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Aliases for APP Gene

Aliases for APP Gene

  • Amyloid Beta (A4) Precursor Protein 2 3
  • CVAP 3 4 6
  • AD1 3 4 6
  • Alzheimer Disease Amyloid Protein 3 4
  • Cerebral Vascular Amyloid Peptide 3 4
  • Peptidase Nexin-II 2 3
  • Protease Nexin-II 3 4
  • PN-II 3 4
  • PreA4 3 4
  • ABPP 3 4
  • APPI 3 4
  • AAA 3 6
  • Beta-Amyloid Peptide(1-40) 3
  • Beta-Amyloid Peptide(1-42) 3
  • Amyloid Beta A4 Protein 3
  • Beta-Amyloid Peptide 3
  • Alzheimer Disease 2
  • CTFgamma 3
  • ABETA 3
  • PN2 3
  • A4 4

External Ids for APP Gene

Previous Symbols for APP Gene

  • AD1

Summaries for APP Gene

Entrez Gene Summary for APP Gene

  • This gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. In addition, two of the peptides are antimicrobial peptides, having been shown to have bacteriocidal and antifungal activities. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Aug 2014]

GeneCards Summary for APP Gene

APP (Amyloid Beta (A4) Precursor Protein) is a Protein Coding gene. Diseases associated with APP include alzheimer disease and cerebral amyloid angiopathy, dutch, italian, iowa, flemish, arctic variants. Among its related pathways are Signaling by GPCR and Disease. GO annotations related to this gene include identical protein binding and heparin binding. An important paralog of this gene is APLP1.

UniProtKB/Swiss-Prot for APP Gene

  • Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.

  • Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts

  • Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.

  • The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis

  • N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6)

Tocris Summary for APP Gene

  • Amyloid beta (Abeta) peptides are the major component of amyloid plaques found in the brains of Alzheimers patients. Abeta is formed from the progressive cleavage of amyloid precursor protein (APP) by beta- and gamma-secretase. Two Abeta peptides are formed from APP degradation; Abeta40 and Abeta42. Abeta40 is the most abundant form, but Abeta42 is more fibrillogenic, thus is associated with disease states. Mutations in APP have been linked to early onset Alzheimers disease, as proteolytic cleavage of the altered protein increases the levels of Abeta42 relative to Abeta40. Furthermore, Abeta proteins have been associated with other diseases including Lewy body dementia, inclusion body myositis and cerebral amyloid angiopathy.

Gene Wiki entry for APP Gene

No data available for PharmGKB "VIP" Summary , fRNAdb sequence ontologies and piRNA Summary for APP Gene

Genomics for APP Gene

Genomic Location for APP Gene

Start:
25,880,550 bp from pter
End:
26,171,128 bp from pter
Size:
290,579 bases
Orientation:
Minus strand

Genomic View for APP Gene

UCSC Golden Path with GeneCards custom track
Cytogenetic band:
Genomic Location for APP Gene
GeneLoc Logo Genomic Neighborhood Exon StructureGene Density

RefSeq DNA sequence for APP Gene

Regulatory Elements for APP Gene

Transcription factor binding sites by QIAGEN in the APP gene promoter:

Proteins for APP Gene

  • Protein details for APP Gene (UniProtKB/Swiss-Prot)

    Protein Symbol:
    P05067-A4_HUMAN
    Recommended name:
    Amyloid beta A4 protein
    Protein Accession:
    P05067
    Secondary Accessions:
    • B2R5V1
    • B4DII8
    • D3DSD1
    • D3DSD2
    • D3DSD3
    • P09000
    • P78438
    • Q13764
    • Q13778
    • Q13793
    • Q16011
    • Q16014
    • Q16019
    • Q16020
    • Q6GSC0
    • Q8WZ99
    • Q9BT38
    • Q9UC33
    • Q9UCA9
    • Q9UCB6
    • Q9UCC8
    • Q9UCD1
    • Q9UQ58

    Protein attributes for APP Gene

    Size:
    770 amino acids
    Molecular mass:
    86943 Da
    Quaternary 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. Interacts with PLD3.
    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
    SequenceCaution:
    • Sequence=AAA58727.1; Type=Miscellaneous discrepancy; Note=Contamination by an Alu repeat.; Evidence={ECO:0000305};

    Three dimensional structures from OCA and Proteopedia for APP Gene

    Alternative splice isoforms for APP Gene

neXtProt entry for APP Gene

Proteomics data for APP Gene at MOPED

Post-translational modifications for APP Gene

  • Beta-amyloid peptides are degraded by IDE
  • 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
  • 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.
  • 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.
  • 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
  • Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are found in cerebral spinal fluid (CSF) including the beta-amyloid X-15 peptides, produced from the cleavage by alpha-secretase and all terminatiing at Gln-686
  • 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)
  • Modification sites at PhosphoSitePlus
  • Ubiquitination at Lys751 and Lys763
  • Glycosylation at Thr107, Thr352, Thr353, Thr366, Thr367, Ser370, Thr371, Thr381, Asn542, Asn571, Thr600, Ser614, Ser623, Ser628, Thr633, Thr651, Thr652, Ser656, Thr659, Thr663, Ser667, Ser679, and Ser697

No data available for DME Specific Peptides for APP Gene

Domains for APP Gene

Gene Families for APP Gene

HGNC:

Graphical View of Domain Structure for InterPro Entry

P05067

UniProtKB/Swiss-Prot:

A4_HUMAN
Domain:
  • The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.:
    • P05067
  • 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.:
    • P05067
  • Contains 1 BPTI/Kunitz inhibitor domain.:
    • P05067
Family:
  • Belongs to the APP family.:
    • P05067
genes like me logo Genes that share domains with APP: view

Function for APP Gene

Molecular function for APP Gene

GENATLAS Biochemistry: amyloid beta (A4) precursor protein (APP 695) undergoing proteolytic cleavages by either alpha,beta or gamma secretases in or near the transmembrane domain,to yield several secreted derivatives,including soluble APP,4kDa,beta peptide (A beta) and a related,3 kDa,protein,expressed ubiquitously by neuronal and non neuronal cells and sorted to axons in neurons and the basolateral surface in epithelial cells (see PN2)
UniProtKB/Swiss-Prot Function: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.
UniProtKB/Swiss-Prot Function: Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with Also bind GPC1 in lipid rafts
UniProtKB/Swiss-Prot Function: Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brain.
UniProtKB/Swiss-Prot Function: The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis
UniProtKB/Swiss-Prot Function: N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6)
UniProtKB/Swiss-Prot Induction: Increased levels during neuronal differentiation

Gene Ontology (GO) - Molecular Function for APP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0003677 DNA binding ISS --
GO:0004867 serine-type endopeptidase inhibitor activity IDA 10652580
GO:0005102 receptor binding IPI 19849849
GO:0005515 protein binding IPI 10049767
GO:0008201 heparin binding IEA --
genes like me logo Genes that share ontologies with APP: view
genes like me logo Genes that share phenotypes with APP: view

Animal Models for APP Gene

MGI Knock Outs for APP:

No data available for Enzyme Numbers (IUBMB) , Transcription Factor Targeting and HOMER Transcription for APP Gene

Localization for APP Gene

Subcellular locations from UniProtKB/Swiss-Prot for APP Gene

Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Colocalizes with SORL1 in a vesicular pattern in cytoplasm and perinuclear regions.

Subcellular locations from

COMPARTMENTS
Jensen Localization Image for APP Gene COMPARTMENTS Subcellular localization image for APP gene
Compartment Confidence
cytosol 4
extracellular 4
golgi apparatus 4
plasma membrane 4
cytoskeleton 2
endoplasmic reticulum 2
endosome 2
mitochondrion 2
nucleus 2
vacuole 2
lysosome 1
peroxisome 1

Gene Ontology (GO) - Cellular Components for APP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0005576 extracellular region TAS --
GO:0005615 extracellular space IDA 16502470
GO:0005641 nuclear envelope lumen IDA 21989385
GO:0005737 cytoplasm ISS --
GO:0005768 endosome IDA 18353773
genes like me logo Genes that share ontologies with APP: view

Pathways for APP Gene

genes like me logo Genes that share pathways with APP: view

Gene Ontology (GO) - Biological Process for APP Gene

GO ID Qualified GO term Evidence PubMed IDs
GO:0001967 suckling behavior IEA --
GO:0002576 platelet degranulation TAS --
GO:0006378 mRNA polyadenylation ISS --
GO:0006417 regulation of translation ISS --
GO:0006468 protein phosphorylation ISS --
genes like me logo Genes that share ontologies with APP: view

Compounds for APP Gene

(5) Tocris Compounds for APP Gene

Compound Action Cas Number
Amyloid beta-Peptide (1-40) (human) Amyloid beta-protein fragment [131438-79-4]
Amyloid beta-Peptide (1-42) (human) Predominant amyloid beta-protein fragment [107761-42-2]
Amyloid beta-peptide (1-42) (rat) Predominant amyloid beta-protein fragment [166090-74-0]
Amyloid beta-peptide (42-1) (human) Inactive control peptide for amyloid beta-peptide (1-42) (Cat. No. 1428) [317366-82-8]
Ro 90-7501 Inhibitor of Abeta42 fibril formation [293762-45-5]

(6) HMDB Compounds for APP Gene

Compound Synonyms Cas Number PubMed IDs
Clotrimazole
  • (Chlorotrityl)imidazole
23593-75-1
Copper
  • Cu
7440-50-8
FAD
  • 1H-Purin-6-amine flavin dinucleotide
146-14-5
Heparin
  • Arteven
9005-49-6
Hydrogen peroxide
  • Hydrogen peroxide
7722-84-1

(1) Drugbank Compounds for APP Gene

Compound Synonyms Cas Number Type Actions PubMed IDs
Methionine Sulfoxide
62697-73-8 target

(120) Novoseek inferred chemical compound relationships for APP Gene

Compound -log(P) Hits PubMed IDs
thioflavin t 82.5 14
happ 76.6 15
clioquinol 69.6 4
aspartate(1-) 68.5 1
thioflavin 67.2 2
genes like me logo Genes that share compounds with APP: view

Transcripts for APP Gene

Unigene Clusters for APP Gene

Amyloid beta (A4) precursor protein:
Representative Sequences:

Alternative Splicing Database (ASD) splice patterns (SP) for APP Gene

No ASD Table

Relevant External Links for APP Gene

GeneLoc Exon Structure for
APP
ECgene alternative splicing isoforms for
APP

Expression for APP Gene

mRNA expression in normal human tissues for APP Gene

mRNA expression in embryonic tissues and stem cells from LifeMap Discovery

Integrated Proteomics: protein expression from ProteomicsDB, PaxDb, MOPED, and MaxQB for APP Gene

SOURCE GeneReport for Unigene cluster for APP Gene Hs.434980

mRNA Expression by UniProt/SwissProt for APP Gene

P05067-A4_HUMAN
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.
genes like me logo Genes that share expressions with APP: view

No data available for mRNA differential expression in normal tissues for APP Gene

Orthologs for APP Gene

This gene was present in the common ancestor of animals.

Orthologs for APP Gene

Organism Taxonomy Gene Similarity Type Details
chimpanzee
(Pan troglodytes)
Mammalia APP 35
  • 99.7 (n)
  • 99.87 (a)
APP 36
  • 100 (a)
OneToOne
cow
(Bos Taurus)
Mammalia APP 35
  • 91.22 (n)
  • 98.06 (a)
APP 36
  • 98 (a)
OneToOne
dog
(Canis familiaris)
Mammalia APP 35
  • 91.17 (n)
  • 96.97 (a)
APP 36
  • 97 (a)
OneToOne
mouse
(Mus musculus)
Mammalia App 35
  • 89.36 (n)
  • 96.81 (a)
App 16
App 36
  • 97 (a)
OneToOne
oppossum
(Monodelphis domestica)
Mammalia APP 36
  • 91 (a)
OneToOne
platypus
(Ornithorhynchus anatinus)
Mammalia APP 36
  • 70 (a)
OneToOne
rat
(Rattus norvegicus)
Mammalia App 35
  • 89.27 (n)
  • 97.07 (a)
chicken
(Gallus gallus)
Aves APP 35
  • 82.54 (n)
  • 93.45 (a)
APP 36
  • 94 (a)
OneToOne
lizard
(Anolis carolinensis)
Reptilia APP 36
  • 70 (a)
OneToOne
African clawed frog
(Xenopus laevis)
Amphibia MGC52816 35
tropical clawed frog
(Silurana tropicalis)
Amphibia app 35
  • 78.76 (n)
  • 88.13 (a)
Str.11113 35
zebrafish
(Danio rerio)
Actinopterygii -- 35
APP (1 of 3) 36
  • 62 (a)
OneToMany
appa 36
  • 69 (a)
OneToMany
appb 35
  • 69.02 (n)
  • 71.47 (a)
appb 36
  • 66 (a)
OneToMany
fruit fly
(Drosophila melanogaster)
Insecta Appl 36
  • 20 (a)
OneToMany
worm
(Caenorhabditis elegans)
Secernentea apl-1 35
  • 45.96 (n)
  • 34.77 (a)
apl-1 36
  • 27 (a)
OneToMany
apl-1 37
  • 37 (a)
Species with no ortholog for APP:
  • A. gosspyii yeast (Ashbya gossypii)
  • Actinobacteria (Mycobacterium tuberculosis)
  • African malaria mosquito (Anopheles gambiae)
  • Alicante grape (Vitis vinifera)
  • alpha proteobacteria (Wolbachia pipientis)
  • amoeba (Dictyostelium discoideum)
  • Archea (Pyrococcus horikoshii)
  • baker's yeast (Saccharomyces cerevisiae)
  • barley (Hordeum vulgare)
  • beta proteobacteria (Neisseria meningitidis)
  • bread mold (Neurospora crassa)
  • Chromalveolata (Phytophthora infestans)
  • common water flea (Daphnia pulex)
  • corn (Zea mays)
  • E. coli (Escherichia coli)
  • filamentous fungi (Aspergillus nidulans)
  • Firmicute bacteria (Streptococcus pneumoniae)
  • fission yeast (Schizosaccharomyces pombe)
  • green algae (Chlamydomonas reinhardtii)
  • honey bee (Apis mellifera)
  • K. lactis yeast (Kluyveromyces lactis)
  • loblloly pine (Pinus taeda)
  • malaria parasite (Plasmodium falciparum)
  • medicago trunc (Medicago Truncatula)
  • moss (Physcomitrella patens)
  • orangutan (Pongo pygmaeus)
  • pig (Sus scrofa)
  • rainbow trout (Oncorhynchus mykiss)
  • rice (Oryza sativa)
  • rice blast fungus (Magnaporthe grisea)
  • schistosome parasite (Schistosoma mansoni)
  • sea anemone (Nematostella vectensis)
  • sea squirt (Ciona intestinalis)
  • sea squirt (Ciona savignyi)
  • sea urchin (Strongylocentrotus purpuratus)
  • sorghum (Sorghum bicolor)
  • soybean (Glycine max)
  • stem rust fungus (Puccinia graminis)
  • sugarcane (Saccharum officinarum)
  • thale cress (Arabidopsis thaliana)
  • tomato (Lycopersicon esculentum)
  • toxoplasmosis (Toxoplasma gondii)
  • Trichoplax (Trichoplax adhaerens)
  • wheat (Triticum aestivum)

Evolution for APP Gene

ENSEMBL:
Gene Tree for APP (if available)
TreeFam:
Gene Tree for APP (if available)

Paralogs for APP Gene

Paralogs for APP Gene

genes like me logo Genes that share paralogs with APP: view

Variants for APP Gene

Sequence variations from dbSNP and Humsavar for APP Gene

SNP ID Clin Chr 21 pos Sequence Context AA Info Type MAF
rs1145 -- 25,887,702(-) TTTGC(A/G)TATCT intron-variant
rs1146 -- 25,887,689(-) taaac(A/C)tagaa intron-variant
rs3991 -- 26,055,940(-) TAAGG(G/T)CAGAT intron-variant
rs4175 -- 25,965,985(-) GGAGC(A/G)CTGCT intron-variant
rs57126 -- 25,939,511(+) CAAGT(A/G)TCAAA intron-variant

Structural Variations from Database of Genomic Variants (DGV) for APP Gene

Variant ID Type Subtype PubMed ID
esv2723294 CNV Deletion 23290073
esv4736 CNV Deletion 18987735
esv2723296 CNV Deletion 23290073
esv2660354 CNV Deletion 23128226
esv2723297 CNV Deletion 23290073
nsv513715 OTHER Inversion 21212237
esv998808 OTHER Inversion 20482838
esv2648254 OTHER Inversion 19546169
nsv513716 OTHER Inversion 21212237
esv2965 OTHER Inversion 18987735
esv1301961 OTHER Inversion 17803354
esv7875 OTHER Inversion 19470904
nsv510502 CNV Loss 20534489
nsv526774 CNV Loss 19592680

Relevant External Links for APP Gene

HapMap Linkage Disequilibrium report
APP
Human Gene Mutation Database (HGMD)
APP
Locus Specific Mutation Databases (LSDB)
APP

No data available for Polymorphic Variants from UniProtKB/Swiss-Prot for APP Gene

Disorders for APP Gene

(2) OMIM Diseases for APP Gene (104760)

UniProtKB/Swiss-Prot

A4_HUMAN
  • Alzheimer disease 1 (AD1) [MIM:104300]: A familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death. {ECO:0000269 PubMed:10097173, ECO:0000269 PubMed:10631141, ECO:0000269 PubMed:10665499, ECO:0000269 PubMed:10867787, ECO:0000269 PubMed:11063718, ECO:0000269 PubMed:11528419, ECO:0000269 PubMed:12034808, ECO:0000269 PubMed:1302033, ECO:0000269 PubMed:1303239, ECO:0000269 PubMed:1303275, ECO:0000269 PubMed:1415269, ECO:0000269 PubMed:15201367, ECO:0000269 PubMed:15365148, ECO:0000269 PubMed:15668448, ECO:0000269 PubMed:1671712, ECO:0000269 PubMed:1678058, ECO:0000269 PubMed:1908231, ECO:0000269 PubMed:1925564, ECO:0000269 PubMed:1944558, ECO:0000269 PubMed:8267572, ECO:0000269 PubMed:8290042, ECO:0000269 PubMed:8476439, ECO:0000269 PubMed:8577393, ECO:0000269 PubMed:9328472, ECO:0000269 PubMed:9754958}. Note=The disease is caused by mutations affecting the gene represented in this entry.
  • 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.

(97) Novoseek inferred disease relationships for APP Gene

Disease -log(P) Hits PubMed IDs
alzheimers disease 97.8 246
senile plaques 96.9 135
neurofibrillary tangles 90.4 103
cerebral amyloid angiopathy 89.2 76
amyloid deposition 87.7 67

Relevant External Links for APP

GeneTests
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GeneReviews
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Genetic Association Database (GAD)
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Human Genome Epidemiology (HuGE) Navigator
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genes like me logo Genes that share disorders with APP: view

Publications for APP Gene

  1. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene. (PMID: 1303239) Hendriks L. … Van Broeckhoven C. (Nat. Genet. 1992) 3 4 23
  2. Mutation in codon 713 of the beta amyloid precursor protein gene presenting with schizophrenia. (PMID: 1307241) Jones C.T. … St Clair D. (Nat. Genet. 1992) 3 4 23
  3. Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region. (PMID: 1415269) Kamino K. … Schellenberg G.D. (Am. J. Hum. Genet. 1992) 3 4 23
  4. DNA diagnosis for hereditary cerebral hemorrhage with amyloidosis (Dutch type) (PMID: 1679289) Bakker E. … Frangione B. (Am. J. Hum. Genet. 1991) 2 3 23
  5. The chondroitin sulfate attachment site of appican is formed by splicing out exon 15 of the amyloid precursor gene. (PMID: 7737970) Pangalos M.N. … Robakis N.K. (J. Biol. Chem. 1995) 3 4 23

Products for APP Gene

  • Addgene plasmids for APP

Sources for APP Gene

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