
Gene Report
Approved Symbol | PSEN1 |
---|---|
Approved Name | presenilin 1 |
Previous Symbol | AD3 |
Previous Name | Alzheimer disease 3 |
Symbol Alias | FAD, S182, PS1 |
Location | 14q24.3 |
Position | chr14:73603143-73690399 (+) |
External Links |
Entrez Gene: 5663 Ensembl: ENSG00000080815 UCSC: uc001xnr.3 HGNC ID: 9508 |
No. of Studies (Positive/Negative) | 1(1/0)
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Type | Literature-origin |
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 |
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Genetic/Epigenetic Locus | Protein and Other Molecule | Cell and Molecular Pathway | Neural System | Cognition and Behavior | Symptoms and Signs | Environment | MDD |
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Approved Name | UniportKB | No. of Studies (Positive/Negative) | Source | |
---|---|---|---|---|
Presenilin-1 | P49768 | 0(0/0) | Gene mapped |
Literature-origin GO terms | ||||
ID | Name | Type | Evidence | |
---|---|---|---|---|
GO:0006915 | apoptotic process | biological process | TAS | |
GO:0048167 | regulation of synaptic plasticity | biological process | IEA |
Gene mapped GO terms | ||||
ID | Name | Type | Evidence | |
---|---|---|---|---|
GO:0006816 | calcium ion transport | biological process | IBA | |
GO:0004190 | aspartic-type endopeptidase activity | molecular function | IEA | |
GO:0000776 | kinetochore | cellular component | IDA[9298903] | |
GO:0005262 | calcium channel activity | molecular function | IMP[16959576] | |
GO:0048011 | nerve growth factor receptor signaling pathway | biological process | TAS | |
GO:0043198 | dendritic shaft | cellular component | IBA | |
GO:0051966 | regulation of synaptic transmission, glutamatergic | biological process | IEA | |
GO:0048854 | brain morphogenesis | biological process | IEA | |
GO:0001764 | neuron migration | biological process | IEA | |
GO:0016324 | apical plasma membrane | cellular component | IBA | |
GO:0009986 | cell surface | cellular component | IBA | |
GO:0002244 | hematopoietic progenitor cell differentiation | biological process | IEA | |
GO:0001708 | cell fate specification | biological process | IEA | |
GO:0005791 | rough endoplasmic reticulum | cellular component | IDA[9632714] | |
GO:0048538 | thymus development | biological process | IEA | |
GO:0043025 | neuronal cell body | cellular component | IBA | |
GO:0030165 | PDZ domain binding | molecular function | IPI[10551805] | |
GO:0005938 | cell cortex | cellular component | IBA | |
GO:0035253 | ciliary rootlet | cellular component | IBA | |
GO:0007219 | Notch signaling pathway | biological process | TAS | |
GO:0016080 | synaptic vesicle targeting | biological process | IEA | |
GO:0048666 | neuron development | biological process | IEA | |
GO:0060075 | regulation of resting membrane potential | biological process | IEA | |
GO:0031293 | membrane protein intracellular domain proteolysis | biological process | TAS | |
GO:0050852 | T cell receptor signaling pathway | biological process | IEA | |
GO:0043065 | positive regulation of apoptotic process | biological process | IEA | |
GO:0030424 | axon | cellular component | IBA | |
GO:0015871 | choline transport | biological process | IEA | |
GO:0016337 | cell-cell adhesion | biological process | IMP[11953314] | |
GO:0000186 | activation of MAPKK activity | biological process | IEA | |
GO:0031594 | neuromuscular junction | cellular component | IBA | |
GO:0001921 | positive regulation of receptor recycling | biological process | IEA | |
GO:2000059 | negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process | biological process | IEA | |
GO:0001756 | somitogenesis | biological process | IEA | |
GO:0000045 | autophagic vacuole assembly | biological process | IEA | |
GO:0006486 | protein glycosylation | biological process | IEA | |
GO:0000139 | Golgi membrane | cellular component | IEA | |
GO:0016020 | membrane | cellular component | TAS[8878479] | |
GO:0070588 | calcium ion transmembrane transport | biological process | IMP[16959576] | |
GO:0005794 | Golgi apparatus | cellular component | IDA[15274632] | |
GO:0048705 | skeletal system morphogenesis | biological process | IEA | |
GO:0015813 | L-glutamate transport | biological process | IEA | |
GO:0043589 | skin morphogenesis | biological process | IEA | |
GO:0032436 | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | biological process | IEA | |
GO:0042987 | amyloid precursor protein catabolic process | biological process | IBA; TAS[15274632] | |
GO:0007613 | memory | biological process | IEA | |
GO:0042325 | regulation of phosphorylation | biological process | IDA[9689133] | |
GO:0004175 | endopeptidase activity | molecular function | IDA[8755489] | |
GO:0005886 | plasma membrane | cellular component | TAS | |
GO:0005739 | mitochondrion | cellular component | IDA[12377771] | |
GO:0050820 | positive regulation of coagulation | biological process | IEA | |
GO:0051402 | neuron apoptotic process | biological process | IEA | |
GO:0043393 | regulation of protein binding | biological process | IEA | |
GO:0015031 | protein transport | biological process | IEA | |
GO:0050673 | epithelial cell proliferation | biological process | IEA | |
GO:0005790 | smooth endoplasmic reticulum | cellular component | IDA[9632714] | |
GO:0005813 | centrosome | cellular component | IDA[9298903] | |
GO:0016485 | protein processing | biological process | IDA[15274632] | |
GO:0002573 | myeloid leukocyte differentiation | biological process | IEA | |
GO:0030326 | embryonic limb morphogenesis | biological process | IEA | |
GO:0042640 | anagen | biological process | IEA | |
GO:0032469 | endoplasmic reticulum calcium ion homeostasis | biological process | IDA[17431506]; IGI[16959576] | |
GO:0030018 | Z disc | cellular component | IBA | |
GO:0001568 | blood vessel development | biological process | IEA | |
GO:0005515 | protein binding | molecular function | IPI | |
GO:0031410 | cytoplasmic vesicle | cellular component | IEA | |
GO:0016021 | integral to membrane | cellular component | TAS[7596406] | |
GO:0006979 | response to oxidative stress | biological process | IEA | |
GO:0005743 | mitochondrial inner membrane | cellular component | IBA | |
GO:0005765 | lysosomal membrane | cellular component | IBA | |
GO:0006974 | response to DNA damage stimulus | biological process | IEA | |
GO:0048471 | perinuclear region of cytoplasm | cellular component | IBA | |
GO:0008013 | beta-catenin binding | molecular function | IPI[11104755] | |
GO:0006839 | mitochondrial transport | biological process | IEA | |
GO:0021904 | dorsal/ventral neural tube patterning | biological process | IEA | |
GO:0021870 | Cajal-Retzius cell differentiation | biological process | IEA | |
GO:0005640 | nuclear outer membrane | cellular component | IDA[9246482] | |
GO:0051444 | negative regulation of ubiquitin-protein ligase activity | biological process | IEA | |
GO:0009791 | post-embryonic development | biological process | IEA | |
GO:0043524 | negative regulation of neuron apoptotic process | biological process | IEA | |
GO:0030426 | growth cone | cellular component | IBA | |
GO:0050435 | beta-amyloid metabolic process | biological process | IBA | |
GO:0007175 | negative regulation of epidermal growth factor-activated receptor activity | biological process | IEA | |
GO:0043085 | positive regulation of catalytic activity | biological process | IDA[15274632] | |
GO:0002286 | T cell activation involved in immune response | biological process | IEA | |
GO:0045121 | membrane raft | cellular component | IBA | |
GO:0006509 | membrane protein ectodomain proteolysis | biological process | IDA[15274632] | |
GO:0031965 | nuclear membrane | cellular component | IDA[9298903] | |
GO:0043066 | negative regulation of apoptotic process | biological process | IDA[10805794] | |
GO:0021795 | cerebral cortex cell migration | biological process | IEA | |
GO:0051563 | smooth endoplasmic reticulum calcium ion homeostasis | biological process | IBA | |
GO:0005783 | endoplasmic reticulum | cellular component | IDA[15274632] | |
GO:0035556 | intracellular signal transduction | biological process | IEA | |
GO:0007220 | Notch receptor processing | biological process | IBA; TAS | |
GO:0050771 | negative regulation of axonogenesis | biological process | IEA | |
GO:0005789 | endoplasmic reticulum membrane | cellular component | IEA | |
GO:0045296 | cadherin binding | molecular function | IBA | |
GO:0005887 | integral to plasma membrane | cellular component | IDA[15274632] | |
GO:0001947 | heart looping | biological process | IEA | |
GO:0000122 | negative regulation of transcription from RNA polymerase II promoter | biological process | IEA | |
GO:0070765 | gamma-secretase complex | cellular component | IDA[10801983] | |
GO:0043406 | positive regulation of MAP kinase activity | biological process | IEA |
Gene mapped KEGG pathways | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
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... | |
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... | |
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... |
Gene mapped BioCarta pathways | ||||
ID | Name | Brief Description | Full Description | |
---|---|---|---|---|
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... | |
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... |
Gene mapped Reactome pathways | |||
ID | Name | Description | |
---|---|---|---|
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_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... | |
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_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_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... |

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