CTSS protein (Canis lupus familiaris) - STRING interaction network

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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 (By similarity). (339 aa)

Predicted Functional Partners:

CTSD

0.920

CD74

0.914

CTSB

0.910

CTSE

0.880

CTSH

0.852

TMPRSS2

0.842

BCL2

0.841

CTSZ

0.837

CTSA

0.834

FURIN

0.828

Your Current Organism:

Canis lupus familiaris

NCBI taxonomy Id: 9615
Other names: C. lupus familiaris, Canis canis, Canis domesticus, Canis familiaris, beagle dog, beagle dogs, dog, dogs

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
BCL2	CTSB	ENSCAFP00000000102	ENSCAFP00000059573	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	Cathepsin B; Belongs to the peptidase C1 family.	0.924
BCL2	CTSD	ENSCAFP00000000102	ENSCAFP00000014791	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	Cathepsin D; Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation; Belongs to the peptidase A1 family.	0.910
BCL2	CTSH	ENSCAFP00000000102	ENSCAFP00000031547	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	Cathepsin H; Belongs to the peptidase C1 family.	0.883
BCL2	CTSS	ENSCAFP00000000102	ENSCAFP00000017782	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	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 (By similarity).	0.841
BCL2	CTSZ	ENSCAFP00000000102	ENSCAFP00000047997	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	Cathepsin Z; Belongs to the peptidase C1 family.	0.887
CD74	CTSB	ENSCAFP00000045678	ENSCAFP00000059573	CD74 molecule.	Cathepsin B; Belongs to the peptidase C1 family.	0.931
CD74	CTSH	ENSCAFP00000045678	ENSCAFP00000031547	CD74 molecule.	Cathepsin H; Belongs to the peptidase C1 family.	0.421
CD74	CTSS	ENSCAFP00000045678	ENSCAFP00000017782	CD74 molecule.	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 (By similarity).	0.914
CD74	CTSZ	ENSCAFP00000045678	ENSCAFP00000047997	CD74 molecule.	Cathepsin Z; Belongs to the peptidase C1 family.	0.472
CTSA	CTSB	ENSCAFP00000014432	ENSCAFP00000059573	Carboxypeptidase; Belongs to the peptidase S10 family.	Cathepsin B; Belongs to the peptidase C1 family.	0.949
CTSA	CTSD	ENSCAFP00000014432	ENSCAFP00000014791	Carboxypeptidase; Belongs to the peptidase S10 family.	Cathepsin D; Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation; Belongs to the peptidase A1 family.	0.869
CTSA	CTSE	ENSCAFP00000014432	ENSCAFP00000014987	Carboxypeptidase; Belongs to the peptidase S10 family.	Cathepsin E; Belongs to the peptidase A1 family.	0.764
CTSA	CTSH	ENSCAFP00000014432	ENSCAFP00000031547	Carboxypeptidase; Belongs to the peptidase S10 family.	Cathepsin H; Belongs to the peptidase C1 family.	0.885
CTSA	CTSS	ENSCAFP00000014432	ENSCAFP00000017782	Carboxypeptidase; Belongs to the peptidase S10 family.	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 (By similarity).	0.834
CTSA	CTSZ	ENSCAFP00000014432	ENSCAFP00000047997	Carboxypeptidase; Belongs to the peptidase S10 family.	Cathepsin Z; Belongs to the peptidase C1 family.	0.915
CTSB	BCL2	ENSCAFP00000059573	ENSCAFP00000000102	Cathepsin B; Belongs to the peptidase C1 family.	Apoptosis regulator Bcl-2; Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (By similarity). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).	0.924
CTSB	CD74	ENSCAFP00000059573	ENSCAFP00000045678	Cathepsin B; Belongs to the peptidase C1 family.	CD74 molecule.	0.931
CTSB	CTSA	ENSCAFP00000059573	ENSCAFP00000014432	Cathepsin B; Belongs to the peptidase C1 family.	Carboxypeptidase; Belongs to the peptidase S10 family.	0.949
CTSB	CTSD	ENSCAFP00000059573	ENSCAFP00000014791	Cathepsin B; Belongs to the peptidase C1 family.	Cathepsin D; Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation; Belongs to the peptidase A1 family.	0.975
CTSB	CTSE	ENSCAFP00000059573	ENSCAFP00000014987	Cathepsin B; Belongs to the peptidase C1 family.	Cathepsin E; Belongs to the peptidase A1 family.	0.841

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