HUMAN:A4

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Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	APP ( synonyms: A4, AD1 )
Protein Name(s)	Amyloid beta A4 protein ABPP APPI APP Alzheimer disease amyloid protein Cerebral vascular amyloid peptide CVAP PreA4 Protease nexin-II PN-II N-APP Soluble APP-alpha S-APP-alpha Soluble APP-beta S-APP-beta 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 Amyloid intracellular domain 59 AICD-59 AID(59) Gamma-CTF(59) Gamma-secretase C-terminal fragment 57 Amyloid intracellular domain 57 AICD-57 AID(57) Gamma-CTF(57) Gamma-secretase C-terminal fragment 50 Amyloid intracellular domain 50 AICD-50 AID(50) Gamma-CTF(50) C31
External Links
UniProt Identifier	A4_HUMAN
UniProt Accessions	P05067, B2R5V1, D3DSD1, D3DSD2, D3DSD3, P09000, P78438, Q13764, Q13778, Q13793, Q16011, Q16014, Q16019, Q16020, Q6GSC0, Q8WZ99, Q9BT38, Q9UC33, Q9UCA9, Q9UCB6, Q9UCC8, Q9UCD1, Q9UQ58,
EMBL	Y00264, X13466, X13467, X13468, X13469, X13470, X13471, X13472, X13473, X13474, X13475, X13476, X13477, X13478, X13479, X13487, X13488, X06989, M33112, M34862, M34863, M34864, M34865, M34866, M34867, M34868, M34869, M34870, M34871, M34872, M34873, M34874, M34876, M34877, M34878, M34879, M34875, M34862, M34863, M34864, M34865, M34866, M34867, M34868, M34869, M34870, M34871, M34872, M34873, D87675, AY919674, CH471079, AK312326, CH471079, CH471079, CH471079, CH471079, CH471079, BC004369, BC065529, M35675, M24547, M24546, M28373, X06982, X06981, M18734, M29270, M29269, AB066441, M15533, M15532, M37896, M37895, S45136, S60317, AF282245, S60721, S61380, S61383, M16765,
PIR	S01442, S02260,
RefSeq	NP_000475.1, NP_001129601.1, NP_001129602.1, NP_001191230.1, NP_001191231.1, NP_001191232.1, NP_958816.1, NP_958817.1,
PDB	1AAP, 1AMB, 1AMC, 1AML, 1BA4, 1BA6, 1BJB, 1BJC, 1BRC, 1CA0, 1HZ3, 1IYT, 1MWP, 1OWT, 1QCM, 1QWP, 1QXC, 1QYT, 1RW6, 1TAW, 1TKN, 1UO7, 1UO8, 1UOA, 1UOI, 1X11, 1Z0Q, 1ZE7, 1ZE9, 1ZJD, 2BEG, 2BOM, 2BP4, 2FJZ, 2FK1, 2FK2, 2FK3, 2FKL, 2FMA, 2G47, 2IPU, 2OTK, 2R0W, 2WK3, 3DXC, 3DXD, 3DXE, 3GCI, 3IFL, 3IFN, 3IFO, 3IFP, 3JTI, 3KTM, 3L33, 3L81, 3MOQ, 3MXC, 3MXY, 3NYJ,
IntAct	P05067,
Ensembl	ENST00000346798,
Pfam	PF10515, PF02177, PF03494, PF00014,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0035253	ciliary rootlet	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0007626	locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0008344	adult locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0051233	spindle midzone	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005794	Golgi apparatus	PMID:18029348^[1]	IDA: Inferred from Direct Assay		C
	GO:0016358	dendrite development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0010952	positive regulation of peptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P
	GO:0004867	serine-type endopeptidase inhibitor activity	PMID:10652580^[2]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:18387811^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NSC5	F
	GO:0005515	protein binding	PMID:15983050^[4]	IPI: Inferred from Physical Interaction	UniProtKB:O43736	F
	GO:0005515	protein binding	PMID:21163940^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0016021	integral to membrane	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0005515	protein binding	PMID:20195357^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P01100	F
	GO:0006417	regulation of translation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0007617	mating behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0048669	collateral sprouting in absence of injury	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:18272596^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q8IWV2	F
	GO:0048669	collateral sprouting in absence of injury	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0007617	mating behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0016021	integral to membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002223	F
	GO:0005576	extracellular region	PMID:12935895^[8]	EXP: Inferred from Experiment		C
	GO:0050885	neuromuscular process controlling balance	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:15896298^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P30101	F
	GO:0005576	extracellular region	PMID:10531386^[10]	EXP: Inferred from Experiment		C
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0006378	mRNA polyadenylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0030414	peptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	F
	GO:0005515	protein binding	PMID:18026102^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P01034	F
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	C
	GO:0005905	coated pit	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0069	C
	GO:0007626	locomotory behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006468	protein phosphorylation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0035235	ionotropic glutamate receptor signaling pathway	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:14983046^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9HCB6	F
	GO:0042802	identical protein binding	PMID:16286452^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P05067	F
	GO:0005515	protein binding	PMID:10081969^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BYD4	F
	GO:0009986	cell surface	PMID:7593229^[15]	IDA: Inferred from Direct Assay		C
	GO:0019717	synaptosome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C
	GO:0005515	protein binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P36544	F
	GO:0005515	protein binding	PMID:19366692^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NQX7	F
	GO:0050803	regulation of synapse structure and activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0003677	DNA binding	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	F
	GO:0042802	identical protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P05067-4	F
	GO:0016504	peptidase activator activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	F
	GO:0031093	platelet alpha granule lumen	Reactome:REACT_21351	TAS: Traceable Author Statement		C
	GO:0005515	protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:Q06481	F
	GO:0005515	protein binding	PMID:11877420^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P29353	F
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	C
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0005515	protein binding	PMID:10673326^[20]	IPI: Inferred from Physical Interaction	UniProtKB:P31696	F
	GO:0030424	axon	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C
	GO:0005905	coated pit	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0168	C
	GO:0005515	protein binding	PMID:8855266^[21]	IPI: Inferred from Physical Interaction	UniProtKB:Q92870	F
	GO:0008219	cell death	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0523	P
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:O00213	F
	GO:0006917	induction of apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P
	GO:0005515	protein binding	PMID:19225519^[23]	IPI: Inferred from Physical Interaction	UniProtKB:P08138	F
	GO:0016322	neuron remodeling	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P
	GO:0035235	ionotropic glutamate receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:10567208^[24]	IPI: Inferred from Physical Interaction	UniProtKB:P04040	F
	GO:0010466	negative regulation of peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	P
	GO:0005515	protein binding	PMID:11350084^[25]	IPI: Inferred from Physical Interaction	UniProtKB:Q13867	F
	GO:0005515	protein binding	PMID:9461550^[26]	IPI: Inferred from Physical Interaction	UniProtKB:O35827	F
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005515	protein binding	PMID:18509662^[27]	IPI: Inferred from Physical Interaction	UniProtKB:P29972	F
	GO:0031410	cytoplasmic vesicle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0030198	extracellular matrix organization	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0006897	endocytosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0254	P
	GO:0051425	PTB domain binding	PMID:12805363^[28]	IPI: Inferred from Physical Interaction	UniProtKB:Q5SW96	F
	GO:0005515	protein binding	PMID:8626687^[29]	IPI: Inferred from Physical Interaction	UniProtKB:Q13564	F
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0722	F
	GO:0005515	protein binding	PMID:14983046^[12]	IPI: Inferred from Physical Interaction	UniProtKB:P35446	F
	GO:0045087	innate immune response	Reactome:REACT_6802	TAS: Traceable Author Statement		P
	GO:0005515	protein binding	PMID:18272596^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9P232	F
	GO:0007219	Notch signaling pathway	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0914	P
	GO:0005576	extracellular region	PMID:1374236^[30]	EXP: Inferred from Experiment		C
	GO:0007596	blood coagulation	Reactome:REACT_604	TAS: Traceable Author Statement		P
	GO:0005515	protein binding	PMID:21163940^[5]	IPI: Inferred from Physical Interaction	UniProtKB:O14879	F
	GO:0007409	axonogenesis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0033130	acetylcholine receptor binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P36544	F
	GO:0005887	integral to plasma membrane	PMID:10806211^[31]	TAS: Traceable Author Statement		C
	GO:0040014	regulation of multicellular organism growth	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0000085	G2 phase of mitotic cell cycle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0000085	G2 phase of mitotic cell cycle	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:12878203^[32]	IPI: Inferred from Physical Interaction	UniProtKB:Q92876	F
	GO:0005102	receptor binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P04233	F
	GO:0005515	protein binding	PMID:18387811^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NSB8	F
	GO:0005515	protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P51693	F
	GO:0007176	regulation of epidermal growth factor receptor activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:20195357^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P61457	F
	GO:0007176	regulation of epidermal growth factor receptor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:11724784^[34]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WVI9-1	F
	GO:0030900	forebrain development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0001967	suckling behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	F
	GO:0005515	protein binding	PMID:20817278^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NP59	F
	GO:0005515	protein binding	PMID:14557245^[36]	IPI: Inferred from Physical Interaction	UniProtKB:Q13564	F
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005515	protein binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NQX7	F
	GO:0031594	neuromuscular junction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0030168	platelet activation	Reactome:REACT_798	TAS: Traceable Author Statement		P
	GO:0045931	positive regulation of mitotic cell cycle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0043198	dendritic shaft	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0005515	protein binding	PMID:19225519^[23]	IPI: Inferred from Physical Interaction	UniProtKB:O75509	F
	GO:0005515	protein binding	PMID:19901339^[38]	IPI: Inferred from Physical Interaction	UniProtKB:Q62151	F
	GO:0045202	synapse	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0051563	smooth endoplasmic reticulum calcium ion homeostasis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0016199	axon midline choice point recognition	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:11278849^[39]	IPI: Inferred from Physical Interaction	UniProtKB:Q13625	F
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:P46933	F
	GO:0006378	mRNA polyadenylation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:16446437^[40]	IPI: Inferred from Physical Interaction	UniProtKB:P10636	F
	GO:0006878	cellular copper ion homeostasis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:10531052^[41]	IPI: Inferred from Physical Interaction	UniProtKB:P56817-1	F
	GO:0005515	protein binding	PMID:16849325^[42]	IPI: Inferred from Physical Interaction	UniProtKB:Q5JRX3	F
	GO:0005515	protein binding	PMID:16446437^[40]	IPI: Inferred from Physical Interaction	UniProtKB:P10636-8	F
	GO:0006878	cellular copper ion homeostasis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0006417	regulation of translation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	C
	GO:0005515	protein binding	PMID:16480949^[43]	IPI: Inferred from Physical Interaction	UniProtKB:O75955	F
	GO:0043005	neuron projection	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005515	protein binding	PMID:10049767^[44]	IPI: Inferred from Physical Interaction	UniProtKB:O96018	F
	GO:0006897	endocytosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:16554819^[45]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QUR7	F
	GO:0005576	extracellular region	PMID:16754659^[46]	EXP: Inferred from Experiment		C
	GO:0005515	protein binding	PMID:11724784^[34]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQF2	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	F
	GO:0005515	protein binding	PMID:11877420^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q92529	F
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	C
	GO:0005515	protein binding	PMID:9338779^[47]	IPI: Inferred from Physical Interaction	UniProtKB:Q99714	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	F
	GO:0030424	axon	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0051124	synaptic growth at neuromuscular junction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0006897	endocytosis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008344	adult locomotory behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0007409	axonogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005576	extracellular region	Reactome:REACT_15291	TAS: Traceable Author Statement		C
	GO:0005624	membrane fraction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P61812	F
	GO:0016322	neuron remodeling	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P61812	F
	GO:0003677	DNA binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	F
	GO:0002576	platelet degranulation	Reactome:REACT_318	TAS: Traceable Author Statement		P
	GO:0005515	protein binding	PMID:16374483^[49]	IPI: Inferred from Physical Interaction	UniProtKB:P21359	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49810	F
	GO:0016020	membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0162	C
	GO:0005515	protein binding	PMID:9774383^[51]	IPI: Inferred from Physical Interaction	UniProtKB:P78536	F
	GO:0043231	intracellular membrane-bounded organelle	PMID:18029348^[1]	IDA: Inferred from Direct Assay		C
	GO:0045931	positive regulation of mitotic cell cycle	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:20817278^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NP59	F
	GO:0005515	protein binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:Q05941	F
	GO:0045177	apical part of cell	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C
	GO:0006468	protein phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:16286452^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P04156	F
	GO:0005515	protein binding	PMID:11756426^[52]	IPI: Inferred from Physical Interaction	UniProtKB:P07174	F
	GO:0005515	protein binding	PMID:16554819^[45]	IPI: Inferred from Physical Interaction	UniProtKB:Q13526	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005515	protein binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y287	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	F
	GO:0008088	axon cargo transport	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0050803	regulation of synapse structure and activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0030198	extracellular matrix organization	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008088	axon cargo transport	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008201	heparin binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0358	F
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	C
	GO:0005515	protein binding	PMID:11297421^[53]	IPI: Inferred from Physical Interaction	UniProtKB:P02647	F
	GO:0016020	membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0005576	extracellular region	Reactome:REACT_21351	TAS: Traceable Author Statement		C
	GO:0016199	axon midline choice point recognition	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:17709753^[54]	IPI: Inferred from Physical Interaction	UniProtKB:Q8BGY9	F
	GO:0008542	visual learning	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0043197	dendritic spine	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:18509662^[27]	IDA: Inferred from Direct Assay		C
	GO:0005794	Golgi apparatus	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0005576	extracellular region	PMID:18577758^[55]	EXP: Inferred from Experiment		C
	GO:0005576	extracellular region	PMID:2834384^[56]	EXP: Inferred from Experiment		C
	GO:0007155	cell adhesion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0130	P
	GO:0040014	regulation of multicellular organism growth	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005576	extracellular region	Reactome:REACT_15538	TAS: Traceable Author Statement		C
	GO:0031175	neuron projection development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q02410	F
	GO:0005515	protein binding	PMID:11756426^[52]	IPI: Inferred from Physical Interaction	UniProtKB:P08138	F
	GO:0008542	visual learning	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0005737	cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0016358	dendrite development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005886	plasma membrane	PMID:12805363^[28]	IDA: Inferred from Direct Assay		C
	GO:0031175	neuron projection development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	P
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P01137	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000073883	C
	GO:0051402	neuron apoptosis	PMID:19225519^[23]	IMP: Inferred from Mutant Phenotype		P
	GO:0016322	transmembrane receptor protein tyrosine kinase activity	PMID:8234269^[57]	IDA: Inferred from Direct Assay		F	Figure 5: Neurite production by APP antisense cell lines - APP funciton in neurite outgrowth	complete
	GO:0000085	G2 phase of mitotic cell cycle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0000085	G2 phase of mitotic cell cycle	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0001967	suckling behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0002218	activation of innate immune response	Reactome:REACT_75913	TAS: Traceable Author Statement		P
	GO:0002576	platelet degranulation	Reactome:REACT_318	TAS: Traceable Author Statement		P
	GO:0003677	DNA binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	F
	GO:0003677	DNA binding	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	F
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002223	F
	GO:0004867	serine-type endopeptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0722	F
	GO:0004867	serine-type endopeptidase inhibitor activity	PMID:10652580^[2]	IDA: Inferred from Direct Assay		F
	GO:0005102	receptor binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:P04233	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	F
	GO:0005488	binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	F
	GO:0005515	protein binding	PMID:10049767^[44]	IPI: Inferred from Physical Interaction	UniProtKB:O96018	F
	GO:0005515	protein binding	PMID:10081969^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BYD4	F
	GO:0005515	protein binding	PMID:10531052^[41]	IPI: Inferred from Physical Interaction	UniProtKB:P56817-1	F
	GO:0005515	protein binding	PMID:10567208^[24]	IPI: Inferred from Physical Interaction	UniProtKB:P04040	F
	GO:0005515	protein binding	PMID:10673326^[20]	IPI: Inferred from Physical Interaction	UniProtKB:P31696	F
	GO:0005515	protein binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P36544	F
	GO:0005515	protein binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:Q05941	F
	GO:0005515	protein binding	PMID:11278849^[39]	IPI: Inferred from Physical Interaction	UniProtKB:Q13625	F
	GO:0005515	protein binding	PMID:11297421^[53]	IPI: Inferred from Physical Interaction	UniProtKB:P02647	F
	GO:0005515	protein binding	PMID:11350084^[25]	IPI: Inferred from Physical Interaction	UniProtKB:Q13867	F
	GO:0005515	protein binding	PMID:11724784^[34]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UQF2	F
	GO:0005515	protein binding	PMID:11724784^[34]	IPI: Inferred from Physical Interaction	UniProtKB:Q9WVI9-1	F
	GO:0005515	protein binding	PMID:11756426^[52]	IPI: Inferred from Physical Interaction	UniProtKB:P07174	F
	GO:0005515	protein binding	PMID:11756426^[52]	IPI: Inferred from Physical Interaction	UniProtKB:P08138	F
	GO:0005515	protein binding	PMID:11877420^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P29353	F
	GO:0005515	protein binding	PMID:11877420^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q92529	F
	GO:0005515	protein binding	PMID:12878203^[32]	IPI: Inferred from Physical Interaction	UniProtKB:Q92876	F
	GO:0005515	protein binding	PMID:14557245^[36]	IPI: Inferred from Physical Interaction	UniProtKB:Q13564	F
	GO:0005515	protein binding	PMID:14983046^[12]	IPI: Inferred from Physical Interaction	UniProtKB:P35446	F
	GO:0005515	protein binding	PMID:14983046^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9HCB6	F
	GO:0005515	protein binding	PMID:15896298^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P30101	F
	GO:0005515	protein binding	PMID:15983050^[4]	IPI: Inferred from Physical Interaction	UniProtKB:O43736	F
	GO:0005515	protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P51693	F
	GO:0005515	protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:Q06481	F
	GO:0005515	protein binding	PMID:16286452^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P04156	F
	GO:0005515	protein binding	PMID:16374483^[49]	IPI: Inferred from Physical Interaction	UniProtKB:P21359	F
	GO:0005515	protein binding	PMID:16446437^[40]	IPI: Inferred from Physical Interaction	UniProtKB:P10636	F
	GO:0005515	protein binding	PMID:16446437^[40]	IPI: Inferred from Physical Interaction	UniProtKB:P10636-8	F
	GO:0005515	protein binding	PMID:16480949^[43]	IPI: Inferred from Physical Interaction	UniProtKB:O75955	F
	GO:0005515	protein binding	PMID:16554819^[45]	IPI: Inferred from Physical Interaction	UniProtKB:Q13526	F
	GO:0005515	protein binding	PMID:16554819^[45]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QUR7	F
	GO:0005515	protein binding	PMID:16849325^[42]	IPI: Inferred from Physical Interaction	UniProtKB:Q5JRX3	F
	GO:0005515	protein binding	PMID:17709753^[54]	IPI: Inferred from Physical Interaction	UniProtKB:Q8BGY9	F
	GO:0005515	protein binding	PMID:18026102^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P01034	F
	GO:0005515	protein binding	PMID:18272596^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q8IWV2	F
	GO:0005515	protein binding	PMID:18272596^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9P232	F
	GO:0005515	protein binding	PMID:18387811^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NSB8	F
	GO:0005515	protein binding	PMID:18387811^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NSC5	F
	GO:0005515	protein binding	PMID:18509662^[27]	IPI: Inferred from Physical Interaction	UniProtKB:P29972	F
	GO:0005515	protein binding	PMID:19225519^[23]	IPI: Inferred from Physical Interaction	UniProtKB:O75509	F
	GO:0005515	protein binding	PMID:19225519^[23]	IPI: Inferred from Physical Interaction	UniProtKB:P08138	F
	GO:0005515	protein binding	PMID:19366692^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NQX7	F
	GO:0005515	protein binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NQX7	F
	GO:0005515	protein binding	PMID:19849849^[33]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y287	F
	GO:0005515	protein binding	PMID:19901339^[38]	IPI: Inferred from Physical Interaction	UniProtKB:Q62151	F
	GO:0005515	protein binding	PMID:20195357^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P01100	F
	GO:0005515	protein binding	PMID:20195357^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P61457	F
	GO:0005515	protein binding	PMID:20817278^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NP59	F
	GO:0005515	protein binding	PMID:20817278^[35]	IPI: Inferred from Physical Interaction	UniProtKB:Q9NP59	F
	GO:0005515	protein binding	PMID:21163940^[5]	IPI: Inferred from Physical Interaction	UniProtKB:O14879	F
	GO:0005515	protein binding	PMID:21163940^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P01137	F
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P61812	F
	GO:0005515	protein binding	PMID:2119582^[48]	IPI: Inferred from Physical Interaction	UniProtKB:P61812	F
	GO:0005515	protein binding	PMID:21593558^[58]	IPI: Inferred from Physical Interaction	UniProtKB:O75069	F
	GO:0005515	protein binding	PMID:8626687^[29]	IPI: Inferred from Physical Interaction	UniProtKB:Q13564	F
	GO:0005515	protein binding	PMID:8855266^[21]	IPI: Inferred from Physical Interaction	UniProtKB:Q92870	F
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:O00213	F
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:P46933	F
	GO:0005515	protein binding	PMID:8887653^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q02410	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49768	F
	GO:0005515	protein binding	PMID:9223340^[50]	IPI: Inferred from Physical Interaction	UniProtKB:P49810	F
	GO:0005515	protein binding	PMID:9338779^[47]	IPI: Inferred from Physical Interaction	UniProtKB:Q99714	F
	GO:0005515	protein binding	PMID:9461550^[26]	IPI: Inferred from Physical Interaction	UniProtKB:O35827	F
	GO:0005515	protein binding	PMID:9774383^[51]	IPI: Inferred from Physical Interaction	UniProtKB:P78536	F
	GO:0005576	extracellular region	Reactome:REACT_15291	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_15538	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_18373	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_21351	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_22239	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_22263	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_22289	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_22436	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_25032	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_25382	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_75876	TAS: Traceable Author Statement		C
	GO:0005576	extracellular region	Reactome:REACT_75905	TAS: Traceable Author Statement		C
	GO:0005624	membrane fraction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0005737	cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0005737	cytoplasm	PMID:18509662^[27]	IDA: Inferred from Direct Assay		C
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0005794	Golgi apparatus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C
	GO:0005794	Golgi apparatus	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0005794	Golgi apparatus	PMID:18029348^[1]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	Reactome:REACT_75761	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_75834	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_75848	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_75877	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	PMID:12805363^[28]	IDA: Inferred from Direct Assay		C
	GO:0005887	integral to plasma membrane	PMID:10806211^[31]	TAS: Traceable Author Statement		C
	GO:0005905	coated pit	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0168	C
	GO:0005905	coated pit	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0069	C
	GO:0006378	mRNA polyadenylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0006378	mRNA polyadenylation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006417	regulation of translation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0006417	regulation of translation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006468	protein phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0006468	protein phosphorylation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006878	cellular copper ion homeostasis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0006878	cellular copper ion homeostasis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006897	endocytosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0254	P
	GO:0006897	endocytosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0006897	endocytosis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P
	GO:0006917	induction of apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P
	GO:0007155	cell adhesion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0130	P
	GO:0007176	regulation of epidermal growth factor receptor activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0007176	regulation of epidermal growth factor receptor activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0007219	Notch signaling pathway	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0914	P
	GO:0007409	axonogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0007409	axonogenesis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0007596	blood coagulation	Reactome:REACT_604	TAS: Traceable Author Statement		P
	GO:0007617	mating behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0007617	mating behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0007626	locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0007626	locomotory behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008088	axon cargo transport	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0008088	axon cargo transport	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008201	heparin binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0358	F
	GO:0008219	cell death	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0523	P
	GO:0008344	adult locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0008344	adult locomotory behavior	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0008542	visual learning	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0008542	visual learning	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0009986	cell surface	PMID:7593229^[15]	IDA: Inferred from Direct Assay		C
	GO:0010466	negative regulation of peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	P
	GO:0010468	regulation of gene expression	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0010952	positive regulation of peptidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	P
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0016020	membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0016020	membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0162	C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008154	C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008155	C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011178	C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013803	C
	GO:0016021	integral to membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR015849	C
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C
	GO:0016021	integral to membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0016021	integral to membrane	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0016199	axon midline choice point recognition	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0016199	axon midline choice point recognition	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0016322	neuron remodeling	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0016322	neuron remodeling	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0016358	dendrite development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0016358	dendrite development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0016504	peptidase activator activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	F
	GO:0019717	synaptosome	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000041613	C
	GO:0030168	platelet activation	Reactome:REACT_798	TAS: Traceable Author Statement		P
	GO:0030198	extracellular matrix organization	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0030414	peptidase inhibitor activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0646	F
	GO:0030424	axon	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0030424	axon	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	C
	GO:0030900	forebrain development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0031093	platelet alpha granule lumen	Reactome:REACT_21351	TAS: Traceable Author Statement		C
	GO:0031175	neuron projection development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0031175	neuron projection development	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0031410	cytoplasmic vesicle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0031594	neuromuscular junction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0033130	acetylcholine receptor binding	PMID:10681545^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P36544	F
	GO:0035235	ionotropic glutamate receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0035235	ionotropic glutamate receptor signaling pathway	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0035253	ciliary rootlet	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0040014	regulation of multicellular organism growth	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0040014	regulation of multicellular organism growth	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0042802	identical protein binding	PMID:16193067^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P05067-4	F
	GO:0042802	identical protein binding	PMID:16286452^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P05067	F
	GO:0043005	neuron projection	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0043197	dendritic spine	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0043198	dendritic shaft	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0043231	intracellular membrane-bounded organelle	PMID:18029348^[1]	IDA: Inferred from Direct Assay		C
	GO:0045087	innate immune response	Reactome:REACT_6802	TAS: Traceable Author Statement		P
	GO:0045177	apical part of cell	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0045202	synapse	PMID:11988176^[37]	IDA: Inferred from Direct Assay		C
	GO:0045665	negative regulation of neuron differentiation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0045931	positive regulation of mitotic cell cycle	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0045931	positive regulation of mitotic cell cycle	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0048669	collateral sprouting in absence of injury	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0048669	collateral sprouting in absence of injury	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0050803	regulation of synapse structure and activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0050803	regulation of synapse structure and activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P12023	P
	GO:0050885	neuromuscular process controlling balance	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0051124	synaptic growth at neuromuscular junction	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
	GO:0051233	spindle midzone	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	C
	GO:0051402	neuron apoptosis	PMID:19225519^[23]	IMP: Inferred from Mutant Phenotype		P
	GO:0051425	PTB domain binding	PMID:12805363^[28]	IPI: Inferred from Physical Interaction	UniProtKB:Q5SW96	F
	GO:0051563	smooth endoplasmic reticulum calcium ion homeostasis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000005406	P
edit table

Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ ^2.0 ^2.1 Nakagawa T et al. (1999) Production of amyloid beta protein precursor as a proteinase inhibitor by human astrocytic tumors. Anticancer Res 19: 2963-8 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Parisiadou L et al. (2008) Homer2 and Homer3 interact with amyloid precursor protein and inhibit Abeta production. Neurobiol Dis 30: 353-64 PubMed GONUTS page
↑ ^4.0 ^4.1 Matsuda S et al. (2005) The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production. J Biol Chem 280: 28912-6 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Soler-López M et al. (2011) Interactome mapping suggests new mechanistic details underlying Alzheimer's disease. Genome Res 21: 364-76 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Miyamoto-Sato E et al. (2010) A comprehensive resource of interacting protein regions for refining human transcription factor networks. PLoS One 5: e9289 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Osterfield M et al. (2008) Interaction of amyloid precursor protein with contactins and NgCAM in the retinotectal system. Development 135: 1189-99 PubMed GONUTS page
↑ Ishihara K et al. (2003) The receptor for advanced glycation end-products (RAGE) directly binds to ERK by a D-domain-like docking site. FEBS Lett 550: 107-13 PubMed GONUTS page
↑ ^9.0 ^9.1 Erickson RR et al. (2005) In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. Biochem Biophys Res Commun 332: 50-7 PubMed GONUTS page
↑ Kislinger T et al. (1999) N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J Biol Chem 274: 31740-9 PubMed GONUTS page
↑ ^11.0 ^11.1 Kaeser SA et al. (2007) Cystatin C modulates cerebral beta-amyloidosis. Nat Genet 39: 1437-9 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 Ho A & Südhof TC (2004) Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc Natl Acad Sci U S A 101: 2548-53 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 Gobbi M et al. (2006) Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model. J Biol Chem 281: 843-9 PubMed GONUTS page
↑ ^14.0 ^14.1 Tanahashi H & Tabira T (1999) Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein. Neurosci Lett 261: 143-6 PubMed GONUTS page
↑ ^15.0 ^15.1 Akaaboune M et al. (1995) Serine proteinase inhibitors in human skeletal muscle: expression of beta-amyloid protein precursor and alpha 1-antichymotrypsin in vivo and during myogenesis in vitro. J Cell Physiol 165: 503-11 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 Wang HY et al. (2000) beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J Biol Chem 275: 5626-32 PubMed GONUTS page
↑ ^17.0 ^17.1 Matsuda S et al. (2009) BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2. J Biol Chem 284: 15815-25 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Soba P et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24: 3624-34 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 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
↑ ^20.0 ^20.1 Cotman SL et al. (2000) Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol Cell Neurosci 15: 183-98 PubMed GONUTS page
↑ ^21.0 ^21.1 Guénette SY et al. (1996) Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein. Proc Natl Acad Sci U S A 93: 10832-7 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 ^22.4 ^22.5 Borg JP et al. (1996) The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol Cell Biol 16: 6229-41 PubMed GONUTS page
↑ ^23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Nikolaev A et al. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457: 981-9 PubMed GONUTS page
↑ ^24.0 ^24.1 Milton NG (1999) Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem J 344 Pt 2: 293-6 PubMed GONUTS page
↑ ^25.0 ^25.1 Lefterov IM et al. (2001) Cysteine 73 in bleomycin hydrolase is critical for amyloid precursor protein processing. Biochem Biophys Res Commun 283: 994-9 PubMed GONUTS page
↑ ^26.0 ^26.1 Duilio A et al. (1998) Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Biochem J 330 ( Pt 1): 513-9 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 ^27.3 Misawa T et al. (2008) Close association of water channel AQP1 with amyloid-beta deposition in Alzheimer disease brains. Acta Neuropathol 116: 247-60 PubMed GONUTS page
↑ ^28.0 ^28.1 ^28.2 ^28.3 Noviello C et al. (2003) Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein. J Biol Chem 278: 31843-7 PubMed GONUTS page
↑ ^29.0 ^29.1 Chow N et al. (1996) APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J Biol Chem 271: 11339-46 PubMed GONUTS page
↑ Ye RD et al. (1992) Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor. Biochem Biophys Res Commun 184: 582-9 PubMed GONUTS page
↑ ^31.0 ^31.1 Walter J et al. (2000) Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2. J Biol Chem 275: 23523-9 PubMed GONUTS page
↑ ^32.0 ^32.1 Magklara A et al. (2003) Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors. Biochem Biophys Res Commun 307: 948-55 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 ^33.3 ^33.4 ^33.5 Matsuda S et al. (2009) CD74 interacts with APP and suppresses the production of Abeta. Mol Neurodegener 4: 41 PubMed GONUTS page
↑ ^34.0 ^34.1 ^34.2 ^34.3 Scheinfeld MH et al. (2002) Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 277: 3767-75 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 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
↑ ^36.0 ^36.1 Chen Y et al. (2003) APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain. J Cell Biol 163: 27-33 PubMed GONUTS page
↑ ^37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 Wemmie JA et al. (2002) The acid-activated ion channel ASIC contributes to synaptic plasticity, learning, and memory. Neuron 34: 463-77 PubMed GONUTS page
↑ ^38.0 ^38.1 Takuma K et al. (2009) RAGE-mediated signaling contributes to intraneuronal transport of amyloid-beta and neuronal dysfunction. Proc Natl Acad Sci U S A 106: 20021-6 PubMed GONUTS page
↑ ^39.0 ^39.1 Kajkowski EM et al. (2001) beta -Amyloid peptide-induced apoptosis regulated by a novel protein containing a g protein activation module. J Biol Chem 276: 18748-56 PubMed GONUTS page
↑ ^40.0 ^40.1 ^40.2 ^40.3 Guo JP et al. (2006) Abeta and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer's disease. Proc Natl Acad Sci U S A 103: 1953-8 PubMed GONUTS page
↑ ^41.0 ^41.1 Vassar R et al. (1999) Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286: 735-41 PubMed GONUTS page
↑ ^42.0 ^42.1 Falkevall A et al. (2006) Degradation of the amyloid beta-protein by the novel mitochondrial peptidasome, PreP. J Biol Chem 281: 29096-104 PubMed GONUTS page
↑ ^43.0 ^43.1 Chen TY et al. (2006) The intracellular domain of amyloid precursor protein interacts with flotillin-1, a lipid raft protein. Biochem Biophys Res Commun 342: 266-72 PubMed GONUTS page
↑ ^44.0 ^44.1 Tanahashi H & Tabira T (1999) X11L2, a new member of the X11 protein family, interacts with Alzheimer's beta-amyloid precursor protein. Biochem Biophys Res Commun 255: 663-7 PubMed GONUTS page
↑ ^45.0 ^45.1 ^45.2 ^45.3 Pastorino L et al. (2006) The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440: 528-34 PubMed GONUTS page
↑ Dowal L et al. (2006) Stable association between G alpha(q) and phospholipase C beta 1 in living cells. J Biol Chem 281: 23999-4014 PubMed GONUTS page
↑ ^47.0 ^47.1 Yan SD et al. (1997) An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease. Nature 389: 689-95 PubMed GONUTS page
↑ ^48.0 ^48.1 ^48.2 ^48.3 ^48.4 ^48.5 Bodmer S et al. (1990) Transforming growth factor-beta bound to soluble derivatives of the beta amyloid precursor protein of Alzheimer's disease. Biochem Biophys Res Commun 171: 890-7 PubMed GONUTS page
↑ ^49.0 ^49.1 De Schepper S et al. (2006) Neurofibromatosis type 1 protein and amyloid precursor protein interact in normal human melanocytes and colocalize with melanosomes. J Invest Dermatol 126: 653-9 PubMed GONUTS page
↑ ^50.0 ^50.1 ^50.2 ^50.3 ^50.4 ^50.5 Xia W et al. (1997) Interaction between amyloid precursor protein and presenilins in mammalian cells: implications for the pathogenesis of Alzheimer disease. Proc Natl Acad Sci U S A 94: 8208-13 PubMed GONUTS page
↑ ^51.0 ^51.1 Buxbaum JD et al. (1998) Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273: 27765-7 PubMed GONUTS page
↑ ^52.0 ^52.1 ^52.2 ^52.3 Yaar M et al. (2002) Amyloid beta binds trimers as well as monomers of the 75-kDa neurotrophin receptor and activates receptor signaling. J Biol Chem 277: 7720-5 PubMed GONUTS page
↑ ^53.0 ^53.1 Koldamova RP et al. (2001) Apolipoprotein A-I directly interacts with amyloid precursor protein and inhibits A beta aggregation and toxicity. Biochemistry 40: 3553-60 PubMed GONUTS page
↑ ^54.0 ^54.1 Wang B et al. (2007) Amyolid precursor protein mediates presynaptic localization and activity of the high-affinity choline transporter. Proc Natl Acad Sci U S A 104: 14140-5 PubMed GONUTS page
↑ Lambert NA (2008) Dissociation of heterotrimeric g proteins in cells. Sci Signal 1: re5 PubMed GONUTS page
↑ Itoh H et al. (1988) Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs. J Biol Chem 263: 6656-64 PubMed GONUTS page
↑ Kibbey MC et al. (1993) beta-Amyloid precursor protein binds to the neurite-promoting IKVAV site of laminin. Proc Natl Acad Sci U S A 90: 10150-3 PubMed GONUTS page
↑ Hopkins PC et al. (2011) The impact of a novel apolipoprotein E and amyloid-β protein precursor-interacting protein on the production of amyloid-β. J Alzheimers Dis 26: 239-53 PubMed GONUTS page

[PMID:18029348-0] 1.0 ^1.1 ^1.2 ^1.3 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:10652580-1] 2.0 ^2.1 Nakagawa T et al. (1999) Production of amyloid beta protein precursor as a proteinase inhibitor by human astrocytic tumors. Anticancer Res 19: 2963-8 PubMed GONUTS page

[PMID:18387811-2] 3.0 ^3.1 ^3.2 ^3.3 Parisiadou L et al. (2008) Homer2 and Homer3 interact with amyloid precursor protein and inhibit Abeta production. Neurobiol Dis 30: 353-64 PubMed GONUTS page

[PMID:15983050-3] 4.0 ^4.1 Matsuda S et al. (2005) The familial dementia BRI2 gene binds the Alzheimer gene amyloid-beta precursor protein and inhibits amyloid-beta production. J Biol Chem 280: 28912-6 PubMed GONUTS page

[PMID:21163940-4] 5.0 ^5.1 ^5.2 ^5.3 Soler-López M et al. (2011) Interactome mapping suggests new mechanistic details underlying Alzheimer's disease. Genome Res 21: 364-76 PubMed GONUTS page

[PMID:20195357-5] 6.0 ^6.1 ^6.2 ^6.3 Miyamoto-Sato E et al. (2010) A comprehensive resource of interacting protein regions for refining human transcription factor networks. PLoS One 5: e9289 PubMed GONUTS page

[PMID:18272596-6] 7.0 ^7.1 ^7.2 ^7.3 Osterfield M et al. (2008) Interaction of amyloid precursor protein with contactins and NgCAM in the retinotectal system. Development 135: 1189-99 PubMed GONUTS page

[PMID:12935895-7] Ishihara K et al. (2003) The receptor for advanced glycation end-products (RAGE) directly binds to ERK by a D-domain-like docking site. FEBS Lett 550: 107-13 PubMed GONUTS page

[PMID:15896298-8] 9.0 ^9.1 Erickson RR et al. (2005) In cerebrospinal fluid ER chaperones ERp57 and calreticulin bind beta-amyloid. Biochem Biophys Res Commun 332: 50-7 PubMed GONUTS page

[PMID:10531386-9] Kislinger T et al. (1999) N(epsilon)-(carboxymethyl)lysine adducts of proteins are ligands for receptor for advanced glycation end products that activate cell signaling pathways and modulate gene expression. J Biol Chem 274: 31740-9 PubMed GONUTS page

[PMID:18026102-10] 11.0 ^11.1 Kaeser SA et al. (2007) Cystatin C modulates cerebral beta-amyloidosis. Nat Genet 39: 1437-9 PubMed GONUTS page

[PMID:14983046-11] 12.0 ^12.1 ^12.2 ^12.3 Ho A & Südhof TC (2004) Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc Natl Acad Sci U S A 101: 2548-53 PubMed GONUTS page

[PMID:16286452-12] 13.0 ^13.1 ^13.2 ^13.3 Gobbi M et al. (2006) Gerstmann-Sträussler-Scheinker disease amyloid protein polymerizes according to the "dock-and-lock" model. J Biol Chem 281: 843-9 PubMed GONUTS page

[PMID:10081969-13] 14.0 ^14.1 Tanahashi H & Tabira T (1999) Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein. Neurosci Lett 261: 143-6 PubMed GONUTS page

[PMID:7593229-14] 15.0 ^15.1 Akaaboune M et al. (1995) Serine proteinase inhibitors in human skeletal muscle: expression of beta-amyloid protein precursor and alpha 1-antichymotrypsin in vivo and during myogenesis in vitro. J Cell Physiol 165: 503-11 PubMed GONUTS page

[PMID:10681545-15] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 ^16.5 Wang HY et al. (2000) beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J Biol Chem 275: 5626-32 PubMed GONUTS page

[PMID:19366692-16] 17.0 ^17.1 Matsuda S et al. (2009) BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2. J Biol Chem 284: 15815-25 PubMed GONUTS page

[PMID:16193067-17] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 Soba P et al. (2005) Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J 24: 3624-34 PubMed GONUTS page

[PMID:11877420-18] 19.0 ^19.1 ^19.2 ^19.3 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

[PMID:10673326-19] 20.0 ^20.1 Cotman SL et al. (2000) Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. Mol Cell Neurosci 15: 183-98 PubMed GONUTS page

[PMID:8855266-20] 21.0 ^21.1 Guénette SY et al. (1996) Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein. Proc Natl Acad Sci U S A 93: 10832-7 PubMed GONUTS page

[PMID:8887653-21] 22.0 ^22.1 ^22.2 ^22.3 ^22.4 ^22.5 Borg JP et al. (1996) The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol Cell Biol 16: 6229-41 PubMed GONUTS page

[PMID:19225519-22] 23.0 ^23.1 ^23.2 ^23.3 ^23.4 ^23.5 Nikolaev A et al. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457: 981-9 PubMed GONUTS page

[PMID:10567208-23] 24.0 ^24.1 Milton NG (1999) Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem J 344 Pt 2: 293-6 PubMed GONUTS page

[PMID:11350084-24] 25.0 ^25.1 Lefterov IM et al. (2001) Cysteine 73 in bleomycin hydrolase is critical for amyloid precursor protein processing. Biochem Biophys Res Commun 283: 994-9 PubMed GONUTS page

[PMID:9461550-25] 26.0 ^26.1 Duilio A et al. (1998) Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein. Biochem J 330 ( Pt 1): 513-9 PubMed GONUTS page

[PMID:18509662-26] 27.0 ^27.1 ^27.2 ^27.3 Misawa T et al. (2008) Close association of water channel AQP1 with amyloid-beta deposition in Alzheimer disease brains. Acta Neuropathol 116: 247-60 PubMed GONUTS page

[PMID:12805363-27] 28.0 ^28.1 ^28.2 ^28.3 Noviello C et al. (2003) Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein. J Biol Chem 278: 31843-7 PubMed GONUTS page

[PMID:8626687-28] 29.0 ^29.1 Chow N et al. (1996) APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J Biol Chem 271: 11339-46 PubMed GONUTS page

[PMID:1374236-29] Ye RD et al. (1992) Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor. Biochem Biophys Res Commun 184: 582-9 PubMed GONUTS page

[PMID:10806211-30] 31.0 ^31.1 Walter J et al. (2000) Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2. J Biol Chem 275: 23523-9 PubMed GONUTS page

[PMID:12878203-31] 32.0 ^32.1 Magklara A et al. (2003) Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors. Biochem Biophys Res Commun 307: 948-55 PubMed GONUTS page

[PMID:19849849-32] 33.0 ^33.1 ^33.2 ^33.3 ^33.4 ^33.5 Matsuda S et al. (2009) CD74 interacts with APP and suppresses the production of Abeta. Mol Neurodegener 4: 41 PubMed GONUTS page

[PMID:11724784-33] 34.0 ^34.1 ^34.2 ^34.3 Scheinfeld MH et al. (2002) Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 277: 3767-75 PubMed GONUTS page

[PMID:20817278-34] 35.0 ^35.1 ^35.2 ^35.3 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:14557245-35] 36.0 ^36.1 Chen Y et al. (2003) APP-BP1 mediates APP-induced apoptosis and DNA synthesis and is increased in Alzheimer's disease brain. J Cell Biol 163: 27-33 PubMed GONUTS page

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HUMAN:A4

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