| + |
PKN3 |
phosphorylation
|
BCAR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264574 |
Ser428 |
PAEGKRLsASSTGST |
in vitro |
|
| pmid |
sentence |
| 30422386 |
These results verified the presence of a PKN3 phosphorylation motif in the sequence surrounding Ser432 and indicated that PKN3 phosphorylates p130Cas on Ser432 in vitro.|Human Ser428 of p130Cas corresponds to mouse p130Cas Ser432| |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
SRC | up-regulates activity 
phosphorylation
|
BCAR1 |
0.797 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246381 |
Tyr115 |
QPQPDSVyLVPTPSK |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197927 |
Tyr128 |
SKAQQGLyQVPGPSP |
Homo sapiens |
|
| pmid |
sentence |
| 22710723 |
Furthermore, we demonstrate that src phosphorylates p130cas y128. We engineered crc cells homozygous for a p130cas y128f knock-in mutant and found that these cells exhibit significantly reduced migration and colony formation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246385 |
Tyr165 |
PSPATDLyQVPPGPG |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246389 |
Tyr179 |
GGPAQDIyQVPPSAG |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246393 |
Tyr192 |
AGMGHDIyQVPPSMD |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246397 |
Tyr234 |
AQPEQDEyDIPRHLL |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100363 |
Tyr249 |
APGPQDIyDVPPVRG |
Homo sapiens |
|
| pmid |
sentence |
| 12972425 |
We tested synthetic peptides modeled on cas phosphorylation sites, and found that the sequence containing tyrosine 253 was phosphorylated by src most efficiently. Using cells derived from cas-deficient mice, we confirmed that cas greatly enhanced the ability of src to transform cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246401 |
Tyr267 |
SQYGQEVyDTPPMAV |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246405 |
Tyr287 |
RDPLLEVyDVPPSVE |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246409 |
Tyr362 |
SPPAEDVyDVPPPAP |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246413 |
Tyr387 |
RPGPGTLyDVPRERV |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246417 |
Tyr653 |
QDSPDGQyENSEGGW |
Mus musculus |
|
| pmid |
sentence |
| 12972425 |
Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111056 |
Tyr664 |
EGGWMEDyDYVHLQG |
Homo sapiens |
|
| pmid |
sentence |
| 11604500 |
The loss of activity in the cas-f668/f670 mutant is consistent with the notion that src, once initially bound by its sh3 domain, phosphorylates the tyr668/670 site to further stabilize its interaction by sh2 binding. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111060 |
Tyr666 |
GWMEDYDyVHLQGKE |
Homo sapiens |
|
| pmid |
sentence |
| 11604500 |
The loss of activity in the cas-f668/f670 mutant is consistent with the notion that src, once initially bound by its sh3 domain, phosphorylates the tyr668/670 site to further stabilize its interaction by sh2 binding. |
|
| Publications: |
14 |
Organism: |
Mus Musculus, Homo Sapiens |
| + |
PTPN14 | down-regulates 
dephosphorylation
|
BCAR1 |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197923 |
Tyr128 |
SKAQQGLyQVPGPSP |
Homo sapiens |
Colonic Cancer Cell |
| pmid |
sentence |
| 22710723 |
We show that p130 crk-associated substrate (p130cas) is a direct substrate of ptpn14 and that ptpn14 specifically regulates p130cas phosphorylation at tyrosine residue 128 (y128) in colorectal cancer (crc) cells. We engineered crc cells homozygous for a p130cas y128f knock-in mutant and found that these cells exhibit significantly reduced migration and colony formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGFR1 | up-regulates
phosphorylation
|
BCAR1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82760 |
Tyr128 |
SKAQQGLyQVPGPSP |
Homo sapiens |
|
| pmid |
sentence |
| 11019781 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98488 |
Tyr128 |
SKAQQGLyQVPGPSP |
Homo sapiens |
|
| pmid |
sentence |
| 12601080 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98492 |
Tyr249 |
APGPQDIyDVPPVRG |
Homo sapiens |
|
| pmid |
sentence |
| 12601080 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98496 |
Tyr306 |
PSNHHAVyDVPPSVS |
Homo sapiens |
|
| pmid |
sentence |
| 12601080 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98500 |
Tyr327 |
PLLREETyDVPPAFA |
Homo sapiens |
|
| pmid |
sentence |
| 12601080 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98569 |
Tyr410 |
GVVDSGVyAVPPPAE |
Homo sapiens |
|
| pmid |
sentence |
| 12601080 |
Five tyrosine phosphorylation sites were identified in p130cas on tyr-128, tyr-249, tyr-306, tyr-327, and tyr-410. These tyrosine residues are all located in the substrate domain of p130cas that mediates binding to the sh2 domain of the adaptor molecule crk. Fgf-1-transduced fibroblasts demonstrated a > 10-fold increase in migration, an observation correlated with increased tyrosine phosphorylation of p125fak and p130cas. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
BCAR1 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177238 |
Tyr165 |
PSPATDLyQVPPGPG |
Homo sapiens |
|
| pmid |
sentence |
| 22084245 |
Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 crk-associated substrate. Tyrosine residues 165 and 664 of p130cas were both phosphorylated by ptk6 in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2 |
phosphorylation
|
BCAR1 |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249111 |
Tyr664 |
EGGWMEDyDYVHLQG |
|
|
| pmid |
sentence |
| 11604500 |
FAK phosphorylates CAS-SBD tyrosines 668 and/or 670, driving an SH2-mediated recruitment of Src which then phosphorylates CAS-SD. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249112 |
Tyr666 |
GWMEDYDyVHLQGKE |
|
|
| pmid |
sentence |
| 11604500 |
FAK phosphorylates CAS-SBD tyrosines 668 and/or 670, driving an SH2-mediated recruitment of Src which then phosphorylates CAS-SD. |
|
| Publications: |
2 |
| + |
PTK6 | up-regulates
phosphorylation
|
BCAR1 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177242 |
Tyr664 |
EGGWMEDyDYVHLQG |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 22084245 |
Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 crk-associated substrate. Tyrosine residues 165 and 664 of p130cas were both phosphorylated by ptk6 in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
BCAR1 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109032 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 11432829 |
Ptp-pest is an efficient negative regulator of lymphocyte activation. This function correlated with the ability of ptp-pest to induce dephosphorylation of shc, pyk2, fak and cas, and inactivate the ras pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCAR1 | down-regulates
binding
|
SMAD3 |
0.283 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161265 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18321991 |
In this study, we show that, after tyrosine phosphorylation of p130cas mediated by integrin signaling, the phosphorylated p130cas is able to interact with phosphorylated smad3 and in turn prevent transcriptional activation by smad3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PXN | up-regulates activity 
|
BCAR1 |
0.917 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263979 |
|
|
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
Together, our data suggest that phosphorylation of paxillin Y88 activates AKT through the paxillin-p130Cas-p85/PI3K-AKT signaling axis and promotes colorectal tumorigenesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCAR1 | up-regulates activity
binding
|
PKN3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264573 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 30422386 |
Taken together, the data suggest that p130Cas expression induces PKN3 activation and this activation is independent of p130Cas–PKN3 interaction. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BCAR1 | up-regulates quantity by expression
transcriptional regulation
|
NAB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253891 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22431919 |
In MCF-7 cells, we identified a positive feedback loop where p130(Cas) positively regulates EGR1 and NAB2, which in turn induce p130(Cas) expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGR1 | up-regulates quantity by expression
transcriptional regulation
|
BCAR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253890 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22431919 |
Overexpression or short interfering RNA (siRNA)-mediated down-regulation of EGR1 or NAB2, and chromatin immunoprecipitations indicated that EGR1 and NAB2 act in concert to positively regulate p130(Cas)/BCAR1 expression in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCAR1 | up-regulates quantity by expression
transcriptional regulation
|
EGR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253892 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22431919 |
In MCF-7 cells, we identified a positive feedback loop where p130(Cas) positively regulates EGR1 and NAB2, which in turn induce p130(Cas) expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCAR1 | up-regulates activity
binding
|
PIK3R1 |
0.538 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263980 |
|
|
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
One such SH2-domain containing protein is the p85 subunit of PI3K, as its docking with tyrosine-phosphorylated p130cas activates the p110alpha subunit| tyrosine-165 and tyrosine-128 on p130cas both are phosphorylated to a greater extent in parental versus paxillin Y88F mutan |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NAB2 | up-regulates quantity by expression
transcriptional regulation
|
BCAR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253889 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22431919 |
Overexpression or short interfering RNA (siRNA)-mediated down-regulation of EGR1 or NAB2, and chromatin immunoprecipitations indicated that EGR1 and NAB2 act in concert to positively regulate p130(Cas)/BCAR1 expression in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BCAR1
- 
- 