MOUSE:A4

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Species (Taxon ID)	Mus musculus (Mouse). ([1])
Gene Name(s)	App
Protein Name(s)	Amyloid beta A4 protein ABPP APP Alzheimer disease amyloid A4 protein homolog Amyloidogenic glycoprotein AG N-APP Soluble APP-alpha S-APP-alpha Soluble APP-beta S-APP-beta C99 APP-C99 Beta-amyloid protein 42 Beta-APP42 Beta-amyloid protein 40 Beta-APP40 C83 P3(42) P3(40) C80 Gamma-secretase C-terminal fragment 59 APP-C59 Amyloid intracellular domain 59 AID(59) Gamma-CTF(59) Gamma-secretase C-terminal fragment 57 APP-C57 Amyloid intracellular domain 57 AID(57) Gamma-CTF(57) Gamma-secretase C-terminal fragment 50 Amyloid intracellular domain 50 AID(50) Gamma-CTF(50) C31
External Links
EMBL	M18373 X59379 U84012 D10603 BC005490 M24397 X15210 U82624
IPI	IPI00114389 IPI00230494 IPI00323079
PIR	A27485 A32282 S04855
RefSeq	NP_001185752.1
UniGene	Mm.277585
PDB	2ROZ 2YSZ 2YT0 2YT1
PDBsum	2ROZ 2YSZ 2YT0 2YT1
ProteinModelPortal	P12023
SMR	P12023
IntAct	P12023
MINT	MINT-208509
STRING	P12023
MEROPS	I02.015
PhosphoSite	P12023
PRIDE	P12023
Ensembl	ENSMUST00000005406 ENSMUST00000074271
GeneID	11820
KEGG	mmu:11820
UCSC	uc007ztn.2
CTD	351
MGI	MGI:88059
eggNOG	roNOG06213
HOGENOM	HBG402865
HOVERGEN	HBG000051
InParanoid	P12023
OMA	RKQCKTH
OrthoDB	EOG45B1F4
PhylomeDB	P12023
ArrayExpress	P12023
Bgee	P12023
CleanEx	MM_APP
Genevestigator	P12023
GermOnline	ENSMUSG00000022892
GO	GO:0045177 GO:0030424 GO:0035253 GO:0005905 GO:0031410 GO:0005794 GO:0016021 GO:0031594 GO:0048471 GO:0051233 GO:0003677 GO:0008201 GO:0046872 GO:0005515 GO:0004867 GO:0008344 GO:0008088 GO:0016199 GO:0007155 GO:0006878 GO:0048669 GO:0016358 GO:0006897 GO:0030900 GO:0000085 GO:0035235 GO:0007617 GO:0006378 GO:0045665 GO:0050885 GO:0016322 GO:0007219 GO:0045931 GO:0045944 GO:0006468 GO:0007176 GO:0040014 GO:0050803 GO:0006417 GO:0051563 GO:0001967 GO:0051124 GO:0008542
InterPro	IPR008155 IPR013803 IPR011178 IPR024329 IPR008154 IPR019744 IPR015849 IPR019745 IPR019543 IPR002223 IPR020901
Gene3D	G3DSA:4.10.230.10 G3DSA:3.30.1490.140 G3DSA:3.90.570.10 G3DSA:4.10.410.10
Pfam	PF10515 PF12924 PF12925 PF02177 PF03494 PF00014
PRINTS	PR00203 PR00759 PR00204
SMART	SM00006 SM00131
SUPFAM	SSF56491 SSF89811 SSF57362 SSF109843
PROSITE	PS00319 PS00320 PS00280 PS50279

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000085	G2 phase of mitotic cell cycle	PMID:15561424^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154535	P	Seeded From UniProt
	GO:0001967	suckling behavior	PMID:9461064^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0003677	DNA binding	PMID:15944124^[3]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002223	F	Seeded From UniProt
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0722	F	Seeded From UniProt
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	F	Seeded From UniProt
	GO:0005102	receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	F	Seeded From UniProt
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:10460257^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P97318	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P98084	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QXJ1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQF2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WVI9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WVI9-1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11517249^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WVI9-1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11877420^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q61120	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16193067^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q03157	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16193067^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q06335	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16227582^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P61812	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17121854^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QXJ1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17727637^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q8C142	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17934213^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q9D1T0	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18278038^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q61330	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20817278^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q9JHI9	F	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:10845772^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:15886206^[15]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005624	membrane fraction	PMID:9535056^[16]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:10845772^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C	Seeded From UniProt
	GO:0005794	Golgi apparatus	PMID:16018997^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0005905	coated pit	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0168	C	Seeded From UniProt
	GO:0005905	coated pit	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0069	C	Seeded From UniProt
	GO:0006378	mRNA polyadenylation	PMID:16314516^[18]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006417	regulation of translation	PMID:16314516^[18]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006468	protein phosphorylation	PMID:16025111^[19]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2652346	P	Seeded From UniProt
	GO:0006878	cellular copper ion homeostasis	PMID:10526140^[20]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0006878	cellular copper ion homeostasis	PMID:15447675^[21]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0006897	endocytosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0254	P	Seeded From UniProt
	GO:0006897	endocytosis	PMID:16025111^[19]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2652346	P	Seeded From UniProt
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P	Seeded From UniProt
	GO:0006917	induction of apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P	Seeded From UniProt
	GO:0007155	cell adhesion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0130	P	Seeded From UniProt
	GO:0007176	regulation of epidermal growth factor-activated receptor activity	PMID:17556541^[22]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0007219	Notch signaling pathway	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0914	P	Seeded From UniProt
	GO:0007409	axonogenesis	PMID:9390996^[23]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0007617	mating behavior	PMID:9461064^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0007626	locomotory behavior	PMID:9461064^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0008088	axon cargo transport	PMID:11740561^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0008088	axon cargo transport	PMID:20829454^[25]	IGI: Inferred from Genetic Interaction	MGI:MGI:97180	P	Seeded From UniProt
	GO:0008201	heparin binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0358	F	Seeded From UniProt
	GO:0008344	adult locomotory behavior	PMID:10188929^[26]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0008344	adult locomotory behavior	PMID:7758106^[27]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0008344	adult locomotory behavior	PMID:8001115^[28]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0008344	adult locomotory behavior	PMID:9754878^[29]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0008542	visual learning	PMID:10338291^[30]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0009986	cell surface	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0010466	negative regulation of peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	P	Seeded From UniProt
	GO:0010468	regulation of gene expression	PMID:12074840^[31]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0010952	positive regulation of peptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0162	C	Seeded From UniProt
	GO:0016020	membrane	PMID:11877420^[6]	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0016020	membrane	PMID:12927782^[32]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C	Seeded From UniProt
	GO:0016021	integral to membrane	PMID:12927782^[32]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0016199	axon midline choice point recognition	PMID:8001115^[28]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0016322	neuron remodeling	PMID:10219973^[33]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0016358	dendrite development	PMID:10188929^[26]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0016358	dendrite development	PMID:15689559^[34]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0016358	dendrite development	PMID:9390996^[23]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0016504	peptidase activator activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	F	Seeded From UniProt
	GO:0019717	synaptosome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C	Seeded From UniProt
	GO:0030414	peptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	F	Seeded From UniProt
	GO:0030424	axon	PMID:11740561^[24]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0030424	axon	PMID:15745965^[35]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0030900	forebrain development	PMID:10200318^[36]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0030900	forebrain development	PMID:10200318^[36]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154535	P	Seeded From UniProt
	GO:0030900	forebrain development	PMID:8001115^[28]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0031175	neuron projection development	PMID:8083748^[37]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0031410	cytoplasmic vesicle	PMID:11740561^[24]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0031410	cytoplasmic vesicle	PMID:15745965^[35]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0031594	neuromuscular junction	PMID:10845772^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0033130	acetylcholine receptor binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	F	Seeded From UniProt
	GO:0035235	ionotropic glutamate receptor signaling pathway	PMID:16025111^[19]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2652346	P	Seeded From UniProt
	GO:0035253	ciliary rootlet	PMID:16018997^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0040014	regulation of multicellular organism growth	PMID:9754878^[29]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154522	P	Seeded From UniProt
	GO:0042802	identical protein binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	F	Seeded From UniProt
	GO:0043005	neuron projection	PMID:16301330^[38]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0043197	dendritic spine	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0043198	dendritic shaft	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0045177	apical part of cell	PMID:15561424^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045202	synapse	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	C	Seeded From UniProt
	GO:0045665	negative regulation of neuron differentiation	PMID:18278038^[12]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0045665	negative regulation of neuron differentiation	PMID:18278038^[12]	IGI: Inferred from Genetic Interaction	MGI:MGI:104518	P	Seeded From UniProt
	GO:0045931	positive regulation of mitotic cell cycle	PMID:15561424^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2154535	P	Seeded From UniProt
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	PMID:15944124^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F	Seeded From UniProt
	GO:0048471	perinuclear region of cytoplasm	PMID:8207383^[39]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0048669	collateral sprouting in absence of injury	PMID:15689559^[34]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0050803	regulation of synapse structure and activity	PMID:10219973^[33]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
	GO:0050885	neuromuscular process controlling balance	PMID:9461064^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0051124	synaptic growth at neuromuscular junction	PMID:15689559^[34]	IGI: Inferred from Genetic Interaction	MGI:MGI:88047	P	Seeded From UniProt
	GO:0051233	spindle midzone	PMID:15561424^[1]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0051402	neuron apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	P	Seeded From UniProt
	GO:0051425	PTB domain binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000284981	F	Seeded From UniProt
	GO:0051563	smooth endoplasmic reticulum calcium ion homeostasis	PMID:12431992^[40]	IGI: Inferred from Genetic Interaction	MGI:MGI:1202717	P	Seeded From UniProt
	GO:0008088	axon cargo transport	PMID:15745965^[35]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2136847	P	Seeded From UniProt
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 López-Sánchez N et al. (2005) Lengthening of G2/mitosis in cortical precursors from mice lacking beta-amyloid precursor protein. Neuroscience 130: 51-60 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 von Koch CS et al. (1997) Generation of APLP2 KO mice and early postnatal lethality in APLP2/APP double KO mice. Neurobiol Aging 18: 661-9 PubMed GONUTS page
↑ ^3.0 ^3.1 Pardossi-Piquard R et al. (2005) Presenilin-dependent transcriptional control of the Abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP. Neuron 46: 541-54 PubMed GONUTS page
↑ Homayouni R et al. (1999) Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J Neurosci 19: 7507-15 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 Matsuda S et al. (2001) c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK. J Neurosci 21: 6597-607 PubMed GONUTS page
↑ ^6.0 ^6.1 Tarr PE et al. (2002) Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J Biol Chem 277: 16798-804 PubMed GONUTS page
↑ ^7.0 ^7.1 Soba P et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24: 3624-34 PubMed GONUTS page
↑ Hashimoto Y et al. (2005) Transforming growth factor beta2 is a neuronal death-inducing ligand for amyloid-beta precursor protein. Mol Cell Biol 25: 9304-17 PubMed GONUTS page
↑ Minopoli G et al. (2007) Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage. J Biol Chem 282: 831-5 PubMed GONUTS page
↑ Mameza MG et al. (2007) Characterization of the adaptor protein ARH expression in the brain and ARH molecular interactions. J Neurochem 103: 927-41 PubMed GONUTS page
↑ Bai Y et al. (2008) The in vivo brain interactome of the amyloid precursor protein. Mol Cell Proteomics 7: 15-34 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Ma QH et al. (2008) A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis. Nat Cell Biol 10: 283-94 PubMed GONUTS page
↑ Duce JA et al. (2010) Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142: 857-67 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Akaaboune M et al. (2000) Developmental regulation of amyloid precursor protein at the neuromuscular junction in mouse skeletal muscle. Mol Cell Neurosci 15: 355-67 PubMed GONUTS page
↑ Vetrivel KS et al. (2005) Spatial segregation of gamma-secretase and substrates in distinct membrane domains. J Biol Chem 280: 25892-900 PubMed GONUTS page
↑ Apert C et al. (1998) Profiles of amyloid precursor and presenilin 2-like proteins are correlated during development of the mouse hypothalamus. J Neuroendocrinol 10: 101-9 PubMed GONUTS page
↑ ^17.0 ^17.1 Yang J & Li T (2005) The ciliary rootlet interacts with kinesin light chains and may provide a scaffold for kinesin-1 vesicular cargos. Exp Cell Res 309: 379-89 PubMed GONUTS page
↑ ^18.0 ^18.1 Cao Q et al. (2005) Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation. Mol Cell Biol 25: 10930-9 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 Snyder EM et al. (2005) Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci 8: 1051-8 PubMed GONUTS page
↑ White AR et al. (1999) Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res 842: 439-44 PubMed GONUTS page
↑ Bellingham SA et al. (2004) Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic fibroblasts. J Neurochem 91: 423-8 PubMed GONUTS page
↑ Zhang YW et al. (2007) Presenilin/gamma-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression. Proc Natl Acad Sci U S A 104: 10613-8 PubMed GONUTS page
↑ ^23.0 ^23.1 Perez RG et al. (1997) The beta-amyloid precursor protein of Alzheimer's disease enhances neuron viability and modulates neuronal polarity. J Neurosci 17: 9407-14 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 Kamal A et al. (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414: 643-8 PubMed GONUTS page
↑ Vossel KA et al. (2010) Tau reduction prevents Abeta-induced defects in axonal transport. Science 330: 198 PubMed GONUTS page
↑ ^26.0 ^26.1 Dawson GR et al. (1999) Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the beta-amyloid precursor protein. Neuroscience 90: 1-13 PubMed GONUTS page
↑ Zheng H et al. (1995) beta-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 81: 525-31 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 Müller U et al. (1994) Behavioral and anatomical deficits in mice homozygous for a modified beta-amyloid precursor protein gene. Cell 79: 755-65 PubMed GONUTS page
↑ ^29.0 ^29.1 Tremml P et al. (1998) Neurobehavioral development, adult openfield exploration and swimming navigation learning in mice with a modified beta-amyloid precursor protein gene. Behav Brain Res 95: 65-76 PubMed GONUTS page
↑ Phinney AL et al. (1999) No hippocampal neuron or synaptic bouton loss in learning-impaired aged beta-amyloid precursor protein-null mice. Neuroscience 90: 1207-16 PubMed GONUTS page
↑ Fukami S et al. (2002) Abeta-degrading endopeptidase, neprilysin, in mouse brain: synaptic and axonal localization inversely correlating with Abeta pathology. Neurosci Res 43: 39-56 PubMed GONUTS page
↑ ^32.0 ^32.1 Rouvinski A et al. (2003) Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes. Biochem Biophys Res Commun 308: 750-8 PubMed GONUTS page
↑ ^33.0 ^33.1 Seabrook GR et al. (1999) Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein. Neuropharmacology 38: 349-59 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 Wang P et al. (2005) Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2. J Neurosci 25: 1219-25 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 Lazarov O et al. (2005) Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: revisited. J Neurosci 25: 2386-95 PubMed GONUTS page
↑ ^36.0 ^36.1 Magara F et al. (1999) Genetic background changes the pattern of forebrain commissure defects in transgenic mice underexpressing the beta-amyloid-precursor protein. Proc Natl Acad Sci U S A 96: 4656-61 PubMed GONUTS page
↑ Jin LW et al. (1994) Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension. J Neurosci 14: 5461-70 PubMed GONUTS page
↑ Muresan Z & Muresan V (2005) Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1. J Cell Biol 171: 615-25 PubMed GONUTS page
↑ Salbaum JM & Ruddle FH (1994) Embryonic expression pattern of amyloid protein precursor suggests a role in differentiation of specific subsets of neurons. J Exp Zool 269: 116-27 PubMed GONUTS page
↑ Herms J et al. (2003) Capacitive calcium entry is directly attenuated by mutant presenilin-1, independent of the expression of the amyloid precursor protein. J Biol Chem 278: 2484-9 PubMed GONUTS page

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[PMID:16193067-6] 7.0 ^7.1 Soba P et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24: 3624-34 PubMed GONUTS page

[PMID:16227582-7] Hashimoto Y et al. (2005) Transforming growth factor beta2 is a neuronal death-inducing ligand for amyloid-beta precursor protein. Mol Cell Biol 25: 9304-17 PubMed GONUTS page

[PMID:17121854-8] Minopoli G et al. (2007) Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage. J Biol Chem 282: 831-5 PubMed GONUTS page

[PMID:17727637-9] Mameza MG et al. (2007) Characterization of the adaptor protein ARH expression in the brain and ARH molecular interactions. J Neurochem 103: 927-41 PubMed GONUTS page

[PMID:17934213-10] Bai Y et al. (2008) The in vivo brain interactome of the amyloid precursor protein. Mol Cell Proteomics 7: 15-34 PubMed GONUTS page

[PMID:18278038-11] 12.0 ^12.1 ^12.2 Ma QH et al. (2008) A TAG1-APP signalling pathway through Fe65 negatively modulates neurogenesis. Nat Cell Biol 10: 283-94 PubMed GONUTS page

[PMID:20817278-12] Duce JA et al. (2010) Iron-export ferroxidase activity of β-amyloid precursor protein is inhibited by zinc in Alzheimer's disease. Cell 142: 857-67 PubMed GONUTS page

[PMID:10845772-13] 14.0 ^14.1 ^14.2 Akaaboune M et al. (2000) Developmental regulation of amyloid precursor protein at the neuromuscular junction in mouse skeletal muscle. Mol Cell Neurosci 15: 355-67 PubMed GONUTS page

[PMID:15886206-14] Vetrivel KS et al. (2005) Spatial segregation of gamma-secretase and substrates in distinct membrane domains. J Biol Chem 280: 25892-900 PubMed GONUTS page

[PMID:9535056-15] Apert C et al. (1998) Profiles of amyloid precursor and presenilin 2-like proteins are correlated during development of the mouse hypothalamus. J Neuroendocrinol 10: 101-9 PubMed GONUTS page

[PMID:16018997-16] 17.0 ^17.1 Yang J & Li T (2005) The ciliary rootlet interacts with kinesin light chains and may provide a scaffold for kinesin-1 vesicular cargos. Exp Cell Res 309: 379-89 PubMed GONUTS page

[PMID:16314516-17] 18.0 ^18.1 Cao Q et al. (2005) Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation. Mol Cell Biol 25: 10930-9 PubMed GONUTS page

[PMID:16025111-18] 19.0 ^19.1 ^19.2 Snyder EM et al. (2005) Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci 8: 1051-8 PubMed GONUTS page

[PMID:10526140-19] White AR et al. (1999) Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice. Brain Res 842: 439-44 PubMed GONUTS page

[PMID:15447675-20] Bellingham SA et al. (2004) Gene knockout of amyloid precursor protein and amyloid precursor-like protein-2 increases cellular copper levels in primary mouse cortical neurons and embryonic fibroblasts. J Neurochem 91: 423-8 PubMed GONUTS page

[PMID:17556541-21] Zhang YW et al. (2007) Presenilin/gamma-secretase-dependent processing of beta-amyloid precursor protein regulates EGF receptor expression. Proc Natl Acad Sci U S A 104: 10613-8 PubMed GONUTS page

[PMID:9390996-22] 23.0 ^23.1 Perez RG et al. (1997) The beta-amyloid precursor protein of Alzheimer's disease enhances neuron viability and modulates neuronal polarity. J Neurosci 17: 9407-14 PubMed GONUTS page

[PMID:11740561-23] 24.0 ^24.1 ^24.2 Kamal A et al. (2001) Kinesin-mediated axonal transport of a membrane compartment containing beta-secretase and presenilin-1 requires APP. Nature 414: 643-8 PubMed GONUTS page

[PMID:20829454-24] Vossel KA et al. (2010) Tau reduction prevents Abeta-induced defects in axonal transport. Science 330: 198 PubMed GONUTS page

[PMID:10188929-25] 26.0 ^26.1 Dawson GR et al. (1999) Age-related cognitive deficits, impaired long-term potentiation and reduction in synaptic marker density in mice lacking the beta-amyloid precursor protein. Neuroscience 90: 1-13 PubMed GONUTS page

[PMID:7758106-26] Zheng H et al. (1995) beta-Amyloid precursor protein-deficient mice show reactive gliosis and decreased locomotor activity. Cell 81: 525-31 PubMed GONUTS page

[PMID:8001115-27] 28.0 ^28.1 ^28.2 Müller U et al. (1994) Behavioral and anatomical deficits in mice homozygous for a modified beta-amyloid precursor protein gene. Cell 79: 755-65 PubMed GONUTS page

[PMID:9754878-28] 29.0 ^29.1 Tremml P et al. (1998) Neurobehavioral development, adult openfield exploration and swimming navigation learning in mice with a modified beta-amyloid precursor protein gene. Behav Brain Res 95: 65-76 PubMed GONUTS page

[PMID:10338291-29] Phinney AL et al. (1999) No hippocampal neuron or synaptic bouton loss in learning-impaired aged beta-amyloid precursor protein-null mice. Neuroscience 90: 1207-16 PubMed GONUTS page

[PMID:12074840-30] Fukami S et al. (2002) Abeta-degrading endopeptidase, neprilysin, in mouse brain: synaptic and axonal localization inversely correlating with Abeta pathology. Neurosci Res 43: 39-56 PubMed GONUTS page

[PMID:12927782-31] 32.0 ^32.1 Rouvinski A et al. (2003) Both raft- and non-raft proteins associate with CHAPS-insoluble complexes: some APP in large complexes. Biochem Biophys Res Commun 308: 750-8 PubMed GONUTS page

[PMID:10219973-32] 33.0 ^33.1 Seabrook GR et al. (1999) Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein. Neuropharmacology 38: 349-59 PubMed GONUTS page

[PMID:15689559-33] 34.0 ^34.1 ^34.2 Wang P et al. (2005) Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2. J Neurosci 25: 1219-25 PubMed GONUTS page

[PMID:15745965-34] 35.0 ^35.1 ^35.2 Lazarov O et al. (2005) Axonal transport, amyloid precursor protein, kinesin-1, and the processing apparatus: revisited. J Neurosci 25: 2386-95 PubMed GONUTS page

[PMID:10200318-35] 36.0 ^36.1 Magara F et al. (1999) Genetic background changes the pattern of forebrain commissure defects in transgenic mice underexpressing the beta-amyloid-precursor protein. Proc Natl Acad Sci U S A 96: 4656-61 PubMed GONUTS page

[PMID:8083748-36] Jin LW et al. (1994) Peptides containing the RERMS sequence of amyloid beta/A4 protein precursor bind cell surface and promote neurite extension. J Neurosci 14: 5461-70 PubMed GONUTS page

[PMID:16301330-37] Muresan Z & Muresan V (2005) Coordinated transport of phosphorylated amyloid-beta precursor protein and c-Jun NH2-terminal kinase-interacting protein-1. J Cell Biol 171: 615-25 PubMed GONUTS page

[PMID:8207383-38] Salbaum JM & Ruddle FH (1994) Embryonic expression pattern of amyloid protein precursor suggests a role in differentiation of specific subsets of neurons. J Exp Zool 269: 116-27 PubMed GONUTS page

[PMID:12431992-39] Herms J et al. (2003) Capacitive calcium entry is directly attenuated by mutant presenilin-1, independent of the expression of the amyloid precursor protein. J Biol Chem 278: 2484-9 PubMed GONUTS page

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MOUSE:A4

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