Reviewed, UniProtKB/Swiss-Prot P05067 (A4_HUMAN)

Names and origin

Protein names

Recommended name:
    Amyloid beta A4 protein
Alternative name(s):
    Alzheimer disease amyloid protein
    ABPP
    APPI
      Short name=APP
    PreA4
    Cerebral vascular amyloid peptide
      Short name=CVAP
    Protease nexin-II
      Short name=PN-II
Cleaved into the following 14 chains:
    1- Recommended name:
            N-APP
    2- Recommended name:
            Soluble APP-alpha
                Short name=S-APP-alpha
    3- Recommended name:
            Soluble APP-beta
                Short name=S-APP-beta
    4- Recommended name:
            C99
    5- Recommended name:
            Beta-amyloid protein 42
        Alternative name(s):
            Beta-APP42
    6- Recommended name:
            Beta-amyloid protein 40
        Alternative name(s):
            Beta-APP40
    7- Recommended name:
            C83
    8- Recommended name:
            P3(42)
    9- Recommended name:
            P3(40)
    10- Recommended name:
            C80
    11- Recommended name:
            Gamma-secretase C-terminal fragment 59
        Alternative name(s):
            Gamma-CTF(59)
            Amyloid intracellular domain 59
              Short name=AICD-59
              Short name=AID(59)
    12- Recommended name:
            Gamma-secretase C-terminal fragment 57
        Alternative name(s):
            Gamma-CTF(57)
            Amyloid intracellular domain 57
              Short name=AICD-57
              Short name=AID(57)
    13- Recommended name:
            Gamma-secretase C-terminal fragment 50
        Alternative name(s):
            Gamma-CTF(50)
            Amyloid intracellular domain 50
              Short name=AICD-50
              Short name=AID(50)
    14- Recommended name:
            C31

Gene names

Name:	APP
Synonyms:	A4, AD1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Ref.36 Ref.63 Ref.65 Ref.87 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 overexpressed HADH2 leads to oxidative stress and neurotoxicity. Ref.36 Ref.63 Ref.65 Ref.87 Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain By similarity. Ref.36 Ref.63 Ref.65 Ref.87 The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. Ref.36 Ref.63 Ref.65 Ref.87 N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Ref.36 Ref.63 Ref.65 Ref.87
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. 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. Ref.63 Ref.65 Ref.87 Ref.45 Ref.46 Ref.47 Ref.49 Ref.50 Ref.53 Ref.56 Ref.57 Ref.59 Ref.60 Ref.62 Ref.64 Ref.66 Ref.69 Ref.80 Ref.85
Subcellular location	Membrane; Single-pass type I membrane protein. Membrane › clathrin-coated pit. Note: Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Ref.63
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.26
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.21 Ref.39 Ref.40 Ref.42 Ref.43 Ref.48 Ref.94 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.21 Ref.39 Ref.40 Ref.42 Ref.43 Ref.48 Ref.94
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-CTF(50), gamma-CTF(57) and gamma-CTF(59). 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.87 Ref.32 Ref.73 Ref.76 Ref.79 Ref.82 N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region By similarity. Ref.81 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.80 Ref.70 Ref.71 Ref.74 Ref.75 Ref.77 Ref.78 Ref.84 Ref.86 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.87 Ref.32 Ref.73 Ref.76 Ref.79 Ref.82
Involvement in disease	Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is 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. Ref.22 Ref.24 Ref.103 Ref.104 Ref.105 Ref.106 Ref.107 Ref.108 Ref.109 Ref.110 Ref.112 Ref.113 Ref.115 Ref.116 Ref.117 Ref.118 Ref.119 Ref.120 Ref.121 Ref.122 Ref.123 Ref.125 Ref.126 Ref.127 Ref.129 Ref.131 Defects in APP are the cause of amyloidosis cerebroarterial Dutch type (AMYLCAD) [MIM:605714]; also known as hereditary cerebral hemorrhage with amyloidosis Dutch type (HCHWAD). AMYLCAD is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. Beta-APP40 is the predominant form of cerebrovascular amyloid. Amyloid is not found outside the nervous system. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Onset of the disease is in middle age (44 to 60 years). 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. Ref.97 Ref.102 Defects in APP are the cause of amyloidosis cerebroarterial Italian type (AMYLCAIT) [MIM:605714]. AMYLCAIT is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels, resulting in cerebral amyloid angiopathy. Amyloid is not found outside the nervous system. It is a condition very similar to AMYLCAD, but the clinical course is less severe. Patients manifest mild cognitive decline, recurrent strokes, and epilepsy in some cases. There are extensive amyloid deposits in leptomeningeal and cortical vessels and, to a lesser extent, in the neuropil of the cerebral cortex, in the absence of neurofibrillary tangles. Defects in APP are the cause of amyloidosis cerebroarterial Iowa type (AMYLCAIW) [MIM:605714]. AMYLCAIW is a hereditary amyloidosis due to amyloid-beta A4 peptide(s) deposition. Patients have progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
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.58 Molecular mass is 6451.6 Da from positions 714 - 770. Determined by MALDI. Ref.58 Molecular mass is 6436.8 Da from positions 715 - 769. Determined by MALDI. Ref.58 Molecular mass is 5752.5 Da from positions 719 - 767. Determined by MALDI. Ref.58
Sequence caution	The sequence AAA58727.1 differs from that shown. Reason: Miscellaneous discrepancy. 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
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
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 Traceable author statement. Source: UniProtKB collateral sprouting in the 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 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 neuron apoptosis Ref.87 Inferred from mutant phenotype. Source: UniProtKB neuron remodeling Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of epidermal growth factor 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 synapse structure and activity Inferred from sequence or structural similarity. Source: UniProtKB regulation of translation Inferred from sequence or structural similarity. Source: UniProtKB visual learning Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA axon Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from direct assay. Source: UniProtKB coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Ref.75 Inferred from Experiment. Source: Reactome integral to plasma membrane Ref.75 Traceable author statement. Source: ProtInc plasma membrane Inferred from direct assay. Source: HPA platelet alpha granule lumen Inferred from Experiment. Source: Reactome
Molecular function	DNA binding Inferred from sequence or structural similarity. Source: UniProtKB acetylcholine receptor binding Ref.57 Inferred from physical interaction. Source: UniProtKB copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW heparin binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase inhibitor activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-77613,EBI-77613
itself		2	EBI-302641,EBI-302641
ADAM17	P78536	1	EBI-77613,EBI-78188
APBA1	Q02410	2	EBI-77613,EBI-368690
APBB1	O00213	2	EBI-77613,EBI-81694
Apbb1	P46933	1	EBI-77613,EBI-286177	From a different organism.
APBB2	Q92870	1	EBI-77613,EBI-79277
Apbb3	O35827	1	EBI-77613,EBI-286163	From a different organism.
APLP1	P51693	1	EBI-302641,EBI-74648
APLP2	Q06481	1	EBI-302641,EBI-79306
APOA1	P02647	5	EBI-77613,EBI-701692
BACE1	P56817-1	1	EBI-77613,EBI-2433297
BLMH	Q13867	1	EBI-302641,EBI-718504
CHRNA7	P36544	1	EBI-77613,EBI-79333
Chrna7	Q05941	1	EBI-77613,EBI-79422	From a different organism.
CNTN3	Q9P232	1	EBI-302641,EBI-2028361
CNTN4	Q8IWV2	1	EBI-302641,EBI-2028276
FLOT1	O75955	4	EBI-77613,EBI-603643
HOMER2	Q9NSB8	1	EBI-302661,EBI-2126733
HOMER3	Q9NSC5	2	EBI-302661,EBI-748420
HSD17B10	Q99714	2	EBI-77613,EBI-79964
ITM2A	O43736	3	EBI-302641,EBI-2431769
KLK6	Q92876	1	EBI-77613,EBI-2432309
MAPK8IP1	Q9UQF2	3	EBI-77613,EBI-78404
Mapk8ip1	Q9WVI9-1	1	EBI-77613,EBI-288461	From a different organism.
MAPT	P10636	4	EBI-77613,EBI-366182
MAPT	P10636-8	1	EBI-77613,EBI-366233
NF1	P21359	1	EBI-77613,EBI-1172917
NGFR	P08138	2	EBI-77613,EBI-1387782
PDIA3	P30101	1	EBI-77613,EBI-979862
PIN1	Q13526	2	EBI-302641,EBI-714158
Pin1	Q9QUR7	1	EBI-302641,EBI-2432975	From a different organism.
PRNP	P04156	1	EBI-77613,EBI-977302
PSEN1	P49768	1	EBI-77613,EBI-297277
PSEN1	P49768	1	EBI-302641,EBI-297277
PSEN1	P49768	1	EBI-302661,EBI-297277
PSEN2	P49810	1	EBI-77613,EBI-2010251
SHC1	P29353	4	EBI-77613,EBI-78835
SHC3	Q92529	2	EBI-77613,EBI-79084
Slc5a7	Q8BGY9	1	EBI-77613,EBI-2010752	From a different organism.
SPON1	Q9HCB6	1	EBI-302641,EBI-2431846
Spon1	P35446	1	EBI-302641,EBI-2432084	From a different organism.
TGFB1	P01137	1	EBI-77613,EBI-779636
TGFB2	P61812	2	EBI-77613,EBI-779581
TNFRSF21	O75509	3	EBI-77613,EBI-2313231
TP53BP2	Q13625	2	EBI-77613,EBI-77642

Alternative products

This entry describes 10 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.16 Ref.17

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

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

137

1

Copper

Metal binding

147

1

Copper

Metal binding

149

1

Copper

Metal binding

151

1

Copper Probable

Metal binding

677

1

Copper or zinc

Metal binding

681

1

Copper or zinc Probable

Metal binding

684

1

Copper or zinc

Metal binding

685

1

Copper or zinc

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.80

Modified residue

206

1

Phosphoserine; by CK1 Ref.80

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.80 Ref.70

Modified residue

757

1

Phosphotyrosine Ref.80 Ref.84 Ref.86

Modified residue

762

1

Phosphotyrosine Ref.80 Ref.84

Glycosylation

542

1

N-linked (GlcNAc...) Ref.81

Glycosylation

571

1

N-linked (GlcNAc...) Probable

Glycosylation

656

1

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

Disulfide bond

144 ↔ 158

Ref.72

Disulfide bond

291 ↔ 341

Ref.72

Disulfide bond

300 ↔ 324

Ref.72

Disulfide bond

316 ↔ 337

Ref.72

Natural variations

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

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: dbSNP rs45588932. Ref.9

VAR_022315

Natural variant

665

1

E → D in a patient with late onset Alzheimer disease. Ref.114

VAR_010107

Natural variant

670 – 671

2

KM → NL in AD1.

VAR_000015

Natural variant

678

1

D → N in AD1. Ref.24

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.109 Ref.118 Ref.125

VAR_000016

Natural variant

693

1

E → G in AD1. Ref.108 Ref.126

VAR_014215

Natural variant

693

1

E → K in AMYLCAIT.

VAR_014216

Natural variant

693

1

E → Q in AMYLCAD. Ref.102

VAR_000017

Natural variant

694

1

D → N in AMYLCAIW. Ref.124 Ref.128

VAR_014217

Natural variant

705

1

L → V in AMYLCAIT. Ref.130

VAR_032276

Natural variant

713

1

A → T in AD1. Ref.112 Ref.129

VAR_000019

Natural variant

713

1

A → V in one chronic schizophrenia patient; could be a polymorphism. dbSNP rs1800557. Ref.111

VAR_000018

Natural variant

714

1

T → A in AD1. Ref.127

VAR_032277

Natural variant

714

1

T → I in AD1; increased beta-APP42/beta-APP40 ratio. Ref.123 Ref.131

VAR_014218

Natural variant

715

1

V → M in AD1; decreased beta-APP40/total APP-beta. Ref.119

VAR_010108

Natural variant

716

1

I → V in AD1. Ref.117

VAR_000020

Natural variant

717

1

V → F in AD1. Ref.22 Ref.107 Ref.113 Ref.115

VAR_000023

Natural variant

717

1

V → G in AD1. Ref.22 Ref.106

VAR_000022

Natural variant

717

1

V → I in AD1. Ref.22 Ref.103 Ref.104 Ref.105 Ref.113 Ref.116 Ref.120

VAR_000021

Natural variant

717

1

V → L in AD1. Ref.122

VAR_014219

Natural variant

723

1

L → P in AD1. Ref.121

VAR_010109

Experimental info

Mutagenesis

99 – 102

4

KRGR → NQGG: Reduced heparin-binding. Ref.43

Mutagenesis

137

1

H → N: Binds copper. Forms dimer. Ref.42

Mutagenesis

141

1

M → T: Binds copper. Forms dimer. Ref.42

Mutagenesis

144

1

C → S: Binds copper. No dimer formation. No copper reducing activity. Ref.42 Ref.55

Mutagenesis

147 – 149

3

HLH → ALA: 50% decrease in copper reducing activity. Ref.42 Ref.55 Ref.67

Mutagenesis

147

1

H → A: Some decrease in copper reducing activity. Ref.42 Ref.67

Mutagenesis

147

1

H → N: Binds copper. Forms dimer. Ref.42 Ref.67

Mutagenesis

147

1

H → Y: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.42 Ref.67

Mutagenesis

151

1

H → K: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.42 Ref.67

Mutagenesis

151

1

H → N: Binds copper. Forms dimer. Ref.42 Ref.67

Mutagenesis

198

1

S → A: Greatly reduced casein kinase phosphorylation. Ref.71 Ref.75

Mutagenesis

206

1

S → A: Reduced casein kinase phosphorylation. Ref.71 Ref.75

Mutagenesis

499

1

R → A: Reduced affinity for heparin; when associated with A-503. Ref.100

Mutagenesis

503

1

K → A: Reduced affinity for heparin; when associated with A-499. Ref.100

Mutagenesis

656

1

S → A: Abolishes chondroitin sulfate binding in L-APP733 isoform. Ref.35

Mutagenesis

676

1

R → G: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.51

Mutagenesis

681

1

Y → F: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.51

Mutagenesis

684

1

H → R: Only 23% zinc-induced beta-APP (28) peptide aggregation. Ref.51

Mutagenesis

704

1

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

Mutagenesis

706

1

M → L: Reduced lipid peroxidation inhibition. Ref.36 Ref.52

Mutagenesis

706

1

M → V: No free radical production. No hippocampal neuron toxicity. Ref.36 Ref.52

Mutagenesis

717

1

V → C or S: Unchanged beta-APP42/total APP-beta ratio. Ref.123 Ref.44

Mutagenesis

717

1

V → F, G or I: Increased beta-APP42/beta-APP40 ratio. Ref.123 Ref.44

Mutagenesis

717

1

V → K: Decreased beta-APP42/total APP-beta ratio. Ref.123 Ref.44

Mutagenesis

717

1

V → M: Increased beta-APP42/beta-APP40 ratio. No change in apoptosis after caspase cleavage. Ref.123 Ref.44

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.46 Ref.50 Ref.54

Mutagenesis

739

1

D → A: No cleavage by caspases during apoptosis. Ref.73 Ref.76 Ref.58

Mutagenesis

739

1

D → N: No effect on FADD-induced apoptosis. Ref.73 Ref.76 Ref.58

Mutagenesis

743

1

T → A: Greatly reduces the binding to SHC1 and APBB family members; no effect on NGF-stimulated neurite extension. Ref.80 Ref.74 Ref.77 Ref.78

Mutagenesis

743

1

T → E: Reduced NGF-stimulated neurite extension. No effect on APP maturation. Ref.80 Ref.74 Ref.77 Ref.78

Mutagenesis

756

1

G → A: APP internalization unchanged. No change in beta-APP42 secretion. Ref.54

Mutagenesis

757

1

Y → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.46 Ref.66 Ref.80 Ref.54

Mutagenesis

757

1

Y → G: Loss of binding to MAPK8IP1, APBA1, APBB1, APPBP2 and SHC1. Ref.46 Ref.66 Ref.80 Ref.54

Mutagenesis

759

1

N → A: No binding to APBA1, no effect on APBB1 binding. Little APP internalization. Reduced beta-APP42 secretion. Ref.46 Ref.54

Mutagenesis

760

1

P → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.54

Mutagenesis

762

1

Y → A: Loss of binding to APBA1 and APBB1. APP internalization unchanged. No change in beta-APP42 secretion. Ref.46 Ref.54

Sequence conflict

15 – 16

2

AR → VW in CAA31830. Ref.3

Sequence conflict

647

1

D → E in AAA51722. Ref.34

Sequence conflict

724

1

Missing in AAB26263. Ref.22

Sequence conflict

724

1

Missing in AAB26264. Ref.22

Sequence conflict

731

1

I → N in AAB26263. Ref.22

Sequence conflict

731

1

I → N in AAB26264. Ref.22

Sequence conflict

731

1

I → N in AAB26265. Ref.22

Sequence conflict

757

1

Y → S in AAA35540. Ref.30

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

461 – 482

22

Helix

487 – 518

32

Helix

520 – 549

30

Helix

552 – 566

15

Helix

680 – 697

18

Helix

703 – 706

4

Turn

707 – 710

4

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. 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. 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). 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. 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. 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. 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). 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. 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. 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

References

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[29]	"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: 3312495] [Abstract] Cited for: PROTEIN SEQUENCE OF 672-681. Tissue: Brain cortex.
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[32]	"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: 16816112] [Abstract] Cited for: PROTEIN SEQUENCE OF 691-698, CLEAVAGE BY THETA-SECRETASE.
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[35]	"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: 7737970] [Abstract] Cited for: CHARACTERIZATION OF L-APP733, MUTAGENESIS OF SER-656.
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[47]	"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: 8855266] [Abstract] Cited for: INTERACTION WITH APBB2.
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[49]	"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: 9338779] [Abstract] Cited for: INTERACTION OF BETA-AMYLOID PEPTIDE WITH HADH2. Tissue: Brain.
[50]	"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: 9843960] [Abstract] Cited for: INTERACTION WITH APPBP2, MUTAGENESIS OF TYR-728.
[51]	"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: 10413512] [Abstract] Cited for: BETA-AMYLOID ZINC-BINDING, MUTAGENESIS OF ARG-676; TYR-681 AND HIS-684.
[52]	"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: 10535332] [Abstract] Cited for: IMPORTANCE OF MET-706 IN FREE RADICAL OXIDATIVE STRESS, MUTAGENESIS OF MET-706.
[53]	"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: 9890987] [Abstract] Cited for: INTERACTION WITH APBA2.
[54]	"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: 10383380] [Abstract] Cited for: ENDOCYTOSIS SIGNAL, MUTAGENESIS OF TYR-728; GLY-756; TYR-757; ASN-759; PRO-760 AND TYR-762.
[55]	"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: 10461923] [Abstract] Cited for: IMPORTANCE OF CYS-144 IN COPPER REDUCTION, MUTAGENESIS OF CYS-144 AND 147-HIS--HIS-149.
[56]	"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: 10816430] [Abstract] Cited for: INTERACTION OF BETA-AMYLOID WITH APOE.
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[78]	"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: 11146006] [Abstract] Cited for: PHOSPHORYLATION BY MAPK10, MUTAGENESIS OF THR-743.
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[97]	"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: 10821838] [Abstract] Cited for: STRUCTURE OF AMYLCAD VARIANTS.
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[103]	"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: 1671712] [Abstract] Cited for: VARIANT AD1 ILE-717.
[104]	"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: 1908231] [Abstract] Cited for: VARIANT AD1 ILE-717.
[105]	"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: 1678058] [Abstract] Cited for: VARIANT AD1 ILE-717.
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[108]	"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: 1415269] [Abstract] Cited for: VARIANT AD1 GLY-693.
[109]	"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: 1303239] [Abstract] Cited for: VARIANT AD1 GLY-692.
[110]	"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: 1302033] [Abstract] Cited for: VARIANT AD1 670-ASN-LEU-671.
[111]	"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: 1307241] [Abstract] Cited for: VARIANT VAL-713.
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[113]	"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: 8267572] [Abstract] Cited for: VARIANTS AD1 ILE-717 AND PHE-717.
[114]	"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: 8154870] [Abstract] Cited for: VARIANT ASP-665.
[115]	"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: 8290042] [Abstract] Cited for: VARIANT AD1 PHE-717.
[116]	"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: 8577393] [Abstract] Cited for: VARIANT AD1 ILE-717.
[117]	"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: 9328472] [Abstract] Cited for: VARIANT AD1 VAL-716.
[118]	"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: 9754958] [Abstract] Cited for: VARIANT AD1 GLY-692, CHARACTERIZATION OF PHENOTYPE.
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[120]	"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: 10631141] [Abstract] Cited for: VARIANT AD1 ILE-717.
[121]	"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: 10665499] [Abstract] Cited for: VARIANT AD1 PRO-723.
[122]	"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: 10867787] [Abstract] Cited for: VARIANT AD1 LEU-717.
[123]	"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: 11063718] [Abstract] Cited for: VARIANT AD1 ILE-714, CHARACTERIZATION OF VARIANT AD1 ILE-714, MUTAGENESIS OF VAL-717.
[124]	"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: 11409420] [Abstract] Cited for: VARIANT AMYLCAIW ASN-694.
[125]	"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: 11311152] [Abstract] Cited for: CHARACTERIZATION OF VARIANT AD1 GLY-692.
[126]	"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: 11528419] [Abstract] Cited for: VARIANT AD1 GLY-693.
[127]	"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: 12034808] [Abstract] Cited for: VARIANT AD1 ALA-714.
[128]	"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: 12654973] [Abstract] Cited for: VARIANT AMYLCAIW ASN-694.
[129]	"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: 15365148] [Abstract] Cited for: VARIANT AD1 THR-713.
[130]	"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: 16178030] [Abstract] Cited for: VARIANT AMYLCAIT VAL-705.
[131]	"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: 15668448] [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.
AY919674 Genomic DNA. Translation: AAW82435.1.
CH471079 Genomic DNA. Translation: EAX09958.1.
AK312326 mRNA. Translation: BAG35248.1.
CH471079 Genomic DNA. Translation: EAX09960.1.
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.
NP_001129601.1.
NP_001129602.1.
NP_958816.1.
NP_958817.1.

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	[»]
1RW6	X-ray	2.80	A	365-570	[»]
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	[»]
2OTK	NMR	-	C	672-711	[»]
2R0W	X-ray	2.50	Q	672-679	[»]
2WK3	X-ray	2.59	C/D	672-713	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-574N.

IntAct

P05067. 72 interactions.

STRING

P05067.

Protein family/group databases

MEROPS

I02.015.

PTM databases

GlycoSuiteDB

P05067.

PhosphoSite

P05067.

2-D gel databases

SWISS-2DPAGE

P05067.

Proteomic databases

PRIDE

P05067.

Genome annotation databases

Ensembl

ENST00000346798; ENSP00000284981; ENSG00000142192; Homo sapiens. [Genome view]

GeneID

351.

KEGG

hsa:351.

UCSC

uc002ylz.1. human.
uc002ymb.1. human.
uc010glj.1. human.
uc010glk.1. human.

Organism-specific databases

CTD

351.

GeneCards

GC21M026174.

H-InvDB

HIX0040845.

HGNC

HGNC:620. APP.

HPA

CAB000157.
HPA001462.

MIM

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

Orphanet

1020. Alzheimer disease, familial.
85458. Cerebral hemorrhage with amyloidosis, hereditary.

PharmGKB

PA24910.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05256.

HOVERGEN

P05067.

InParanoid

P05067.

OMA

KAAQIRS.

OrthoDB

EOG9D55HV.

PhylomeDB

P05067.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P05067.

Bgee

P05067.

Genevestigator

P05067.

GermOnline

ENSG00000142192. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:4.10.230.10. Amyloid_glyco_Abeta. 1 hit.
G3DSA:3.30.1490.140. Amyloid_glyco_Cu-bd. 1 hit.
G3DSA:3.90.570.10. Amyloid_glyco_heparin-bd. 1 hit.
G3DSA:4.10.410.10. Prot_inh_Kunz-m. 1 hit.

Pfam

PF02177. A4_EXTRA. 1 hit.
PF10515. APP_amyloid. 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]

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 Resources

NextBio

1445.

PMAP-CutDB

P05067.

SOURCE

Search...

Entry information

Entry name

A4_HUMAN

Accession

Primary (citable) accession number: P05067
Secondary accession number(s): B2R5V1 , 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:	January 19, 2010
This is version 177 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.