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P05067 (A4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 229. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length770 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.90 Ref.91

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.90 Ref.91

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.90 Ref.91

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.90 Ref.91

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.90 Ref.91

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. Interacts with SORL1. 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.91 Ref.92 Ref.95 Ref.113

Subcellular location

Membrane; Single-pass type I membrane protein. Membraneclathrin-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. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions. Ref.65 Ref.71 Ref.87

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.101

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.101

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.90 Ref.94

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.94

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.90 Ref.94

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.116 Ref.117 Ref.118 Ref.119 Ref.120 Ref.121 Ref.122 Ref.123 Ref.125 Ref.126 Ref.128 Ref.129 Ref.130 Ref.131 Ref.132 Ref.133 Ref.134 Ref.135 Ref.136 Ref.138 Ref.139 Ref.140 Ref.142 Ref.144

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.104 Ref.115 Ref.137 Ref.141 Ref.143

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 processApoptosis
Cell adhesion
Endocytosis
Notch signaling pathway
   Cellular componentAmyloid
Coated pit
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseAlzheimer disease
Amyloidosis
Disease mutation
Neurodegeneration
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Heparin-binding
Iron
Metal-binding
Zinc
   Molecular functionProtease inhibitor
Serine protease inhibitor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNotch 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

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

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: Ensembl

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: Ensembl

innate immune response

Traceable author statement. Source: Reactome

ionotropic glutamate receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

locomotory behavior

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

mitotic G2 phase

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endopeptidase activity

Inferred from direct assay PubMed 10652580. Source: GOC

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuron apoptotic process

Inferred from mutant phenotype Ref.90. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. 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 G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

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: Ensembl

smooth endoplasmic reticulum calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

suckling behavior

Inferred from electronic annotation. Source: Ensembl

synaptic growth at neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

visual learning

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 20427278. Source: UniProtKB

apical part of cell

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 18509662. Source: UniProtKB

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

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

integral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.78. Source: ProtInc

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane raft

Inferred from direct assay PubMed 24499793. Source: ParkinsonsUK-UCL

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

nuclear envelope lumen

Inferred from direct assay PubMed 21989385. Source: Alzheimers_University_of_Toronto

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20427278. Source: UniProt

plasma membrane

Inferred from direct assay PubMed 20427278. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

spindle midzone

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay PubMed 11988176. Source: MGI

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

PTB domain binding

Inferred from physical interaction PubMed 12805363. Source: BHF-UCL

acetylcholine receptor binding

Inferred from physical interaction Ref.59. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 24499793. Source: ParkinsonsUK-UCL

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 16286452PubMed 18805418PubMed 19549187PubMed 19754881PubMed 20573181PubMed 20818335PubMed 21205198PubMed 21320494PubMed 21527912PubMed 22200570PubMed 22584060PubMed 23103738PubMed 23353684PubMed 23416305PubMed 23551356PubMed 23603391PubMed 23907009PubMed 16193067PubMed 16492752PubMed 23907583. Source: IntAct

peptidase activator activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 18387811PubMed 16384638PubMed 19542224PubMed 23585889PubMed 23907583PubMed 24117177PubMed 10673326PubMed 11756426PubMed 23585889. Source: IntAct

receptor binding

Inferred from physical interaction PubMed 19849849. Source: BHF-UCL

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

itself79EBI-77613,EBI-77613
Q306T33EBI-77613,EBI-8294101From a different organism.
AGRNP316963EBI-2431589,EBI-457650From a different organism.
APBA1Q024103EBI-77613,EBI-368690
APBB1O002135EBI-77613,EBI-81694
APBB2Q928702EBI-77613,EBI-79277
APLP1P516932EBI-302641,EBI-74648
APLP2Q064812EBI-302641,EBI-79306
APOA1P026475EBI-77613,EBI-701692
BLMHQ138672EBI-302641,EBI-718504
CALRP152533EBI-77613,EBI-9005200From a different organism.
CALRQ8K3H72EBI-3894543,EBI-9005068From a different organism.
COL18A1P390602EBI-821758,EBI-2566375
CTSDP073392EBI-77613,EBI-2115097
FLOT1O759555EBI-77613,EBI-603643
FOSP011003EBI-77613,EBI-852851
GPR3P460892EBI-302641,EBI-3909653
HOMER3Q9NSC53EBI-302661,EBI-748420
HSD17B10Q997144EBI-77613,EBI-79964
ITM2AO437363EBI-302641,EBI-2431769
JUNP054122EBI-77613,EBI-852823
MAPTP106369EBI-77613,EBI-366182
MED12Q930742EBI-77613,EBI-394357
MT-ND3P038972EBI-821758,EBI-1246249
NF1P213593EBI-77613,EBI-1172917
NGFRP081382EBI-77613,EBI-1387782
NgfrP071742EBI-2431589,EBI-1038810From a different organism.
PCBD1P614572EBI-77613,EBI-740475
PCOLCEQ151133EBI-821758,EBI-8869614
PDIA3P301013EBI-77613,EBI-979862
PIN1Q135262EBI-302641,EBI-714158
PRNPP041563EBI-77613,EBI-977302
PSEN1P497686EBI-77613,EBI-297277
SHC1P293535EBI-77613,EBI-78835
SHC3Q925292EBI-77613,EBI-79084
SLC40A1Q9NP594EBI-77613,EBI-725153
Slc5a7Q8BGY92EBI-77613,EBI-2010752From a different organism.
SPON1Q9HCB63EBI-302641,EBI-2431846
TGFB1P011372EBI-77613,EBI-779636
TGFB2P618126EBI-77613,EBI-779581
TNFRSF21O755093EBI-77613,EBI-2313231
TP53BP2Q136253EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.17 Ref.18
Chain18 – 770753Amyloid beta A4 protein
PRO_0000000088
Chain18 – 687670Soluble APP-alpha
PRO_0000000089
Chain18 – 671654Soluble APP-beta
PRO_0000000090
Chain18 – 286269N-APP
PRO_0000381966
Chain672 – 77099C99
PRO_0000000091
Chain672 – 71342Beta-amyloid protein 42
PRO_0000000092
Chain672 – 71140Beta-amyloid protein 40
PRO_0000000093
Chain688 – 77083C83
PRO_0000000094
Peptide688 – 71326P3(42)
PRO_0000000095
Peptide688 – 71124P3(40)
PRO_0000000096
Chain691 – 77080C80
PRO_0000384574
Chain712 – 77059Gamma-secretase C-terminal fragment 59
PRO_0000000097
Chain714 – 77057Gamma-secretase C-terminal fragment 57
PRO_0000000098
Chain721 – 77050Gamma-secretase C-terminal fragment 50 By similarity
PRO_0000000099
Chain740 – 77031C31
PRO_0000000100

Regions

Topological domain18 – 699682Extracellular Potential
Transmembrane700 – 72324Helical; Potential
Topological domain724 – 77047Cytoplasmic Potential
Domain291 – 34151BPTI/Kunitz inhibitor
Region96 – 11015Heparin-binding
Region181 – 1888Zinc-binding
Region391 – 42333Heparin-binding
Region491 – 52232Heparin-binding
Region523 – 54018Collagen-binding
Region732 – 75120Interaction with G(o)-alpha
Motif724 – 73411Basolateral sorting signal
Motif759 – 7624NPXY motif; contains endocytosis signal
Compositional bias230 – 26031Asp/Glu-rich (acidic)
Compositional bias274 – 2807Poly-Thr

Sites

Metal binding1471Copper 1
Metal binding1511Copper 1
Metal binding1681Copper 1
Metal binding6771Copper or zinc 2
Metal binding6811Copper or zinc 2 Probable
Metal binding6841Copper or zinc 2
Metal binding6851Copper or zinc 2
Site1441Required for Cu(2+) reduction
Site301 – 3022Reactive bond
Site671 – 6722Cleavage; by beta-secretase
Site672 – 6732Cleavage; by caspase-6; when associated with variant 670-N-L-671
Site687 – 6882Cleavage; by alpha-secretase
Site690 – 6912Cleavage; by theta-secretase
Site7041Implicated in free radical propagation By similarity
Site7061Susceptible to oxidation
Site711 – 7122Cleavage; by gamma-secretase; site 1
Site713 – 7142Cleavage; by gamma-secretase; site 2
Site720 – 7212Cleavage; by gamma-secretase; site 3
Site739 – 7402Cleavage; by caspase-6, caspase-8 or caspase-9

Amino acid modifications

Modified residue1981Phosphoserine; by CK2 Ref.74
Modified residue2061Phosphoserine; by CK1 Ref.74
Modified residue7291Phosphothreonine By similarity
Modified residue7301Phosphoserine; by APP-kinase I By similarity
Modified residue7431Phosphothreonine; by CDK5 and MAPK10 Ref.73
Modified residue7571Phosphotyrosine Ref.83
Glycosylation5421N-linked (GlcNAc...) Ref.84
Glycosylation5711N-linked (GlcNAc...) Probable
Glycosylation6141O-linked (GalNAc...) Ref.33
Glycosylation6231O-linked (GalNAc...) Ref.33
Glycosylation6281O-linked (GalNAc...) Ref.33
Glycosylation6331O-linked (GalNAc...) Ref.94
Glycosylation6511O-linked (GalNAc...) Ref.94
Glycosylation6521O-linked (GalNAc...) Ref.94
Glycosylation6561O-linked (Xyl...) (chondroitin sulfate); in L-APP isoforms Ref.94
Glycosylation6591O-linked (GalNAc...)
Glycosylation6631O-linked (GalNAc...) Probable
Glycosylation6671O-linked (GalNAc...) Probable
Glycosylation6791O-linked (GalNAc...) Ref.33
Glycosylation6971O-linked (GalNAc...) Ref.33
Disulfide bond38 ↔ 62 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond73 ↔ 117 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond98 ↔ 105 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond133 ↔ 187 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond144 ↔ 174 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond158 ↔ 186 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond291 ↔ 341 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond300 ↔ 324 Ref.75 Ref.109 Ref.110 Ref.113
Disulfide bond316 ↔ 337 Ref.75 Ref.109 Ref.110 Ref.113

Natural variations

Alternative sequence1 – 1919MLPGL…ARALE → MDQLEDLLVLFINY in isoform 11.
VSP_045446
Alternative sequence19 – 7456Missing in isoform APP639.
VSP_009116
Alternative sequence289 – 36375Missing in isoform APP639.
VSP_009117
Alternative sequence2891E → V in isoform APP695, isoform L-APP696, isoform L-APP677 and isoform APP714.
VSP_000002
Alternative sequence290 – 36475Missing in isoform APP695 and isoform L-APP677.
VSP_000004
Alternative sequence290 – 34556Missing in isoform L-APP696 and isoform APP714.
VSP_000003
Alternative sequence290 – 30516VCSEQ…RAMIS → KWYKEVHSGQARWLML in isoform APP305.
VSP_000005
Alternative sequence306 – 770465Missing in isoform APP305.
VSP_000006
Alternative sequence345 – 36420MSQSL…DPVKL → I in isoform 11.
VSP_045447
Alternative sequence3451M → I in isoform L-APP733 and isoform APP751.
VSP_000007
Alternative sequence346 – 36419Missing in isoform L-APP733 and isoform APP751.
VSP_000008
Alternative sequence3641L → V in isoform APP639.
VSP_009118
Alternative sequence637 – 65418Missing in isoform L-APP677, isoform L-APP696, isoform L-APP733 and isoform L-APP752.
VSP_000009
Natural variant5011E → K. Ref.10
Corresponds to variant rs45588932 [ dbSNP | Ensembl ].
VAR_022315
Natural variant6651E → D in a patient with late onset Alzheimer disease. Ref.127
VAR_010107
Natural variant670 – 6712KM → NL in AD1.
VAR_000015
Natural variant6781D → N in AD1. Ref.25
VAR_044424
Natural variant6921A → G in AD1; Flemish mutation; increases the solubility of processed beta-amyloid peptides and increases the stability of peptide oligomers. Ref.122 Ref.131 Ref.138
VAR_000016
Natural variant6931E → G in AD1. Ref.121 Ref.139
VAR_014215
Natural variant6931E → K in CAA-APP; Italian type.
VAR_014216
Natural variant6931E → Q in CAA-APP; Dutch type. Ref.115
VAR_000017
Natural variant6941D → N in CAA-APP; Iowa type. Ref.137 Ref.141
VAR_014217
Natural variant7051L → V in CAA-APP; Italian type. Ref.143
VAR_032276
Natural variant7131A → T in AD1. Ref.125 Ref.142
VAR_000019
Natural variant7131A → V in one chronic schizophrenia patient; unknown pathological significance. Ref.124
Corresponds to variant rs1800557 [ dbSNP | Ensembl ].
VAR_000018
Natural variant7141T → A in AD1. Ref.140
VAR_032277
Natural variant7141T → I in AD1; increased beta-APP42/beta-APP40 ratio. Ref.136 Ref.144
VAR_014218
Natural variant7151V → M in AD1; decreased beta-APP40/total APP-beta. Ref.132
VAR_010108
Natural variant7161I → V in AD1. Ref.130
VAR_000020
Natural variant7171V → F in AD1. Ref.23 Ref.120 Ref.126 Ref.128
VAR_000023
Natural variant7171V → G in AD1. Ref.23 Ref.119
VAR_000022
Natural variant7171V → I in AD1. Ref.23 Ref.116 Ref.117 Ref.118 Ref.126 Ref.129 Ref.133
VAR_000021
Natural variant7171V → L in AD1. Ref.135
VAR_014219
Natural variant7231L → P in AD1. Ref.134
VAR_010109

Experimental info

Mutagenesis99 – 1024KRGR → NQGG: Reduced heparin-binding. Ref.45
Mutagenesis1371H → N: Binds copper. Forms dimer. Ref.44
Mutagenesis1411M → T: Binds copper. Forms dimer. Ref.44
Mutagenesis1441C → S: Binds copper. No dimer formation. No copper reducing activity. Ref.44 Ref.57
Mutagenesis147 – 1493HLH → ALA: 50% decrease in copper reducing activity. Ref.44 Ref.57 Ref.69
Mutagenesis1471H → A: Some decrease in copper reducing activity. Ref.44 Ref.69
Mutagenesis1471H → N: Binds copper. Forms dimer. Ref.44 Ref.69
Mutagenesis1471H → Y: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.44 Ref.69
Mutagenesis1511H → K: Greatly reduced copper-mediated low-density lipoprotein oxidation. Ref.44 Ref.69
Mutagenesis1511H → N: Binds copper. Forms dimer. Ref.44 Ref.69
Mutagenesis1981S → A: Greatly reduced casein kinase phosphorylation. Ref.74 Ref.78
Mutagenesis2061S → A: Reduced casein kinase phosphorylation. Ref.74 Ref.78
Mutagenesis4991R → A: Reduced affinity for heparin; when associated with A-503. Ref.107
Mutagenesis5031K → A: Reduced affinity for heparin; when associated with A-499. Ref.107
Mutagenesis6561S → A: Abolishes chondroitin sulfate binding in L-APP733 isoform. Ref.37
Mutagenesis6761R → G: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.53
Mutagenesis6811Y → F: 60-70% zinc-induced beta-APP (28) peptide aggregation. Ref.53
Mutagenesis6841H → R: Only 23% zinc-induced beta-APP (28) peptide aggregation. Ref.53
Mutagenesis7041G → V: Reduced protein oxidation. No hippocampal neuron toxicity.
Mutagenesis7061M → L: Reduced lipid peroxidation inhibition. Ref.38 Ref.54
Mutagenesis7061M → V: No free radical production. No hippocampal neuron toxicity. Ref.38 Ref.54
Mutagenesis7171V → C or S: Unchanged beta-APP42/total APP-beta ratio. Ref.46 Ref.136
Mutagenesis7171V → F, G or I: Increased beta-APP42/beta-APP40 ratio. Ref.46 Ref.136
Mutagenesis7171V → K: Decreased beta-APP42/total APP-beta ratio. Ref.46 Ref.136
Mutagenesis7171V → M: Increased beta-APP42/beta-APP40 ratio. No change in apoptosis after caspase cleavage. Ref.46 Ref.136
Mutagenesis7281Y → 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
Mutagenesis7391D → A: No cleavage by caspases during apoptosis. Ref.60 Ref.76 Ref.79
Mutagenesis7391D → N: No effect on FADD-induced apoptosis. Ref.60 Ref.76 Ref.79
Mutagenesis7431T → 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
Mutagenesis7431T → E: Reduced NGF-stimulated neurite extension. No effect on APP maturation. Ref.77 Ref.80 Ref.81 Ref.83
Mutagenesis7561G → A: APP internalization unchanged. No change in beta-APP42 secretion. Ref.56
Mutagenesis7571Y → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.48 Ref.56 Ref.68 Ref.83
Mutagenesis7571Y → G: Loss of binding to MAPK8IP1, APBA1, APBB1, APPBP2 and SHC1. Ref.48 Ref.56 Ref.68 Ref.83
Mutagenesis7591N → A: No binding to APBA1, no effect on APBB1 binding. Little APP internalization. Reduced beta-APP42 secretion. Ref.48 Ref.56
Mutagenesis7601P → A: Little APP internalization. Reduced beta-APP42 secretion. Ref.56
Mutagenesis7621Y → A: Loss of binding to APBA1 and APBB1. APP internalization unchanged. No change in beta-APP42 secretion. Ref.48 Ref.56
Sequence conflict15 – 162AR → VW in CAA31830. Ref.3
Sequence conflict6471D → E in AAA51722. Ref.36
Sequence conflict7241Missing in AAB26263. Ref.23
Sequence conflict7241Missing in AAB26264. Ref.23
Sequence conflict7311I → N in AAB26263. Ref.23
Sequence conflict7311I → N in AAB26264. Ref.23
Sequence conflict7311I → N in AAB26265. Ref.23
Sequence conflict7571Y → S in AAA35540. Ref.31

Secondary structure

................................................................................ 770
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform APP770 (PreA4 770) [UniParc].

Last modified November 1, 1991. Version 3.
Checksum: A12EE761403740F5

FASTA77086,943
        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 

« Hide

Isoform APP305 [UniParc].

Checksum: D1CCD7237262687A
Show »

FASTA30534,358
Isoform L-APP677 [UniParc].

Checksum: 48334D3EEF26990E
Show »

FASTA67776,760
Isoform APP695 (PreA4 695) [UniParc].

Checksum: 4F6EA0139F969D56
Show »

FASTA69578,663
Isoform L-APP696 [UniParc].

Checksum: 66DFDFFCFDB75A72
Show »

FASTA69678,866
Isoform APP714 [UniParc].

Checksum: 124EA691773DC13B
Show »

FASTA71480,769
Isoform L-APP733 [UniParc].

Checksum: 44528239D68A53EE
Show »

FASTA73382,916
Isoform APP751 (PreA4 751) [UniParc].

Checksum: C987C557C5A3714E
Show »

FASTA75184,819
Isoform L-APP752 [UniParc].

Checksum: 074CFF767CBED2E0
Show »

FASTA75285,040
Isoform APP639 [UniParc].

Checksum: C4120DEC51A59A95
Show »

FASTA63972,553
Isoform 11 [UniParc].

Checksum: 843411EFBDEFACE3
Show »

FASTA74684,521

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 AT SER-198 AND SER-206 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 TYR-757, 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.
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]"Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein."
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X., Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J., Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORL1, SUBCELLULAR LOCATION.
[88]"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.
[89]"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.
[90]"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.
[91]"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.
[92]"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.
[93]"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].
[94]"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, IDENTIFICATION BY MASS SPECTROMETRY.
[95]"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.
[96]"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.
[97]"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.
[98]"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.
[99]"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.
[100]"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.
[101]"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.
[102]"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.
[103]"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.
[104]"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.
[105]"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.
[106]"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.
[107]"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, MUTAGENESIS OF ARG-499 AND LYS-503, IDENTIFICATION BY MASS SPECTROMETRY.
[108]"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.
[109]"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.
[110]"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.
[111]"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.
[112]"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. expand/collapse author list , 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.
[113]"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, SUBUNIT, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
[114]"Framing beta-amyloid."
Hardy J.
Nat. Genet. 1:233-234(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[115]"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.
[116]"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. expand/collapse author list , Rossor M., Owen M., Hardy J.
Nature 349:704-706(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AD1 ILE-717.
[117]"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.
[118]"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.
[119]"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.
[120]"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.
[121]"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. expand/collapse author list , 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.
[122]"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.
[123]"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.
[124]"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.
[125]"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.
[126]"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.
[127]"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.
[128]"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.
[129]"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.
[130]"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.
[131]"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.
[132]"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.
[133]"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.
[134]"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.
[135]"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.
[136]"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.
[137]"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.
[138]"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.
[139]"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.
[140]"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.
[141]"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.
[142]"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.
[143]"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.
[144]"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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00264 mRNA. Translation: CAA68374.1.
X13466 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , M34862, M34863, M34864, M34865, M34866, M34867, M34868, M34869, M34870, M34871, M34872, M34873, M34874, M34876, M34877, M34878, M34879 Genomic DNA. Translation: AAB59502.1.
M34875 expand/collapse EMBL AC list , 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.
CCDSCCDS13576.1. [P05067-1]
CCDS13577.1. [P05067-4]
CCDS33523.1. [P05067-8]
CCDS46638.1. [P05067-10]
CCDS56212.1. [P05067-11]
CCDS56213.1. [P05067-9]
PIRS01442.
QRHUA4. S02260.
RefSeqNP_000475.1. NM_000484.3. [P05067-1]
NP_001129488.1. NM_001136016.3. [P05067-11]
NP_001129601.1. NM_001136129.2. [P05067-10]
NP_001129602.1. NM_001136130.2.
NP_001129603.1. NM_001136131.2.
NP_001191230.1. NM_001204301.1. [P05067-9]
NP_001191231.1. NM_001204302.1. [P05067-7]
NP_001191232.1. NM_001204303.1. [P05067-3]
NP_958816.1. NM_201413.2. [P05067-8]
NP_958817.1. NM_201414.2. [P05067-4]
UniGeneHs.434980.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AAPX-ray1.50A/B287-344[»]
1AMBNMR-A672-699[»]
1AMCNMR-A672-699[»]
1AMLNMR-A672-711[»]
1BA4NMR-A672-711[»]
1BA6NMR-A672-711[»]
1BJBNMR-A672-699[»]
1BJCNMR-A672-699[»]
1BRCX-ray2.50I287-342[»]
1CA0X-ray2.10D/I289-342[»]
1HZ3NMR-A681-706[»]
1IYTNMR-A672-713[»]
1MWPX-ray1.80A28-123[»]
1OWTNMR-A124-189[»]
1QCMNMR-A696-706[»]
1QWPNMR-A696-706[»]
1QXCNMR-A696-706[»]
1QYTNMR-A696-706[»]
1TAWX-ray1.80B287-344[»]
1TKNNMR-A460-569[»]
1UO7model-A672-713[»]
1UO8model-A672-713[»]
1UOAmodel-A672-713[»]
1UOImodel-A672-713[»]
1X11X-ray2.50C/D754-766[»]
1Z0QNMR-A672-713[»]
1ZE7NMR-A672-687[»]
1ZE9NMR-A672-687[»]
1ZJDX-ray2.60B289-344[»]
2BEGNMR-A/B/C/D/E672-713[»]
2BOMmodel-A/B681-713[»]
2BP4NMR-A672-687[»]
2FJZX-ray1.61A133-189[»]
2FK1X-ray1.60A133-189[»]
2FK2X-ray1.65A133-189[»]
2FK3X-ray2.40A/B/C/D/E/F/G/H133-189[»]
2FKLX-ray2.50A/B124-189[»]
2FMAX-ray0.85A133-189[»]
2G47X-ray2.10C/D672-711[»]
2IPUX-ray1.65P/Q672-679[»]
2LFMNMR-A672-711[»]
2LLMNMR-A686-726[»]
2LMNNMR-A/B/C/D/E/F/G/H/I/J/K/L672-711[»]
2LMONMR-A/B/C/D/E/F/G/H/I/J/K/L672-711[»]
2LMPNMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R672-711[»]
2LMQNMR-A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R672-711[»]
2LNQNMR-A/B/C/D/E/F/G/H672-711[»]
2LOHNMR-A/B686-726[»]
2LP1NMR-A671-770[»]
2LZ3NMR-A/B699-726[»]
2LZ4NMR-A/B699-726[»]
2M4JNMR-A/B/C/D/E/F/G/H/I672-711[»]
2M9RNMR-A672-711[»]
2M9SNMR-A672-711[»]
2OTKNMR-C672-711[»]
2R0WX-ray2.50Q672-679[»]
2WK3X-ray2.59C/D672-713[»]
2Y29X-ray2.30A687-692[»]
2Y2AX-ray1.91A687-692[»]
2Y3JX-ray1.99A/B/C/D/E/F/G/H701-706[»]
2Y3KX-ray1.90A/B/C/D/E/F/G/H706-713[»]
2Y3LX-ray2.10A/B/C/G706-713[»]
3AYUX-ray2.00B586-595[»]
3BAEX-ray1.59A672-699[»]
3BKJX-ray1.59A672-687[»]
3DXCX-ray2.10B/D739-770[»]
3DXDX-ray2.20B/D739-770[»]
3DXEX-ray2.00B/D739-770[»]
3GCIX-ray2.04P707-713[»]
3IFLX-ray1.50P672-678[»]
3IFNX-ray1.50P672-711[»]
3IFOX-ray2.15P/Q672-678[»]
3IFPX-ray2.95P/Q/R/S672-678[»]
3JQ5X-ray2.03B672-679[»]
3JQLX-ray1.20B687-692[»]
3JTIX-ray1.80B699-706[»]
3KTMX-ray2.70A/B/C/D/E/F/G/H18-190[»]
3L33X-ray2.48E/F/G/H290-341[»]
3L81X-ray1.60B761-767[»]
3MOQX-ray2.05A/B/C/D689-712[»]
3MXCX-ray2.00L754-762[»]
3MXYX-ray2.30L754-762[»]
3NYJX-ray3.20A365-567[»]
3NYLX-ray2.80A365-570[»]
3OVJX-ray1.80A/B/C/D687-692[»]
3OW9X-ray1.80A/B687-692[»]
3SV1X-ray3.30D/E/F754-767[»]
3U0TX-ray2.50E/F701-711[»]
3UMHX-ray2.00A370-575[»]
3UMIX-ray2.40A370-575[»]
3UMKX-ray2.60A370-575[»]
4HIXX-ray2.20A672-699[»]
4MDRX-ray1.85B758-767[»]
4NGEX-ray2.70B/E672-711[»]
ProteinModelPortalP05067.
SMRP05067. Positions 26-192, 287-342, 385-567, 683-728, 741-768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106848. 1971 interactions.
DIPDIP-574N.
IntActP05067. 113 interactions.
MINTMINT-150767.

Chemistry

BindingDBP05067.
ChEMBLCHEMBL2487.

Protein family/group databases

MEROPSI02.015.
TCDB1.C.50.1.2. the amyloid -protein peptide (app) family.

PTM databases

PhosphoSiteP05067.
UniCarbKBP05067.

Polymorphism databases

DMDM112927.

2D gel databases

SWISS-2DPAGEP05067.

Proteomic databases

MaxQBP05067.
PaxDbP05067.
PRIDEP05067.

Protocols and materials databases

DNASU351.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346798; ENSP00000284981; ENSG00000142192. [P05067-1]
ENST00000348990; ENSP00000345463; ENSG00000142192. [P05067-4]
ENST00000354192; ENSP00000346129; ENSG00000142192. [P05067-10]
ENST00000357903; ENSP00000350578; ENSG00000142192. [P05067-8]
ENST00000358918; ENSP00000351796; ENSG00000142192. [P05067-9]
ENST00000359726; ENSP00000352760; ENSG00000142192. [P05067-6]
ENST00000440126; ENSP00000387483; ENSG00000142192. [P05067-11]
GeneID351.
KEGGhsa:351.
UCSCuc002ylz.3. human. [P05067-1]
uc002yma.3. human. [P05067-8]
uc002ymb.3. human. [P05067-4]
uc010glj.3. human. [P05067-10]
uc010glk.3. human.
uc011acj.2. human. [P05067-2]
uc021whz.1. human. [P05067-9]
uc021wia.1. human. [P05067-7]
uc021wib.1. human. [P05067-3]

Organism-specific databases

CTD351.
GeneCardsGC21M027252.
GeneReviewsAPP.
HGNCHGNC:620. APP.
HPACAB000157.
HPA001462.
MIM104300. phenotype.
104760. gene.
605714. phenotype.
neXtProtNX_P05067.
Orphanet1020. 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.
PharmGKBPA24910.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289770.
HOVERGENHBG000051.
InParanoidP05067.
KOK04520.
OMATHAHIVI.
OrthoDBEOG7RNJZP.
PhylomeDBP05067.
TreeFamTF317274.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000142192-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SABIO-RKP05067.

Gene expression databases

ArrayExpressP05067.
BgeeP05067.
GenevestigatorP05067.

Family and domain databases

Gene3D3.30.1490.140. 1 hit.
3.90.570.10. 1 hit.
4.10.230.10. 1 hit.
4.10.410.10. 1 hit.
InterProIPR008155. 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.
IPR028866. APP.
IPR019543. APP_amyloid_C.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PANTHERPTHR23103:SF7. PTHR23103:SF7. 1 hit.
PfamPF10515. 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]
PRINTSPR00203. AMYLOIDA4.
PR00759. BASICPTASE.
PR00204. BETAAMYLOID.
SMARTSM00006. A4_EXTRA. 1 hit.
SM00131. KU. 1 hit.
[Graphical view]
SUPFAMSSF109843. SSF109843. 1 hit.
SSF56491. SSF56491. 1 hit.
SSF57362. SSF57362. 1 hit.
SSF89811. SSF89811. 1 hit.
PROSITEPS00319. A4_EXTRA. 1 hit.
PS00320. A4_INTRA. 1 hit.
PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSapp. human.
EvolutionaryTraceP05067.
GeneWikiAmyloid_precursor_protein.
GenomeRNAi351.
NextBio1445.
PMAP-CutDBP05067.
PROP05067.
SOURCESearch...

Entry information

Entry nameA4_HUMAN
AccessionPrimary (citable) accession number: P05067
Secondary accession number(s): B2R5V1 expand/collapse secondary AC list , 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: July 9, 2014
This is version 229 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM