7 items (Homo sapiens) - STRING network view

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.

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protein of unknown 3D structure

large nodes:
some 3D structure is known or predicted

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query proteins and first shell of interactors

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second shell of interactors

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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.

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Predicted Interactions

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Your Input:
	PI3	peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis (117 aa)
	CELA1	chymotrypsin-like elastase family, member 1; Acts upon elastin (258 aa)
	LPA	lipoprotein, Lp(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330 (2040 aa)
	A2M	alpha-2-macroglobulin; 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 the co [...] (1474 aa)
	CSN2	casein beta; Important role in determination of the surface properties of the casein micelles (226 aa)
	SERPINA1	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1 (418 aa)
	SERPINA3	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3 (423 aa)

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
A2M	CELA1	ENSP00000323929	ENSP00000293636	alpha-2-macroglobulin; 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 the co [...]	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.576
A2M	SERPINA1	ENSP00000323929	ENSP00000348068	alpha-2-macroglobulin; 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 the co [...]	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	0.948
A2M	SERPINA3	ENSP00000323929	ENSP00000376793	alpha-2-macroglobulin; 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 the co [...]	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3	0.499
CELA1	A2M	ENSP00000293636	ENSP00000323929	chymotrypsin-like elastase family, member 1; Acts upon elastin	alpha-2-macroglobulin; 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 the co [...]	0.576
CELA1	CSN2	ENSP00000293636	ENSP00000341030	chymotrypsin-like elastase family, member 1; Acts upon elastin	casein beta; Important role in determination of the surface properties of the casein micelles	0.576
CELA1	LPA	ENSP00000293636	ENSP00000321334	chymotrypsin-like elastase family, member 1; Acts upon elastin	lipoprotein, Lp(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330	0.580
CELA1	PI3	ENSP00000293636	ENSP00000243924	chymotrypsin-like elastase family, member 1; Acts upon elastin	peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis	0.576
CELA1	SERPINA1	ENSP00000293636	ENSP00000348068	chymotrypsin-like elastase family, member 1; Acts upon elastin	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	0.617
CELA1	SERPINA3	ENSP00000293636	ENSP00000376793	chymotrypsin-like elastase family, member 1; Acts upon elastin	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3	0.610
CSN2	CELA1	ENSP00000341030	ENSP00000293636	casein beta; Important role in determination of the surface properties of the casein micelles	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.576
LPA	CELA1	ENSP00000321334	ENSP00000293636	lipoprotein, Lp(a); Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.580
PI3	CELA1	ENSP00000243924	ENSP00000293636	peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.576
PI3	SERPINA1	ENSP00000243924	ENSP00000348068	peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	0.472
SERPINA1	A2M	ENSP00000348068	ENSP00000323929	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	alpha-2-macroglobulin; 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 the co [...]	0.948
SERPINA1	CELA1	ENSP00000348068	ENSP00000293636	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.617
SERPINA1	PI3	ENSP00000348068	ENSP00000243924	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1	peptidase inhibitor 3, skin-derived; Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis	0.472
SERPINA3	A2M	ENSP00000376793	ENSP00000323929	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3	alpha-2-macroglobulin; 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 the co [...]	0.499
SERPINA3	CELA1	ENSP00000376793	ENSP00000293636	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3	chymotrypsin-like elastase family, member 1; Acts upon elastin	0.610

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