Protein family
The protein has not catalytic activity
Protein sequence
Protein function
Catalytic activity
PDB | Resolution (Å) | PDB name |
---|---|---|
1CA0 | 2.1 | BOVINE CHYMOTRYPSIN COMPLEXED TO APPI |
1BJB | SOLUTION NMR STRUCTURE OF AMYLOID BETA[E16], RESIDUES 1-28, 14 STRUCTURES | |
6ITU | 2.17 | Crystal Structure of the GULP1 PTB domain-APP peptide complex |
1AMC | SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE | |
5AEF | 5.0 | Electron cryo-microscopy of an Abeta(1-42)amyloid fibril |
7Y3J | 2.6 | 24B3 antibody-peptide complex |
7Q4B | 2.5 | Type I beta-amyloid 42 Filaments from Human Brain |
5LV0 | 2.7 | Structure of Human Neurolysin (E475Q) in complex with amyloid-beta 35-40 peptide product |
3OVJ | 1.8 | Structure of an amyloid forming peptide KLVFFA from amyloid beta in complex with orange G |
4M1C | 3.5007 | Crystal Structure Analysis of Fab-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Amyloid-Beta (1-40) |
6YHX | Solution NMR Structure of APP I45T mutant TMD | |
4HIX | 2.204 | Crystal structure of a humanised 3D6 Fab bound to amyloid beta peptide |
3IFO | 2.15 | X-ray structure of amyloid beta peptide:antibody (Abeta1-7:10D5) complex |
1QYT | Solution structure of fragment (25-35) of beta amyloid peptide in SDS micellar solution | |
2M9S | 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside | |
5MY4 | 2.211 | Structure of Pyroglutamate-Abeta-specific Fab c#17 in complex with human Abeta-pE3-12PEGb |
6XOV | 3.3 | CryoEM structure of human presequence protease in partial closed state 1 |
3L33 | 2.48 | Human mesotrypsin complexed with amyloid precursor protein inhibitor(APPI) |
2LFM | A partially folded structure of amyloid-beta(1 40) in an aqueous environment | |
6TI5 | A New Structural Model of Abeta(1-40) Fibrils | |
2LMP | Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Positive Stagger | |
5LFY | Zinc bound dimer of the fragment of human amyloid-beta peptide with Alzheimer's disease pathogenic Taiwanese mutation D7H | |
8EZD | 2.83 | Brain-derived 42-residue amyloid-beta fibril type A |
3KTM | 2.7 | Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP) |
4XXD | 2.41 | Crystal Structure of mid-region amyloid beta capture by solanezumab |
1AMB | SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE | |
3MXY | 2.3 | Structures of Grb2-SH2 Domain and AICD peptide Complexes Reveal a Conformational Switch and Their Functional Implications. |
2Y3L | 2.1 | Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 2 |
3NYJ | 3.2 | Crystal Structure Analysis of APP E2 domain |
2MJ1 | NMR structure of the soluble A beta 17-34 peptide | |
2BEG | 3D Structure of Alzheimer's Abeta(1-42) fibrils | |
5ONQ | 1.17 | Alzheimer's Amyloid-Beta Peptide Fragment 29-40 in Complex with Cd-substituted Thermolysin |
3DXE | 2.0 | Crystal structure of the intracellular domain of human APP (T668A mutant) in complex with Fe65-PTB2 |
1AAP | 1.5 | X-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR |
7OW1 | 1.4 | Crystal Structure of TAP01 in complex with amyloid beta peptide |
6YHF | Solution NMR Structure of APP TMD | |
6W0O | 2.77 | Amyloid-beta(1-40) fibril derived from Alzheimer's disease cortical tissue |
3IFP | 2.95 | X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12B4) complex |
4PQD | 1.332 | The longer crystal structure of the grow factor like domain from Beta amypoid precusor protein (APP22-126) |
2WK3 | 2.59 | Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-42) |
7U4P | 1.803 | Covalently stabilized triangular trimer composed of Abeta17-36 beta-hairpins |
2G47 | 2.1 | Crystal structure of human insulin-degrading enzyme in complex with amyloid-beta (1-40) |
2FMA | 0.85 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution |
8BFZ | 2.8 | Amyloid-beta 42 filaments extracted from the human brain with Arctic mutation (E22G) of Alzheimer's disease | ABeta42 |
3GCI | 2.04 | Crystal Structure of the Complex Formed Between a New Isoform of Phospholipase A2 with C-terminal Amyloid Beta Heptapeptide at 2 A Resolution |
2MPZ | Atomic model of the Abeta D23N Iowa mutant using solid-state NMR, EM and Rosetta modeling | |
1X11 | 2.5 | X11 PTB DOMAIN |
5BUO | 2.31 | A receptor molecule |
2LZ3 | Solution NMR structure of transmembrane domain of amyloid precursor protein WT | |
3UMI | 2.4 | X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with zinc |
2MGT | Zinc induced dimer of the metal binding domain 1-16 of human amyloid beta-peptide with Alzheimer's disease pathogenic English mutation H6R | |
4MDR | 1.85 | Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain D190A mutant, in complex with a sorting peptide from the amyloid precursor protein (APP) |
4MVI | 1.7 | Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide Abeta(1-40) |
2Y3K | 1.9 | Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1 |
2LOH | Dimeric structure of transmembrane domain of amyloid precursor protein in micellar environment | |
2LZ4 | Solution NMR structure of transmembrane domain of amyloid precursor protein V44M | |
3IFN | 1.5 | X-ray structure of amyloid beta peptide:antibody (Abeta1-40:12A11) complex |
4ONF | 2.0 | Fab fragment of 3D6 in complex with amyloid beta 1-7 |
6WXM | 2.3 | X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36 |
6RHY | Structure of pore-forming amyloid-beta tetramers | |
5AMB | 1.55 | Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 35-42 |
2MVX | Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation | |
3IFL | 1.5 | X-ray structure of amyloid beta peptide:antibody (Abeta1-7:12A11) complex |
8EZE | 2.76 | Brain-derived 42-residue amyloid-beta fibril type B |
2BP4 | Zinc-binding domain of Alzheimer's disease amyloid beta-peptide in TFE-water (80-20) solution | |
6OIZ | 1.1 | Amyloid-Beta (20-34) wild type |
1BJC | SOLUTION NMR STRUCTURE OF AMYLOID BETA[F16], RESIDUES 1-28, 15 STRUCTURES | |
3MOQ | 2.054 | Amyloid beta(18-41) peptide fusion with new antigen receptor variable domain from sharks |
5C67 | 1.83 | Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant APPI-M17G/I18F/F34V |
3NYL | 2.8 | The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain |
8C3H | 1.71 | Cereblon isoform 4 from Magnetospirillum gryphiswaldense in complex a long aspartimide degron peptide |
2FK3 | 2.4 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'large unit cell' form |
6TI6 | Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils | |
2FK1 | 1.6 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, Cu(II)-bound |
7O1Q | 3.4 | Amyloid beta oligomer displayed on the alpha hemolysin scaffold |
4MVK | 1.5 | Crystal structure of an engineered lipocalin (Anticalin US7) in complex with the Alzheimer amyloid peptide fragment VFFAED |
2Y3J | 1.99 | Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35) |
2LMQ | Structural Model for a 40-residue Beta-Amyloid Fibril with Three-Fold Symmetry, Negative Stagger | |
7JXO | 2.81 | Triangular trimer of beta-hairpins derived from Abeta17-36 with an F20Cha mutation |
5HOY | 2.295 | X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV). |
5TXD | 1.452 | Structure of amyloid-beta derived peptide - NKGAIF |
1ZE9 | Zinc-binding domain of Alzheimer's disease amyloid beta-peptide complexed with a zinc (II) cation | |
8BG0 | 1.99 | Amyloid-beta tetrameric filaments with the Arctic mutation (E22G) from Alzheimer's disease brains | ABeta40 |
2Y2A | 1.91 | Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph I |
2FKL | 2.5 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain (Residues 126- 189 of APP) |
3U0T | 2.5 | Fab-antibody complex |
5MYX | 1.492 | Structure of Pyroglutamate-Abeta-specific Fab c#24 in complex with human Abeta-pE3-18 |
2LLM | Structure of amyloid precursor protein's transmembrane domain | |
1IYT | Solution structure of the Alzheimer's disease amyloid beta-peptide (1-42) | |
3PZZ | 1.29 | Structure of an amyloid forming peptide GAIIGL (29-34) from amyloid beta |
5VOS | 1.42 | VGSNKGAIIGL from Amyloid Beta determined by MicroED |
3BKJ | 1.59 | Crystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16) |
7Q4M | 2.8 | Type II beta-amyloid 42 Filaments from Human Brain |
6YHP | Solution NMR Structure of APP V44M mutant TMD | |
2IPU | 1.65 | PFA1 Fab fragment complexed with Abeta 1-8 peptide |
6SHS | 4.4 | Abeta fibril (Morphology I) |
5AM8 | 1.9 | Crystal structure of the Angiotensin-1 converting enzyme N-domain in complex with amyloid-beta 4-10 |
3L81 | 1.6 | Crystal structure of adaptor protein complex 4 (AP-4) mu4 subunit C-terminal domain, in complex with a sorting peptide from the amyloid precursor protein (APP) |
3SV1 | 3.3 | Crystal structure of APP peptide bound rat Mint2 PARM |
6SZF | Solution structure of the amyloid beta-peptide (1-42) | |
5HOX | 1.9 | X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. Synchrotron data set. (LVFFAEDCGSNKCAII(SAR)LMV). |
2FK2 | 1.65 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, Cu(I)-bound |
2FJZ | 1.61 | Structure of the Alzheimer's Amyloid Precursor Protein (APP) copper binding domain (residues 133 to 189) in 'small unit cell' form, metal-free |
1QCM | AMYLOID BETA PEPTIDE (25-35), NMR, 20 STRUCTURES | |
6IYC | 2.6 | Recognition of the Amyloid Precursor Protein by Human gamma-secretase |
6OC9 | S8 phosphorylated beta amyloid 40 fibrils | |
7RTZ | 2.1 | X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 14-40 |
3OW9 | 1.8 | Structure of an amyloid forming peptide KLVFFA from amyloid beta, alternate polymorph II |
7B3J | Dynamic complex between all-D-enantiomeric peptide D3 with wild-type amyloid precursor protein 672-726 fragment (amyloid beta 1-55) | |
2R0W | 2.503 | PFA2 FAB complexed with Abeta1-8 |
5OQV | 4.0 | Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM |
3UMK | 2.6 | X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with copper |
3UMH | 2.0 | X-ray structure of the E2 domain of the human amyloid precursor protein (APP) in complex with cadmium |
5CSZ | 1.8 | CRYSTAL STRUCTURE OF GANTENERUMAB FAB FRAGMENT IN COMPLEX WITH ABETA 1-11 |
3BAE | 1.593 | Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28) |
2M4J | 40-residue beta-amyloid fibril derived from Alzheimer's disease brain | |
7OXN | 2.5 | Crystal Structure of TAP01 in complex with cyclised amyloid beta peptide |
4OJF | 1.998 | Humanised 3D6 Fab complexed to amyloid beta 1-8 |
1Z0Q | Aqueous Solution Structure of the Alzheimer's Disease Abeta Peptide (1-42) | |
7E6P | 2.5 | Fab-amyloid beta fragment complex |
2LNQ | 40-residue D23N beta amyloid fibril | |
4JFN | 1.75 | Crystal structure of the N-terminal, growth factor-like domain of the amyloid precursor protein bound to copper |
1HZ3 | ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35) | |
6O4J | 1.402 | Amyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutation |
2LMO | Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger | |
2OTK | Structure of Alzheimer Ab peptide in complex with an engineered binding protein | |
6GFI | 2.3 | Structure of Human Mesotrypsin in complex with APPI variant T11V/M17R/I18F/F34V |
3JQL | 1.2 | Crystal Structure of the Complex Formed Between Phospholipase A2 and a Hexapeptide Fragment of Amyloid Beta Peptide, Lys-Leu-Val-Phe-Phe-Ala at 1.2 A Resolution |
2MXU | 42-Residue Beta Amyloid Fibril | |
1MWP | 1.8 | N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN |
5VZY | 2.32 | Crystal structure of crenezumab Fab in complex with Abeta |
5ONP | 1.34 | Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Cd-substituted Thermolysin |
3JTI | 1.8 | Crystal structure of the complex formed between Phospholipase A2 with beta-amyloid fragment, Lys-Gly-Ala-Ile-Ile-Gly-Leu-Met at 1.8 A resolution |
6CO3 | 2.384 | aducanumab abeta complex |
6TI7 | Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils | |
1ZE7 | Zinc-binding domain of Alzheimer's disease amyloid beta-peptide in water solution at pH 6.5 | |
1BA6 | SOLUTION STRUCTURE OF THE METHIONINE-OXIDIZED AMYLOID BETA-PEPTIDE (1-40). DOES OXIDATION AFFECT CONFORMATIONAL SWITCHING? NMR, 10 STRUCTURES | |
7JXN | 2.0 | Beta hairpin derived from Abeta17-36 with an F20Cha mutation |
4ONG | 2.2 | Fab fragment of 3D6 in complex with amyloid beta 1-40 |
1BRC | 2.5 | RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN |
3DXD | 2.2 | Crystal structure of the intracellular domain of human APP (T668E mutant) in complex with Fe65-PTB2 |
7B3K | Dynamic complex between all-D-enantiomeric peptide D3 with L723P mutant of amyloid precursor protein (APP) 672-726 fragment (amyloid beta 1-55) | |
1QWP | NMR analysis of 25-35 fragment of beta amyloid peptide | |
3Q2X | 1.451 | Structure of an amyloid forming peptide NKGAII (residues 27-32) from amyloid beta |
4NGE | 2.704 | Crystal Structure of Human Presequence Protease in Complex with Amyloid-beta (1-40) |
1QXC | NMR structure of the fragment 25-35 of beta amyloid peptide in 20/80 v:v hexafluoroisopropanol/water mixture | |
8AZT | 3.7 | Type II amyloid-beta 42 filaments from high-spin supernatants of aqueous extracts from Alzheimer's disease brains | ABeta42 |
7WVY | 3.0 | Cryo-EM structure of the human formyl peptide receptor 2 in complex with Abeta42 and Gi2 |
2NAO | Atomic resolution structure of a disease-relevant Abeta(1-42) amyloid fibril | |
1TAW | 1.8 | BOVINE TRYPSIN COMPLEXED TO APPI |
2M9R | 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside | |
1BA4 | THE SOLUTION STRUCTURE OF AMYLOID BETA-PEPTIDE (1-40) IN A WATER-MICELLE ENVIRONMENT. IS THE MEMBRANE-SPANNING DOMAIN WHERE WE THINK IT IS? NMR, 10 STRUCTURES | |
8AZS | 2.9 | Type I amyloid-beta 42 filaments from high-spin supernatants of aqueous extracts from Alzheimer's disease brains | ABeta42 |
2LP1 | The solution NMR structure of the transmembrane C-terminal domain of the amyloid precursor protein (C99) | |
2Y29 | 2.3 | Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III |
6YHI | Solution NMR Structure of APP G38L mutant TMD | |
4PWQ | 1.4 | HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE E1-DOMAIN of THE AMYLOID PRECURSOR PROTEIN |
5MYO | 1.59 | Structure of Pyroglutamate-Abeta-specific Fab c#6 in complex with human Abeta-pE3-12-PEGb |
3JQ5 | 2.03 | Phospholipase A2 Prevents the Aggregation of Amyloid Beta Peptides: Crystal Structure of the Complex of Phospholipase A2 with Octapeptide Fragment of Amyloid Beta Peptide, Asp-Ala-Glu-Phe-Arg-His-Asp-Ser at 2 A Resolution |
5HOW | 2.295 | X-ray crystallographic structure of an Abeta 17-36 beta-hairpin. LV(PHI)FAEDCGSNKCAII(SAR)L(ORN)V |
4MVL | 2.3 | Crystal structure of an engineered lipocalin (Anticalin H1GA) in complex with the Alzheimer amyloid peptide Abeta1-40 |
6YHO | Solution NMR Structure of APP G38P mutant TM | |
3MXC | 2.0 | Structures of Grb2-SH2 Domain and AICD peptide Complexes Reveal a Conformational Switch and Their Functional Implications. |
1TKN | Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein | |
1AML | THE ALZHEIMER`S DISEASE AMYLOID A4 PEPTIDE (RESIDUES 1-40) | |
5W3P | 1.92 | ANTIBODY C706 IN COMPLEX WTH BETA-AMYLOID PEPTIDE 1-16 |
6NB9 | 1.05 | Amyloid-Beta (20-34) with L-isoaspartate 23 |
5KK3 | Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils | |
3AYU | 2.0 | Crystal structure of MMP-2 active site mutant in complex with APP-drived decapeptide inhibitor |
3DXC | 2.1 | Crystal structure of the intracellular domain of human APP in complex with Fe65-PTB2 |
2LMN | Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Positive Stagger | |
1OWT | Structure of the Alzheimer's disease amyloid precursor protein copper binding domain | |
1ZJD | 2.6 | Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Kunitz Protease Inhibitor Domain of Protease Nexin II |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:1903381 | regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway |
Biological Process | GO:1990535 | neuron projection maintenance |
Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
Biological Process | GO:0010823 | negative regulation of mitochondrion organization |
Biological Process | GO:0070206 | protein trimerization |
Biological Process | GO:0070555 | response to interleukin-1 |
Biological Process | GO:0061844 | antimicrobial humoral immune response mediated by antimicrobial peptide |
Biological Process | GO:0061098 | positive regulation of protein tyrosine kinase activity |
Biological Process | GO:0034121 | regulation of toll-like receptor signaling pathway |
Biological Process | GO:1902894 | negative regulation of miRNA transcription |
Biological Process | GO:1904646 | cellular response to amyloid-beta |
Biological Process | GO:0045931 | positive regulation of mitotic cell cycle |
Biological Process | GO:0032729 | positive regulation of type II interferon production |
Biological Process | GO:0007417 | central nervous system development |
Biological Process | GO:0043408 | regulation of MAPK cascade |
Biological Process | GO:0010466 | negative regulation of peptidase activity |
Biological Process | GO:0030198 | extracellular matrix organization |
Biological Process | GO:0045665 | negative regulation of neuron differentiation |
Biological Process | GO:0050890 | cognition |
Biological Process | GO:0050808 | synapse organization |
Biological Process | GO:0016358 | dendrite development |
Biological Process | GO:0002265 | astrocyte activation involved in immune response |
Biological Process | GO:0007626 | locomotory behavior |
Biological Process | GO:0050830 | defense response to Gram-positive bacterium |
Biological Process | GO:0001878 | response to yeast |
Biological Process | GO:0051563 | smooth endoplasmic reticulum calcium ion homeostasis |
Biological Process | GO:0007176 | regulation of epidermal growth factor-activated receptor activity |
Biological Process | GO:0016322 | neuron remodeling |
Biological Process | GO:0051124 | synaptic assembly at neuromuscular junction |
Biological Process | GO:1905898 | positive regulation of response to endoplasmic reticulum stress |
Biological Process | GO:0007189 | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
Biological Process | GO:0008344 | adult locomotory behavior |
Biological Process | GO:0050729 | positive regulation of inflammatory response |
Biological Process | GO:0051247 | positive regulation of protein metabolic process |
Biological Process | GO:0051091 | positive regulation of DNA-binding transcription factor activity |
Biological Process | GO:0035235 | ionotropic glutamate receptor signaling pathway |
Biological Process | GO:0042327 | positive regulation of phosphorylation |
Biological Process | GO:0043406 | positive regulation of MAP kinase activity |
Biological Process | GO:0007611 | learning or memory |
Biological Process | GO:0010800 | positive regulation of peptidyl-threonine phosphorylation |
Biological Process | GO:0014005 | microglia development |
Biological Process | GO:0031175 | neuron projection development |
Biological Process | GO:0007204 | positive regulation of cytosolic calcium ion concentration |
Biological Process | GO:0032731 | positive regulation of interleukin-1 beta production |
Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
Biological Process | GO:0007193 | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
Biological Process | GO:0051260 | protein homooligomerization |
Biological Process | GO:0045429 | positive regulation of nitric oxide biosynthetic process |
Biological Process | GO:0010971 | positive regulation of G2/M transition of mitotic cell cycle |
Biological Process | GO:0010739 | positive regulation of protein kinase A signaling |
Biological Process | GO:0001774 | microglial cell activation |
Biological Process | GO:0071874 | cellular response to norepinephrine stimulus |
Biological Process | GO:0010288 | response to lead ion |
Biological Process | GO:0008306 | associative learning |
Biological Process | GO:1900122 | positive regulation of receptor binding |
Biological Process | GO:0042157 | lipoprotein metabolic process |
Biological Process | GO:0008542 | visual learning |
Biological Process | GO:0006979 | response to oxidative stress |
Biological Process | GO:1902951 | negative regulation of dendritic spine maintenance |
Biological Process | GO:0098815 | modulation of excitatory postsynaptic potential |
Biological Process | GO:0045745 | positive regulation of G protein-coupled receptor signaling pathway |
Biological Process | GO:2000310 | regulation of NMDA receptor activity |
Biological Process | GO:0032930 | positive regulation of superoxide anion generation |
Biological Process | GO:2000406 | positive regulation of T cell migration |
Biological Process | GO:0007409 | axonogenesis |
Biological Process | GO:0008088 | axo-dendritic transport |
Biological Process | GO:0010628 | positive regulation of gene expression |
Biological Process | GO:0045821 | positive regulation of glycolytic process |
Biological Process | GO:0019732 | antifungal humoral response |
Biological Process | GO:1903523 | negative regulation of blood circulation |
Biological Process | GO:0050803 | regulation of synapse structure or activity |
Biological Process | GO:1900273 | positive regulation of long-term synaptic potentiation |
Biological Process | GO:0043280 | positive regulation of cysteine-type endopeptidase activity involved in apoptotic process |
Biological Process | GO:1900221 | regulation of amyloid-beta clearance |
Biological Process | GO:1905908 | positive regulation of amyloid fibril formation |
Biological Process | GO:0043410 | positive regulation of MAPK cascade |
Biological Process | GO:0035066 | positive regulation of histone acetylation |
Biological Process | GO:0040014 | regulation of multicellular organism growth |
Biological Process | GO:0016199 | axon midline choice point recognition |
Biological Process | GO:0010469 | regulation of signaling receptor activity |
Biological Process | GO:0030111 | regulation of Wnt signaling pathway |
Biological Process | GO:0048169 | regulation of long-term neuronal synaptic plasticity |
Biological Process | GO:0070050 | neuron cellular homeostasis |
Biological Process | GO:0006897 | endocytosis |
Biological Process | GO:0071287 | cellular response to manganese ion |
Biological Process | GO:0048143 | astrocyte activation |
Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
Biological Process | GO:0008285 | negative regulation of cell population proliferation |
Biological Process | GO:0008203 | cholesterol metabolic process |
Biological Process | GO:0007617 | mating behavior |
Biological Process | GO:0051897 | positive regulation of protein kinase B signaling |
Biological Process | GO:0007155 | cell adhesion |
Biological Process | GO:1990090 | cellular response to nerve growth factor stimulus |
Biological Process | GO:0043065 | positive regulation of apoptotic process |
Biological Process | GO:2000463 | positive regulation of excitatory postsynaptic potential |
Biological Process | GO:0046330 | positive regulation of JNK cascade |
Biological Process | GO:0070374 | positive regulation of ERK1 and ERK2 cascade |
Biological Process | GO:0090026 | positive regulation of monocyte chemotaxis |
Biological Process | GO:2001238 | positive regulation of extrinsic apoptotic signaling pathway |
Biological Process | GO:0033138 | positive regulation of peptidyl-serine phosphorylation |
Biological Process | GO:0007186 | G protein-coupled receptor signaling pathway |
Biological Process | GO:0051402 | neuron apoptotic process |
Biological Process | GO:0030178 | negative regulation of Wnt signaling pathway |
Biological Process | GO:1900454 | positive regulation of long-term synaptic depression |
Biological Process | GO:0032722 | positive regulation of chemokine production |
Biological Process | GO:0050730 | regulation of peptidyl-tyrosine phosphorylation |
Biological Process | GO:1904472 | positive regulation of endothelin production |
Biological Process | GO:0048669 | collateral sprouting in absence of injury |
Biological Process | GO:1905945 | regulation of response to calcium ion |
Biological Process | GO:0006378 | mRNA polyadenylation |
Biological Process | GO:0007612 | learning |
Biological Process | GO:0006468 | protein phosphorylation |
Biological Process | GO:1902949 | positive regulation of tau-protein kinase activity |
Biological Process | GO:1900181 | negative regulation of protein localization to nucleus |
Biological Process | GO:0010629 | negative regulation of gene expression |
Biological Process | GO:1900272 | negative regulation of long-term synaptic potentiation |
Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
Biological Process | GO:0043525 | positive regulation of neuron apoptotic process |
Biological Process | GO:0051092 | positive regulation of NF-kappaB transcription factor activity |
Biological Process | GO:1902950 | regulation of dendritic spine maintenance |
Biological Process | GO:0071280 | cellular response to copper ion |
Biological Process | GO:0006417 | regulation of translation |
Biological Process | GO:0051262 | protein tetramerization |
Biological Process | GO:0061903 | positive regulation of 1-phosphatidylinositol-3-kinase activity |
Biological Process | GO:0050867 | positive regulation of cell activation |
Biological Process | GO:0032755 | positive regulation of interleukin-6 production |
Biological Process | GO:0007219 | Notch signaling pathway |
Biological Process | GO:0030900 | forebrain development |
Biological Process | GO:0045666 | positive regulation of neuron differentiation |
Biological Process | GO:1902961 | positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process |
Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
Biological Process | GO:0007613 | memory |
Biological Process | GO:0061097 | regulation of protein tyrosine kinase activity |
Biological Process | GO:1904591 | positive regulation of protein import |
Biological Process | GO:0050885 | neuromuscular process controlling balance |
Biological Process | GO:0019731 | antibacterial humoral response |
Biological Process | GO:0045087 | innate immune response |
Biological Process | GO:0032092 | positive regulation of protein binding |
Biological Process | GO:0071320 | cellular response to cAMP |
Biological Process | GO:1903048 | regulation of acetylcholine-gated cation channel activity |
Biological Process | GO:0001934 | positive regulation of protein phosphorylation |
Biological Process | GO:0019722 | calcium-mediated signaling |
Biological Process | GO:0150003 | regulation of spontaneous synaptic transmission |
Biological Process | GO:0032760 | positive regulation of tumor necrosis factor production |
Biological Process | GO:0001967 | suckling behavior |
Biological Process | GO:1905606 | regulation of presynapse assembly |
Biological Process | GO:1905906 | regulation of amyloid fibril formation |
Biological Process | GO:0006878 | intracellular copper ion homeostasis |
Biological Process | GO:0051044 | positive regulation of membrane protein ectodomain proteolysis |
Biological Process | GO:0010468 | regulation of gene expression |
Biological Process | GO:1901224 | positive regulation of NIK/NF-kappaB signaling |
Biological Process | GO:1904022 | positive regulation of G protein-coupled receptor internalization |
Biological Process | GO:0050829 | defense response to Gram-negative bacterium |
Biological Process | GO:1990000 | amyloid fibril formation |
Molecular Function | GO:0003677 | DNA binding |
Molecular Function | GO:0001664 | G protein-coupled receptor binding |
Molecular Function | GO:0051425 | PTB domain binding |
Molecular Function | GO:0050786 | RAGE receptor binding |
Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
Molecular Function | GO:0030549 | acetylcholine receptor activator activity |
Molecular Function | GO:0033130 | acetylcholine receptor binding |
Molecular Function | GO:0097645 | amylin binding |
Molecular Function | GO:0034185 | apolipoprotein binding |
Molecular Function | GO:0042056 | chemoattractant activity |
Molecular Function | GO:0003682 | chromatin binding |
Molecular Function | GO:0019899 | enzyme binding |
Molecular Function | GO:0046875 | ephrin receptor binding |
Molecular Function | GO:0005109 | frizzled binding |
Molecular Function | GO:0070851 | growth factor receptor binding |
Molecular Function | GO:1904399 | heparan sulfate binding |
Molecular Function | GO:0043395 | heparan sulfate proteoglycan binding |
Molecular Function | GO:0008201 | heparin binding |
Molecular Function | GO:0042802 | identical protein binding |
Molecular Function | GO:0005158 | insulin receptor binding |
Molecular Function | GO:0005178 | integrin binding |
Molecular Function | GO:0050750 | low-density lipoprotein particle receptor binding |
Molecular Function | GO:0016504 | peptidase activator activity |
Molecular Function | GO:0046983 | protein dimerization activity |
Molecular Function | GO:0046982 | protein heterodimerization activity |
Molecular Function | GO:0042803 | protein homodimerization activity |
Molecular Function | GO:0051087 | protein-folding chaperone binding |
Molecular Function | GO:0048018 | receptor ligand activity |
Molecular Function | GO:0004867 | serine-type endopeptidase inhibitor activity |
Molecular Function | GO:0030546 | signaling receptor activator activity |
Molecular Function | GO:0005102 | signaling receptor binding |
Molecular Function | GO:0046914 | transition metal ion binding |
Cellular Component | GO:0030134 | COPII-coated ER to Golgi transport vesicle |
Cellular Component | GO:0005794 | Golgi apparatus |
Cellular Component | GO:0005796 | Golgi lumen |
Cellular Component | GO:0005798 | Golgi-associated vesicle |
Cellular Component | GO:0106003 | amyloid-beta complex |
Cellular Component | GO:0045177 | apical part of cell |
Cellular Component | GO:0097449 | astrocyte projection |
Cellular Component | GO:0030424 | axon |
Cellular Component | GO:0009986 | cell surface |
Cellular Component | GO:0005911 | cell-cell junction |
Cellular Component | GO:0035253 | ciliary rootlet |
Cellular Component | GO:0005905 | clathrin-coated pit |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0043198 | dendritic shaft |
Cellular Component | GO:0043197 | dendritic spine |
Cellular Component | GO:0005769 | early endosome |
Cellular Component | GO:0005783 | endoplasmic reticulum |
Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
Cellular Component | GO:0005768 | endosome |
Cellular Component | GO:0031904 | endosome lumen |
Cellular Component | GO:0070381 | endosome to plasma membrane transport vesicle |
Cellular Component | GO:0070062 | extracellular exosome |
Cellular Component | GO:0005576 | extracellular region |
Cellular Component | GO:0005615 | extracellular space |
Cellular Component | GO:1990812 | growth cone filopodium |
Cellular Component | GO:1990761 | growth cone lamellipodium |
Cellular Component | GO:0034364 | high-density lipoprotein particle |
Cellular Component | GO:0034363 | intermediate-density lipoprotein particle |
Cellular Component | GO:1990777 | lipoprotein particle |
Cellular Component | GO:0044304 | main axon |
Cellular Component | GO:0016020 | membrane |
Cellular Component | GO:0045121 | membrane raft |
Cellular Component | GO:0005739 | mitochondrion |
Cellular Component | GO:0031594 | neuromuscular junction |
Cellular Component | GO:0098992 | neuronal dense core vesicle |
Cellular Component | GO:0005641 | nuclear envelope lumen |
Cellular Component | GO:0005634 | nucleus |
Cellular Component | GO:0043204 | perikaryon |
Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
Cellular Component | GO:0005886 | plasma membrane |
Cellular Component | GO:0031093 | platelet alpha granule lumen |
Cellular Component | GO:0048786 | presynaptic active zone |
Cellular Component | GO:0032991 | protein-containing complex |
Cellular Component | GO:0043235 | receptor complex |
Cellular Component | GO:0055037 | recycling endosome |
Cellular Component | GO:0005791 | rough endoplasmic reticulum |
Cellular Component | GO:0005790 | smooth endoplasmic reticulum |
Cellular Component | GO:0051233 | spindle midzone |
Cellular Component | GO:0045202 | synapse |
Cellular Component | GO:0008021 | synaptic vesicle |
Cellular Component | GO:0032588 | trans-Golgi network membrane |
InterPro | InterPro name |
---|---|
IPR002223 | Pancreatic trypsin inhibitor Kunitz domain |
IPR008154 | Amyloidogenic glycoprotein, extracellular |
IPR008155 | Amyloidogenic glycoprotein |
IPR011178 | Amyloidogenic glycoprotein, copper-binding |
IPR011993 | PH-like domain superfamily |
IPR013803 | Amyloidogenic glycoprotein, amyloid-beta peptide |
IPR015849 | Amyloidogenic glycoprotein, heparin-binding |
IPR019543 | Beta-amyloid precursor protein C-terminal |
IPR019744 | Amyloidogenic glycoprotein, copper-binding domain conserved site |
IPR019745 | Amyloidogenic glycoprotein, intracellular domain, conserved site |
IPR020901 | Proteinase inhibitor I2, Kunitz, conserved site |
IPR024329 | Amyloidogenic glycoprotein, E2 domain |
IPR036176 | E2 domain superfamily |
IPR036454 | Amyloidogenic glycoprotein, heparin-binding domain superfamily |
IPR036669 | Amyloidogenic glycoprotein, copper-binding domain superfamily |
IPR036880 | Pancreatic trypsin inhibitor Kunitz domain superfamily |
IPR037071 | Amyloidogenic glycoprotein, amyloid-beta peptide superfamily |
Pfam | Pfam name |
---|---|
PF00014 | Kunitz/Bovine pancreatic trypsin inhibitor domain |
PF02177 | Amyloid A4 N-terminal heparin-binding |
PF03494 | Beta-amyloid peptide (beta-APP) |
PF10515 | Beta-amyloid precursor protein C-terminus |
PF12924 | Copper-binding of amyloid precursor, CuBD |
PF12925 | E2 domain of amyloid precursor protein |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-114608 | Platelet degranulation | Leaf | R-HSA-109582 | Hemostasis |
R-HSA-3000178 | ECM proteoglycans | Leaf | R-HSA-1474244 | Extracellular matrix organization |
R-HSA-381426 | Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) | Leaf | R-HSA-392499 | Metabolism of proteins |
R-HSA-416476 | G alpha (q) signalling events | Internal node | R-HSA-162582 | Signal Transduction |
R-HSA-418594 | G alpha (i) signalling events | Internal node | R-HSA-162582 | Signal Transduction |
R-HSA-432720 | Lysosome Vesicle Biogenesis | Leaf | R-HSA-5653656 | Vesicle-mediated transport |
R-HSA-444473 | Formyl peptide receptors bind formyl peptides and many other ligands | Leaf | R-HSA-162582 | Signal Transduction |
R-HSA-445989 | TAK1-dependent IKK and NF-kappa-B activation | Internal node | R-HSA-168256 | Immune System |
R-HSA-844456 | The NLRP3 inflammasome | Leaf | R-HSA-168256 | Immune System |
R-HSA-879415 | Advanced glycosylation endproduct receptor signaling | Leaf | R-HSA-168256 | Immune System |
R-HSA-8862803 | Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models | Leaf | R-HSA-1643685 | Disease |
R-HSA-8957275 | Post-translational protein phosphorylation | Leaf | R-HSA-392499 | Metabolism of proteins |
R-HSA-933542 | TRAF6 mediated NF-kB activation | Leaf | R-HSA-168256 | Immune System |
R-HSA-9609523 | Insertion of tail-anchored proteins into the endoplasmic reticulum membrane | Leaf | R-HSA-9609507 | Protein localization |
R-HSA-9660826 | Purinergic signaling in leishmaniasis infection | Leaf | R-HSA-1643685 | Disease |
R-HSA-977225 | Amyloid fiber formation | Leaf | R-HSA-392499 | Metabolism of proteins |
HPO ID | HPO name |
---|---|
HP:0000006 | Autosomal dominant inheritance |
HP:0000504 | Abnormality of vision |
HP:0000657 | Oculomotor apraxia |
HP:0000708 | Atypical behavior |
HP:0000713 | Agitation |
HP:0000726 | Dementia |
HP:0000734 | Disinhibition |
HP:0000738 | Hallucinations |
HP:0001249 | Intellectual disability |
HP:0001250 | Seizure |
HP:0001251 | Ataxia |
HP:0001259 | Coma |
HP:0001263 | Global developmental delay |
HP:0001268 | Mental deterioration |
HP:0001276 | Hypertonia |
HP:0001288 | Gait disturbance |
HP:0001289 | Confusion |
HP:0001297 | Stroke |
HP:0001300 | Parkinsonism |
HP:0001336 | Myoclonus |
HP:0001342 | Cerebral hemorrhage |
HP:0002015 | Dysphagia |
HP:0002076 | Migraine |
HP:0002120 | Cerebral cortical atrophy |
HP:0002138 | Subarachnoid hemorrhage |
HP:0002185 | Neurofibrillary tangles |
HP:0002186 | Apraxia |
HP:0002315 | Headache |
HP:0002354 | Memory impairment |
HP:0002373 | Febrile seizure (within the age range of 3 months to 6 years) |
HP:0002381 | Aphasia |
HP:0002423 | Long-tract signs |
HP:0002463 | Language impairment |
HP:0002511 | Alzheimer disease |
HP:0002514 | Cerebral calcification |
HP:0002637 | Cerebral ischemia |
HP:0003401 | Paresthesia |
HP:0003474 | Somatic sensory dysfunction |
HP:0003581 | Adult onset |
HP:0003584 | Late onset |
HP:0003596 | Middle age onset |
HP:0003791 | Deposits immunoreactive to beta-amyloid protein |
HP:0004938 | Tortuous cerebral arteries |
HP:0004968 | Recurrent cerebral hemorrhage |
HP:0010525 | Finger agnosia |
HP:0010526 | Dysgraphia |
HP:0011446 | Abnormality of higher mental function |
HP:0011695 | Cerebellar hemorrhage |
HP:0011970 | Cerebral amyloid angiopathy |
HP:0012433 | Abnormal social behavior |
HP:0012759 | Neurodevelopmental abnormality |
HP:0030219 | Semantic dementia |
HP:0100613 | Death in early adulthood |
HP:0100659 | Abnormal cerebral vascular morphology |
HP:0410054 | Decreased circulating GABA concentration |
Disease name | MONDO ID | ICD10 | ICD10 chapter | OMIM | Orphanet |
---|---|---|---|---|---|
alzheimer disease type 1 | MONDO:0007088 | G30 | chapter6, Diseases of the nervous system | OMIM:104300 | |
abeta amyloidosis, dutch type | MONDO:0015033 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:100006 | |
abeta amyloidosis, dutch type | MONDO:0015033 | I68 | chapter9, Diseases of the circulatory system | Orphanet:100006 | |
abetal34v amyloidosis | MONDO:0017945 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:324703 | |
abetal34v amyloidosis | MONDO:0017945 | I68 | chapter9, Diseases of the circulatory system | Orphanet:324703 | |
abeta amyloidosis, iowa type | MONDO:0017946 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:324708 | |
abeta amyloidosis, iowa type | MONDO:0017946 | I68 | chapter9, Diseases of the circulatory system | Orphanet:324708 | |
abeta amyloidosis, italian type | MONDO:0017947 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:324713 | |
abeta amyloidosis, italian type | MONDO:0017947 | I68 | chapter9, Diseases of the circulatory system | Orphanet:324713 | |
abetaa21g amyloidosis | MONDO:0017948 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:324718 | |
abetaa21g amyloidosis | MONDO:0017948 | I68 | chapter9, Diseases of the circulatory system | Orphanet:324718 | |
abeta amyloidosis, arctic type | MONDO:0017949 | E85 | chapter4, Endocrine, nutritional and metabolic diseases | Orphanet:324723 | |
abeta amyloidosis, arctic type | MONDO:0017949 | I68 | chapter9, Diseases of the circulatory system | Orphanet:324723 |