.108 Ref.109 Ref.112

Disulfide bond

316 ↔ 337

Ref.75 Ref.108 Ref.109 Ref.112

Natural variations

Alternative sequence

1 – 19

19

MLPGL…ARALE → MDQLEDLLVLFINY in isoform 11.

VSP_045446

Alternative sequence

19 – 74

56

Missing in isoform APP639.

VSP_009116

Alternative sequence

289 – 363

75

Missing in isoform APP639.

VSP_009117

Alternative sequence

289

1

E → V in isoform APP695, isoform L-APP696, isoform L-APP677 and isoform APP714.

VSP_000002

Alternative sequence

290 – 364

75

Missing in isoform APP695 and isoform L-APP677.

VSP_000004

Alternative sequence

290 – 345

56

Missing in isoform L-APP696 and isoform APP714.

VSP_000003

Alternative sequence

290 – 305

16

VCSEQ…RAMIS → KWYKEVHSGQARWLML in isoform APP305.

VSP_000005

Alternative sequence

306 – 770

465

Missing in isoform APP305.

VSP_000006

Alternative sequence

345 – 364

20

MSQSL…DPVKL → I in isoform 11.

VSP_045447

Alternative sequence

345

1

M → I in isoform L-APP733 and isoform APP751.

VSP_000007

Alternative sequence

346 – 364

19

Missing in isoform L-APP733 and isoform APP751.

VSP_000008

Alternative sequence

364

1

L → V in isoform APP639.

VSP_009118

Alternative sequence

637 – 654

18

Missing in isoform L-APP677, isoform L-APP696, isoform L-APP733 and isoform L-APP752.

VSP_000009

Natural variant

501

1

E → K. Ref.10
Corresponds to variant rs45588932 [ dbSNP | Ensembl ].

VAR_022315

Natural variant

665

1

E → D in a patient with late onset Alzheimer disease. Ref.126

VAR_010107

Natural variant

670 – 671

2

KM → NL in AD1.

VAR_000015

Natural variant

678

1

D → N in AD1. Ref.25

VAR_044424

Natural variant

692

1

A → G in AD1; Flemish mutation; increases the solubility of processed beta-amyloid peptides and increases the stability of peptide oligomers. Ref.121 Ref.130 Ref.137

VAR_000016

Natural variant

693

1

E → G in AD1. Ref.120 Ref.138

VAR_014215

Natural variant

693

1

E → K in CAA-APP; Italian type.

VAR_014216

Natural variant

693

1

E → Q in CAA-APP; Dutch type. Ref.114

VAR_000017

Natural variant

694

1

D → N in CAA-APP; Iowa type. Ref.136 Ref.140

VAR_014217

Natural variant

705

1

L → V in CAA-APP; Italian type. Ref.142

VAR_032276

Natural variant

713

1

A → T in AD1. Ref.124 Ref.141

VAR_000019

Natural variant

713

1

A → V in one chronic schizophrenia patient; unknown pathological significance. Ref.123
Corresponds to variant rs1800557 [ dbSNP | Ensembl ].

VAR_000018

Natural variant

714

1

T → A in AD1. Ref.139

VAR_032277

Natural variant

714

1

T → I in AD1; increased beta-APP42/beta-APP40 ratio. Ref.135 Ref.143

VAR_014218

Natural variant

715

1

V → M in AD1; decreased beta-APP40/total APP-beta. Ref.131

VAR_010108

Natural variant

716

1

I → V in AD1. Ref.129

VAR_000020

Natural variant

717

1

V → F in AD1. Ref.23 Ref.119 Ref.125 Ref.127

VAR_000023

Natural variant

717

1

V → G in AD1. Ref.23 Ref.118

VAR_000022

Natural variant

717

1

V → I in AD1. Ref.23 Ref.115 Ref.116 Ref.117 Ref.125 Ref.128 Ref.132

VAR_000021

Natural variant

717

1

V → L in AD1. Ref.134

VAR_014219

Natural variant

723

1

L → P in AD1. Ref.133

VAR_010109

Experimental info

Mutagenesis

99 – 102

4

KRGR → NQGG: Reduced heparin-binding. Ref.45

Mutagenesis

137

1

H → N: Binds copper. Forms dimer. Ref.44

Mutagenesis

141

1

M → T: Binds copper. Forms dimer. Ref.44

Mutagenesis

144

1

C → S: Binds copper. No dimer formation. No copper reducing activity. Ref.44 Ref.57

Mutagenesis

147 – 149

3

HLH → ALA: 50% decrease in copper reducing activity. Ref.44 Ref.57 Ref.69

Mutagenesis

147

1

H → A: Some decrease in copper reducing activity. Ref.44 Ref.69

Mutagenesis

147

1

H → N: Binds copper. Forms dimer. Ref.44 Ref.69

Mutagenesis

147

1

H → Y: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.44 Ref.69

Mutagenesis

151

1

H → K: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.44 Ref.69

Mutagenesis

151

1

H → N: Binds copper. Forms dimer. Ref.44 Ref.69

Mutagenesis

198

1

S → A: Greatly reduced casein kinase phosphorylation. Ref.74 Ref.78

Mutagenesis

206

1

S → A: Reduced casein kinase phosphorylation. Ref.74 Ref.78

Mutagenesis

499

1

R → A: Reduced affinity for heparin; when associated with A-503. Ref.106

Mutagenesis

503

1

K → A: Reduced affinity for heparin; when associated with A-499. Ref.106

Mutagenesis

656

1

S → A: Abolishes chondroitin sulfate binding in L-APP733 isoform. Ref.37

Mutagenesis

676

1

R → G: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.53

Mutagenesis

681

1

Y → F: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.53

Mutagenesis

684

1

H → R: Only 23% zinc-induced beta-APP (28) peptide aggregation. Ref.53

Mutagenesis

704

1

G → V: Reduced protein oxidation. No hippocampal neuron toxicity.

Mutagenesis

706

1

M → L: Reduced lipid peroxidation inhibition. Ref.38 Ref.54

Mutagenesis

706

1

M → V: No free radical production. No hippocampal neuron toxicity. Ref.38 Ref.54

Mutagenesis

717

1

V → C or S: Unchanged beta-APP42/total APP-beta ratio. Ref.46 Ref.135

Mutagenesis

717

1

V → F, G or I: Increased beta-APP42/beta-APP40 ratio. Ref.46 Ref.135

Mutagenesis

717

1

V → K: Decreased beta-APP42/total APP-beta ratio. Ref.46 Ref.135

Mutagenesis

717

1

V → M: Increased beta-APP42/beta-APP40 ratio. No change in apoptosis after caspase cleavage. Ref.46 Ref.135

Mutagenesis

728

1

Y → A: No effect on APBA1 nor APBB1 binding. Greatly reduces the binding to APPBP2. APP internalization unchanged. No change in beta-APP42 secretion. Ref.48 Ref.52 Ref.56

Mutagenesis

739

1

D → A: No cleavage by caspases during apoptosis. Ref.60 Ref.76 Ref.79

Mutagenesis

739

1

D → N: No effect on FADD-induced apoptosis. Ref.60 Ref.76 Ref.79

Mutagenesis

743

1

T → A: Greatly reduces the binding to SHC1 and APBB family members; no effect on NGF-stimulated neurite extension. Ref.77 Ref.80 Ref.81 Ref.83

Mutagenesis

743

1

T → E: Reduced NGF-stimulated neurite extension. No effect on APP maturation. Ref.77 Ref.80 Ref.81 Ref.83

Mutagenesis

756

1

G → A: APP internalization unchanged. No change in beta-APP42 secretion. Ref.56

Mutagenesis

757

1

Y → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.48 Ref.56 Ref.68 Ref.83

Mutagenesis

757

1

Y → G: Loss of binding to MAPK8IP1, APBA1, APBB1, APPBP2 and SHC1. Ref.48 Ref.56 Ref.68 Ref.83

Mutagenesis

759

1

N → A: No binding to APBA1, no effect on APBB1 binding. Little APP internalization. Reduced beta-APP42 secretion. Ref.48 Ref.56

Mutagenesis

760

1

P → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.56

Mutagenesis

762

1

Y → A: Loss of binding to APBA1 and APBB1. APP internalization unchanged. No change in beta-APP42 secretion. Ref.48 Ref.56

Sequence conflict

15 – 16

2

AR → VW in CAA31830. Ref.3

Sequence conflict

647

1

D → E in AAA51722. Ref.36

Sequence conflict

724

1

Missing in AAB26263. Ref.23

Sequence conflict

724

1

Missing in AAB26264. Ref.23

Sequence conflict

731

1

I → N in AAB26263. Ref.23

Sequence conflict

731

1

I → N in AAB26264. Ref.23

Sequence conflict

731

1

I → N in AAB26265. Ref.23

Sequence conflict

757

1

Y → S in AAA35540. Ref.31

Secondary structure

1

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770

Helix Strand Turn

Details...

Beta strand

33 – 35

3

Beta strand

43 – 45

3

Turn

47 – 49

3

Beta strand

52 – 54

3

Helix

66 – 76

11

Beta strand

82 – 87

6

Beta strand

92 – 94

3

Beta strand

97 – 99

3

Helix

100 – 102

3

Beta strand

103 – 106

4

Beta strand

110 – 112

3

Beta strand

115 – 119

5

Beta strand

134 – 139

6

Helix

147 – 160

14

Beta strand

163 – 174

12

Turn

175 – 177

3

Beta strand

178 – 188

11

Helix

288 – 292

5

Beta strand

299 – 301

3

Beta strand

304 – 310

7

Turn

311 – 314

4

Beta strand

315 – 321

7

Beta strand

323 – 325

3

Beta strand

331 – 333

3

Helix

334 – 341

8

Helix

374 – 380

7

Helix

389 – 418

30

Beta strand

421 – 423

3

Helix

425 – 480

56

Beta strand

482 – 484

3

Helix

487 – 518

32

Helix

520 – 546

27

Helix

547 – 550

4

Helix

552 – 566

15

Helix

673 – 675

3

Beta strand

679 – 682

4

Beta strand

683 – 685

3

Beta strand

688 – 691

4

Helix

695 – 697

3

Beta strand

698 – 700

3

Beta strand

702 – 705

4

Beta strand

707 – 712

6

Helix

744 – 754

11

Beta strand

755 – 758

4

Beta strand

763 – 765

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform APP770 (PreA4 770) [UniParc]. Last modified November 1, 1991. Version 3. Checksum: A12EE761403740F5	FASTA	770	86,943
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 310 320 330 340 350 360 RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAMSQSLL KTTQEPLARD 370 380 390 400 410 420 PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA 430 440 450 460 470 480 KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL 490 500 510 520 530 540 QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER 550 560 570 580 590 600 MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET 610 620 630 640 650 660 KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN 670 680 690 700 710 720 IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL 730 740 750 760 770 VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN
	Isoform APP305 [UniParc]. Checksum: D1CCD7237262687A	FASTA	305	34,358
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREK WYKEVHSGQA RWLML
	Isoform L-APP677 [UniParc]. Checksum: 48334D3EEF26990E	FASTA	677	76,760
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVRVP TTAASTPDAV 310 320 330 340 350 360 DKYLETPGDE NEHAHFQKAK ERLEAKHRER MSQVMREWEE AERQAKNLPK ADKKAVIQHF 370 380 390 400 410 420 QEKVESLEQE AANERQQLVE THMARVEAML NDRRRLALEN YITALQAVPP RPRHVFNMLK 430 440 450 460 470 480 KYVRAEQKDR QHTLKHFEHV RMVDPKKAAQ IRSQVMTHLR VIYERMNQSL SLLYNVPAVA 490 500 510 520 530 540 EEIQDEVDEL LQKEQNYSDD VLANMISEPR ISYGNDALMP SLTETKTTVE LLPVNGEFSL 550 560 570 580 590 600 DDLQPWHSFG ADSVPANTEN EGSGLTNIKT EEISEVKMDA EFRHDSGYEV HHQKLVFFAE 610 620 630 640 650 660 DVGSNKGAII GLMVGGVVIA TVIVITLVML KKKQYTSIHH GVVEVDAAVT PEERHLSKMQ 670 QNGYENPTYK FFEQMQN
	Isoform APP695 (PreA4 695) [UniParc]. Checksum: 4F6EA0139F969D56	FASTA	695	78,663
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVRVP TTAASTPDAV 310 320 330 340 350 360 DKYLETPGDE NEHAHFQKAK ERLEAKHRER MSQVMREWEE AERQAKNLPK ADKKAVIQHF 370 380 390 400 410 420 QEKVESLEQE AANERQQLVE THMARVEAML NDRRRLALEN YITALQAVPP RPRHVFNMLK 430 440 450 460 470 480 KYVRAEQKDR QHTLKHFEHV RMVDPKKAAQ IRSQVMTHLR VIYERMNQSL SLLYNVPAVA 490 500 510 520 530 540 EEIQDEVDEL LQKEQNYSDD VLANMISEPR ISYGNDALMP SLTETKTTVE LLPVNGEFSL 550 560 570 580 590 600 DDLQPWHSFG ADSVPANTEN EVEPVDARPA ADRGLTTRPG SGLTNIKTEE ISEVKMDAEF 610 620 630 640 650 660 RHDSGYEVHH QKLVFFAEDV GSNKGAIIGL MVGGVVIATV IVITLVMLKK KQYTSIHHGV 670 680 690 VEVDAAVTPE ERHLSKMQQN GYENPTYKFF EQMQN
	Isoform L-APP696 [UniParc]. Checksum: 66DFDFFCFDB75A72	FASTA	696	78,866
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVRVS QSLLKTTQEP 310 320 330 340 350 360 LARDPVKLPT TAASTPDAVD KYLETPGDEN EHAHFQKAKE RLEAKHRERM SQVMREWEEA 370 380 390 400 410 420 ERQAKNLPKA DKKAVIQHFQ EKVESLEQEA ANERQQLVET HMARVEAMLN DRRRLALENY 430 440 450 460 470 480 ITALQAVPPR PRHVFNMLKK YVRAEQKDRQ HTLKHFEHVR MVDPKKAAQI RSQVMTHLRV 490 500 510 520 530 540 IYERMNQSLS LLYNVPAVAE EIQDEVDELL QKEQNYSDDV LANMISEPRI SYGNDALMPS 550 560 570 580 590 600 LTETKTTVEL LPVNGEFSLD DLQPWHSFGA DSVPANTENE GSGLTNIKTE EISEVKMDAE 610 620 630 640 650 660 FRHDSGYEVH HQKLVFFAED VGSNKGAIIG LMVGGVVIAT VIVITLVMLK KKQYTSIHHG 670 680 690 VVEVDAAVTP EERHLSKMQQ NGYENPTYKF FEQMQN
	Isoform APP714 [UniParc]. Checksum: 124EA691773DC13B	FASTA	714	80,769
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVRVS QSLLKTTQEP 310 320 330 340 350 360 LARDPVKLPT TAASTPDAVD KYLETPGDEN EHAHFQKAKE RLEAKHRERM SQVMREWEEA 370 380 390 400 410 420 ERQAKNLPKA DKKAVIQHFQ EKVESLEQEA ANERQQLVET HMARVEAMLN DRRRLALENY 430 440 450 460 470 480 ITALQAVPPR PRHVFNMLKK YVRAEQKDRQ HTLKHFEHVR MVDPKKAAQI RSQVMTHLRV 490 500 510 520 530 540 IYERMNQSLS LLYNVPAVAE EIQDEVDELL QKEQNYSDDV LANMISEPRI SYGNDALMPS 550 560 570 580 590 600 LTETKTTVEL LPVNGEFSLD DLQPWHSFGA DSVPANTENE VEPVDARPAA DRGLTTRPGS 610 620 630 640 650 660 GLTNIKTEEI SEVKMDAEFR HDSGYEVHHQ KLVFFAEDVG SNKGAIIGLM VGGVVIATVI 670 680 690 700 710 VITLVMLKKK QYTSIHHGVV EVDAAVTPEE RHLSKMQQNG YENPTYKFFE QMQN
	Isoform L-APP733 [UniParc]. Checksum: 44528239D68A53EE	FASTA	733	82,916
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 310 320 330 340 350 360 RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAIPTTAA STPDAVDKYL 370 380 390 400 410 420 ETPGDENEHA HFQKAKERLE AKHRERMSQV MREWEEAERQ AKNLPKADKK AVIQHFQEKV 430 440 450 460 470 480 ESLEQEAANE RQQLVETHMA RVEAMLNDRR RLALENYITA LQAVPPRPRH VFNMLKKYVR 490 500 510 520 530 540 AEQKDRQHTL KHFEHVRMVD PKKAAQIRSQ VMTHLRVIYE RMNQSLSLLY NVPAVAEEIQ 550 560 570 580 590 600 DEVDELLQKE QNYSDDVLAN MISEPRISYG NDALMPSLTE TKTTVELLPV NGEFSLDDLQ 610 620 630 640 650 660 PWHSFGADSV PANTENEGSG LTNIKTEEIS EVKMDAEFRH DSGYEVHHQK LVFFAEDVGS 670 680 690 700 710 720 NKGAIIGLMV GGVVIATVIV ITLVMLKKKQ YTSIHHGVVE VDAAVTPEER HLSKMQQNGY 730 ENPTYKFFEQ MQN
	Isoform APP751 (PreA4 751) [UniParc]. Checksum: C987C557C5A3714E	FASTA	751	84,819
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 310 320 330 340 350 360 RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAIPTTAA STPDAVDKYL 370 380 390 400 410 420 ETPGDENEHA HFQKAKERLE AKHRERMSQV MREWEEAERQ AKNLPKADKK AVIQHFQEKV 430 440 450 460 470 480 ESLEQEAANE RQQLVETHMA RVEAMLNDRR RLALENYITA LQAVPPRPRH VFNMLKKYVR 490 500 510 520 530 540 AEQKDRQHTL KHFEHVRMVD PKKAAQIRSQ VMTHLRVIYE RMNQSLSLLY NVPAVAEEIQ 550 560 570 580 590 600 DEVDELLQKE QNYSDDVLAN MISEPRISYG NDALMPSLTE TKTTVELLPV NGEFSLDDLQ 610 620 630 640 650 660 PWHSFGADSV PANTENEVEP VDARPAADRG LTTRPGSGLT NIKTEEISEV KMDAEFRHDS 670 680 690 700 710 720 GYEVHHQKLV FFAEDVGSNK GAIIGLMVGG VVIATVIVIT LVMLKKKQYT SIHHGVVEVD 730 740 750 AAVTPEERHL SKMQQNGYEN PTYKFFEQMQ N
	Isoform L-APP752 [UniParc]. Checksum: 074CFF767CBED2E0	FASTA	752	85,040
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 70 80 90 100 110 120 TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 130 140 150 160 170 180 EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 190 200 210 220 230 240 GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 250 260 270 280 290 300 EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 310 320 330 340 350 360 RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAMSQSLL KTTQEPLARD 370 380 390 400 410 420 PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA 430 440 450 460 470 480 KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL 490 500 510 520 530 540 QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER 550 560 570 580 590 600 MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET 610 620 630 640 650 660 KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEGSGL TNIKTEEISE VKMDAEFRHD 670 680 690 700 710 720 SGYEVHHQKL VFFAEDVGSN KGAIIGLMVG GVVIATVIVI TLVMLKKKQY TSIHHGVVEV 730 740 750 DAAVTPEERH LSKMQQNGYE NPTYKFFEQM QN
	Isoform APP639 [UniParc]. Checksum: C4120DEC51A59A95	FASTA	639	72,553
	10 20 30 40 50 60 MLPGLALLLL AAWTARALEV YPELQITNVV EANQPVTIQN WCKRGRKQCK THPHFVIPYR 70 80 90 100 110 120 CLVGEFVSDA LLVPDKCKFL HQERMDVCET HLHWHTVAKE TCSEKSTNLH DYGMLLPCGI 130 140 150 160 170 180 DKFRGVEFVC CPLAEESDNV DSADAEEDDS DVWWGGADTD YADGSEDKVV EVAEEEEVAE 190 200 210 220 230 240 VEEEEADDDE DDEDGDEVEE EAEEPYEEAT ERTTSIATTT TTTTESVEEV VRVPTTAAST 250 260 270 280 290 300 PDAVDKYLET PGDENEHAHF QKAKERLEAK HRERMSQVMR EWEEAERQAK NLPKADKKAV 310 320 330 340 350 360 IQHFQEKVES LEQEAANERQ QLVETHMARV EAMLNDRRRL ALENYITALQ AVPPRPRHVF 370 380 390 400 410 420 NMLKKYVRAE QKDRQHTLKH FEHVRMVDPK KAAQIRSQVM THLRVIYERM NQSLSLLYNV 430 440 450 460 470 480 PAVAEEIQDE VDELLQKEQN YSDDVLANMI SEPRISYGND ALMPSLTETK TTVELLPVNG 490 500 510 520 530 540 EFSLDDLQPW HSFGADSVPA NTENEVEPVD ARPAADRGLT TRPGSGLTNI KTEEISEVKM 550 560 570 580 590 600 DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IATVIVITLV MLKKKQYTSI 610 620 630 HHGVVEVDAA VTPEERHLSK MQQNGYENPT YKFFEQMQN
	Isoform 11 [UniParc]. Checksum: 843411EFBDEFACE3	FASTA	746	84,521
	10 20 30 40 50 60 MDQLEDLLVL FINYVPTDGN AGLLAEPQIA MFCGRLNMHM NVQNGKWDSD PSGTKTCIDT 70 80 90 100 110 120 KEGILQYCQE VYPELQITNV VEANQPVTIQ NWCKRGRKQC KTHPHFVIPY RCLVGEFVSD 130 140 150 160 170 180 ALLVPDKCKF LHQERMDVCE THLHWHTVAK ETCSEKSTNL HDYGMLLPCG IDKFRGVEFV 190 200 210 220 230 240 CCPLAEESDN VDSADAEEDD SDVWWGGADT DYADGSEDKV VEVAEEEEVA EVEEEEADDD 250 260 270 280 290 300 EDDEDGDEVE EEAEEPYEEA TERTTSIATT TTTTTESVEE VVREVCSEQA ETGPCRAMIS 310 320 330 340 350 360 RWYFDVTEGK CAPFFYGGCG GNRNNFDTEE YCMAVCGSAI PTTAASTPDA VDKYLETPGD 370 380 390 400 410 420 ENEHAHFQKA KERLEAKHRE RMSQVMREWE EAERQAKNLP KADKKAVIQH FQEKVESLEQ 430 440 450 460 470 480 EAANERQQLV ETHMARVEAM LNDRRRLALE NYITALQAVP PRPRHVFNML KKYVRAEQKD 490 500 510 520 530 540 RQHTLKHFEH VRMVDPKKAA QIRSQVMTHL RVIYERMNQS LSLLYNVPAV AEEIQDEVDE 550 560 570 580 590 600 LLQKEQNYSD DVLANMISEP RISYGNDALM PSLTETKTTV ELLPVNGEFS LDDLQPWHSF 610 620 630 640 650 660 GADSVPANTE NEVEPVDARP AADRGLTTRP GSGLTNIKTE EISEVKMDAE FRHDSGYEVH 670 680 690 700 710 720 HQKLVFFAED VGSNKGAIIG LMVGGVVIAT VIVITLVMLK KKQYTSIHHG VVEVDAAVTP 730 740 EERHLSKMQQ NGYENPTYKF FEQMQN

References

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[1]	"The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor." Kang J., Lemaire H.-G., Unterbeck A., Salbaum J.M., Masters C.L., Grzeschik K.-H., Multhaup G., Beyreuther K., Mueller-Hill B. Nature 325:733-736(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695). Tissue: Brain.
[2]	"A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors." Ponte P., Gonzalez-Dewhitt P., Schilling J., Miller J., Hsu D., Greenberg B., Davis K., Wallace W., Lieberburg I., Fuller F., Cordell B. Nature 331:525-527(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751). Tissue: Brain.
[3]	"The PreA4(695) precursor protein of Alzheimer's disease A4 amyloid is encoded by 16 exons." Lemaire H.-G., Salbaum J.M., Multhaup G., Kang J., Bayney R.M., Unterbeck A., Beyreuther K., Mueller-Hill B. Nucleic Acids Res. 17:517-522(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP695).
[4]	"Genomic organization of the human amyloid beta-protein precursor gene." Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y. Gene 87:257-263(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770).
[5]	Erratum Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y. Gene 102:291-292(1991) [PubMed] [Europe PMC] [Abstract]
[6]	"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." Koenig G., Moenning U., Czech C., Prior R., Banati R., Schreiter-Gasser U., Bauer J., Masters C.L., Beyreuther K. J. Biol. Chem. 267:10804-10809(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-APP733). Tissue: Leukocyte.
[7]	"A novel method for making nested deletions and its application for sequencing of a 300 kb region of human APP locus." Hattori M., Tsukahara F., Furuhata Y., Tanahashi H., Hirose M., Saito M., Tsukuni S., Sakaki Y. Nucleic Acids Res. 25:1802-1808(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770).
[8]	"Identification of a novel alternative splicing isoform of human amyloid precursor protein gene, APP639." Tang K., Wang C., Shen C., Sheng S., Ravid R., Jing N. Eur. J. Neurosci. 18:102-108(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP639), TISSUE SPECIFICITY. Tissue: Brain.
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP770 AND 11). Tissue: Cerebellum and Hippocampus.
[10]	NIEHS SNPs program Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-501.
[11]	"The DNA sequence of human chromosome 21." 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. Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP305 AND APP751). Tissue: Eye and Pancreas.
[14]	"A cDNA specifying the human amyloid beta precursor protein (ABPP) encodes a 95-kDa polypeptide." Schon E.A., Mita S., Sadlock J., Herbert J. Nucleic Acids Res. 16:9351-9351(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-10. Tissue: Liver.
[15]	Erratum Schon E.A., Mita S., Sadlock J., Herbert J. Nucleic Acids Res. 16:11402-11402(1988) Cited for: SEQUENCE REVISION.
[16]	"Characterization of the 5'-end region and the first two exons of the beta-protein precursor gene." La Fauci G., Lahiri D.K., Salton S.R., Robakis N.K. Biochem. Biophys. Res. Commun. 159:297-304(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
[17]	"Purification of protease nexin II from human fibroblasts." van Nostrand W.E., Cunningham D.D. J. Biol. Chem. 262:8508-8514(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-50. Tissue: Fibroblast.
[18]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-40. Tissue: Platelet.
[19]	"Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease." Tanzi R.E., McClatchey A.I., Lamperti E.D., Villa-Komaroff L., Gusella J.F., Neve R.L. Nature 331:528-530(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 286-366.
[20]	"Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity." Kitaguchi N., Takahashi Y., Tokushima Y., Shiojiri S., Ito H. Nature 331:530-532(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 287-367.
[21]	"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." Zain S.B., Salim M., Chou W.G., Sajdel-Sulkowska E.M., Majocha R.E., Marotta C.A. Proc. Natl. Acad. Sci. U.S.A. 85:929-933(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 507-770. Tissue: Brain cortex.
[22]	"Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I." Beher D., Hesse L., Masters C.L., Multhaup G. J. Biol. Chem. 271:1613-1620(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 523-555, DOMAIN COLLAGEN-BINDING.
[23]	"A system for studying the effect(s) of familial Alzheimer disease mutations on the processing of the beta-amyloid peptide precursor." Denman R.B., Rosenzcwaig R., Miller D.L. Biochem. Biophys. Res. Commun. 192:96-103(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 655-737, VARIANTS AD1 GLY-717; ILE-717 AND PHE-717.
[24]	"Alzheimer's disease amyloid peptide is encoded by two exons and shows similarity to soybean trypsin inhibitor." Johnstone E.M., Chaney M.O., Moore R.E., Ward K.E., Norris F.H., Little S.P. Biochem. Biophys. Res. Commun. 163:1248-1255(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737.
[25]	"Novel amyloid precursor protein gene missense mutation (D678N) in probable familial Alzheimer's disease." Wakutani Y., Watanabe K., Adachi Y., Wada-Isoe K., Urakami K., Ninomiya H., Saido T.C., Hashimoto T., Iwatsubo T., Nakashima K. J. Neurol. Neurosurg. Psych. 75:1039-1042(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 672-723, VARIANT AD1 ASN-678.
[26]	"Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease." Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., Gowing E., Ball M.J. Proc. Natl. Acad. Sci. U.S.A. 90:10836-10840(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-713. Tissue: Blood vessel.
[27]	"Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids." Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., Sinha S., Schlossmacher M., Whaley J., Swindlehurst C. Nature 359:325-327(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-704, TISSUE SPECIFICITY.
[28]	"The amino acid sequence of neuritic plaque amyloid from a familial Alzheimer's disease patient." Wisniewski T., Lalowski M., Levy E., Marques M.R.F., Frangione B. Ann. Neurol. 35:245-246(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-701 AND 707-713.
[29]	"Characterization of beta-amyloid peptide from human cerebrospinal fluid." Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B. J. Neurochem. 61:1965-1968(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-701. Tissue: Cerebrospinal fluid.
[30]	"Amyloid angiopathy of Alzheimer's disease: amino acid composition and partial sequence of a 4,200-dalton peptide isolated from cortical microvessels." Pardridge W.M., Vinters H.V., Yang J., Eisenberg J., Choi T.B., Tourtellotte W.W., Huebner V., Shively J.E. J. Neurochem. 49:1394-1401(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-681. Tissue: Brain cortex.
[31]	"Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease." Goldgaber D., Lerman M.I., McBride O.W., Saffiotti U., Gajdusek D.C. Science 235:877-880(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 674-770. Tissue: Brain.
[32]	"Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus." 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. Science 235:880-884(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 674-703. Tissue: Fetal brain.
[33]	"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." 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. J. Mass Spectrom. 47:591-603(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 609-713, GLYCOSYLATION AT SER-614; SER-623; SER-628; SER-679 AND SER-697. Tissue: Cerebrospinal fluid.
[34]	"BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome." Sun X., He G., Song W. FASEB J. 20:1369-1376(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 691-698, CLEAVAGE BY THETA-SECRETASE.
[35]	"A novel mRNA of the A4 amyloid precursor gene coding for a possibly secreted protein." de Sauvage F., Octave J.-N. Science 245:651-653(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751). Tissue: Brain.
[36]	"Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides." Robakis N.K., Ramakrishna N., Wolfe G., Wisniewski H.M. Proc. Natl. Acad. Sci. U.S.A. 84:4190-4194(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695). Tissue: Brain.
[37]	"The chondroitin sulfate attachment site of appican is formed by splicing out exon 15 of the amyloid precursor gene." Pangalos M.N., Efthimiopoulos S., Shioi J., Robakis N.K. J. Biol. Chem. 270:10388-10391(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF L-APP733, MUTAGENESIS OF SER-656.
[38]	"Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions." Walter M.F., Mason P.E., Mason R.P. Biochem. Biophys. Res. Commun. 233:760-764(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF BETA-AMYLOID PEPTIDE AS LIPID PEROXIDATION INHIBITOR, MUTAGENESIS OF MET-706.
[39]	"Alzheimer's amyloid-beta as a preventive antioxidant for brain lipoproteins." Kontush A. Cell. Mol. Neurobiol. 21:299-315(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION OF BETA-AMYLOID AS ANTIOXIDANT.
[40]	"The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II." 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. Nature 341:144-147(1989) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTITY OF APP WITH NEXIN-II.
[41]	"Protease-specificity of Kunitz inhibitor domain of Alzheimer's disease amyloid protein precursor." Kido H., Fukutomi A., Schilling J., Wang Y., Cordell B., Katunuma N. Biochem. Biophys. Res. Commun. 167:716-721(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEASE-SPECIFICITY OF INHIBITOR DOMAIN.
[42]	"A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease." Bush A.I., Multhaup G., Moir R.D., Williamson T.G., Small D.H., Rumble B., Pollwein P., Beyreuther K., Masters C.L. J. Biol. Chem. 268:16109-16112(1993) [PubMed] [Europe PMC] [Abstract] Cited for: EXTRACELLULAR ZINC-BINDING DOMAIN.
[43]	"Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o)." Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Okamoto T., Murayama Y., Ogata E. Nature 362:75-79(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH G(O).
[44]	"The beta A4 amyloid precursor protein binding to copper." Hesse L., Beher D., Masters C.L., Multhaup G. FEBS Lett. 349:109-116(1994) [PubMed] [Europe PMC] [Abstract] Cited for: EXTRACELLULAR COPPER-BINDING DOMAIN, MUTAGENESIS OF HIS-137; MET-141; CYS-144; HIS-147 AND HIS-151.
[45]	"A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth." Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., Masters C.L. J. Neurosci. 14:2117-2127(1994) [PubMed] [Europe PMC] [Abstract] Cited for: N-TERMINAL HEPARIN-BINDING DOMAIN, MUTAGENESIS OF 99-LYS--ARG-102.
[46]	"Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43)." Maruyama K., Tomita T., Shinozaki K., Kume H., Asada H., Saido T.C., Ishiura S., Iwatsubo T., Obata K. Biochem. Biophys. Res. Commun. 227:730-735(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF VAL-717.
[47]	"APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein." Chow N., Korenberg J.R., Chen X.-N., Neve R.L. J. Biol. Chem. 271:11339-11346(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APP-BP1.
[48]	"The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein." Borg J.-P., Ooi J., Levy E., Margolis B. Mol. Cell. Biol. 16:6229-6241(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APBA1 AND APBB1, MUTAGENESIS OF TYR-728; TYR-757; ASN-759 AND TYR-762.
[49]	"Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein." Guenette S.Y., Chen J., Jondro P.D., Tanzi R.E. Proc. Natl. Acad. Sci. U.S.A. 93:10832-10837(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APBB2.
[50]	"Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease." 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. FEBS Lett. 415:303-307(1997) [PubMed] [Europe PMC] [Abstract] Cited for: HEPARIN-BINDING DOMAINS.
[51]	"An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease." 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. Nature 389:689-695(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF BETA-AMYLOID PEPTIDE WITH HADH2. Tissue: Brain.
[52]	"PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein." Zheng P., Eastman J., Vande Pol S., Pimplikar S.W. Proc. Natl. Acad. Sci. U.S.A. 95:14745-14750(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APPBP2, MUTAGENESIS OF TYR-728.
[53]	"Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease." Liu S.T., Howlett G., Barrow C.J. Biochemistry 38:9373-9378(1999) [PubMed] [Europe PMC] [Abstract] Cited for: BETA-AMYLOID ZINC-BINDING, MUTAGENESIS OF ARG-676; TYR-681 AND HIS-684.
[54]	"Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress." Varadarajan S., Yatin S., Kanski J., Jahanshahi F., Butterfield D.A. Brain Res. Bull. 50:133-141(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IMPORTANCE OF MET-706 IN FREE RADICAL OXIDATIVE STRESS, MUTAGENESIS OF MET-706.
[55]	"Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein." Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., Sakiyama S., Kirino Y., Suzuki T. J. Biol. Chem. 274:2243-2254(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APBA2.
[56]	"Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42." Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W., Selkoe D.J., Chen X., Stokin G.B., Koo E.H. J. Biol. Chem. 274:18851-18856(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENDOCYTOSIS SIGNAL, MUTAGENESIS OF TYR-728; GLY-756; TYR-757; ASN-759; PRO-760 AND TYR-762.
[57]	"Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein." Ruiz F.H., Gonzalez M., Bodini M., Opazo C., Inestrosa N.C. J. Neurochem. 73:1288-1292(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IMPORTANCE OF CYS-144 IN COPPER REDUCTION, MUTAGENESIS OF CYS-144 AND 147-HIS--HIS-149.
[58]	"Lipidation of apolipoprotein E influences its isoform-specific interaction with Alzheimer's amyloid beta peptides." 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. Biochem. J. 348:359-365(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF BETA-AMYLOID WITH APOE.
[59]	"Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology." Wang H.-Y., Lee D.H.S., D'Andrea M.R., Peterson P.A., Shank R.P., Reitz A.B. J. Biol. Chem. 275:5626-5632(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF BETA-APP42 WITH CHRNA7.
[60]	"Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor." Passer B., Pellegrini L., Russo C., Siegel R.M., Lenardo M.J., Schettini G., Bachmann M., Tabaton M., D'Adamio L. J. Alzheimers Dis. 2:289-301(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION OF GAMMA-CTFS BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-739.
[61]	"Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages." Yazawa H., Yu Z.-X., Takeda K., Le Y., Gong W., Ferrans V.J., Oppenheim J.J., Li C.C.H., Wang J.M. FASEB J. 15:2454-2462(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FPRL1.
[62]	"Beta-amyloid peptide-induced apoptosis regulated by a novel protein containing a G protein activation module." 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. J. Biol. Chem. 276:18748-18756(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BBP.
[63]	"Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered structure containing superoxide dismutase-like subunits." 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. J. Biol. Chem. 276:20466-20473(2001) [PubMed] [Europe PMC] [Abstract] Cited for: BETA-AMYLOID COPPER AND ZINC-BINDING.
[64]	"Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease." Scheuermann S., Hambsch B., Hesse L., Stumm J., Schmidt C., Beher D., Bayer T.A., Beyreuther K., Multhaup G. J. Biol. Chem. 276:33923-33929(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[65]	"The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner." Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J. J. Biol. Chem. 276:40288-40292(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APBB1, FUNCTION, SUBCELLULAR LOCATION.
[66]	"Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function." Ohsawa I., Takamura C., Kohsaka S. J. Neurochem. 76:1411-1420(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBLN1.
[67]	"Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II." Rank K.B., Pauley A.M., Bhattacharya K., Wang Z., Evans D.B., Fleck T.J., Johnston J.A., Sharma S.K. FEBS Lett. 514:263-268(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPT, FUNCTION.
[68]	"Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)." Scheinfeld M.H., Roncarati R., Vito P., Lopez P.A., Abdallah M., D'Adamio L. J. Biol. Chem. 277:3767-3775(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP1, MUTAGENESIS OF TYR-757.
[69]	"Contrasting species-dependent modulation of copper-mediated neurotoxicity by the Alzheimer's disease amyloid precursor protein." White A.R., Multhaup G., Galatis D., McKinstry W.J., Parker M.W., Pipkorn R., Beyreuther K., Masters C.L., Cappai R. J. Neurosci. 22:365-376(2002) [PubMed] [Europe PMC] [Abstract] Cited for: COPPER-MEDIATED LIPID PEROXIDATION, MUTAGENESIS OF HIS-147 AND HIS-151.
[70]	"The galvanization of beta-amyloid in Alzheimer's disease." Bush A.I., Tanzi R.E. Proc. Natl. Acad. Sci. U.S.A. 99:7317-7319(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ZINC-BINDING.
[71]	"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." Watanabe N., Araki W., Chui D.H., Makifuchi T., Ihara Y., Tabira T. FASEB J. 18:1013-1015(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ASSOCIATION OF AMYLOID FIBRILS WITH GCP1.
[72]	"Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner." Ghersi E., Noviello C., D'Adamio L. J. Biol. Chem. 279:49105-49112(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ANKS1B.
[73]	"Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein." Suzuki T., Oishi M., Marshak D.R., Czernik A.J., Nairn A.C., Greengard P. EMBO J. 13:1114-1122(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-743.
[74]	"Ectodomain phosphorylation of beta-amyloid precursor protein at two distinct cellular locations." Walter J., Capell A., Hung A.Y., Langen H., Schnoelzer M., Thinakaran G., Sisodia S.S., Selkoe D.J., Haass C. J. Biol. Chem. 272:1896-1903(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY CASEIN KINASES, MUTAGENESIS OF SER-198 AND SER-206.
[75]	"Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide." Multhaup G., Ruppert T., Schlicksupp A., Hesse L., Bill E., Pipkorn R., Masters C.L., Beyreuther K. Biochemistry 37:7224-7230(1998) [PubMed] [Europe PMC] [Abstract] Cited for: COPPER-BINDING, DISULFIDE BOND FORMATION.
[76]	"Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation." 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. Cell 97:395-406(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-739.
[77]	"Role of phosphorylation of Alzheimer's amyloid precursor protein during neuronal differentiation." Ando K., Oishi M., Takeda S., Iijima K., Isohara T., Nairn A.C., Kirino Y., Greengard P., Suzuki T. J. Neurosci. 19:4421-4427(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, MUTAGENESIS OF THR-743.
[78]	"Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2." Walter J., Schindzielorz A., Hartung B., Haass C. J. Biol. Chem. 275:23523-23529(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF CASEIN KINASE PHOSPHORYLATION, MUTAGENESIS OF SER-198 AND SER-206.
[79]	"A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor." Lu D.C., Rabizadeh S., Chandra S., Shayya R.F., Ellerby L.M., Ye X., Salvesen G.S., Koo E.H., Bredesen D.E. Nat. Med. 6:397-404(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-739.
[80]	"Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid." Ando K., Iijima K., Elliott J.I., Kirino Y., Suzuki T. J. Biol. Chem. 276:40353-40361(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH APBB1, MUTAGENESIS OF THR-743.
[81]	"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)." Standen C.L., Brownlees J., Grierson A.J., Kesavapany S., Lau K.-F., McLoughlin D.M., Miller C.C.J. J. Neurochem. 76:316-320(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MAPK10, MUTAGENESIS OF THR-743.
[82]	"A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing." Weidemann A., Eggert S., Reinhard F.B.M., Vogel M., Paliga K., Baier G., Masters C.L., Beyreuther K., Evin G. Biochemistry 41:2825-2835(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE AT LEU-720.
[83]	"Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc." Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., D'Adamio L. J. Biol. Chem. 277:16798-16804(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH SHC1, MUTAGENESIS OF THR-743 AND TYR-757.
[84]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-542, MASS SPECTROMETRY. Tissue: Plasma.
[85]	"Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease." Dyrks T., Weidemann A., Multhaup G., Salbaum J.M., Lemaire H.-G., Kang J., Mueller-Hill B., Masters C.L., Beyreuther K. EMBO J. 7:949-957(1988) [PubMed] [Europe PMC] [Abstract] Cited for: SIGNAL SEQUENCE CLEAVAGE SITE, TOPOLOGY.
[86]	"A cell biological perspective on Alzheimer's disease." Annaert W., De Strooper B. Annu. Rev. Cell Dev. Biol. 18:25-51(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[87]	"Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells." Nakaya T., Kawai T., Suzuki T. J. Biol. Chem. 283:19119-19131(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APBB1.
[88]	"BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2." Matsuda S., Matsuda Y., D'Adamio L. J. Biol. Chem. 284:15815-15825(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITM2C.
[89]	"APP binds DR6 to trigger axon pruning and neuron death via distinct caspases." Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M. Nature 457:981-989(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE, INTERACTION WITH TNFRSF21.
[90]	"RAGE-mediated signaling contributes to intraneuronal transport of amyloid-{beta} and neuronal dysfunction." 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. Proc. Natl. Acad. Sci. U.S.A. 106:20021-20026(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH AGER.
[91]	"Gamma-secretase activating protein is a therapeutic target for Alzheimer's disease." He G., Luo W., Li P., Remmers C., Netzer W.J., Hendrick J., Bettayeb K., Flajolet M., Gorelick F., Wennogle L.P., Greengard P. Nature 467:95-98(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GSAP.
[92]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[93]	"Site-specific characterization of threonine, serine, and tyrosine glycosylations of amyloid precursor protein/amyloid beta-peptides in human cerebrospinal fluid." Halim A., Brinkmalm G., Ruetschi U., Westman-Brinkmalm A., Portelius E., Zetterberg H., Blennow K., Larson G., Nilsson J. Proc. Natl. Acad. Sci. U.S.A. 108:11848-11853(2011) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-633; THR-651; THR-652; SER-656; THR-663 AND SER-667 PROTEOLYTIC PROCESSING, STRUCTURE OF CARBOHYDRATES, MASS SPECTROMETRY.
[94]	"MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide and induces its fibrillization." Zhang C., Liu Y., Gilthorpe J., van der Maarel J.R. PLoS ONE 7:E32953-E32953(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH S100A9.
[95]	"X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor." Hynes T.R., Randal M., Kennedy L.A., Eigenbrot C., Kossiakof A.A. Biochemistry 29:10018-10022(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 287-344.
[96]	"Sequential NMR resonance assignment and structure determination of the Kunitz-type inhibitor domain of the Alzheimer's beta-amyloid precursor protein." 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. Biochemistry 30:10467-10478(1991) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 289-344.
[97]	"Solution structure of residues 1-28 of the amyloid beta-peptide." Talafous J., Marcinowski K.J., Klopman G., Zagorski M.G. Biochemistry 33:7788-7796(1994) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 672-699.
[98]	"Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease." Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K., Frank R.W., Rosch P. Eur. J. Biochem. 233:293-298(1995) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 672-711.
[99]	"Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment." Kohno T., Kobayashi K., Maeda T., Sato K., Takashima A. Biochemistry 35:16094-16104(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 696-706.
[100]	"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." Scheidig A.J., Hynes T.R., Pelletier L.A., Wells J.A., Kossiakoff A.A. Protein Sci. 6:1806-1824(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF KUNITZ DOMAIN IN COMPLEX WITH CHYMOTRYPSIN; TRYPSIN AND BASIC PANCREATIC TRYPSIN INHIBITOR.
[101]	"Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?" Coles M., Bicknell W., Watson A.A., Fairlie D.P., Craik D.J. Biochemistry 37:11064-11077(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 672-711.
[102]	"Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein." 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. Nat. Struct. Biol. 6:327-331(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-123.
[103]	"Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells." Miravalle L., Tokuda T., Chiarle R., Giaccone G., Bugiani O., Tagliavini F., Frangione B., Ghiso J. J. Biol. Chem. 275:27110-27116(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CAA-APP VARIANTS.
[104]	"The Alzheimer's peptide a beta adopts a collapsed coil structure in water." 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. J. Struct. Biol. 130:130-141(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 681-706.
[105]	"Solution structures in aqueous SDS micelles of two amyloid beta peptides of Abeta(1-28) mutated at the alpha-secretase cleavage site." Poulsen S.-A., Watson A.A., Craik D.J. J. Struct. Biol. 130:142-152(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 672-699.
[106]	"The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain." Wang Y., Ha Y. Mol. Cell 15:343-353(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 346-551, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, MUTAGENESIS OF ARG-499 AND LYS-503.
[107]	"Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism." Shen Y., Joachimiak A., Rosner M.R., Tang W.-J. Nature 443:870-874(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-711 IN COMPLEX WITH IDE.
[108]	"Structure of Alzheimer's disease amyloid precursor protein copper-binding domain at atomic resolution." Kong G.K., Adams J.J., Cappai R., Parker M.W. Acta Crystallogr. F 63:819-824(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 133-189, DISULFIDE BONDS.
[109]	"Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions." 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. J. Mol. Biol. 367:148-161(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 133-189 IN COMPLEXES WITH COPPER IONS, DISULFIDE BONDS.
[110]	"Molecular basis for passive immunotherapy of Alzheimer's disease." 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. Proc. Natl. Acad. Sci. U.S.A. 104:15659-15664(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 672-679 IN COMPLEX WITH IGG.
[111]	"Structural correlates of antibodies associated with acute reversal of amyloid beta-related behavioral deficits in a mouse model of Alzheimer disease." 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. J. Biol. Chem. 285:3417-3427(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 672-678 IN COMPLEXES WITH ANTIBODY FAB FRAGMENTS.
[112]	"Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein." Dahms S.O., Hoefgen S., Roeser D., Schlott B., Guhrs K.H., Than M.E. Proc. Natl. Acad. Sci. U.S.A. 107:5381-5386(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 18-190, PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBUNIT, DISULFIDE BONDS.
[113]	"Framing beta-amyloid." Hardy J. Nat. Genet. 1:233-234(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[114]	"Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type." 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. Science 248:1124-1126(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAA-APP GLN-693.
[115]	"Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease." 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. Nature 349:704-706(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-717.
[116]	"The 717Val-->Ile substitution in amyloid precursor protein is associated with familial Alzheimer's disease regardless of ethnic groups." Yoshioka K., Miki T., Katsuya T., Ogihara T., Sakaki Y. Biochem. Biophys. Res. Commun. 178:1141-1146(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-717.
[117]	"Mis-sense mutation Val->Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease." Naruse S., Igarashi S., Kobayashi H., Aoki K., Inuzuka T., Kaneko K., Shimizu T., Iihara K., Kojima T., Miyatake T., Tsuji S. Lancet 337:978-979(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-717.
[118]	"Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene." Chartier-Harlin M.-C., Crawford F., Houlden H., Warren A., Hughes D., Fidani L., Goate A., Rossor M., Roques P., Hardy J., Mullan M. Nature 353:844-846(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 GLY-717.
[119]	"A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease." Murrell J.R., Farlow M., Ghetti B., Benson M.D. Science 254:97-99(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 PHE-717.
[120]	"Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region." 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. Am. J. Hum. Genet. 51:998-1014(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 GLY-693.
[121]	"Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene." 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. Nat. Genet. 1:218-221(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 GLY-692.
[122]	"A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid." Mullan M., Crawford F., Axelman K., Houlden H., Lilius L., Winblad B., Lannfelt L. Nat. Genet. 1:345-347(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 670-ASN-LEU-671.
[123]	"Mutation in codon 713 of the beta amyloid precursor protein gene presenting with schizophrenia." Jones C.T., Morris S., Yates C.M., Moffoot A., Sharpe C., Brock D.J.H., St Clair D. Nat. Genet. 1:306-309(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VAL-713.
[124]	"More missense in amyloid gene." Carter D.A., Desmarais E., Bellis M., Campion D., Clerget-Darpoux F., Brice A., Agid Y., Jaillard-Serradt A., Mallet J. Nat. Genet. 2:255-256(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 THR-713.
[125]	"Characterization of amyloid fibril beta-peptide in familial Alzheimer's disease with APP717 mutations." Liepnieks J.J., Ghetti B., Farlow M., Roses A.D., Benson M.D. Biochem. Biophys. Res. Commun. 197:386-392(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS AD1 ILE-717 AND PHE-717.
[126]	"Novel amyloid precursor protein gene mutation (codon 665Asp) in a patient with late-onset Alzheimer's disease." Peacock M.L., Murman D.L., Sima A.A.F., Warren J.T. Jr., Roses A.D., Fink J.K. Ann. Neurol. 35:432-438(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASP-665.
[127]	"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." Farlow M., Murrell J., Ghetti B., Unverzagt F., Zeldenrust S., Benson M.D. Neurology 44:105-111(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 PHE-717.
[128]	"A mutation in codon 717 of the amyloid precursor protein gene in an Australian family with Alzheimer's disease." 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. Neurosci. Lett. 199:183-186(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-717.
[129]	"A new pathogenic mutation in the APP gene (I716V) increases the relative proportion of A beta 42(43)." 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. Hum. Mol. Genet. 6:2087-2089(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 VAL-716.
[130]	"Presenile Alzheimer dementia characterized by amyloid angiopathy and large amyloid core type senile plaques in the APP 692Ala-->Gly mutation." 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. Acta Neuropathol. 96:253-260(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 GLY-692, CHARACTERIZATION OF PHENOTYPE.
[131]	"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." Ancolio K., Dumanchin C., Barelli H., Warter J.-M., Brice A., Campion D., Frebourg T., Checler F. Proc. Natl. Acad. Sci. U.S.A. 96:4119-4124(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 MET-715, CHARACTERIZATION OF VARIANT AD1 MET-715.
[132]	"High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes." Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J., Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A. Am. J. Hum. Genet. 66:110-117(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-717.
[133]	"Novel Leu723Pro amyloid precursor protein mutation increases amyloid beta42(43) peptide levels and induces apoptosis." Kwok J.B.J., Li Q.X., Hallupp M., Whyte S., Ames D., Beyreuther K., Masters C.L., Schofield P.R. Ann. Neurol. 47:249-253(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 PRO-723.
[134]	"Early-onset Alzheimer disease caused by a new mutation (V717L) in the amyloid precursor protein gene." Murrell J.R., Hake A.M., Quaid K.A., Farlow M.R., Ghetti B. Arch. Neurol. 57:885-887(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 LEU-717.
[135]	"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." 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. Hum. Mol. Genet. 9:2589-2598(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-714, CHARACTERIZATION OF VARIANT AD1 ILE-714, MUTAGENESIS OF VAL-717.
[136]	"Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy." Grabowski T.J., Cho H.S., Vonsattel J.P.G., Rebeck G.W., Greenberg S.M. Ann. Neurol. 49:697-705(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAA-APP ASN-694.
[137]	"In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692-->Gly) Alzheimer's disease." Walsh D.M., Hartley D.M., Condron M.M., Selkoe D.J., Teplow D.B. Biochem. J. 355:869-877(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AD1 GLY-692.
[138]	"The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation." 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. Nat. Neurosci. 4:887-893(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 GLY-693.
[139]	"An Iranian family with Alzheimer's disease caused by a novel APP mutation (Thr714Ala)." Pasalar P., Najmabadi H., Noorian A.R., Moghimi B., Jannati A., Soltanzadeh A., Krefft T., Crook R., Hardy J. Neurology 58:1574-1575(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ALA-714.
[140]	"Hemorrhagic stroke associated with the Iowa amyloid precursor protein mutation." Greenberg S.M., Shin Y., Grabowski T.J., Cooper G.E., Rebeck G.W., Iglesias S., Chapon F., Tournier-Lasserve E., Baron J.-C. Neurology 60:1020-1022(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAA-APP ASN-694.
[141]	"A family with Alzheimer disease and strokes associated with A713T mutation of the APP gene." 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. Neurology 63:910-912(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 THR-713.
[142]	"A novel AbetaPP mutation exclusively associated with cerebral amyloid angiopathy." 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. Ann. Neurol. 58:639-644(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAA-APP VAL-705.
[143]	"An African American family with early-onset Alzheimer disease and an APP (T714I) mutation." 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. Neurology 64:377-379(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AD1 ILE-714.
+	Additional computationally mapped references.

Web resources

Alzheimer Research Forum

APP mutations

AD mutations

GeneReviews

NIEHS-SNPs

Wikipedia

Amyloid beta entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00264 mRNA. Translation: CAA68374.1.
X13466 , X13467, X13468, X13469, X13470, X13471, X13472, X13473, X13474, X13475, X13476, X13477, X13478, X13479, X13487, X13488 Genomic DNA. Translation: CAA31830.1.
X06989 mRNA. Translation: CAA30050.1.
M33112 , M34862, M34863, M34864, M34865, M34866, M34867, M34868, M34869, M34870, M34871, M34872, M34873, M34874, M34876, M34877, M34878, M34879 Genomic DNA. Translation: AAB59502.1.
M34875 , M34862, M34863, M34864, M34865, M34866, M34867, M34868, M34869, M34870, M34871, M34872, M34873 Genomic DNA. Translation: AAB59501.1. Different termination.
D87675 Genomic DNA. Translation: BAA22264.1.
AK312326 mRNA. Translation: BAG35248.1.
AK295621 mRNA. Translation: BAG58500.1.
AY919674 Genomic DNA. Translation: AAW82435.1.
AP001439 Genomic DNA. No translation available.
AP001440 Genomic DNA. No translation available.
AP001441 Genomic DNA. No translation available.
AP001442 Genomic DNA. No translation available.
AP001443 Genomic DNA. No translation available.
CH471079 Genomic DNA. Translation: EAX09958.1.
CH471079 Genomic DNA. Translation: EAX09959.1.
CH471079 Genomic DNA. Translation: EAX09960.1.
CH471079 Genomic DNA. Translation: EAX09961.1.
CH471079 Genomic DNA. Translation: EAX09963.1.
CH471079 Genomic DNA. Translation: EAX09965.1.
BC004369 mRNA. Translation: AAH04369.1.
BC065529 mRNA. Translation: AAH65529.1.
M35675 mRNA. Translation: AAA60163.1. Sequence problems.
M24547, M24546 Genomic DNA. Translation: AAC13654.1.
M28373 mRNA. Translation: AAA58727.1. Sequence problems.
X06982 mRNA. Translation: CAA30042.1.
X06981 mRNA. Translation: CAA30041.1.
M18734 mRNA. Translation: AAA51726.1.
M29270, M29269 Genomic DNA. Translation: AAA51768.1.
AB066441 mRNA. Translation: BAB71958.2.
M15533 mRNA. Translation: AAA35540.1.
M15532 mRNA. Translation: AAA51564.1.
M37896, M37895 Genomic DNA. Translation: AAA51727.1.
S45136 Genomic DNA. Translation: AAB23646.1.
S60317 Genomic DNA. Translation: AAC60601.2.
AF282245 mRNA. Translation: AAQ14327.1.
S60721 mRNA. Translation: AAB26263.2.
S61380 mRNA. Translation: AAB26264.2.
S61383 mRNA. Translation: AAB26265.2.
M16765 mRNA. Translation: AAA51722.1.

IPI

IPI00006608.
IPI00219182.
IPI00219183.
IPI00219185.
IPI00219186.
IPI00219187.
IPI00394658.
IPI00412568.
IPI00412681.
IPI00412924.

PIR

S01442.
QRHUA4. S02260.

RefSeq

NP_000475.1. NM_000484.3.
NP_001129488.1. NM_001136016.3.
NP_001129601.1. NM_001136129.2.
NP_001129602.1. NM_001136130.2.
NP_001129603.1. NM_001136131.2.
NP_001191230.1. NM_001204301.1.
NP_001191231.1. NM_001204302.1.
NP_001191232.1. NM_001204303.1.
NP_958816.1. NM_201413.2.
NP_958817.1. NM_201414.2.

UniGene

Hs.434980.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AAP	X-ray	1.50	A/B	287-344	[»]
1AMB	NMR	-	A	672-699	[»]
1AMC	NMR	-	A	672-699	[»]
1AML	NMR	-	A	672-711	[»]
1BA4	NMR	-	A	672-711	[»]
1BA6	NMR	-	A	672-711	[»]
1BJB	NMR	-	A	672-699	[»]
1BJC	NMR	-	A	672-699	[»]
1BRC	X-ray	2.50	I	287-342	[»]
1CA0	X-ray	2.10	D/I	289-342	[»]
1HZ3	NMR	-	A	681-706	[»]
1IYT	NMR	-	A	672-713	[»]
1MWP	X-ray	1.80	A	28-123	[»]
1OWT	NMR	-	A	124-189	[»]
1QCM	NMR	-	A	696-706	[»]
1QWP	NMR	-	A	696-706	[»]
1QXC	NMR	-	A	696-706	[»]
1QYT	NMR	-	A	696-706	[»]
1TAW	X-ray	1.80	B	287-344	[»]
1TKN	NMR	-	A	460-569	[»]
1UO7	model	-	A	672-713	[»]
1UO8	model	-	A	672-713	[»]
1UOA	model	-	A	672-713	[»]
1UOI	model	-	A	672-713	[»]
1X11	X-ray	2.50	C/D	754-766	[»]
1Z0Q	NMR	-	A	672-713	[»]
1ZE7	NMR	-	A	672-687	[»]
1ZE9	NMR	-	A	672-687	[»]
1ZJD	X-ray	2.60	B	289-344	[»]
2BEG	NMR	-	A/B/C/D/E	672-713	[»]
2BOM	model	-	A/B	681-713	[»]
2BP4	NMR	-	A	672-687	[»]
2FJZ	X-ray	1.61	A	133-189	[»]
2FK1	X-ray	1.60	A	133-189	[»]
2FK2	X-ray	1.65	A	133-189	[»]
2FK3	X-ray	2.40	A/B/C/D/E/F/G/H	133-189	[»]
2FKL	X-ray	2.50	A/B	124-189	[»]
2FMA	X-ray	0.85	A	133-189	[»]
2G47	X-ray	2.10	C/D	672-711	[»]
2IPU	X-ray	1.65	P/Q	672-679	[»]
2LFM	NMR	-	A	672-711	[»]
2LLM	NMR	-	A	686-726	[»]
2LMN	NMR	-	A/B/C/D/E/F/G/H/I/J/K/L	672-711	[»]
2LMO	NMR	-	A/B/C/D/E/F/G/H/I/J/K/L	672-711	[»]
2LMP	NMR	-	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R	672-711	[»]
2LMQ	NMR	-	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R	672-711	[»]
2LNQ	NMR	-	A/B/C/D/E/F/G/H	672-711	[»]
2LOH	NMR	-	A/B	686-726	[»]
2LP1	NMR	-	A	671-770	[»]
2OTK	NMR	-	C	672-711	[»]
2R0W	X-ray	2.50	Q	672-679	[»]
2WK3	X-ray	2.59	C/D	672-713	[»]
2Y29	X-ray	2.30	A	687-692	[»]
2Y2A	X-ray	1.91	A	687-692	[»]
2Y3J	X-ray	1.99	A/B/C/D/E/F/G/H	701-706	[»]
2Y3K	X-ray	1.90	A/B/C/D/E/F/G/H	706-713	[»]
2Y3L	X-ray	2.10	A/B/C/G	706-713	[»]
3AYU	X-ray	2.00	B	586-595	[»]
3DXC	X-ray	2.10	B/D	739-770	[»]
3DXD	X-ray	2.20	B/D	739-770	[»]
3DXE	X-ray	2.00	B/D	739-770	[»]
3GCI	X-ray	2.04	P	707-713	[»]
3IFL	X-ray	1.50	P	672-678	[»]
3IFN	X-ray	1.50	P	672-711	[»]
3IFO	X-ray	2.15	P/Q	672-678	[»]
3IFP	X-ray	2.95	P/Q/R/S	672-678	[»]
3JTI	X-ray	1.80	B	699-706	[»]
3KTM	X-ray	2.70	A/B/C/D/E/F/G/H	18-190	[»]
3L33	X-ray	2.48	E/F/G/H	290-341	[»]
3L81	X-ray	1.60	B	761-767	[»]
3MOQ	X-ray	2.05	A/B/C/D	689-712	[»]
3MXC	X-ray	2.00	L	754-762	[»]
3MXY	X-ray	2.30	L	754-762	[»]
3NYJ	X-ray	3.20	A	365-567	[»]
3NYL	X-ray	2.80	A	365-570	[»]
3OVJ	X-ray	1.80	A/B/C/D	687-692	[»]
3OW9	X-ray	1.80	A/B	687-692	[»]
3SV1	X-ray	3.30	D/E/F	754-767	[»]
3U0T	X-ray	2.50	E/F	701-711	[»]
3UMH	X-ray	2.00	A	370-575	[»]
3UMI	X-ray	2.40	A	370-575	[»]
3UMK	X-ray	2.60	A	370-575	[»]
4HIX	X-ray	2.20	A	672-699	[»]

ProteinModelPortal

P05067.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-574N.

IntAct

P05067. 96 interactions.

MINT

MINT-150767.

Protein family/group databases

MEROPS

I02.015.

TCDB

1.C.50.1.2. amyloid beta,-protein peptide (Abeta,PP) family.

PTM databases

GlycoSuiteDB

P05067.

PhosphoSite

P05067.

Polymorphism databases

DMDM

112927.

2D gel databases

SWISS-2DPAGE

P05067.

Proteomic databases

PaxDb

P05067.

PRIDE

P05067.

Protocols and materials databases

DNASU

351.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346798; ENSP00000284981; ENSG00000142192.
ENST00000348990; ENSP00000345463; ENSG00000142192.
ENST00000354192; ENSP00000346129; ENSG00000142192.
ENST00000357903; ENSP00000350578; ENSG00000142192.
ENST00000358918; ENSP00000351796; ENSG00000142192.
ENST00000359726; ENSP00000352760; ENSG00000142192.
ENST00000440126; ENSP00000387483; ENSG00000142192.

GeneID

351.

KEGG

hsa:351.

UCSC

uc002ylz.3. human.
uc002yma.3. human.
uc002ymb.3. human.
uc010glj.3. human.
uc010glk.3. human.
uc011acj.2. human.
uc021whz.1. human.
uc021wia.1. human.
uc021wib.1. human.

Organism-specific databases

CTD

351.

GeneCards

GC21M027252.

HGNC

HGNC:620. APP.

HPA

CAB000157.
HPA001462.

MIM

104300. phenotype.
104760. gene+phenotype.
605714. phenotype.

neXtProt

NX_P05067.

Orphanet

1020. Early-onset autosomal dominant Alzheimer disease.
324723. Hereditary cerebral hemorrhage with amyloidosis, Arctic type.
100006. Hereditary cerebral hemorrhage with amyloidosis, Dutch type.
324718. Hereditary cerebral hemorrhage with amyloidosis, Flemish type.
324708. Hereditary cerebral hemorrhage with amyloidosis, Iowa type.
324713. Hereditary cerebral hemorrhage with amyloidosis, Italian type.
324703. Hereditary cerebral hemorrhage with amyloidosis, Piedmont type.

PharmGKB

PA24910.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG289770.

HOVERGEN

HBG000051.

InParanoid

P05067.

KO

K04520.

OMA

THAHIVI.

PhylomeDB

P05067.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000142192-MONOMER.

Pathway_Interaction_DB

caspase_pathway. Caspase cascade in apoptosis.
glypican_1pathway. Glypican 1 network.
p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SABIO-RK

P05067.

Gene expression databases

ArrayExpress

P05067.

Bgee

P05067.

Genevestigator

P05067.

GermOnline

ENSG00000142192. Homo sapiens.

Family and domain databases

Gene3D

3.30.1490.140. 1 hit.
3.90.570.10. 1 hit.
4.10.230.10. 1 hit.
4.10.410.10. 1 hit.

InterPro

IPR008155. Amyloid_glyco.
IPR013803. Amyloid_glyco_Abeta.
IPR011178. Amyloid_glyco_Cu-bd.
IPR024329. Amyloid_glyco_E2_domain.
IPR008154. Amyloid_glyco_extra.
IPR019744. Amyloid_glyco_extracell_CS.
IPR015849. Amyloid_glyco_heparin-bd.
IPR019745. Amyloid_glyco_intracell_CS.
IPR019543. APP_amyloid_C.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]

Pfam

PF10515. APP_amyloid. 1 hit.
PF12924. APP_Cu_bd. 1 hit.
PF12925. APP_E2. 1 hit.
PF02177. APP_N. 1 hit.
PF03494. Beta-APP. 1 hit.
PF00014. Kunitz_BPTI. 1 hit.
[Graphical view]

PRINTS

PR00203. AMYLOIDA4.
PR00759. BASICPTASE.
PR00204. BETAAMYLOID.

SMART

SM00006. A4_EXTRA. 1 hit.
SM00131. KU. 1 hit.
[Graphical view]

SUPFAM

SSF56491. A4_extra. 1 hit.
SSF89811. Amyloid_glyco_Cu-bd. 1 hit.
SSF57362. Prot_inh_Kunz-m. 1 hit.
SSF109843. SSF109843. 1 hit.

PROSITE

PS00319. A4_EXTRA. 1 hit.
PS00320. A4_INTRA. 1 hit.
PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05067.

ChEMBL

CHEMBL2487.

ChiTaRS

app. human.

EvolutionaryTrace

P05067.

GenomeRNAi

351.

NextBio

1445.

PMAP-CutDB

P05067.

SOURCE

Search...

Entry information

Entry name

A4_HUMAN

Accession

Primary (citable) accession number: P05067
Secondary accession number(s): B2R5V1 , B4DII8, D3DSD1, D3DSD2, D3DSD3, P09000, P78438, Q13764, Q13778, Q13793, Q16011, Q16014, Q16019, Q16020, Q6GSC0, Q8WZ99, Q9BT38, Q9UC33, Q9UCA9, Q9UCB6, Q9UCC8, Q9UCD1, Q9UQ58

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	November 1, 1991
Last modified:	May 29, 2013
This is version 216 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.