| + |
LYN | up-regulates activity 
phosphorylation
|
CD79B |
0.665 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251398 |
Tyr196 |
GMEEDHTyEGLDIDQ |
in vitro |
|
| pmid |
sentence |
| 9531288 |
Y182 of CD79a appears to be the initial and preferred site of Ag receptor phosphorylation by Src family kinases. In vitro, Src family Lyn and Fyn predominantly phosphorylate this residue in CD79a, and Y195 does so in CD79b |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
FYN | up-regulates activity
phosphorylation
|
CD79B |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251154 |
Tyr196 |
GMEEDHTyEGLDIDQ |
in vitro |
|
| pmid |
sentence |
| 9531288 |
CD79b cytoplasmic tail-containing GST fusion proteins were phosphorylated in vitro by baculovirus-produced Fyn, >80% of phosphorylation occurred on the N-terminal ITAM tyrosine. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). pY195 and pY206 in CD79b |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251155 |
Tyr207 |
DIDQTATyEDIVTLR |
in vitro |
|
| pmid |
sentence |
| 9531288 |
CD79b cytoplasmic tail-containing GST fusion proteins were phosphorylated in vitro by baculovirus-produced Fyn, >80% of phosphorylation occurred on the N-terminal ITAM tyrosine. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). pY195 and pY206 in CD79b |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
CD79B | form complex 
binding
|
BCR-Ml |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268193 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
BCR consists of a pair of identical immunoglob- ulin heavy (IgH) and light (IgL) chains. though membrane BCR per se is not able to transduce downstream signaling, it does so by making BCR complex with CD79. The extracellular portion of the BCR is non-covalently coupled to a disulfide-linked heterodimer of the CD79A and CD79B. This association allows expression of BCR on the plasma membrane and BCR internalization after antigen recognition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
CD79B | form complex
binding
|
BCR-Mk |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268189 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
BCR consists of a pair of identical immunoglob- ulin heavy (IgH) and light (IgL) chains. though membrane BCR per se is not able to transduce downstream signaling, it does so by making BCR complex with CD79. The extracellular portion of the BCR is non-covalently coupled to a disulfide-linked heterodimer of the CD79A and CD79B. This association allows expression of BCR on the plasma membrane and BCR internalization after antigen recognition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SH2B1 | down-regulates activity 
dephosphorylation
|
CD79B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268458 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
SHP-1 is recruited by the phosphorylated ITIM-bearing receptors such as CD22 and it dephosphorylates proximal BCR signaling molecules such as CD79, SYK, BLNK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
CD79B | form complex
binding
|
BCR-Dl |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268201 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
BCR consists of a pair of identical immunoglob- ulin heavy (IgH) and light (IgL) chains. though membrane BCR per se is not able to transduce downstream signaling, it does so by making BCR complex with CD79. The extracellular portion of the BCR is non-covalently coupled to a disulfide-linked heterodimer of the CD79A and CD79B. This association allows expression of BCR on the plasma membrane and BCR internalization after antigen recognition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
CD79B | up-regulates 
|
TP53 |
0.314 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-93526 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 12324477 |
Bcr ligation resulted in p53 activation including its phosphorylation at ser15 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CD79B | form complex
binding
|
BCR-Dk |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268197 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
BCR consists of a pair of identical immunoglob- ulin heavy (IgH) and light (IgL) chains. though membrane BCR per se is not able to transduce downstream signaling, it does so by making BCR complex with CD79. The extracellular portion of the BCR is non-covalently coupled to a disulfide-linked heterodimer of the CD79A and CD79B. This association allows expression of BCR on the plasma membrane and BCR internalization after antigen recognition. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
3.0
CD79B
- 
- 