+ |
BCR |
phosphorylation
|
YWHAQ |
0.31 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250594 |
Ser232 |
LTLWTSDsAGEECDA |
in vitro |
|
pmid |
sentence |
16045749 |
We show here that BCR interacts with at least five isoforms of 14-3-3 in vivo and phosphorylates 14-3-3tau on Ser233 and to a lesser extent 14-3-3zeta on Thr233 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
BCR |
phosphorylation
|
YWHAZ |
0.336 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250595 |
Thr232 |
LTLWTSDtQGDEAEA |
in vitro |
|
pmid |
sentence |
16045749 |
We show here that BCR interacts with at least five isoforms of 14-3-3 in vivo and phosphorylates 14-3-3tau on Ser233 and to a lesser extent 14-3-3zeta on Thr233 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
BCR-ABL | down-regulates activity
phosphorylation
|
BCR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-40611 |
Tyr177 |
ADAEKPFyVNVEFHH |
Homo sapiens |
|
pmid |
sentence |
8622703 |
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrosine 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260829 |
Tyr328 |
YSPRSFEdCGGGYTP |
Homo sapiens |
|
pmid |
sentence |
9467953 |
Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr ± Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260828 |
Tyr360 |
YSPRSFEdCGGGYTP |
Homo sapiens |
|
pmid |
sentence |
9467953 |
Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr-Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262530 |
Tyr360 |
VSPSPTTyRMFRDKS |
Chlorocebus aethiops |
|
pmid |
sentence |
8622703 |
These results indicate that tyrosine phosphorylation of Bcr by Bcr-Abl inhibits Bcr’s serine/threonine kinase activity. |
|
Publications: |
4 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
+ |
FES | down-regulates activity
phosphorylation
|
BCR |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251136 |
Tyr177 |
ADAEKPFyVNVEFHH |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
8955135 |
Mutagenesis of BCR Tyr-177 to Phe completely abolished FES-induced BCR binding to the GRB2 SH2 domain, identifying Tyr-177 as an additional phosphorylation site for FES. Co-expression of BCR and FES in human 293T cells stimulated the tyrosine autophosphorylation of FES. By contrast, tyrosine phosphorylation of BCR by FES suppressed BCR serine/threonine kinase activity toward the 14-3-3 protein and BCR substrate, BAP-1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251137 |
Tyr246 |
SCGVDGDyEDAELNP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
8955135 |
In the present study, we demonstrate that BCR Tyr-246 and at least one of the closely spaced tyrosine residues, Tyr-279, Tyr-283, and Tyr-289 (3Y cluster), are phosphorylated by FES both in vitro and in 32Pi-labeled cells. Co-expression of BCR and FES in human 293T cells stimulated the tyrosine autophosphorylation of FES. By contrast, tyrosine phosphorylation of BCR by FES suppressed BCR serine/threonine kinase activity toward the 14-3-3 protein and BCR substrate, BAP-1. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
FES | down-regulates
phosphorylation
|
BCR |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45330 |
Tyr246 |
SCGVDGDyEDAELNP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45334 |
Tyr279 |
PPLEYQPyQSIYVGG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-45343 |
Tyr283 |
YQPYQSIyVGGMMEG |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
8955135 |
In the present study, we demonstrate that bcr tyr-246 and at least one of the closely spaced tyrosine residues, tyr-279, tyr-283, and tyr- 289 (3y cluster), are phosphorylated by fes both in vitro and in 32p(i)- labeled cells. tyrosine phosphorylation of bcr by fes suppressed bcr serine/threonine kinase activity toward the 14-3-3 protein and bcr substrate, bap-1. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
BCR-ABL | down-regulates
phosphorylation
|
BCR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-40615 |
Tyr283 |
YQPYQSIyVGGMMEG |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
8622703 |
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-40619 |
Tyr360 |
VSPSPTTyRMFRDKS |
Homo sapiens |
Leukemia Cell |
pmid |
sentence |
8622703 |
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
MYC | up-regulates quantity by expression
transcriptional regulation
|
BCR |
0.371 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272144 |
|
|
Homo sapiens |
K-562 Cell, LAMA-84 Cell |
pmid |
sentence |
26179066 |
In the present study we demonstrate that MYC and its partner MAX bind to the BCR promoter, leading to up-regulation of BCR and BCR/ABL1 at both transcriptional and protein levels.|Here we describe a regulatory pathway modulating BCR and BCR/ABL1 expression, showing that the BCR promoter is under the transcriptional control of the MYC/MAX heterodimer. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN1 | down-regulates
dephosphorylation
|
BCR |
0.335 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-56818 |
|
|
Homo sapiens |
|
pmid |
sentence |
9566916 |
These results illustrate selectivity in the effects of ptps in a cellular context and suggest that ptp1b may function as a specific, negative regulator of p210 bcr-abl signalling in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BCR | down-regulates activity
gtpase-activating protein
|
RAC1 |
0.583 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260526 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
32203420 |
We therefore developed a screening-compatible live-cell imaging assay, using FRET-based biosensors for the prototype GTPases RHOA, RAC1 and CDC4215,19,20 (Extended Data Fig. 2 and Supplementary Note 1)|We found catalytic activities for 45/75 RhoGEFs and 48/63 RhoGAPs| Our data thus not only reveal extensive promiscuity among regulators, but also that the inactivating RhoGAPs are less selective than the activating RhoGEFs (p-value=0.02)(Supplementary Table 2). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LNX1 | down-regulates quantity by destabilization
ubiquitination
|
BCR |
0.27 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272903 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22889411 |
We used the Ligand of Numb protein X (LNX) family of E3s, a group of PDZ domain-containing RING-type E3 ubiquitin ligases, to demonstrate the feasibility of this strategy. Many potential substrates of LNX E3s were identified. Eight of the nine selected candidates were ubiquitinated in vitro, and two novel endogenous substrates, PDZ-binding kinase (PBK) and breakpoint cluster region protein (BCR), were confirmed in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |