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  • 11.0 [archived version]
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CNTFR CNTFR APBA1 APBA1 APBB2 APBB2 APBA3 APBA3 ENSG00000259680 ENSG00000259680 APLP1 APLP1 APBB1 APBB1 DICER1 DICER1 MXRA8 MXRA8 APBA2 APBA2 APLP2 APLP2 APP APP GPCPD1 GPCPD1 TNFRSF21 TNFRSF21 IGHV3-15 IGHV3-15 IGHV3-43D IGHV3-43D IGHV3-11 IGHV3-11 IGLL5 IGLL5 PRSS3P2 PRSS3P2 CORIN CORIN PRSS3 PRSS3 VPREB1 VPREB1 IGHV4-38-2 IGHV4-38-2 PRSS1 PRSS1 ENSG00000278782 ENSG00000278782 ENSG00000267748 ENSG00000267748
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
APLP1Amyloid-like protein 1; May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I; Belongs to the APP family (651 aa)
APLP2Amyloid-like protein 2; May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5’-GTCACATG-3’(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity) (763 aa)
APBA1Amyloid-beta A4 precursor protein-binding family A member 1; Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP- beta; PDZ domain containing (837 aa)
CORINAtrial natriuretic peptide-converting enzyme; Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptid [...] (1042 aa)
APPAmyloid-beta A4 protein; N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6); Endogenous ligands (770 aa)
TNFRSF21Tumor necrosis factor receptor superfamily member 21; Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Plays a role in neuronal apoptosis, including apoptosis in response to amyloid peptides derived from APP, and is required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal frag [...] (655 aa)
PRSS1Trypsin-1; Has activity against the synthetic substrates Boc-Phe- Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val- Pro-Arg-Mec. The single-chain form is more active than the two- chain form against all of these substrates; Belongs to the peptidase S1 family (247 aa)
APBA3Amyloid-beta A4 precursor protein-binding family A member 3; May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. May enhance the activity of HIF1A in macrophages by inhibiting the activity of HIF1AN; PDZ domain containing (575 aa)
PRSS3Trypsin-3; Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5; Belongs to the peptidase S1 family (304 aa)
CNTFRCiliary neurotrophic factor receptor subunit alpha; Binds to CNTF. The alpha subunit provides the receptor specificity; Belongs to the type I cytokine receptor family. Type 3 subfamily (372 aa)
GPCPD1Glycerophosphocholine phosphodiesterase GPCPD1; May be involved in the negative regulation of skeletal muscle differentiation, independently of its glycerophosphocholine phosphodiesterase activity; Belongs to the glycerophosphoryl diester phosphodiesterase family (672 aa)
VPREB1Immunoglobulin iota chain; Associates with the Ig-mu chain to form a molecular complex that is expressed on the surface of pre-B-cells. This complex presumably regulates Ig gene rearrangements in the early steps of B-cell differentiation; CD molecules (145 aa)
MXRA8Matrix remodeling-associated protein 8; May play a role in the maturation and maintenance of blood-brain barrier; V-set domain containing (450 aa)
APBB2Amyloid-beta A4 precursor protein-binding family B member 2; May modulate the internalization of amyloid-beta precursor protein (759 aa)
IGLL5Immunoglobulin lambda like polypeptide 5; C1-set domain containing (214 aa)
DICER1Endoribonuclease Dicer; Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3’ overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA- induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, a [...] (1922 aa)
APBA2Amyloid-beta A4 precursor protein-binding family A member 2; Putative function in synaptic vesicle exocytosis by binding to STXBP1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta; PDZ domain containing (749 aa)
ENSG00000267748annotation not available (153 aa)
ENSG00000259680Uncharacterized protein (116 aa)
APBB1Amyloid-beta A4 precursor protein-binding family B member 1; Transcription coregulator that can have both coactivator and corepressor functions. Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on ’Tyr-142’ (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro- apoptosis factors such as MAPK8/JNK [...] (710 aa)
IGHV4-38-2Immunoglobulin heavy variable 4-38-2; V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, whi [...] (117 aa)
IGHV3-11Immunoglobulin heavy variable 3-11; V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which [...] (96 aa)
ENSG00000278782annotation not available (95 aa)
IGHV3-15Immunoglobulin heavy variable 3-15; V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which [...] (112 aa)
IGHV3-43DImmunoglobulin heavy variable 3-43D; V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, whic [...] (98 aa)
PRSS3P2Trypsin-2; In the ileum, may be involved in defensin processing, including DEFA5; Belongs to the peptidase S1 family (261 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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