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  • 11.0 [archived version]
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F12 F12 ENSG00000244255 ENSG00000244255 F11 F11 CFD CFD PLG PLG F10 F10 F2 F2 CFI CFI CFB CFB CLU CLU C7 C7 ICE2 ICE2 C5 C5 C1S C1S CORIN CORIN C2 C2 HP HP IGLL5 IGLL5 PRTN3 PRTN3 ELANE ELANE MASP1 MASP1 C1R C1R PRSS53 PRSS53 C1RL C1RL GZMB GZMB GZMA GZMA
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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:
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)
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)
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)
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)
ICE2Little elongation complex subunit 2; Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III; Belongs to the ICE2 family (982 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)
CORINAtrial natriuretic peptide-converting enzyme; Serine-type endopeptidase involved in atrial natriuretic peptide hormone (NPPA) processing. Converts through proteolytic cleavage the non-functional propeptide NPPA into the active hormone, thereby regulating blood pressure in heart and promoting natriuresis, diuresis and vasodilation. Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Also acts as a regulator of sodium reabsorption in kidney. May also process pro-NPPB the B-type natriuretic peptid [...] (1042 aa)
GZMAGranzyme A; Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after ’Lys-31’ and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after ’Lys-189’, which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA; Belongs to the peptidase S1 family. Granzyme [...] (262 aa)
PRSS53Serine protease 53; In vitro can degrade the fibrinogen alpha chain of as well as pro-urokinase-type plasminogen activator; Serine proteases (553 aa)
MASP1Mannan binding lectin serine peptidase 1 (728 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)
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)
CLUClusterin; Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress- induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosom [...] (449 aa)
C7Complement component C7; Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C7 serves as a membrane anchor; Belongs to the complement C6/C7/C8/C9 family (843 aa)
CFDComplement factor D; Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway; Belongs to the peptidase S1 family (253 aa)
HPHaptoglobin; As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an Antimicrobial; Antioxidant, has antibacterial activity and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidely cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation [...] (406 aa)
F10Coagulation factor X; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Gla domain containing (488 aa)
CFIComplement factor I; Responsible for cleaving the alpha-chains of C4b and C3b in the presence of the cofactors C4-binding protein and factor H respectively; Belongs to the peptidase S1 family (583 aa)
F11Coagulation factor XI; Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX (625 aa)
C1SComplement C1s subcomponent; C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 (688 aa)
ENSG00000244255Complement factor B; Uncharacterized protein; cDNA FLJ55673, highly similar to Complement factor B ; Belongs to the peptidase S1 family (1266 aa)
CFBComplement factor B; Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments- Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B- lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes; Belongs to the peptidase S1 family (764 aa)
IGLL5Immunoglobulin lambda like polypeptide 5; C1-set domain containing (214 aa)
C1RComplement C1r subcomponent; C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system; Belongs to the peptidase S1 family (705 aa)
ELANENeutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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