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  • 11.0 [archived version]
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KLK13 KLK13 KLK9 KLK9 CTSG CTSG PRSS54 PRSS54 PZP PZP A2M A2M ACR ACR FN1 FN1 GZMB GZMB PLG PLG TPSD1 TPSD1 PLAT PLAT GZMH GZMH CELA3A CELA3A CPB2 CPB2 PRSS21 PRSS21 F2 F2 CTRC CTRC CELA2B CELA2B PRSS22 PRSS22 C5 C5 CELA3B CELA3B KLK12 KLK12 PRSS45 PRSS45 TMPRSS9 TMPRSS9 CELA2A CELA2A
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)
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)
CPB2Carboxypeptidase B2; Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down- regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin; Belongs to the peptidase M14 family (423 aa)
TPSD1Tryptase delta; Tryptase is the major neutral protease present in mast cells and is secreted upon the coupled activation-degranulation response of this cell type; Belongs to the peptidase S1 family. Tryptase subfamily (242 aa)
ACRAcrosin; Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome; Belongs to the peptidase S1 family (421 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)
GZMHGranzyme H; Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3’ and P4’ sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication (246 aa)
GZMBGranzyme B; This enzyme is necessary for target cell lysis in cell- mediated immune responses. It cleaves after Asp. Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -7, -9 and 10 to give rise to active enzymes mediating apoptosis; Belongs to the peptidase S1 family. Granzyme subfamily (247 aa)
PRSS54Serine protease 54 (395 aa)
PLATTissue-type plasminogen activator; Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. Plays a direct role in facilitating neuronal migration (562 aa)
C5Complement C5; Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled; C3 and PZP like, alpha-2-macroglobulin domain containing (1676 aa)
KLK12Kallikrein-12; Kallikrein related peptidase 12; Belongs to the peptidase S1 family. Kallikrein subfamily (254 aa)
PZPPregnancy zone protein; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the c [...] (1482 aa)
CELA3AChymotrypsin-like elastase family member 3A; Efficient protease with alanine specificity but only little elastolytic activity (270 aa)
F2Prothrombin; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family (622 aa)
PLGPlasminogen; Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated b [...] (810 aa)
A2MAlpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...] (1474 aa)
TMPRSS9Transmembrane protease serine 9; Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln- Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala- Pro-Ala-AMC are not significantly hydrolyzed; Belongs to the peptidase S1 family (1059 aa)
CELA3BChymotrypsin-like elastase family member 3B; Efficient protease with alanine specificity but only little elastolytic activity (270 aa)
FN1Fibronectin type III domain containing; Endogenous ligands (2477 aa)
CELA2AChymotrypsin-like elastase family member 2A; Acts upon elastin (269 aa)
CELA2BChymotrypsin-like elastase family member 2B; Acts upon elastin; Belongs to the peptidase S1 family. Elastase subfamily (269 aa)
CTRCChymotrypsin-C; Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity (268 aa)
PRSS45Uncharacterized protein; Serine protease 45 (228 aa)
KLK9Kallikrein-9; Kallikrein related peptidase 9; Kallikreins (250 aa)
KLK13Kallikrein-13; Kallikrein related peptidase 13; Kallikreins (277 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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