17 items (human) - STRING interaction network

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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query proteins and first shell of interactors

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second shell of interactors

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proteins of unknown 3D structure

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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.

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Your Input:
	GRN	Granulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling (593 aa)
	PRSS22	Brain-specific serine protease 4; Preferentially cleaves the synthetic substrate H-D-Leu- Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA; Serine proteases (317 aa)
	CTSZ	Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa)
	CTSH	Pro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa)
	FBL	rRNA 2’-O-methyltransferase fibrillarin; S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2’-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of ’Gln-105’ of histone H2A (H2AQ104me), a modification [...] (321 aa)
	CTSC	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII (463 aa)
	TMPRSS11E	Transmembrane protease serine 11E; Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (423 aa)
	KLK2	Kallikrein-2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin (261 aa)
	KLK3	Prostate-specific antigen; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum; Kallikreins (261 aa)
	MPI	Mannose-6-phosphate isomerase; Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions; Belongs to the mannose-6-phosphate isomerase type 1 family (423 aa)
	CTSL	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa)
	DNAJC1	DnaJ homolog subfamily C member 1; May modulate protein synthesis; DNAJ heat shock proteins (554 aa)
	GIG25	Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors (423 aa)
	CTSV	Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa)
	AACT	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors (423 aa)
	ELANE	Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa)
	KLK13	Kallikrein-13; Kallikrein related peptidase 13; Kallikreins (277 aa)

Your Current Organism:

Homo sapiens

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

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a tab-delimited file describing the names, domains and annotated functions of the network proteins

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AACT	CTSL	ENSP00000450540	ENSP00000345344	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	0.426
AACT	DNAJC1	ENSP00000450540	ENSP00000366179	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	DnaJ homolog subfamily C member 1; May modulate protein synthesis; DNAJ heat shock proteins	0.940
AACT	ELANE	ENSP00000450540	ENSP00000466090	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.515
AACT	GIG25	ENSP00000450540	ENSP00000376793	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	0.802
AACT	KLK2	ENSP00000450540	ENSP00000313581	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	Kallikrein-2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin	0.498
AACT	KLK3	ENSP00000450540	ENSP00000314151	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	Prostate-specific antigen; Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum; Kallikreins	0.851
CTSC	CTSL	ENSP00000227266	ENSP00000345344	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	0.518
CTSC	CTSZ	ENSP00000227266	ENSP00000217131	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins	0.929
CTSC	ELANE	ENSP00000227266	ENSP00000466090	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.951
CTSC	GRN	ENSP00000227266	ENSP00000053867	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	Granulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling	0.923
CTSH	CTSL	ENSP00000220166	ENSP00000345344	Pro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	0.620
CTSL	AACT	ENSP00000345344	ENSP00000450540	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Alpha-1-antichymotrypsin; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	0.426
CTSL	CTSC	ENSP00000345344	ENSP00000227266	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	0.518
CTSL	CTSH	ENSP00000345344	ENSP00000220166	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Pro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family	0.620
CTSL	CTSV	ENSP00000345344	ENSP00000445052	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family	0.703
CTSL	CTSZ	ENSP00000345344	ENSP00000217131	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins	0.446
CTSL	ELANE	ENSP00000345344	ENSP00000466090	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Neutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis	0.443
CTSL	GIG25	ENSP00000345344	ENSP00000376793	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 3; Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2; Serpin peptidase inhibitors	0.411
CTSV	CTSL	ENSP00000445052	ENSP00000345344	Cathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family	Cathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins	0.703
CTSZ	CTSC	ENSP00000217131	ENSP00000227266	Cathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins	Dipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII	0.929

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