| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| A2ML1 | CWH43 | ENSP00000299698 | ENSP00000226432 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | cell wall biogenesis 43 C-terminal homolog (S. cerevisiae); Involved in lipid remodeling during GPI-anchor maturation (By similarity) | 0.685 |
| A2ML1 | EVPL | ENSP00000299698 | ENSP00000301607 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | envoplakin; Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments | 0.453 |
| A2ML1 | KLK6 | ENSP00000299698 | ENSP00000309148 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | kallikrein-related peptidase 6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells [...] | 0.749 |
| A2ML1 | KLK7 | ENSP00000299698 | ENSP00000375683 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | kallikrein-related peptidase 7; May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. SCCE cleaves insulin B chain at ’6-Leu-|-Cys-7’, ’16-Tyr-|-Leu-17’, ’25-Phe-|-Tyr-26’ and ’26-Tyr-|-Thr-27’. Could play a role in the activation of precursors to inflammatory cytokines | 0.757 |
| A2ML1 | MAST2 | ENSP00000299698 | ENSP00000354671 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | microtubule associated serine/threonine kinase 2; Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity) | 0.451 |
| A2ML1 | QPCTL | ENSP00000299698 | ENSP00000012049 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | glutaminyl-peptide cyclotransferase-like; Responsible for the biosynthesis of pyroglutamyl peptides | 0.414 |
| A2ML1 | RNPC3 | ENSP00000299698 | ENSP00000391432 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | RNA-binding region (RNP1, RRM) containing 3; Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3’-stem-loop of m(7)G-capped U12 snRNA | 0.416 |
| A2ML1 | SYCP2L | ENSP00000299698 | ENSP00000283141 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | synaptonemal complex protein 2-like | 0.501 |
| A2ML1 | TMEM63C | ENSP00000299698 | ENSP00000298351 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | transmembrane protein 63C | 0.457 |
| A2ML1 | TRAF3IP2 | ENSP00000299698 | ENSP00000357750 | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | TRAF3 interacting protein 2 | 0.517 |
| CWH43 | A2ML1 | ENSP00000226432 | ENSP00000299698 | cell wall biogenesis 43 C-terminal homolog (S. cerevisiae); Involved in lipid remodeling during GPI-anchor maturation (By similarity) | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.685 |
| CWH43 | KLK6 | ENSP00000226432 | ENSP00000309148 | cell wall biogenesis 43 C-terminal homolog (S. cerevisiae); Involved in lipid remodeling during GPI-anchor maturation (By similarity) | kallikrein-related peptidase 6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells [...] | 0.477 |
| EVPL | A2ML1 | ENSP00000301607 | ENSP00000299698 | envoplakin; Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.453 |
| KLK6 | A2ML1 | ENSP00000309148 | ENSP00000299698 | kallikrein-related peptidase 6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells [...] | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.749 |
| KLK6 | CWH43 | ENSP00000309148 | ENSP00000226432 | kallikrein-related peptidase 6; Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells [...] | cell wall biogenesis 43 C-terminal homolog (S. cerevisiae); Involved in lipid remodeling during GPI-anchor maturation (By similarity) | 0.477 |
| KLK7 | A2ML1 | ENSP00000375683 | ENSP00000299698 | kallikrein-related peptidase 7; May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. SCCE cleaves insulin B chain at ’6-Leu-|-Cys-7’, ’16-Tyr-|-Leu-17’, ’25-Phe-|-Tyr-26’ and ’26-Tyr-|-Thr-27’. Could play a role in the activation of precursors to inflammatory cytokines | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.757 |
| MAST2 | A2ML1 | ENSP00000354671 | ENSP00000299698 | microtubule associated serine/threonine kinase 2; Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins. Functions in a multi-protein complex in spermatid maturation. Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation (By similarity) | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.451 |
| QPCTL | A2ML1 | ENSP00000012049 | ENSP00000299698 | glutaminyl-peptide cyclotransferase-like; Responsible for the biosynthesis of pyroglutamyl peptides | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.414 |
| RNPC3 | A2ML1 | ENSP00000391432 | ENSP00000299698 | RNA-binding region (RNP1, RRM) containing 3; Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3’-stem-loop of m(7)G-capped U12 snRNA | alpha-2-macroglobulin-like 1; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates [...] | 0.416 |
| RNPC3 | SYCP2L | ENSP00000391432 | ENSP00000283141 | RNA-binding region (RNP1, RRM) containing 3; Participates in pre-mRNA U12-dependent splicing, performed by the minor spliceosome which removes U12-type introns. U12-type introns comprises less than 1% of all non-coding sequences. Binds to the 3’-stem-loop of m(7)G-capped U12 snRNA | synaptonemal complex protein 2-like | 0.564 |
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