A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Gene Hsap\APP

General Information
SymbolHsap\APPSpeciesH. sapiens
Nameamyloid beta (A4) precursor proteinAnnotation symbol
Feature typeengineered_foreign_geneFlyBase IDFBgn0025823
Gene Model StatusNot Applicable Stock availability 60 publicly available
Also Known AsAPP, Aβ, Aβ42, Abeta, hAPP, Alz
Genomic Location
Chromosome (arm)Recombination map
Cytogenetic mapSequence location
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Automatically generated summary

See sections below for more information
The gene amyloid beta (A4) precursor protein is referred to in FlyBase by the symbol Hsap\APP (FBgn0025823). It is a engineered_foreign_gene from Homo sapiens. Its molecular function is unknown. The biological processes in which it is involved are not known. 100 alleles are reported. The phenotypes of these alleles are annotated with: organ system subdivision; organ system; external compound sense organ; adult; adult segment; sense organ; peripheral nervous system; cytoplasmic part; multicellular structure; organelle. It has no annotated transcripts. Gene has not been localized to the genome sequence.
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FB2013_03
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Experimentally Determined Cytological Location
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Experimentally Determined Recombination Data
Location
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Annotated Polypeptides
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Length (aa)
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GenBank protein
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Protein sequence
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Marker for
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Reference
See Gelbart and Emmert, 2010.10.13 for analysis details and data files for all genes.
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Lethality
Allele
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Allele
Phenotype manifest in
Allele
hide Classical Alleles ( 0 )
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Allele of Hsap\APPClassMutagenStocksKnown lesion
hide Alleles Carried on Transgenic Constructs ( 100 )
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Allele of Hsap\APPClassMutagenStocksKnown lesion
Hsap\APP695.Scer\UAS.Exel6 Yes
Hsap\APPAβ42.Scer\UAS.cBa4 Yes
Hsap\APPC99.Scer\UAS.Exel.T:Hsap\MYC4 Yes
Hsap\APPAβ42.D694N.Scer\UAS.VTR3 Yes
Hsap\APP1-42.Scer\UAS2 Yes
Hsap\APP695.E693Q.Scer\UAS.Exel2 Yes
Hsap\APP695.Scer\UAS.T:Hsap\MYC2 Yes
Hsap\APPAβ42.A692G.Scer\UAS.VTR2 Yes
Hsap\APPAβ42.E693G.Scer\UAS.VTR2 Yes
Hsap\APPAβ42.E693K.Scer\UAS.VTR2 Yes
Hsap\APPAβ42.E693Q.Scer\UAS.VTR2 Yes
Hsap\APPC99.V717I.Scer\UAS.Exel.T:Ivir\HA12 Yes
Hsap\APPC99.YIPLFL.Scer\UAS.Exel.T:Ivir\HA12 Yes
Hsap\APPScer\UAS.T:Hsap\MYC.T:SV40\nls2.T:Ecol\lexA.T:Hsim\VP162 Yes
Hsap\APPSPA4CT.Scer\UAS.T:SV40\nls2.T:Ecol\lexA.T:Hsim\VP162 Yes
Hsap\APPΔICD.Scer\UAS.T:Hsap\MYC,T:Avic\GFP-EGFP2 Yes
Hsap\APPΔNPTY.Scer\UAS.T:Hsap\MYC2 Yes
Hsap\APP695-Swedish.Scer\UAST:Hsap\MYC1 Yes
Hsap\APP695SPA4CT.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APP695ΔCT.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APP770.E693Q.V715A.Scer\UAS.VTR.T:Hsap\MYC1 Yes
Hsap\APP770.E693Q.V715M.Scer\UAS.VTR.T:Hsap\MYC1 Yes
Hsap\APP770.K670N.M671L.E693G.Scer\UAS.VTR1 Yes
Hsap\APP770.K670N.M671L.Scer\UAS.VTR1 Yes
Hsap\APPC99.Scer\UAS.Exel.T:SS-Lcp2,T:Ivir\HA11 Yes
Hsap\APPM596I.F615P.Scer\UAS1 Yes
Hsap\APPN684A.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APPScer\UAS.T:Avic\GFP-YFP1 --
Hsap\APPV717F.LOND.Scer\UAS1 Yes
Hsap\APPY682A.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APPΔBASS.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APPΔEC.Scer\UAS.T:SV40\nls2,T:Ecol\lexA,T:Hsim\VP161 Yes
Hsap\APPΔGo.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APPΔPEER.Scer\UAS.T:Hsap\MYC1 Yes
Hsap\APP+1.Tn10\tetO0 Yes
Hsap\APP1-40.Scer\UAS.T:SS-nec0 Yes
Hsap\APP3HR.attB.Aβ42.Scer\UAS0 Yes
Hsap\APP695-Swedish.Scer\UAS0 Yes
Hsap\APP695.Scer\UAS0 Yes
Hsap\APP695.T.Scer\UAS0 Yes
Hsap\APPA2F.Scer\UAS.T:SS-nec0 Yes
Hsap\APPArctic.Scer\UAS.T:SS-nec0 Yes
Hsap\APPAβ1-42.Scer\UAS.Arc0 Yes
Hsap\APPAβ1-42.Scer\UAS.art0 Yes
Hsap\APPAβ1-42.Scer\UAS.cIa0 Yes
Hsap\APPAβ1-42.Scer\UAS0 Yes
Hsap\APPAβ1-42.TRH.Scer\UAS0 Yes
Hsap\APPAβ3Q-42.TRH.Scer\UAS0 Yes
Hsap\APPAβ40.GMR0 Yes
Hsap\APPAβ40.Scer\UAS.att0 Yes
Hsap\APPAβ40.Scer\UAS.T:Rnor\PENK0 Yes
Hsap\APPAβ40.Scer\UAS0 Yes
Hsap\APPAβ42.GMR0 Yes
Hsap\APPAβ42.Scer\UAS.att0 Yes
Hsap\APPAβ42.Scer\UAS.attB0 Yes
Hsap\APPAβ42.Scer\UAS.cHa0 Yes
Hsap\APPAβ42.Scer\UAS.T:Rnor\PENK0 Yes
Hsap\APPAβ42.Scer\UAS.T:SS-hh0 Yes
Hsap\APPAβ42.Scer\UAS0 Yes
Hsap\APPC59.MtnA.T:Scer\GAL4,T:Hsim\VP160 Yes
Hsap\APPC99.MtnA.T:Scer\GAL4,T:Hsim\VP160 Yes
Hsap\APPC99.Scer\UAS0 Yes
Hsap\APPC99.T:Scer\GAL4,T:Hsim\VP160 Yes
Hsap\APPD7R.Scer\UAS.T:SS-nec0 Yes
Hsap\APPE11G.Scer\UAS.T:SS-nec0 Yes
Hsap\APPF20E.Scer\UAS.T:SS-nec0 Yes
Hsap\APPF4DE22G.Scer\UAS.T:SS-nec0 Yes
Hsap\APPG9TE22G.Scer\UAS.T:SS-nec0 Yes
Hsap\APPH14W.Scer\UAS.T:SS-nec0 Yes
Hsap\APPH6WE22G.Scer\UAS.T:SS-nec0 Yes
Hsap\APPI31EE22G.Scer\UAS.T:SS-nec0 Yes
Hsap\APPK16W.Scer\UAS.T:SS-nec0 Yes
Hsap\APPL17R.Scer\UAS.T:SS-nec0 Yes
Hsap\APPM35F.Scer\UAS.T:SS-nec0 Yes
Hsap\APPN27W.Scer\UAS.T:SS-nec0 Yes
Hsap\APPR5Y.Scer\UAS.T:SS-nec0 Yes
Hsap\APPs.α.Scer\UAS.T:Ivir\HA10 Yes
Hsap\APPs.β.Scer\UAS.T:Ivir\HA10 Yes
Hsap\APPS8D.Scer\UAS.T:SS-nec0 Yes
Hsap\APPSC100.Act5C0 Yes
Hsap\APPSC100.I716F.Act5C0 Yes
Hsap\APPSC100.T:Scer\GAL40 Yes
Hsap\APPScer\UAS.T:Hsap\MYC0 Yes
Hsap\APPScer\UAS.T:SS-nec0 Yes
Hsap\APPScer\UAS.T:SV40\nls2.T:Ecol\lexA.T:Hsim\VP160 Yes
Hsap\APPsecα.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPsecβ.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPT12.Aβ40.Scer\UAS0 Yes
Hsap\APPT12.Aβ42.Scer\UAS0 Yes
Hsap\APPT22.Aβ40.Scer\UAS0 Yes
Hsap\APPT22.Aβ42.Scer\UAS0 Yes
Hsap\APPTn10\tetO.cHa0 Yes
Hsap\APPTNL.Aβ40.Scer\UAS0 Yes
Hsap\APPTNL.Aβ42.Scer\UAS0 Yes
Hsap\APPY687A.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPΔ.hs.T:Scer\GAL4,T:Hsim\VP160 Yes
Hsap\APPΔE1.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPΔE2.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPΔEC.Scer\UAS.T:Hsap\MYC0 Yes
Hsap\APPΔECD.Scer\UAS.T:Hsap\MYC0 Yes
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Transgenic Constructs
Type of construct
Name
Expression data
Insertions
Type of insertions
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Interacts with
Please look at the allele data for full details of the genetic interactions
Hsap\APP allele
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hide OrthoDB Orthologs (0) - based on analysis using Dmel annotation version 5.41
OrthoDB Ortholog Groups
Drosophila inclusive ortholog search
No orthologs identified
Dipteran inclusive ortholog search
No orthologs identified
Insect inclusive ortholog search
No orthologs identified
Arthropod inclusive ortholog search
No orthologs identified
Metazoa inclusive ortholog search
No orthologs identified
Ortholog(s) in Drosophila melanogaster (None identified)
No D. melanogaster orthologies identified
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Gene
OMIM
HGNC
hideAAA Orthologs (0) based on analysis using Dmel annotation version 4.3
No orthologs identified
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Bloomington
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Additional comments
FlyBase curator comment: Name changed to reflect current HGNC name (19th Nov. 2012).
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  • Foreign sequence; species == Homo sapiens; gene == APP; HGNC:620.
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hide Synonyms & Secondary IDs ( 25 )
Reported As
Symbol Synonym
Hsap\APP
 
Name Synonym
amyloid beta (A4) precursor protein
 
amyloid-beta (Aβ) peptide
Amyloid beta A4 precursor protein
 
amyloid-β peptide
amyloid-β protein
human amyloid precursor protein
β-amyloid
Secondary FlyBase IDs
hide References ( 88 )
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hide Recent research papers ( 22 )
Hopkins, 2013, PLoS ONE 8(2): e55810
Neurodegeneration in a Drosophila Model for the Function of TMCC2, an Amyloid Protein Precursor-Interacting and Apolipoprotein E-Binding Protein. [FBrf0220834]
Caesar et al., 2012, PLoS ONE 7(2): e31424
Curcumin Promotes A-beta Fibrillation and Reduces Neurotoxicity in Transgenic Drosophila. [FBrf0217504]
Lang et al., 2012, PLoS Genet. 8(4): e1002683
Genetic inhibition of solute-linked carrier 39 family transporter 1 ameliorates aβ pathology in a Drosophila model of Alzheimer's disease. [FBrf0218220]
Lloyd et al., 2012, Neuron 74(2): 344--360
The p150(Glued) CAP-Gly Domain Regulates Initiation of Retrograde Transport at Synaptic Termini. [FBrf0218160]
Pirooznia et al., 2012, Genetics 192(4): 1327--1345
Epigenetic regulation of axonal growth of Drosophila pacemaker cells by histone acetyltransferase tip60 controls sleep. [FBrf0220123]
Reis et al., 2012, Mol. Biol. Cell 23(9): 1700--1714
Molecular motor function in axonal transport in vivo probed by genetic and computational analysis in Drosophila. [FBrf0218178]
Rogers et al., 2012, PLoS ONE 7(7): e40569
Ageing increases vulnerability to abeta42 toxicity in Drosophila. [FBrf0218882]
Scherzer-Attali et al., 2012, Neurobiol. Disease 46(3): 663--672
Naphthoquinone-tyrptophan reduces neurotoxic Aβ*56 levels and improves cognition in Alzheimer's disease animal model. [FBrf0219431]
Singh and Mlodzik, 2012, Dev. Cell 23(1): 82--96
Hibris, a Drosophila Nephrin Homolog, Is Required for Presenilin-Mediated Notch and APP-like Cleavages. [FBrf0218978]
Speretta et al., 2012, J. Biol. Chem. 287(24): 20748--20754
Expression in Drosophila of Tandem Amyloid β Peptides Provides Insights into Links between Aggregation and Neurotoxicity. [FBrf0218555]
Wentzell et al., 2012, Neurobiol. Disease 46(1): 78--87
Amyloid precursor proteins are protective in Drosophila models of progressive neurodegeneration. [FBrf0217742]
Chakraborty et al., 2011, PLoS ONE 6(6): e20799
Characterization of a Drosophila Alzheimer's disease model: pharmacological rescue of cognitive defects. [FBrf0213930]
Copenhaver et al., 2011, Dis. Model Mech. 4(5): 634--648
A translational continuum of model systems for evaluating treatment strategies in Alzheimer's disease: isradipine as a candidate drug. [FBrf0215047]
Diangelo et al., 2011, PLoS ONE 6(5): e19921
The central clock neurons regulate lipid storage in Drosophila. [FBrf0213791]
Frydman-Marom et al., 2011, ACS Chem. Biol. 6(11): 1265--1276
Structural basis for inhibiting β-amyloid oligomerization by a non-coded β-breaker-substituted endomorphin analogue. [FBrf0218223]
Goguel et al., 2011, J. Neurosci. 31(3): 1032--1037
Drosophila amyloid precursor protein-like is required for long-term memory. [FBrf0212809]
Hoe et al., 2011, Aging 3(3): 237--261
Ubiquitin over-expression phenotypes and ubiquitin gene molecular misreading during aging in Drosophila melanogaster. [FBrf0213373]
Hua et al., 2011, Biol. Chem. 392(10): 919--926
Toxicity of Alzheimer's disease-associated Aβ peptide is ameliorated in a Drosophila model by tight control of zinc and copper availability. [FBrf0215055]
Kim et al., 2011, BMC Physiol. 11: 7
Expression of human amyloid precursor protein in the skeletal muscles of Drosophila results in age- and activity-dependent muscle weakness. [FBrf0213903]
Kumar et al., 2011, EMBO J. 30(11): 2255--2265
Extracellular phosphorylation of the amyloid β-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease. [FBrf0213841]
Lee et al., 2011, Mol. Cells 31(4): 337--342
The effects of hempseed meal intake and linoleic acid on Drosophila models of neurodegenerative diseases and hypercholesterolemia. [FBrf0213599]
Liu et al., 2011, J. Biol. Chem. 286(6): 4248--4256
Iron Promotes the Toxicity of Amyloid {beta} Peptide by Impeding Its Ordered Aggregation. [FBrf0212930]
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All reviews listed in FlyBase were published before 2011