Gene Report

Basic Information

Approved Symbol	PSEN1
Approved Name	presenilin 1
Previous Symbol	AD3
Previous Name	"Alzheimer disease 3"
Symbol Alias	FAD, S182, PS1
Location	14q24.3
Position	chr14:73685998-73690399 (+)
External Links	Entrez Gene: 5663 Ensembl: ENSG00000080815 UCSC: uc001xnr.3 HGNC ID: 9508
No. of Studies (Positive/Negative)	1(1/0)
Type	Literature-origin

Positive relationships between PSEN1 and MDD (count: 1)

Name in Literature	Reference	Research Type	Statistical Result	Relation Description
PSEN1	Aston, 2005	patients and normal controls		Genes altered in major depressive disorder Genes altered in major depressive disorder

Positive relationships between PSEN1 and other components at different levels (count: 0)

Positive relationship network of PSEN1 in MK4MDD

Network loading ...

Note:
1. The different color of the nodes denotes the level of the nodes.

Genetic/Epigenetic Locus	Protein and Other Molecule	Cell and Molecular Pathway	Neural System	Cognition and Behavior	Symptoms and Signs	Environment	MDD

2. Besides the component related relationships from literature, gene mapped protein and protein mapped gene are also shown in the network. If the mapped gene or protein is not from literature, square node would be used instead of Circle node. Accordingly, the relationship is marked with dot line.
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web

Negative relationships between PSEN1 and MDD (count: 0)

Negative relationships between PSEN1 and other components at different levels (count: 0)

PSEN1 related SNPs in MK4MDD (count: 0)

PSEN1 related proteins in MK4MDD (count: 0)

PSEN1 related GO terms (count: 106)

ID	Name	Type	Evidence
Literature-origin GO terms
GO:0048167	regulation of synaptic plasticity	biological process	IEA
GO:0030054	cell junction	cellular component	IDA

ID	Name	Type	Evidence
Gene mapped GO terms
GO:0005789	endoplasmic reticulum membrane	cellular component	IEA
GO:0016235	aggresome	cellular component	IDA[21143716]
GO:0045121	membrane raft	cellular component	IDA[20299451]
GO:0030424	axon	cellular component	IEA
GO:0042987	amyloid precursor protein catabolic process	biological process	TAS[15274632]
GO:0043025	neuronal cell body	cellular component	IEA
GO:0043065	positive regulation of apoptotic process	biological process	IEA
GO:0000186	activation of MAPKK activity	biological process	IEA
GO:0050820	positive regulation of coagulation	biological process	IEA
GO:0060075	regulation of resting membrane potential	biological process	IEA
GO:0043011	myeloid dendritic cell differentiation	biological process	IEA
GO:0070588	calcium ion transmembrane transport	biological process	IMP[16959576]
GO:0034205	beta-amyloid formation	biological process	IEA
GO:0030426	growth cone	cellular component	IEA
GO:0001764	neuron migration	biological process	IEA
GO:0001708	cell fate specification	biological process	IEA
GO:0021795	cerebral cortex cell migration	biological process	IEA
GO:0005886	plasma membrane	cellular component	IDA[21143716]
GO:0048538	thymus development	biological process	IEA
GO:0009791	post-embryonic development	biological process	IEA
GO:0001568	blood vessel development	biological process	IEA
GO:0004190	aspartic-type endopeptidase activity	molecular function	IEA
GO:0043406	positive regulation of MAP kinase activity	biological process	IEA
GO:0005790	smooth endoplasmic reticulum	cellular component	IDA[9632714]
GO:0005887	integral component of plasma membrane	cellular component	IDA[15274632]
GO:0004175	endopeptidase activity	molecular function	IDA[8755489]
GO:0050673	epithelial cell proliferation	biological process	IEA
GO:0098793	presynapse	cellular component	IEA
GO:0030198	extracellular matrix organization	biological process	TAS
GO:0022617	extracellular matrix disassembly	biological process	TAS
GO:0015871	choline transport	biological process	IEA
GO:0005743	mitochondrial inner membrane	cellular component	IEA
GO:0007175	negative regulation of epidermal growth factor-activated receptor activity	biological process	IEA
GO:0015813	L-glutamate transport	biological process	IEA
GO:0021870	Cajal-Retzius cell differentiation	biological process	IEA
GO:0045296	cadherin binding	molecular function	IBA
GO:0031965	nuclear membrane	cellular component	IDA[9298903]
GO:0043066	negative regulation of apoptotic process	biological process	IDA[10805794]
GO:2000059	negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process	biological process	IEA
GO:0032469	endoplasmic reticulum calcium ion homeostasis	biological process	IDA[17431506]; IGI[16959576]
GO:0045893	positive regulation of transcription, DNA-templated	biological process	IMP[23794287]
GO:0005515	protein binding	molecular function	IPI[9223340\|9689133\|11076969\|11083918\|12297508\|16007100\|16306047\|16641999\|18201567\|21143716\|21163940\|22036569]
GO:0001947	heart looping	biological process	IEA
GO:0051563	smooth endoplasmic reticulum calcium ion homeostasis	biological process	IBA
GO:0000139	Golgi membrane	cellular component	IEA
GO:0008013	beta-catenin binding	molecular function	IPI[9632714\|11104755]
GO:0002244	hematopoietic progenitor cell differentiation	biological process	IEA
GO:0030326	embryonic limb morphogenesis	biological process	IEA
GO:0043524	negative regulation of neuron apoptotic process	biological process	IEA
GO:0001756	somitogenesis	biological process	IEA
GO:0005791	rough endoplasmic reticulum	cellular component	IDA[9632714]
GO:0005262	calcium channel activity	molecular function	IMP[16959576]
GO:0021904	dorsal/ventral neural tube patterning	biological process	IEA
GO:0006974	cellular response to DNA damage stimulus	biological process	IEA
GO:0051966	regulation of synaptic transmission, glutamatergic	biological process	IEA
GO:0043393	regulation of protein binding	biological process	IEA
GO:2001234	negative regulation of apoptotic signaling pathway	biological process	IEA
GO:0015031	protein transport	biological process	IEA
GO:0043589	skin morphogenesis	biological process	IEA
GO:0006979	response to oxidative stress	biological process	IEA
GO:0016337	single organismal cell-cell adhesion	biological process	IMP[11953314]
GO:0042325	regulation of phosphorylation	biological process	IDA[9689133]
GO:0005739	mitochondrion	cellular component	IDA[12377771]
GO:0043198	dendritic shaft	cellular component	IEA
GO:0060999	positive regulation of dendritic spine development	biological process	IMP[21951279]
GO:0016021	integral component of membrane	cellular component	TAS[7596406]
GO:0060070	canonical Wnt signaling pathway	biological process	IBA
GO:0000122	negative regulation of transcription from RNA polymerase II promoter	biological process	IEA
GO:0030165	PDZ domain binding	molecular function	IPI[10551805]
GO:0005765	lysosomal membrane	cellular component	IEA
GO:0050771	negative regulation of axonogenesis	biological process	IEA
GO:0007220	Notch receptor processing	biological process	TAS[15274632]
GO:0005813	centrosome	cellular component	IDA[9298903]
GO:0070765	gamma-secretase complex	cellular component	IDA[10801983]
GO:0035253	ciliary rootlet	cellular component	IEA
GO:0050852	T cell receptor signaling pathway	biological process	IEA
GO:0005783	endoplasmic reticulum	cellular component	IDA[9246482\|15274632]
GO:0031594	neuromuscular junction	cellular component	IEA
GO:0006509	membrane protein ectodomain proteolysis	biological process	IDA[15274632]
GO:0002286	T cell activation involved in immune response	biological process	IEA
GO:0031410	cytoplasmic vesicle	cellular component	IEA
GO:0001921	positive regulation of receptor recycling	biological process	IEA
GO:0005634	nucleus	cellular component	IDA
GO:0006486	protein glycosylation	biological process	IEA
GO:0006839	mitochondrial transport	biological process	IEA
GO:0005640	nuclear outer membrane	cellular component	IDA[9246482]
GO:0051444	negative regulation of ubiquitin-protein transferase activity	biological process	IEA
GO:0043085	positive regulation of catalytic activity	biological process	IDA[15274632]
GO:0032436	positive regulation of proteasomal ubiquitin-dependent protein catabolic process	biological process	IEA
GO:0016020	membrane	cellular component	IDA[22375059]
GO:0007219	Notch signaling pathway	biological process	IEA
GO:0048666	neuron development	biological process	IEA
GO:0016485	protein processing	biological process	IDA[15274632]
GO:0048705	skeletal system morphogenesis	biological process	IEA
GO:0003407	neural retina development	biological process	IEA
GO:0048854	brain morphogenesis	biological process	IEA
GO:0000776	kinetochore	cellular component	IDA[9298903]
GO:0000045	autophagosome assembly	biological process	IEA
GO:0009986	cell surface	cellular component	IEA
GO:0035556	intracellular signal transduction	biological process	IEA
GO:0051402	neuron apoptotic process	biological process	IEA
GO:0016080	synaptic vesicle targeting	biological process	IEA
GO:0005794	Golgi apparatus	cellular component	IDA[9246482\|9632714\|15274632]
GO:0007613	memory	biological process	IEA

PSEN1 related KEGG pathways (count: 4)

ID	Name	Brief Description	Full Description
Gene mapped KEGG pathways
hsa04310	wnt signaling_pathway	Wnt signaling pathway	Wnt proteins are secreted morphogens that are required for b...... Wnt proteins are secreted morphogens that are required for basic developmental processes, such as cell-fate specification, progenitor-cell proliferation and the control of asymmetric cell division, in many different species and organs. There are at least three different Wnt pathways: the canonical pathway, the planar cell polarity (PCP) pathway and the Wnt/Ca2+ pathway. In the canonical Wnt pathway, the major effect of Wnt ligand binding to its receptor is the stabilization of cytoplasmic beta-catenin through inhibition of the bea-catenin degradation complex. Beta-catenin is then free to enter the nucleus and activate Wnt-regulated genes through its interaction with TCF (T-cell factor) family transcription factors and concomitant recruitment of coactivators. Planar cell polarity (PCP) signaling leads to the activation of the small GTPases RHOA (RAS homologue gene-family member A) and RAC1, which activate the stress kinase JNK (Jun N-terminal kinase) and ROCK (RHO-associated coiled-coil-containing protein kinase 1) and leads to remodelling of the cytoskeleton and changes in cell adhesion and motility. WNT-Ca2+ signalling is mediated through G proteins and phospholipases and leads to transient increases in cytoplasmic free calcium that subsequently activate the kinase PKC (protein kinase C) and CAMKII (calcium calmodulin mediated kinase II) and the phosphatase calcineurin. More...
hsa05010	alzheimers disease	Alzheimer's disease	Alzheimer's disease (AD) is a chronic disorder that slowly d...... Alzheimer's disease (AD) is a chronic disorder that slowly destroys neurons and causes serious cognitive disability. AD is associated with senile plaques and neurofibrillary tangles (NFTs). Amyloid-beta (Abeta), a major component of senile plaques, has various pathological effects on cell and organelle function. The extracellular Abeta oligomers may activate caspases through activation of cell surface death receptors. Alternatively, intracellular Abeta may contribute to pathology by facilitating tau hyper-phosphorylation, disrupting mitochondria function, and triggering calcium dysfunction. To date genetic studies have revealed four genes that may be linked to autosomal dominant or familial early onset AD (FAD). These four genes include: amyloid precursor protein (APP), presenilin 1 (PS1), presenilin 2 (PS2) and apolipoprotein E (ApoE). All mutations associated with APP and PS proteins can lead to an increase in the production of Abeta peptides, specifically the more amyloidogenic form, Abeta42. FAD-linked PS1 mutation downregulates the unfolded protein response and leads to vulnerability to ER stress. More...
hsa04330	notch signaling_pathway	Notch signaling pathway	The Notch signaling pathway is an evolutionarily conserved, ...... The Notch signaling pathway is an evolutionarily conserved, intercellular signaling mechanism essential for proper embryonic development in all metazoan organisms in the Animal kingdom. The Notch proteins (Notch1-Notch4 in vertebrates) are single-pass receptors that are activated by the Delta (or Delta-like) and Jagged/Serrate families of membrane-bound ligands. They are transported to the plasma membrane as cleaved, but otherwise intact polypeptides. Interaction with ligand leads to two additional proteolytic cleavages that liberate the Notch intracellular domain (NICD) from the plasma membrane. The NICD translocates to the nucleus, where it forms a complex with the DNA binding protein CSL, displacing a histone deacetylase (HDAc)-co-repressor (CoR) complex from CSL. Components of an activation complex, such as MAML1 and histone acetyltransferases (HATs), are recruited to the NICD-CSL complex, leading to the transcriptional activation of Notch target genes. More...
hsa04722	neurotrophin signaling_pathway	Neurotrophin signaling pathway	Neurotrophins are a family of trophic factors involved in di...... Neurotrophins are a family of trophic factors involved in differentiation and survival of neural cells. The neurotrophin family consists of nerve growth factor (NGF), brain derived neurotrophic factor (BDNF), neurotrophin 3 (NT-3), and neurotrophin 4 (NT-4). Neurotrophins exert their functions through engagement of Trk tyrosine kinase receptors or p75 neurotrophin receptor (p75NTR). Neurotrophin/Trk signaling is regulated by connecting a variety of intracellular signaling cascades, which include MAPK pathway, PI-3 kinase pathway, and PLC pathway, transmitting positive signals like enhanced survival and growth. On the other hand, p75NTR transmits both positive and nagative signals. These signals play an important role for neural development and additional higher-order activities such as learning and memory. More...

PSEN1 related BioCarta pathways (count: 2)

ID	Name	Brief Description	Full Description
Gene mapped BioCarta pathways
PS1_PATHWAY	ps1 pathway	Presenilin action in Notch and Wnt signaling	Presenilin-1 (PS1) is associated with gamma secretase activi...... Presenilin-1 (PS1) is associated with gamma secretase activity that cleaves amyloid precursor protein (APP) and is implicated in Alzheimer's disease. Presenilin-1 is also a component in gamma-secretase activity involved in signaling by the transmembrane protein Notch. Active gamma secretase requires PS-1 N-terminal fragment and a C-terminal fragment and is unique in catalyzing proteolysis within the transmembrane region of proteins. Other proteins such as nicastrin may also be components of the gamma-secretase. Binding of the ligand Delta by Notch appears to trigger two proteolytic cleavages of Notch. The first step cleaves an extracellular domain and is catalyzed by a metalloprotease termed alpha-secretase or TACE. The second cleavage step appears to occur within the transmembrane domain of Notch, and releases a Notch intracellular doman (NICD). Once released, NICD moves into the nucleus where it is involved in transcriptional regulation through CSL family transcription factors (CBF1, Su(H), Lag-1) or other transcriptional regulators such as LEF-1. Presenilin is also involved in the Wnt/frizzled signaling pathway through beta-catenin. Beta-catenin is a cytoskeletal component that enters the nucleus to act as a transcriptional cofactor. Binding of WNT to Frizzled causes disheveled (DSH) to inhibit Glycogen synthase kinase 3 beta (GSK-3b) activity. Phosphorylation of Beta-catenin induces the ubiquitination and proteolytic degradation of beta-catenin by the proteasome. Non-phosphorylated beta-catenin is stable and enters the nucleus to regulate transcription with TCF. The beta-catenin/TCF complex activates genes that promote cellular survival, proliferation and differentiation during development. Presenilin stimulates beta-catenin turnover, reducing its transcriptional activation. More...
HIVNEF_PATHWAY	hivnef pathway	HIV-I Nef: negative effector of Fas and TNF	HIV infection leads to drastic declines in CD4 T helper cell...... HIV infection leads to drastic declines in CD4 T helper cells, in part through apoptosis of uninfected cells. Apoptosis of uninfected cells may be induced through the expression of Fas ligand on the surface of HIV-infected cells, stimulating the Fas-dependent apoptotic pathway in cells that come in contact with infected cells. The NEF protein expressed by HIV may play induce the expression of Fas-ligand by infected cells. If this is the case, then a question that arises is how infected cells themselves escape Fas-mediated apoptosis. The NEF protein appears to play a role in this process as well. NEF interacts with the ASK1 kinase (apoptosis signal-regulating kinase) involved in apoptotic signaling by TNF and Fas-ligand. Interaction of NEF with ASK1 prevents phosphorylation of downstream MAP kinases and JNK kinases involved in apoptotic signaling. More...

PSEN1 related Reactome pathways (count: 7)

ID	Name	Description
Gene mapped Reactome pathways
REACT_299	signaling by_notch	The Notch Signaling Pathway (NSP) is a highly conserved path...... The Notch Signaling Pathway (NSP) is a highly conserved pathway for cell-cell communication. NSP is involved in the regulation of cellular differentiation, proliferation, and specification. For example, it is utilised by continually renewing adult tissues such as blood, skin, and gut epithelium not only to maintain stem cells in a proliferative, pluripotent, and undifferentiated state but also to direct the cellular progeny to adopt different developmental cell fates. Analogously, it is used during embryonic development to create fine-grained patterns of differentiated cells, notably during neurogenesis where the NSP controls patches such as that of the vertebrate inner ear where individual hair cells are surrounded by supporting cells. This process is known as lateral inhibition: a molecular mechanism whereby individual cells within a field are stochastically selected to adopt particular cell fates and the NSP inhibits their direct neighbours from doing the same. The NSP has been adopted by several other biological systems for binary cell fate choice. In addition, the NSP is also used during vertebrate segmentation to divide the growing embryo into regular blocks called somites which eventually form the vertebrae. The core of this process relies on regular pulses of Notch signaling generated from a molecular oscillator in the presomatic mesoderm. The Notch receptor is synthesized in the rough endoplasmic reticulum as a single polypeptide precursor. Newly synthesized Notch receptor is proteolytically cleaved in the trans-golgi network, creating a heterodimeric mature receptor comprising of non-covalently associated extracellular and transmembrane subunits. This assembly travels to the cell surface ready to interact with specific ligands. Following ligand activation and further proteolytic cleavage, an intracellular domain is released and translocates to the nucleus where it regulates gene expression. More...
REACT_691	a third_proteolytic_cleavage_releases_nicd	The third proteolytic cleavage releases the Notch IntraCellu...... The third proteolytic cleavage releases the Notch IntraCellular Domain (NICD) from the NEXT fragment. The catalyst for this cleavage is a membrane protease complex called gamma-secretase (GS). GS cleaves type I membrane proteins such as the Notch receptor and amyloid beta-protein precursor (APP, implicated in Alzheimer's Disease). GS is made up of 4 components; Presenilin, nicastrin, APH-1 and PEN-2. Presenilins are homodimeric, multipass transmembrane proteins and are believed to be the catalytic core of GS. All aspartyl proteases have two catalytic aspartates and presenilin contains these residues. The others are essential cofactors for the correct function of GS. More...
REACT_13776	p75 ntr_receptor_mediated_signalling	Besides signalling through the tyrosine kinase receptors TRK...... Besides signalling through the tyrosine kinase receptors TRK A, B, and C, the mature neurotrophins NGF, BDNF, and NT3/4 signal through their common receptor p75NTR. NGF binding to p75NTR activates a number of downstream signalling events controlling survival, death, proliferation, and axonogenesis, according to the cellular context. p75NTR is devoid of enzymatic activity, and signals by recruiting other proteins to its own intracellular domain. p75 interacting proteins include NRIF, TRAF2, 4, and 6, NRAGE, necdin, SC1, NADE, RhoA, Rac, ARMS, RIP2, FAP and PLAIDD. Here we annotate only the proteins for which a clear involvement in p75NTR signalling was demonstrated. A peculiarity of p75NTR is the ability to bind the pro-neurotrophins proNGF and proBDNF. Proneurotrophins do not associate with TRK receptors, whereas they efficiently signal cell death by apoptosis through p75NTR. The biological action of neurotrophins is thus regulated by proteolytic cleavage, with proforms preferentially activating p75NTR, mediating apoptosis, and mature forms activating TRK receptors, to promote survival. Moreover, the two receptors are utilised to differentially modulate neuronal plasticity. For instance, proBDNF-p75NTR signalling facilitates LTD, long term depression, in the hippocampus , while BDNF-TRKB signalling promotes LTP (long term potentiation). Many biological observations indicate a functional interaction between p75NTR and TRKA signaling pathways. More...
REACT_11061	signalling by_ngf	Neurotrophins (NGF, BDNF, NT-3, NT-4/5) play pivotal roles i...... Neurotrophins (NGF, BDNF, NT-3, NT-4/5) play pivotal roles in survival, differentiation, and plasticity of neurons in the peripheral and central nervous system. They are produced, and secreted in minute amounts, by a variety of tissues. They signal through two types of receptors: TRK tyrosine kinase receptors (TRKA, TRKB, TRKC), which specifically interact with the different neurotrophins, and p75NTR, which interacts with all neurotrophins. TRK receptors are reported in a variety of tissues in addition to neurons. p75NTRs are also widespread. Neurotrophins and their receptors are synthesized as several different splice variants, which differ in terms of their biological activities. The nerve growth factor (NGF) was the first growth factor to be identified and has served as a model for studying the mechanisms of action of neurotrophins and growth factors. The mechanisms by which NGF generates diverse cellular responses have been studied extensively in the rat pheochromocytoma cell line PC12. When exposed to NGF, PC12 cells exit the cell cycle and differentiate into sympathetic neuron-like cells. Current data show that signalling by the other neurotrophins is similar to NGF signalling. More...
REACT_13443	regulated proteolysis_of_p75ntr	p75NTR undergoes a process of regulated intramembrane proteo...... p75NTR undergoes a process of regulated intramembrane proteolysis (RIP) similar to other transmembrane proteins such as NOTCH, beta-amyloid precursor protein (APP), and ERBB4. Each of these proteins is subjected to two sequential cleavages. The first one occurs in the extracellular part of the protein and is mediated by the metalloproteinase alpha-secretase which causes shedding of the extracellular domain. The second cleavage occurs in the intramembrane region and is mediated by gamma-secretase and causes release of the intracellular domain, ICD, and of a small peptide. The ICD often traffics to the nucleus and, in some instances (e.g. NOTCH), was found to act as transcriptional regulator. Whether the p75NTR ICD does translocate to the nucleus to regulate gene expression in a way similar to the NOTCH receptor remains to be seen. The alpha- and gamma-secretase mediated cleavage of p75 appears to be regulated by neurotrophin (NGF, BDNF) binding to TRKA or TRKB. p75NTR processing also occurs in response to MAG in cerebellar granule neurons. More...
REACT_13643	nrif signals_cell_death_from_the_nucleus	NRIF (nuclear receptor-interacting factor) is a DNA binding ...... NRIF (nuclear receptor-interacting factor) is a DNA binding protein that is essential for p75-mediated apoptosis in retina and sympathetic neurons. Neurotrophin or proneurotrophin binding to p75TR induces nuclear translocation of NRIF, which involves gamma-secretase cleavage of p75NTR ICD (Intra Cellular Domain). Once in the nucleus, NRIF mediates apoptosis, probably by acting as transcription factor. More...
REACT_13720	cell death_signalling_via_nrage_nrif_and_nade	p75NTR is a key regulator of neuronal apoptosis, both during...... p75NTR is a key regulator of neuronal apoptosis, both during development and after injury. Apoptosis is triggered by binding of either mature neurotrophin or proneurotrophin (proNGF, proBDNF). ProNGF is at least 10 times more potent than mature NGF in inducing apoptosis. TRKA signalling protects neurons from apoptosis. The molecular mechanisms involved in p75NTR-apoptosis are not well understood. The death signalling requires activation of c-JUN N-terminal Kinase (JNK), as well as transcriptional events. JNK activation appears to involve the receptor interacting proteins TRAF6, NRAGE, and Rac. The transcription events are thought to be regulated by another p75-interacting protein, NRIF. Two other p75-interacting proteins, NADE and Necdin, have been implicated in apoptosis, but their role is less clear. More...

PSEN1 related interactors from protein-protein interaction data in HPRD (count: 53)

Gene	Interactor	Interactor in MK4MDD?	Experiment Type	PMID
PSEN1	PSEN1	Yes	yeast 2-hybrid	12535650
PSEN1	PRKACA	No	in vitro	14576165
PSEN1	CDK5	No	in vitro;in vivo	12056836
PSEN1	CTNNA1	No	in vivo	10635315
PSEN1	DOCK3	No	in vitro;yeast 2-hybrid	10854253
PSEN1	RAB11A	No	in vivo;yeast 2-hybrid	10369872
PSEN1	CTNNB1	No	in vitro;in vivo	9738936 , 10092585 , 12070348 , 11168528 , 16306047 , 11226248 , 10341227
PSEN1	NCSTN	No	in vivo	10993067 , 12603837
PSEN1	CASP8	No	in vitro;in vivo	10069390
PSEN1	CDH1	No	in vitro;in vivo	10635315 , 11953314 , 11226248
PSEN1	SFRS2IP	No	in vitro;in vivo	10069390
PSEN1	FLNB	No	in vitro;in vivo;yeast 2-hybrid	9437013
PSEN1	GFAP	Yes	in vitro;yeast 2-hybrid	12058025
PSEN1	APH1B	No	in vivo	12471034
PSEN1	PSENEN	No	in vitro;in vivo	12198112 , 12639958
PSEN1	CASP1	No	in vitro;in vivo	10069390
PSEN1	UBQLN1	No	in vitro;in vivo;yeast 2-hybrid	11076969
PSEN1	PRKCZ	No	in vitro;in vivo	14576165
PSEN1	CTNND1	No	in vivo	11226248
PSEN1	APBA1	No	in vitro	12196555
PSEN1	METTL2B	No	yeast 2-hybrid	11738826
PSEN1	MAPT	No	in vivo	9689133
PSEN1	HERPUD1	No	in vivo	11799129
PSEN1	EFNB2	No	in vitro;in vivo	16511561
PSEN1	NOTCH3	No	in vivo	11518718
PSEN1	FBXW7	No	in vivo	12354302
PSEN1	MTCH1	No	in vitro;in vivo	10551805
PSEN1	FLNA	No	in vivo;yeast 2-hybrid	9437013
PSEN1	JUP	No	in vitro;in vivo	16306047 , 11226248
PSEN1	BCL2L1	Yes	in vivo;yeast 2-hybrid	10446169
PSEN1	NOTCH4	No	in vivo	11518718
PSEN1	APP	No	in vitro	10593990
PSEN1	KCNIP3	No	in vivo	12207970
PSEN1	NOTCH2	No	in vivo	11518718
PSEN1	APH1A	No	in vitro;in vivo	12297508 , 12471034
PSEN1	BACE1	Yes	in vitro;in vivo;yeast 2-hybrid	12901838
PSEN1	ERN1	No	in vitro;in vivo	10587643
PSEN1	CIB1	No	yeast 2-hybrid	10366599
PSEN1	DLL1	No	in vitro	12794186
PSEN1	PIK3R1	Yes	in vitro	15192701
PSEN1	YME1L1	No	yeast 2-hybrid	12214059
PSEN1	CTNND2	No	in vitro;in vivo;yeast 2-hybrid	9223106 , 10208590 , 10037471
PSEN1	PKP4	No	in vitro;in vivo;yeast 2-hybrid	10092585 , 10037471
PSEN1	CASP3	No	in vitro;in vivo	10069390
PSEN1	ICAM5	No	in vitro;in vivo;yeast 2-hybrid	11719200
PSEN1	CASP7	No	in vitro;in vivo	10069390
PSEN1	GSK3B	Yes	in vivo	11104755 , 16814287
PSEN1	BCL2	No	in vitro;in vivo;yeast 2-hybrid	10521466
PSEN1	GDI1	No	in vitro	15480879
PSEN1	CASP6	No	in vitro;in vivo	10069390
PSEN1	NOTCH1	No	in vivo	10077672 , 10206645 , 12374741
PSEN1	TCF7L2	No	in vitro;in vivo	11504726 , 16306047
PSEN1	CASP4	No	in vitro	10069390

Gene Report

Literature-origin GO terms

Gene mapped GO terms

Gene mapped KEGG pathways

Gene mapped BioCarta pathways

Gene mapped Reactome pathways