| + |
MASP2 | up-regulates activity 
cleavage
|
C2 |
0.434 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263416 |
Arg243 |
KTKESLGrKIQIQRS |
Homo sapiens |
Plasma Cell |
| pmid |
sentence |
| 11907111 |
The MASPs in the preparations had proteolytic activities against C4, C2, and C3 in the fluid phase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263419 |
Ser20 |
LYPGLADsAPSCPQN |
Homo sapiens |
Plasma Cell |
| pmid |
sentence |
| 11907111 |
The MASPs in the preparations had proteolytic activities against C4, C2, and C3 in the fluid phase |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Complement Signaling |
| + |
MASP2 | up-regulates activity
cleavage
|
C4B |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263422 |
Arg679 |
EKTTRKKrNVNFQKA |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263425 |
Arg756 |
KGQAGLQrALEILQE |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263428 |
Gly1446 |
TPLQLFEgRRNRRRR |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
MASP2 | up-regulates activity
cleavage
|
C4A |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263431 |
Arg679 |
EKTTRKKrNVNFQKA |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263434 |
Arg756 |
KGQAGLQrALEILQE |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263437 |
Gly1446 |
TPLQLFEgRRNRRRR |
in vitro |
|
| pmid |
sentence |
| 17204478 |
MASP-2 cleaves C4 releasing C4a and generating C4b, which attaches covalently to the pathogen surface upon exposure of its reactive thioester. C2 binds to C4b and is also cleaved by MASP-2 to form the C3 convertase (C4b2a). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| Pathways: | Complement Signaling |
| + |
FCN2 | up-regulates activity
binding
|
MASP2 |
0.613 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263413 |
|
|
|
|
| pmid |
sentence |
| 17204478 |
In the lectin pathway, mannose-binding lectin (MBL) and ficolins bind to pathogens and activate MBL-associated serine protease-2 (MASP-2) |
|
| Publications: |
1 |
| + |
MBL2 | up-regulates activity
binding
|
MASP2 |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263415 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9087411 |
The results (Fig. 3A) show that the anti-MBL antibody, in addition to binding MBL captures both MASP-1 and MASP-2|Our results emphasize the similarity between complement activation through the MBL, or 'MBLectin' pathway of the innate immune system and the classical pathway of complement activation (Fig. 5). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Complement Signaling |
| + |
FCN3 | up-regulates activity
binding
|
MASP2 |
0.523 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263412 |
|
|
|
|
| pmid |
sentence |
| 17204478 |
In the lectin pathway, mannose-binding lectin (MBL) and ficolins bind to pathogens and activate MBL-associated serine protease-2 (MASP-2) |
|
| Publications: |
1 |
| + |
MASP2 | form complex 
binding
|
Ficolin lectin-protease complex |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281090 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16116205 |
M-ficolin was localized in secretory granules in the cytoplasm of neutrophils, monocytes, and type II alveolar epithelial cells in lung. M-ficolin precipitated with mannose-binding lectin-associated serine proteases (MASP)-1 and MASP-2 in a co-immunoprecipitation assay, indicating that M-ficolin forms complexes with MASP-1 and MASP-2. M-ficolin-MASP complexes activated complement on N-acetylglucosamine (GlcNAc)-coated microplates in a C4 deposition assay. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
MASP2
- 
- 