STRINGSTRING
Ctss Ctss Ctsl Ctsl Capn15 Capn15 Capn11 Capn11 Ctsf Ctsf Capn13 Capn13 Capn9 Capn9 Ctsj Ctsj Capn12 Capn12 Capn2 Capn2 Capn5 Capn5 Capn8 Capn8 Ctsll3 Ctsll3 Ctsh Ctsh Ctsc Ctsc Ctso Ctso Capn3 Capn3 Capn10 Capn10 BC051665 BC051665 Capn1 Capn1 Cts7 Cts7 Blmh Blmh Ctsk Ctsk Ctsb Ctsb
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.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
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
Others
textmining
co-expression
protein homology
Your Input:
CtssCathepsin 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)
CtslCathepsin 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)
Capn15Calpain-15; Belongs to the peptidase C2 family. (1196 aa)
Capn11Calpain-11; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction; Belongs to the peptidase C2 family. (714 aa)
CtsfCathepsin 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)
Capn13Calpain-13; Probable non-lysosomal thiol-protease. (665 aa)
Capn9Calpain-9; Calcium-regulated non-lysosomal thiol-protease. (690 aa)
CtsjCathepsin J; Belongs to the peptidase C1 family. (333 aa)
Capn12Calpain-12; Calcium-regulated non-lysosomal thiol-protease. (720 aa)
Capn2Calpain-2 catalytic subunit; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs. (700 aa)
Capn5Calpain-5; Calcium-regulated non-lysosomal thiol-protease. (640 aa)
Capn8Calpain-8; Calcium-regulated non-lysosomal thiol-protease (By similarity). Involved in membrane trafficking in the gastric surface mucus cells (pit cells) and may involve the membrane trafficking of mucus cells via interactions with coat protein. Proteolytically cleaves the beta-subunit of coatomer complex. (703 aa)
Ctsll3Cathepsin L-like 3; Belongs to the peptidase C1 family. (331 aa)
CtshCathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family. (333 aa)
CtscDipeptidyl 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)
CtsoCathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover. (312 aa)
Capn3Calpain-3; Calcium-regulated non-lysosomal thiol-protease; Belongs to the peptidase C2 family. (821 aa)
Capn10Calpain-10; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. May play a role in insulin- stimulated glucose uptake (By similarity). (666 aa)
BC051665cDNA sequence BC051665; Belongs to the peptidase C1 family. (330 aa)
Capn1Calpain-1 catalytic subunit; Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. (713 aa)
Cts7Cathepsin 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)
BlmhBleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity; Belongs to the peptidase C1 family. (455 aa)
CtskCathepsin 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)
CtsbCathepsin 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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