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  • 11.0 [archived version]
STRINGSTRING
WDR37 WDR37 CTSS CTSS CTSH CTSH SERPINA11 SERPINA11 PRSS33 PRSS33 CELA3A CELA3A CTSB CTSB CTSF CTSF CTSL CTSL CTSV CTSV CTSW CTSW GRN GRN CTSO CTSO CTSG CTSG CTSZ CTSZ CTSK CTSK CTSC CTSC F12 F12 HPN HPN PRSS21 PRSS21 C2 C2 PROC PROC F9 F9 TMPRSS15 TMPRSS15 CMA1 CMA1 HABP2 HABP2
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)
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)
F9Coagulation factor IX; Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa; Belongs to the peptidase S1 family (461 aa)
CTSHPro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 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)
PROCVitamin K-dependent protein C; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function; Belongs to the peptidase S1 family (461 aa)
CMA1Chymase; Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion (247 aa)
F12Coagulation factor XII; Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta- factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (615 aa)
HPNSerine protease hepsin; Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization; Belongs to the peptidase S1 family (417 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)
HABP2Hyaluronan-binding protein 2; Cleaves the alpha-chain at multiple sites and the beta- chain between ’Lys-53’ and ’Lys-54’ but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro- urokinase) to the active two chain form. Activates coagulation factor VII. May function as a tumor suppressor negatively regulating cell proliferation and cell migration (560 aa)
TMPRSS15Enteropeptidase; Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases; Scavenger receptor cysteine rich domain containing (1019 aa)
CELA3AChymotrypsin-like elastase family member 3A; Efficient protease with alanine specificity but only little elastolytic activity (270 aa)
PRSS33Serine protease 33; Serine protease that has amidolytic activity, cleaving its substrates before Arg residues (280 aa)
C2Complement C2; Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments- C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase; Belongs to the peptidase S1 family (752 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)
SERPINA11Serpin peptidase inhibitors (422 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)
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)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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