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CTSF CTSF CTSV CTSV CTSO CTSO GRN GRN CTSZ CTSZ CTSK CTSK KLK1 KLK1 CTSG CTSG TMPRSS11E TMPRSS11E KLK2 KLK2 CTSD CTSD CTSC CTSC CTSL CTSL SERPINA4 SERPINA4 PDPK1 PDPK1 CTSB CTSB CTSH CTSH CTSW CTSW CTSS CTSS FKBP14 FKBP14 FN1 FN1 PRSS22 PRSS22 PRSS21 PRSS21 FDFT1 FDFT1 WDR37 WDR37 FBL FBL
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:
some 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 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:
PRSS21Testisin; Could regulate proteolytic events associated with testicular germ cell maturation; Serine proteases (314 aa)
GRNGranulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling (593 aa)
PRSS22Brain-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)
CTSGCathepsin G; Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe- CH2Cl and phenylmethylsulfonyl fluoride; Belongs to the peptidase S1 family (255 aa)
CTSZCathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa)
CTSHPro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa)
FBLrRNA 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)
FKBP14Peptidyl-prolyl cis-trans isomerase FKBP14; PPIases accelerate the folding of proteins during protein synthesis; EF-hand domain containing (211 aa)
CTSCDipeptidyl 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)
CTSDCathepsin 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. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease; Cathepsins (412 aa)
CTSKCathepsin K; Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation; Cathepsins (329 aa)
KLK1Kallikrein-1; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin; Belongs to the peptidase S1 family. Kallikrein subfamily (262 aa)
TMPRSS11ETransmembrane protease serine 11E; Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position (423 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; Cathepsins (484 aa)
CTSWCathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins (376 aa)
KLK2Kallikrein-2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin (261 aa)
PDPK13-phosphoinositide-dependent protein kinase 1; Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include- protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central rol [...] (556 aa)
CTSLCathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa)
CTSBCathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (339 aa)
FN1Fibronectin type III domain containing; Endogenous ligands (2477 aa)
WDR37WD repeat-containing protein 37; WD repeat domain containing (494 aa)
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 and cathepsin N; Cathepsins (331 aa)
CTSOCathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa)
CTSVCathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa)
SERPINA4Kallistatin; Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein; Belongs to the serpin family (427 aa)
FDFT1Squalene synthase; Farnesyl-diphosphate farnesyltransferase 1 (417 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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