(21 nodes) Cysteine peptidase, histidine active site network (Mus musculus)

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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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query proteins and first shell of interactors

white nodes:
second shell of interactors

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proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

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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 to each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

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textmining

co-expression

protein homology

Your Input:
	Ctsk	Cathepsin K; Thiol protease involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen ; Belongs to the peptidase C1 family. (329 aa)
	Ctsm	Cathepsin M. (333 aa)
	Ctsl	Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. Belongs to the peptidase C1 family. (334 aa)
	Ctsf	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis. (462 aa)
	Tinagl1	Tubulointerstitial nephritis antigen-like; May be implicated in the adrenocortical zonation and in mechanisms for repressing the CYP11B1 gene expression in adrenocortical cells. This is a non catalytic peptidase C1 family protein. (466 aa)
	4930486L24Rik	Testin-1; Belongs to the peptidase C1 family. (333 aa)
	Ctsj	Cathepsin J; Belongs to the peptidase C1 family. (333 aa)
	Cts3	Cts3 protein; Belongs to the peptidase C1 family. (332 aa)
	Ctsll3	Cathepsin L-like 3; Belongs to the peptidase C1 family. (331 aa)
	Ctsh	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family. (333 aa)
	Ctsc	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family. (462 aa)
	Ctso	Cathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover. (312 aa)
	BC051665	cDNA sequence BC051665; Belongs to the peptidase C1 family. (330 aa)
	Ctsw	Cathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Belongs to the peptidase C1 family. (371 aa)
	Cts7	Cathepsin 7; Involved in trophoblast cell proliferation and differentiation probably by affecting mitotic cell cycle progression. Proteolytic activity and nuclear localization are essential for its role in cell cycle progression; Belongs to the peptidase C1 family. (331 aa)
	Cts8	Cathepsin 8; Probable protease (By similarity). In placenta, plays a role in promoting giant cell differentiation. Also plays a role in placental spiral artery remodeling by direct degradation of smooth muscle alpha-actin. Belongs to the peptidase C1 family. (333 aa)
	Cts6	Cathepsin-6; Belongs to the peptidase C1 family. (334 aa)
	Ctsr	Cathepsin R. (334 aa)
	Ctsq	Cathepsin Q; Belongs to the peptidase C1 family. (343 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; Belongs to the peptidase C1 family. (341 aa)
	Ctsb	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family. (339 aa)

Your Current Organism:

Mus musculus

NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Cts3	Ctsm	ENSMUSP00000058359	ENSMUSP00000153101	Cts3 protein; Belongs to the peptidase C1 family.	Cathepsin M.	0.680
Ctsb	Ctsc	ENSMUSP00000006235	ENSMUSP00000032779	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	0.404
Ctsb	Ctsf	ENSMUSP00000006235	ENSMUSP00000112481	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.	0.620
Ctsb	Ctsh	ENSMUSP00000006235	ENSMUSP00000034915	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family.	0.520
Ctsb	Ctsk	ENSMUSP00000006235	ENSMUSP00000015664	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	Cathepsin K; Thiol protease involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen ; Belongs to the peptidase C1 family.	0.676
Ctsb	Ctsl	ENSMUSP00000006235	ENSMUSP00000152169	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	Cathepsin L1 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. Belongs to the peptidase C1 family.	0.969
Ctsb	Ctss	ENSMUSP00000006235	ENSMUSP00000015667	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 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; Belongs to the peptidase C1 family.	0.953
Ctsc	Ctsb	ENSMUSP00000032779	ENSMUSP00000006235	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	0.404
Ctsc	Ctsf	ENSMUSP00000032779	ENSMUSP00000112481	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.	0.545
Ctsc	Ctsh	ENSMUSP00000032779	ENSMUSP00000034915	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family.	0.463
Ctsc	Ctss	ENSMUSP00000032779	ENSMUSP00000015667	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 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; Belongs to the peptidase C1 family.	0.503
Ctsf	Ctsb	ENSMUSP00000112481	ENSMUSP00000006235	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	0.620
Ctsf	Ctsc	ENSMUSP00000112481	ENSMUSP00000032779	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	0.545
Ctsf	Ctsk	ENSMUSP00000112481	ENSMUSP00000015664	Cathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis.	Cathepsin K; Thiol protease involved in osteoclastic bone resorption. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation (By similarity). Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen ; Belongs to the peptidase C1 family.	0.486
Ctsf	Ctsl	ENSMUSP00000112481	ENSMUSP00000152169	Cathepsin F; 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 heavy chain; Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen. Belongs to the peptidase C1 family.	0.568
Ctsh	Ctsb	ENSMUSP00000034915	ENSMUSP00000006235	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family.	Cathepsin B heavy chain; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity). Belongs to the peptidase C1 family.	0.520
Ctsh	Ctsc	ENSMUSP00000034915	ENSMUSP00000032779	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family.	Dipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase. Can degrade glucagon. Plays a role in the generation of cytotoxic lymphocyte effector function; Belongs to the peptidase C1 family.	0.463
Ctsh	Ctss	ENSMUSP00000034915	ENSMUSP00000015667	Cathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 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; Belongs to the peptidase C1 family.	0.402
Ctsj	Ctsq	ENSMUSP00000071457	ENSMUSP00000021888	Cathepsin J; Belongs to the peptidase C1 family.	Cathepsin Q; Belongs to the peptidase C1 family.	0.411
Ctsj	Ctsr	ENSMUSP00000071457	ENSMUSP00000021889	Cathepsin J; Belongs to the peptidase C1 family.	Cathepsin R.	0.812