| + |
C3 | up-regulates activity 
cleavage
|
C3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263483 |
Arg671 |
QPAARRRrSVQLTEK |
Homo sapiens |
|
| pmid |
sentence |
| 26806831 |
C3 autoactivates in a process known as “tick-over,” which is characterized by spontaneous hydrolysis of a reactive thiol-ester to generate C3(H2O). Although C3(H2O)Bb produces only relatively small amounts of C3b compared to the other C3 convertases, it nevertheless generates enough C3b to set the C3 convertase amplification loop in motion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263484 |
Arg748 |
ASHLGLArSNLDEDI |
Homo sapiens |
|
| pmid |
sentence |
| 26806831 |
C3 autoactivates in a process known as “tick-over,” which is characterized by spontaneous hydrolysis of a reactive thiol-ester to generate C3(H2O). Although C3(H2O)Bb produces only relatively small amounts of C3b compared to the other C3 convertases, it nevertheless generates enough C3b to set the C3 convertase amplification loop in motion. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood |
| Pathways: | Complement Signaling |
| + |
C3 convertase complex (C3bBb) | up-regulates activity
cleavage
|
C3 |
0.906 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263477 |
Arg671 |
QPAARRRrSVQLTEK |
Homo sapiens |
|
| pmid |
sentence |
| 26489954 |
In addition to the surface‐bound C3 convertase, a fluid‐phase convertase can be formed by association of water‐reacted C3, termed C3(H20), to FB thus constantly maintaining a low level of complement activation in solution (tick‐over). Both of the surface‐bound C3 convertases can bind a C3b molecule whereby the C5 convertases are formed. These cleave C5 into C5a and C5b, thus initiating the terminal pathway and leading to formation of the membrane attack complex (MAC). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263478 |
Arg748 |
ASHLGLArSNLDEDI |
Homo sapiens |
|
| pmid |
sentence |
| 26489954 |
In addition to the surface‐bound C3 convertase, a fluid‐phase convertase can be formed by association of water‐reacted C3, termed C3(H20), to FB thus constantly maintaining a low level of complement activation in solution (tick‐over). Both of the surface‐bound C3 convertases can bind a C3b molecule whereby the C5 convertases are formed. These cleave C5 into C5a and C5b, thus initiating the terminal pathway and leading to formation of the membrane attack complex (MAC). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood |
| + |
C3 convertase complex | up-regulates activity
cleavage
|
C3 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263449 |
Arg671 |
QPAARRRrSVQLTEK |
|
|
| pmid |
sentence |
| 31331124 |
This forms the C4b2a complex, which is a classical pathway C3 convertase. C4b2a cleaves C3, which is the central component of the complement cascade, to C3a, and anaphylatoxin, and C3b results in the activation of the lytic pathway |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263450 |
Arg748 |
ASHLGLArSNLDEDI |
|
|
| pmid |
sentence |
| 31331124 |
This forms the C4b2a complex, which is a classical pathway C3 convertase. C4b2a cleaves C3, which is the central component of the complement cascade, to C3a, and anaphylatoxin, and C3b results in the activation of the lytic pathway |
|
| Publications: |
2 |
| Pathways: | Complement Signaling |
| + |
CTSG | up-regulates activity
cleavage
|
C3 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256347 |
Arg748 |
ASHLGLArSNLDEDI |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 1861080 |
Plasma membrane elastase and cathepsin G from U937 cells cleave C3 into C3a- and C3b-like fragments; further incubation leads to C3c- and C3dg-like fragments, as judged from SDS-PAGE analysis of the digests. Sequencing of the C3b-like fragment purified by reverse phase chromatography indicates that initial cleavage of C3 by purified cathepsin G occurs at two positions in the amino-terminal part of the alpha-chain, at a Arg-Ser bond located between residues 748 and 749 and at a Leu-Asp bond between residues 751 and 752. These proteases are, thus, able to generate, on the U937 surface, active fragments of C3, which are likely to be involved in cell-protein and cell-cell interactions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256348 |
Leu751 |
LGLARSNlDEDIIAE |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 1861080 |
Plasma membrane elastase and cathepsin G from U937 cells cleave C3 into C3a- and C3b-like fragments; further incubation leads to C3c- and C3dg-like fragments, as judged from SDS-PAGE analysis of the digests. Sequencing of the C3b-like fragment purified by reverse phase chromatography indicates that initial cleavage of C3 by purified cathepsin G occurs at two positions in the amino-terminal part of the alpha-chain, at a Arg-Ser bond located between residues 748 and 749 and at a Leu-Asp bond between residues 751 and 752. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
C3 | up-regulates activity
binding
|
C3AR1 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263451 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8765043 |
A cDNA clone encoding the human C3a anaphylatoxin receptor (C3aR) was isolated from a pcDNAI/Amp expression library prepared from U-937 cells|The cDNA clone contained an insert of 4.3 kbp and was able to confer to transfected human HEK-293 cells the capacity to bind specifically iodinated human C3a. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Complement Signaling |
| + |
C3 | form complex 
binding
|
C5 convertase complex |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263448 |
|
|
|
|
| pmid |
sentence |
| 31331124 |
C3b associates with C3 convertase to form C5 convertase and cleaves C5. |
|
| Publications: |
1 |
| Pathways: | Complement Signaling |
| + |
C3 | form complex
binding
|
C3 convertase complex (C3bBb) |
0.906 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263485 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26489954 |
Surface‐associated C3b recruits FB, which leads to FB activation and the formation of C3bBb, the AP C3 convertase, which cleaves more C3 and amplifies complement activation. In addition to the surface‐bound C3 convertase, a fluid‐phase convertase can be formed by association of water‐reacted C3, termed C3(H20), to FB thus constantly maintaining a low level of complement activation in solution (tick‐over) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood |
| + |
CFHR1 | up-regulates activity
binding
|
C3 |
0.833 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263475 |
|
|
in vitro |
|
| pmid |
sentence |
| 27814381 |
Finally, we have been able to establish that CFHR1 can sterically inhibit the interaction that CFH/CFHL-1 SCR1-4 makes with C3b.|CFH regulates the alternative pathway of complement in both the fluid phase and on self-surfaces: It competes with complement factor B (CFB) for binding to C3b and C3(H2O) thereby blocking the formation of the pro-convertase complexes, C3bB and C3(H2O)B. It also accelerates the decay of any existing C3bBb or C3(H2O)Bb. |these data have allowed us to consolidate one possible model of CFHR1-mediated deregulation of CFH/CFHL-1 on an activating surface in which CFHR1 directly competes with or blocks both CFH-binding sites on C3b |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CEBPB | up-regulates quantity by expression
transcriptional regulation
|
C3 |
0.259 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261927 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 25617152 |
CCAAT/enhancer binding protein β directly regulates the expression of the complement component 3 gene in neural cells: implications for the pro-inflammatory effects of this transcription factor |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CFH | down-regulates activity 
binding
|
C3 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252141 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19050261 |
As a regulator of the alternative pathway, FH binds to C3b and inhibits the binding of factor B to C3b, acts as a cofactor for the factor I-mediated cleavage of C3b to iC3b (cofactor activity), and accelerates the decay of C3bBb, the alternative pathway C3 convertase (decay-accelerating activity) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
C3 | form complex
binding
|
C5 convertase complex (C3bBbC3b) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263480 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26489954 |
In addition to the surface‐bound C3 convertase, a fluid‐phase convertase can be formed by association of water‐reacted C3, termed C3(H20), to FB thus constantly maintaining a low level of complement activation in solution (tick‐over). Both of the surface‐bound C3 convertases can bind a C3b molecule whereby the C5 convertases are formed. These cleave C5 into C5a and C5b, thus initiating the terminal pathway and leading to formation of the membrane attack complex (MAC). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood |
| + |
CFI | down-regulates activity
cleavage
|
C3 |
0.878 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263489 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26806831 |
FH also serves as cofactor for the serine protease factor I (FI) that cleaves C3b into iC3b, unable to form C3 convertase (Fig 1B). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Blood |
| + |
CSMD1 | down-regulates quantity
binding
|
C3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265148 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28345259 |
CUB and sushi multiple domains 1 (CSMD1) is a relatively poorly studied large transmembrane protein of 390 kDa composed of 14 N-terminal CUB domains interspersed with complement control protein (CCP) domains followed by 15 consecutive CCP domains. The active domains of CSMD1 were then identified in CCP17-21, which were shown to interact with C4b and C3b and present these complement proteins for degradation by factor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
C3
- 
- 