| + |
BLK | down-regulates activity 
phosphorylation
|
CGAS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275844 |
Tyr215 |
LLNTGSYyEHVKISA |
|
|
| pmid |
sentence |
| 30356214 |
DNA damage induces nuclear translocation of cGAS in a manner that is dependent on importin-α, and the phosphorylation of cGAS at tyrosine 215-mediated by B-lymphoid tyrosine kinase-facilitates the cytosolic retention of cGAS. |
|
| Publications: |
1 |
| + |
BLK | up-regulates activity 
phosphorylation
|
FCGR2A |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249311 |
Tyr288 |
YETADGGyMTLNPRA |
in vitro |
|
| pmid |
sentence |
| 8756631 |
To identify the FcgammaRII-phosphorylating protein tyrosine kinase (PTK), we used the combination of an in vitro and an in vivo approach. In an in vitro assay using recombinant cytoplasmic tails of the different FcgammaRII isoforms as well as tyrosine exchange mutants, we show that each of the BCR-associated PTKs (Lyn, Blk, Fyn, and Syk) shows different phosphorylation patterns with regard to the different FcgammaR isoforms and point|Fyn and Blk definitely phosphorylate Y-282 in the ITAM of Fc_RIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addi-tion to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249312 |
Tyr304 |
TDDDKNIyLTLPPND |
in vitro |
|
| pmid |
sentence |
| 8756631 |
To identify the FcgammaRII-phosphorylating protein tyrosine kinase (PTK), we used the combination of an in vitro and an in vivo approach. In an in vitro assay using recombinant cytoplasmic tails of the different FcgammaRII isoforms as well as tyrosine exchange mutants, we show that each of the BCR-associated PTKs (Lyn, Blk, Fyn, and Syk) shows different phosphorylation patterns with regard to the different FcgammaR isoforms and point|Fyn and Blk definitely phosphorylate Y-282 in the ITAM of Fc_RIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addi-tion to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
BLK | up-regulates activity
phosphorylation
|
FCGR2C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262672 |
Tyr294 |
YETADGGyMTLNPRA |
in vitro |
|
| pmid |
sentence |
| 8756631 |
Fyn and Blk definitely phosphorylate Y-282 in the ITAM of FcgRIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addition to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262673 |
Tyr310 |
TDDDKNIyLTLPPND |
in vitro |
|
| pmid |
sentence |
| 8756631 |
Fyn and Blk definitely phosphorylate Y-282 in the ITAM of FcgRIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addition to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
BLK | up-regulates activity
phosphorylation
|
BCR-Dl |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268217 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BLK | up-regulates activity
phosphorylation
|
BCR-Mk |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268208 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BLK | up-regulates activity
phosphorylation
|
BCR-Dk |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268214 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BLK | up-regulates activity
phosphorylation
|
BCR-Ml |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268211 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
3.0
BLK
- 
- 