+ |
MAPK3 | up-regulates activity
phosphorylation
|
GAB1 |
0.618 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249459 |
Ser381 |
CIPTAGMsPSRSNTI |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249460 |
Ser454 |
YVPMNPNsPPRQHSS |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249461 |
Ser551 |
ELQAPVRsPITRSFA |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249462 |
Ser567 |
DSSRFPMsPRPDSVH |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249463 |
Thr312 |
ISYDIPPtPGNTYQI |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249464 |
Thr476 |
EANYVPMtPGTFDFS |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Publications: |
6 |
Organism: |
Cricetulus Griseus |
+ |
MAPK1 | up-regulates activity
phosphorylation
|
GAB1 |
0.584 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249395 |
Ser381 |
CIPTAGMsPSRSNTI |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249396 |
Ser454 |
YVPMNPNsPPRQHSS |
Cricetulus griseus |
|
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249397 |
Ser551 |
ELQAPVRsPITRSFA |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249398 |
Ser567 |
DSSRFPMsPRPDSVH |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249399 |
Thr312 |
ISYDIPPtPGNTYQI |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249400 |
Thr476 |
EANYVPMtPGTFDFS |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Publications: |
6 |
Organism: |
Cricetulus Griseus |
+ |
ERK1/2 | up-regulates activity
phosphorylation
|
GAB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129188 |
Ser454 |
YVPMNPNsPPRQHSS |
Homo sapiens |
|
pmid |
sentence |
15379552 |
Erk phosphorylation enhances hgf-dependent gab1/pi3k but inhibits egf-dependent gab1/pi3k association and activation implicates that mapk activation provides another specific regulatory mechanism which can result in divergent effects for distinct rtks.we identified four serine and two threonine residues that are phosphorylated by erk in vitro. Five of these phosphorylation sites (t312, s454, t476, s581, s597) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129192 |
Ser597 |
VPMNPNLsSEDPNLF |
Homo sapiens |
|
pmid |
sentence |
15379552 |
Erk phosphorylation enhances hgf-dependent gab1/pi3k but inhibits egf-dependent gab1/pi3k association and activation implicates that mapk activation provides another specific regulatory mechanism which can result in divergent effects for distinct rtks.we identified four serine and two threonine residues that are phosphorylated by erk in vitro. Five of these phosphorylation sites (t312, s454, t476, s581, s597) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129196 |
Thr312 |
ISYDIPPtPGNTYQI |
Homo sapiens |
|
pmid |
sentence |
15379552 |
Erk phosphorylation enhances hgf-dependent gab1/pi3k but inhibits egf-dependent gab1/pi3k association and activation implicates that mapk activation provides another specific regulatory mechanism which can result in divergent effects for distinct rtks.we identified four serine and two threonine residues that are phosphorylated by erk in vitro. Five of these phosphorylation sites (t312, s454, t476, s581, s597) |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-129200 |
Thr476 |
EANYVPMtPGTFDFS |
Homo sapiens |
|
pmid |
sentence |
15379552 |
Erk phosphorylation enhances hgf-dependent gab1/pi3k but inhibits egf-dependent gab1/pi3k association and activation implicates that mapk activation provides another specific regulatory mechanism which can result in divergent effects for distinct rtks.we identified four serine and two threonine residues that are phosphorylated by erk in vitro. Five of these phosphorylation sites (t312, s454, t476, s581, s597) |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling, Rhabdomyosarcoma |
+ |
SRC | up-regulates
phosphorylation
|
GAB1 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236314 |
Tyr242 |
FFQQQMIyDSPPSRA |
Homo sapiens |
|
pmid |
sentence |
19881549 |
Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Rhabdomyosarcoma |
+ |
INSR | up-regulates activity
phosphorylation
|
GAB1 |
0.492 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251310 |
Tyr242 |
FFQQQMIyDSPPSRA |
Mus musculus |
|
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251311 |
Tyr285 |
TEADGELyVFNTPSG |
Mus musculus |
|
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251312 |
Tyr373 |
ASDTDSSyCIPTAGM |
Mus musculus |
|
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251313 |
Tyr447 |
SEELDENyVPMNPNS |
Mus musculus |
|
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251314 |
Tyr472 |
EPIQEANyVPMTPGT |
Mus musculus |
|
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251315 |
Tyr589 |
SHDSEENyVPMNPNL |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251316 |
Tyr627 |
KGDKQVEyLDLDLDS |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251317 |
Tyr659 |
VADERVDyVVVDQQK |
Mus musculus |
NIH-3T3 Cell |
pmid |
sentence |
10978177 |
HGab-1 was phosphorylated by IR at eight tyrosine residues (Y242, Y285, Y373, Y447, Y472, Y619, Y657, and Y689). t Gab-1 is the major binding partner of PI-3 kinase in 3T3L1 cells when stimulated with insulin |
|
Publications: |
8 |
Organism: |
Mus Musculus |
+ |
SRC | up-regulates activity
phosphorylation
|
GAB1 |
0.693 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236310 |
Tyr259 |
ASVDSSLyNLPRSYS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19881549 |
Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236306 |
Tyr317 |
PPTPGNTyQIPRTFP |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19881549 |
Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236318 |
Tyr373 |
ASDTDSSyCIPTAGM |
Homo sapiens |
|
pmid |
sentence |
19881549 |
Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236302 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19881549 |
Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Rhabdomyosarcoma |
+ |
EGFR | up-regulates
phosphorylation
|
GAB1 |
0.751 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236400 |
Tyr285 |
TEADGELyVFNTPSG |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236396 |
Tyr406 |
DASSQDCyDIPRAFP |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236420 |
Tyr447 |
SEELDENyVPMNPNS |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236392 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236404 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling |
+ |
MET | up-regulates activity
phosphorylation
|
GAB1 |
0.661 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250552 |
Tyr285 |
TEADGELyVFNTPSG |
Homo sapiens |
A-549 Cell |
pmid |
sentence |
10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250288 |
Tyr589 |
SHDSEENyVPMNPNL |
Homo sapiens |
A-549 Cell |
pmid |
sentence |
10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250289 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
A-549 Cell |
pmid |
sentence |
10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250290 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
A-549 Cell |
pmid |
sentence |
10734310 |
Gab-1 is phosphorylated on the same residues by HGF and EGF receptors. Among 16 peptides only nine were phosphorylated by the EGF and HGF receptors, namely peptides containing the tyrosine residues 285, 307, 373, 407, 448, 473, 590, 628 and 660. we show that in the response to HGF or EGF, Gab1 is phosphorylated in vivo on the same residues. However, a sustained activation of signaling pathways downstream to Gab1 (as a result of its sustained phosphorylation) is achieved only in response to HGF. |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | Hepatocellular Tumor, Rhabdomyosarcoma |
+ |
EGFR | up-regulates activity
phosphorylation
|
GAB1 |
0.751 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-233233 |
Tyr307 |
MRHVSISyDIPPTPG |
in vitro |
|
pmid |
sentence |
10734310 |
Gab1 is also phosphorylated in response to epidermal growth factor (egf) but is unable to induce tubule formation. nine tyrosines are phosphorylated by both receptors. Three of them (y307, y373, y407) bind phospholipase c-gamma (plc-gamma). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236408 |
Tyr373 |
ASDTDSSyCIPTAGM |
Homo sapiens |
|
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236412 |
Tyr472 |
EPIQEANyVPMTPGT |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236416 |
Tyr589 |
SHDSEENyVPMNPNL |
Homo sapiens |
Glioblastoma Cell, A-431 Cell |
pmid |
sentence |
9890893 |
Gab-1 is a multisubstrate docking protein downstream in the signaling pathways of different receptor tyrosine kinases, including the epidermal growth factor receptor (egfr)the entire protein was phosphorylated by regfr at eight tyrosine residues (y285, y373, y406, y447, y472, y619, y657, and y689). |
|
Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens |
Pathways: | EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling |
+ |
PTPN11 | down-regulates activity
dephosphorylation
|
GAB1 |
0.952 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236258 |
Tyr589 |
SHDSEENyVPMNPNL |
Homo sapiens |
|
pmid |
sentence |
10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248674 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
|
pmid |
sentence |
11323411 |
These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2.|Thus, physical association of activated SHP2 with Gab1 is necessary and sufficient to mediate the ERK mitogen-activated protein kinase activation. Phosphopeptides derived from Gab1 were dephosphorylated by active SHP2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248675 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
|
pmid |
sentence |
11323411 |
These results suggest that Tyr(P)-627 and Tyr(P)-659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) that binds and activates SHP2.|Thus, physical association of activated SHP2 with Gab1 is necessary and sufficient to mediate the ERK mitogen-activated protein kinase activation. Phosphopeptides derived from Gab1 were dephosphorylated by active SHP2 in vitro. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Noonan syndrome |
+ |
PTPN11 | down-regulates
dephosphorylation
|
GAB1 |
0.952 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236262 |
Tyr627 |
KGDKQVEyLDLDLDS |
Homo sapiens |
|
pmid |
sentence |
10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-236254 |
Tyr659 |
VADERVDyVVVDQQK |
Homo sapiens |
|
pmid |
sentence |
10068651 |
Tyrosine phosphorylation of gab2 was induced by stimulation through gp130, il-2r, il-3r, tpor, scfr, and tcr. Gab1 and gab2 were shown to be substrates for shp-2 in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Noonan syndrome |
+ |
PTPN1 | down-regulates activity
dephosphorylation
|
GAB1 |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276965 |
|
|
Homo sapiens |
|
pmid |
sentence |
23521888 |
Since Gab1 is negatively regulated by PTP1B, a part of the retinal neuroprotective effect we have observed previously in PTP1B deficient mice could be contributed by Gab1 as well.|The results indicate that PTP1B completely dephosphorylated Gab1 and the mutant protein failed to dephosphorylate Gab1 (Figure\u00a0 xref C). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GRB2 | up-regulates
binding
|
GAB1 |
0.868 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-235917 |
|
|
Homo sapiens |
|
pmid |
sentence |
12766170 |
The gab1 docking protein forms a platform for the assembly of a multiprotein signaling complex downstream from receptor tyrosine kinases. In general, recruitment of gab1 occurs indirectly, via the adapter protein grb2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Hepatocellular Tumor, Noonan syndrome, PI3K/AKT Signaling, Rhabdomyosarcoma |
+ |
GAB1 | up-regulates
binding
|
PIK3CA |
0.428 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-83343 |
|
|
Homo sapiens |
|
pmid |
sentence |
11043767 |
We have shown that gab1 colocalizes pi3k with sh2 domain-containing inositol phosphatase (ship) and shp2, two enzymes that regulate pi3k-dependent signaling. The src homology 2 (sh2) domain of the phosphatidylinositol 3-kinase (pi3k) regulatory subunit binds gab1 in a phosphorylation-independent manner. Moreover, the regulatory subunit of pi3k can mediate the association of gab1 and receptor protein-tyrosine kinases including the insulin, egf, and ngf receptors, all of which phosphorylate gab1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | EGFR Signaling, Rhabdomyosarcoma |
+ |
GAB1 | up-regulates
binding
|
PI3K |
0.491 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252676 |
|
|
Homo sapiens |
|
pmid |
sentence |
11043767 |
We have shown that gab1 colocalizes pi3k with sh2 domain-containing inositol phosphatase (ship) and shp2, two enzymes that regulate pi3k-dependent signaling. The src homology 2 (sh2) domain of the phosphatidylinositol 3-kinase (pi3k) regulatory subunit binds gab1 in a phosphorylation-independent manner. Moreover, the regulatory subunit of pi3k can mediate the association of gab1 and receptor protein-tyrosine kinases including the insulin, egf, and ngf receptors, all of which phosphorylate gab1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Hepatocellular Tumor, PI3K/AKT Signaling |
+ |
Gbeta | up-regulates activity
phosphorylation
|
GAB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270060 |
|
|
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
15379552 |
Our results demonstrate that ERK1/2 phosphorylate Gab1 at six serine/threonine residues (T312, S381, S454, T476, S581, S597) in consensus motifs for MAP kinase phosphorylation. |serine and threonine phosphorylation are capable of modulating the initial signal |
|
Publications: |
1 |
Organism: |
Cricetulus Griseus |
+ |
GAB1 | up-regulates
relocalization
|
ARHGAP32 |
0.319 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-102586 |
|
|
Homo sapiens |
|
pmid |
sentence |
12819203 |
Gc-gap, a rho family gtpase-activating protein that interacts with signaling adapters gab1 and gab2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |