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  • 11.0 [archived version]
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PPM1G PPM1G AMER1 AMER1 CMA1 CMA1 GZMK GZMK PRSS54 PRSS54 CPA6 CPA6 FBXO15 FBXO15 GZMB GZMB PRTN3 PRTN3 GZMH GZMH TPSG1 TPSG1 AZU1 AZU1 CTSG CTSG PRSS22 PRSS22 DICER1 DICER1 F12 F12 PRSS21 PRSS21 C1RL C1RL KLKB1 KLKB1 TPSD1 TPSD1 GZMM GZMM ACR ACR PLAT PLAT KLK12 KLK12 HPN HPN PPP6R1 PPP6R1
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.
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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
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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)
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)
GZMKGranzyme K; Belongs to the peptidase S1 family. Granzyme subfamily (264 aa)
AZU1Azurocidin; This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram- negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-nagative bacterium P.aeruginosa, this [...] (251 aa)
PRTN3Myeloblastin; Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration. May play a role in neutrophil transendothelial migration, probably when associated with CD177; Belongs to the peptidase S1 family. Elastase subfamily (256 aa)
TPSG1Tryptase gamma; Serine proteases (321 aa)
KLK12Kallikrein-12; Kallikrein related peptidase 12; Belongs to the peptidase S1 family. Kallikrein subfamily (254 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)
GZMMGranzyme M; Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha- tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (257 aa)
KLKB1Plasma kallikrein; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin; Belongs to the peptidase S1 family. Plasma kallikrein subfamily (638 aa)
C1RLComplement C1r subcomponent-like protein; Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum; Belongs to the peptidase S1 family (487 aa)
CPA6Carboxypeptidase A6; May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine; M14 carboxypeptidases (437 aa)
AMER1APC membrane recruitment protein 1; Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context- acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta- cate [...] (1135 aa)
PPM1GProtein phosphatase, Mg2+/Mn2+ dependent 1G; Belongs to the PP2C family (546 aa)
FBXO15F-box only protein 15; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex; F-boxes other (510 aa)
PPP6R1Serine/threonine-protein phosphatase 6 regulatory subunit 1; Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6- mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF-alpha (881 aa)
DICER1Endoribonuclease Dicer; Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3’ overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA- induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, a [...] (1922 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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