12 items (Homo sapiens) - STRING network view

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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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Your Input:
	GRN	granulin (593 aa)
	ELANE	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa)
	KLK3	kallikrein-related peptidase 3; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum (261 aa)
	MAPK8IP2	mitogen-activated protein kinase 8 interacting protein 2; The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins (By similarity) (823 aa)
	CTSB	cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis (339 aa)
	SLPI	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues (132 aa)
	CTSL1	cathepsin L1; Important for the overall degradation of proteins in lysosomes (333 aa)
	PLSCR1	phospholipid scramblase 1; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system (318 aa)
	PRSS3	protease, serine, 3; Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5 (304 aa)
	CTSS	cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N (331 aa)
	IDO1	indoleamine 2,3-dioxygenase 1; Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen (403 aa)
	IDO2	indoleamine 2,3-dioxygenase 2; Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism (420 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
CTSB	CTSL1	ENSP00000342070	ENSP00000345344	cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis	cathepsin L1; Important for the overall degradation of proteins in lysosomes	0.700
CTSB	SLPI	ENSP00000342070	ENSP00000342082	cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.702
CTSL1	CTSB	ENSP00000345344	ENSP00000342070	cathepsin L1; Important for the overall degradation of proteins in lysosomes	cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis	0.700
CTSL1	CTSS	ENSP00000345344	ENSP00000357981	cathepsin L1; Important for the overall degradation of proteins in lysosomes	cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N	0.905
CTSL1	SLPI	ENSP00000345344	ENSP00000342082	cathepsin L1; Important for the overall degradation of proteins in lysosomes	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.590
CTSS	CTSL1	ENSP00000357981	ENSP00000345344	cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N	cathepsin L1; Important for the overall degradation of proteins in lysosomes	0.905
CTSS	SLPI	ENSP00000357981	ENSP00000342082	cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.717
ELANE	GRN	ENSP00000263621	ENSP00000053867	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	granulin	0.677
ELANE	PRSS3	ENSP00000263621	ENSP00000354280	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	protease, serine, 3; Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5	0.770
ELANE	SLPI	ENSP00000263621	ENSP00000342082	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.972
GRN	ELANE	ENSP00000053867	ENSP00000263621	granulin	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.677
GRN	SLPI	ENSP00000053867	ENSP00000342082	granulin	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.963
KLK3	SLPI	ENSP00000314151	ENSP00000342082	kallikrein-related peptidase 3; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.602
PLSCR1	SLPI	ENSP00000345494	ENSP00000342082	phospholipid scramblase 1; May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	0.620
PRSS3	ELANE	ENSP00000354280	ENSP00000263621	protease, serine, 3; Digestive protease specialized for the degradation of trypsin inhibitors. In the ileum, may be involved in defensin processing, including DEFA5	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.770
SLPI	CTSB	ENSP00000342082	ENSP00000342070	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	cathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis	0.702
SLPI	CTSL1	ENSP00000342082	ENSP00000345344	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	cathepsin L1; Important for the overall degradation of proteins in lysosomes	0.590
SLPI	CTSS	ENSP00000342082	ENSP00000357981	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	cathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N	0.717
SLPI	ELANE	ENSP00000342082	ENSP00000263621	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.972
SLPI	GRN	ENSP00000342082	ENSP00000053867	secretory leukocyte peptidase inhibitor; Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. May prevent elastase-mediated damage to oral and possibly other mucosal tissues	granulin	0.963

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