| + |
CHEK1 | down-regulates 
phosphorylation
|
SYK |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197528 |
Ser295 |
GIISRIKsYSFPKPG |
Homo sapiens |
|
| pmid |
sentence |
| 22585575 |
We found that chk1 phosphorylated the tumor suppressor spleen tyrosine kinase (l) (syk[l]) and identified the phosphorylation site at ser295. Furthermore, chk1 phosphorylation of syk(l) promoted its subsequent proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates 
phosphorylation
|
IKZF1 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199096 |
Ser361 |
LAEGTPRsNHSAQDS |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 23071339 |
Syk phoshorylatesikarosat unique c-terminal serine phosphorylation sites s358 and s361, thereby augmenting its nuclear localization and sequence-specific dna binding activity. Mechanistically, we establish that syk-inducedikarosactivation is essential for its nuclear localization and optimal transcription factor function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199100 |
Ser364 |
GTPRSNHsAQDSAVE |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 23071339 |
Syk phoshorylatesikarosat unique c-terminal serine phosphorylation sites s358 and s361, thereby augmenting its nuclear localization and sequence-specific dna binding activity. Mechanistically, we establish that syk-inducedikarosactivation is essential for its nuclear localization and optimal transcription factor function. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SYK | down-regulates activity
phosphorylation
|
PIP5K1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276227 |
Tyr105 |
FGIKPDDyLYSICSE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 19553680 |
We identified spleen tyrosine kinase (Syk), which is activated by oxidants, as a candidate PIP5Kbeta kinase in this pathway, and mapped the oxidant-sensitive tyrosine phosphorylation site to residue 105. The PIP5KbetaY105E phosphomimetic is catalytically inactive and cytosolic, whereas the Y105F non-phosphorylatable mutant has higher intrinsic lipid kinase activity and is much more membrane associated than wild type PIP5Kbeta. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SYK | up-regulates activity
phosphorylation
|
GCSAM |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273570 |
Tyr106 |
SGNSAEEyYENVPCK |
in vitro |
|
| pmid |
sentence |
| 31362927 |
Herein, we demonstrate phosphorylation of HGAL by Syk and Lyn kinases at tyrosines Y80, Y86, Y106Y107, Y128, and Y148. Y148 (in black) was already phosphorylated before the addition of kinases. We demonstrate that Grb2 facilitates HGAL and Syk binding following BCR stimulation but does not affect the HGAL-mediated increase in Syk kinase activity. Previous studies showed that Grb2 inhibits BCR signaling by decreasing the activation of Syk by Lyn.11 Thus, while HGAL and Grb2 oppositely affect Syk kinase activity, this is not due to direct Grb2 effects on HGAL-mediated Syk kinase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273571 |
Tyr107 |
GNSAEEYyENVPCKA |
in vitro |
|
| pmid |
sentence |
| 31362927 |
Herein, we demonstrate phosphorylation of HGAL by Syk and Lyn kinases at tyrosines Y80, Y86, Y106Y107, Y128, and Y148. Y148 (in black) was already phosphorylated before the addition of kinases. We demonstrate that Grb2 facilitates HGAL and Syk binding following BCR stimulation but does not affect the HGAL-mediated increase in Syk kinase activity. Previous studies showed that Grb2 inhibits BCR signaling by decreasing the activation of Syk by Lyn.11 Thus, while HGAL and Grb2 oppositely affect Syk kinase activity, this is not due to direct Grb2 effects on HGAL-mediated Syk kinase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273573 |
Tyr128 |
LGGTETEySLLHMPS |
in vitro |
|
| pmid |
sentence |
| 31362927 |
Herein, we demonstrate phosphorylation of HGAL by Syk and Lyn kinases at tyrosines Y80, Y86, Y106Y107, Y128, and Y148. Y148 (in black) was already phosphorylated before the addition of kinases. We demonstrate that Grb2 facilitates HGAL and Syk binding following BCR stimulation but does not affect the HGAL-mediated increase in Syk kinase activity. Previous studies showed that Grb2 inhibits BCR signaling by decreasing the activation of Syk by Lyn.11 Thus, while HGAL and Grb2 oppositely affect Syk kinase activity, this is not due to direct Grb2 effects on HGAL-mediated Syk kinase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273572 |
Tyr80 |
QDNVDQTySEELCYT |
in vitro |
|
| pmid |
sentence |
| 31362927 |
Herein, we demonstrate phosphorylation of HGAL by Syk and Lyn kinases at tyrosines Y80, Y86, Y106Y107, Y128, and Y148. Y148 (in black) was already phosphorylated before the addition of kinases. We demonstrate that Grb2 facilitates HGAL and Syk binding following BCR stimulation but does not affect the HGAL-mediated increase in Syk kinase activity. Previous studies showed that Grb2 inhibits BCR signaling by decreasing the activation of Syk by Lyn.11 Thus, while HGAL and Grb2 oppositely affect Syk kinase activity, this is not due to direct Grb2 effects on HGAL-mediated Syk kinase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273574 |
Tyr86 |
TYSEELCyTLINHRV |
in vitro |
|
| pmid |
sentence |
| 31362927 |
Herein, we demonstrate phosphorylation of HGAL by Syk and Lyn kinases at tyrosines Y80, Y86, Y106Y107, Y128, and Y148. Y148 (in black) was already phosphorylated before the addition of kinases. We demonstrate that Grb2 facilitates HGAL and Syk binding following BCR stimulation but does not affect the HGAL-mediated increase in Syk kinase activity. Previous studies showed that Grb2 inhibits BCR signaling by decreasing the activation of Syk by Lyn.11 Thus, while HGAL and Grb2 oppositely affect Syk kinase activity, this is not due to direct Grb2 effects on HGAL-mediated Syk kinase activation. |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
SYK | down-regulates
phosphorylation
|
SNCA |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113061 |
Tyr125 |
VDPDNEAyEMPSEEG |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113065 |
Tyr133 |
EMPSEEGyQDYEPEA |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-113069 |
Tyr136 |
SEEGYQDyEPEA |
Homo sapiens |
|
| pmid |
sentence |
| 11744621 |
Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (syk), which phosphorylates three tyrosyl residues in its c-terminal domain (y-125, y-133, and y-136), here, we show that _-syn is an outstanding substrate for syk and that once it is tyrosine phosphorylated, it loses the ability to form oligomers. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary, Brain |
| + |
SYK | up-regulates activity
phosphorylation
|
SYK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246601 |
Tyr131 |
KENLIREyVKQTWNL |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246605 |
Tyr323 |
STVSFNPyEPELAPW |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246609 |
Tyr348 |
LPMDTEVyESPYADP |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246613 |
Tyr352 |
TEVYESPyADPEEIR |
Homo sapiens |
|
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246617 |
Tyr525 |
ALRADENyYKAQTHG |
Homo sapiens |
|
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246621 |
Tyr526 |
LRADENYyKAQTHGK |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9820500 |
These represented sites of tyrosine phosphorylation previously identified from the study of in vitro autophosphorylated Syk. Phosphorylation was observed on peptides corresponding to Tyr130, Tyr317, Tyr342, Tyr346, Tyr519, and Tyr520 |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SYK | up-regulates activity
phosphorylation
|
LAT2 |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273576 |
Tyr136 |
EDDDANSyENVLICK |
Mus musculus |
A20 Cell |
| pmid |
sentence |
| 14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273575 |
Tyr193 |
EDEESEDyQNSASIH |
Mus musculus |
A20 Cell |
| pmid |
sentence |
| 14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273577 |
Tyr233 |
EEDGEPDyVNGEVAA |
Mus musculus |
A20 Cell |
| pmid |
sentence |
| 14722116 |
Our results indicated that human LAB was primarily phosphorylated on three membrane-distal tyrosines, Tyr(136), Tyr(193), and Tyr(233). Mutation of these three tyrosines abolished Grb2 binding and LAB function. Our data suggested that these tyrosines are the most important tyrosines for LAB function.The dramatic reduction in phosphorylation of the LAB Y233F mutant suggested that Tyr233 is a primary target of the Syk family kinases. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
SYK | up-regulates activity
phosphorylation
|
DUSP3 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275999 |
Tyr138 |
SPTLVIAyLMMRQKM |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12447358 |
ZAP-70 and Syk also tyrosine-phosphorylated VHR in COS-1 cells (Fig. 2d), whereas other kinases (Csk, Lck, Fyn, Jak2, Bcr-Abl and Itk) had little effect. Finally, recombinant ZAP-70 readily phosphorylated VHR in vitro (Fig. 2f). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
SYK | up-regulates activity
phosphorylation
|
SH3BP2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246587 |
Tyr174 |
YPTDNEDyEHDDEDD |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12709437 |
By using the transient expression system in COS-7 cells, we have demonstrated that 3BP2 was predominantly phosphorylated on Tyr174, Tyr183, and Tyr446 when it was coexpressed with Syk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246592 |
Tyr183 |
HDDEDDSyLEPDSPE |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12709437 |
By using the transient expression system in COS-7 cells, we have demonstrated that 3BP2 was predominantly phosphorylated on Tyr174, Tyr183, and Tyr446 when it was coexpressed with Syk |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246596 |
Tyr448 |
GDDSDEDyEKVPLPN |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 12709437 |
By using the transient expression system in COS-7 cells, we have demonstrated that 3BP2 was predominantly phosphorylated on Tyr174, Tyr183, and Tyr446 when it was coexpressed with Syk. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
SYK | up-regulates
phosphorylation
|
BLNK |
0.799 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96040 |
Tyr178 |
LLEDEADyVVPVEDN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 12456653 |
The phosphorylation of multiple tyrosine residues not only amplifies plcgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96044 |
Tyr72 |
SDDFDSDyENPDEHS |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 12456653 |
The phosphorylation of multiple tyrosine residues not only amplifies plcgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96048 |
Tyr84 |
EHSDSEMyVMPAEEN |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 12456653 |
The phosphorylation of multiple tyrosine residues not only amplifies plcgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96052 |
Tyr96 |
EENADDSyEPPPVEQ |
Homo sapiens |
|
| pmid |
sentence |
| 12456653 |
The phosphorylation of multiple tyrosine residues not only amplifies plcgamma-mediated signaling but also supports 'cis'-mediated interaction between distinct signaling effectors within a large molecular complex. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SYK | down-regulates
phosphorylation
|
MAPT |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159648 |
Tyr18 |
MEDHAGTyGLGDRKD |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18070606 |
We established that tyrosine 18 was the primary residue in tau phosphorylated by sykphosphorylation of tau by syk could be involved in neurite outgrowth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | down-regulates activity
phosphorylation
|
LCK |
0.573 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246562 |
Tyr192 |
NLDNGGFyISPRITF |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 8798764 |
Our experiments indicate that the TCR-induced activation of Erk2 depends on the function of SH2 domain of Lck and is reduced by phosphorylation of wild type Lck at Tyr192 or by mutation of this site to a negatively charged amino acid. Such dependence on the SH2 domain has also been reported for the bulk of TCR-induced tyrosine phosphorylation and activation of the interleukin 2 gene (26). Thus, phosphorylation of Lck at Tyr192 may represent a negative feedback mechanism in the interplay between Src and Syk family PTKs in TCR signaling |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates activity
phosphorylation
|
LAX1 |
0.386 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273532 |
Tyr193 |
SSEDSHDyVNVPTAE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12359715 |
Upon stimulation via the B or T cell receptors, LAX is rapidly phosphorylated by Src and Syk family tyrosine kinases and interacts with Grb2, Gads, and p85. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273533 |
Tyr268 |
SSQISNDyVNMTGLD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12359715 |
Upon stimulation via the B or T cell receptors, LAX is rapidly phosphorylated by Src and Syk family tyrosine kinases and interacts with Grb2, Gads, and p85. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273534 |
Tyr294 |
AFQCCRDyENVPAAD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12359715 |
Upon stimulation via the B or T cell receptors, LAX is rapidly phosphorylated by Src and Syk family tyrosine kinases and interacts with Grb2, Gads, and p85. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273535 |
Tyr373 |
SNEDSSDyENVLTAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12359715 |
Upon stimulation via the B or T cell receptors, LAX is rapidly phosphorylated by Src and Syk family tyrosine kinases and interacts with Grb2, Gads, and p85. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates
phosphorylation
|
SLC4A1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80788 |
Tyr21 |
ENLEQEEyEDPDIPE |
Homo sapiens |
|
| pmid |
sentence |
| 10942405 |
Our findings suggest that, upon phosphorylation by p72syk, y8 and y21 act as docking sites for the sh2 domain of lyn, which subsequently phosphorylates band 3 at additional secondary sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80792 |
Tyr8 |
MEELQDDyEDMMEEN |
Homo sapiens |
|
| pmid |
sentence |
| 10942405 |
Our findings suggest that, upon phosphorylation by p72syk, y8 and y21 act as docking sites for the sh2 domain of lyn, which subsequently phosphorylates band 3 at additional secondary sites. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SYK |
phosphorylation
|
SLC4A1 |
0.462 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251411 |
Tyr21 |
ENLEQEEyEDPDIPE |
in vitro |
|
| pmid |
sentence |
| 10942405 |
The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251413 |
Tyr8 |
MEELQDDyEDMMEEN |
in vitro |
|
| pmid |
sentence |
| 10942405 |
The primary phosphorylation of band 3 catalyzed by p72syk generates the SH2 binding motifs that are a prerequisite for the following recruitment of Lyn. p72syk as the most likely candidate to perform this task and indicates Y8 and Y21. Syk and Lyn phosphorylate band 3 at both cytosolic and membrane domains, Y-phosphorylation/dephosphorylation is likely involved in the regulation of several erythrocyte functions (ie, glycolysis, cell shape, cytoskeleton |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SYK | up-regulates activity
phosphorylation
|
IL15RA |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246556 |
Tyr227 |
AVSLLACyLKSRQTP |
Homo sapiens |
RAJI Cell |
| pmid |
sentence |
| 11714793 |
Mutation of a defined region of the intracellular signaling portion of IL-15Ralpha (Tyr227) abrogates both the IL-15Ralpha/Syk association and IL-15Ralpha phosphorylation. Taken together, this suggests that Syk kinase physically and functionally associates with the IL-15Ralpha chain in B cells and that Syk plays a key role in mediating IL-15-induced signal transduction, thus accounting for the distinct functional consequences of IL-15 vs IL-2 binding to B cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates activity
phosphorylation
|
FCGR2A |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247590 |
Tyr281 |
LEETNNDyETADGGY |
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 pointFyn 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-246551 |
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 pointFyn 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 |
| + |
SYK | up-regulates activity
phosphorylation
|
FCGR2C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262674 |
Tyr287 |
PEETNNDyETADGGY |
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-262675 |
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 |
| + |
SYK | down-regulates activity
phosphorylation
|
DEPTOR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277572 |
Tyr289 |
SSCGSSGyFSSSPTL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 34634301 |
We found that tyrosine (Tyr) 289 phosphorylation of DEPTOR impairs its interaction with mTOR, leading to increased mTOR activation. Using proximity biotinylation assays, we identified SYK (spleen tyrosine kinase) as a kinase involved in DEPTOR Tyr 289 phosphorylation in an ephrin (erythropoietin-producing hepatocellular carcinoma) receptor-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates
phosphorylation
|
SHC1 |
0.753 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59635 |
Tyr349 |
EEPPDHQyYNDFPGK |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 9710204 |
The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on sch1 (iso2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59639 |
Tyr350 |
EPPDHQYyNDFPGKE |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 9710204 |
The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on sch1 (iso2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59643 |
Tyr427 |
ELFDDPSyVNVQNLD |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 9710204 |
The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on sch1 (iso2). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates
phosphorylation
|
HCLS1 |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47338 |
Tyr378 |
EPEPENDyEDVEEMD |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Here, we show that bcr-associated tyrosine kinases lyn and syk synergistically phosphorylate hs1, and that tyr-378 and tyr-397 of hs1 are the critical residues for its bcr-induced phosphorylation. once the two tyrosine residues are both phosphorylated, processive phosphorylation of hs1 by lyn and the other src family kinases would take place, producing hyperphosphorylated form of hs1. Finally, it is this hyperphosphorylated form of hs1 that translocates to the nucleus and activates b cell apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-47342 |
Tyr397 |
EDEPEGDyEEVLEPE |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9104825 |
Here, we show that bcr-associated tyrosine kinases lyn and syk synergistically phosphorylate hs1, and that tyr-378 and tyr-397 of hs1 are the critical residues for its bcr-induced phosphorylation. once the two tyrosine residues are both phosphorylated, processive phosphorylation of hs1 by lyn and the other src family kinases would take place, producing hyperphosphorylated form of hs1. Finally, it is this hyperphosphorylated form of hs1 that translocates to the nucleus and activates b cell apoptosis. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates activity
phosphorylation
|
MAP4K1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246567 |
Tyr381 |
SESSDDDyDDVDIPT |
Homo sapiens |
|
| pmid |
sentence |
| 11514608 |
BCR ligation induced rapid tyrosine-phosphorylation of HPK1 mainly by Syk and Lyn, resulting in its association with BASH and catalytic activation. BCR-mediated activation of HPK1 was impaired in Syk- or BASH-deficient B cells. The functional SH2 domain of BASH and Tyr-379 within HPK1 which we identified as a Syk-phosphorylation site were both necessary for interaction of both proteins and efficient HPK1 activation after BCR stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates activity
phosphorylation
|
TUBA4A |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246626 |
Tyr432 |
MAALEKDyEEVGIDS |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 9490415 |
Syk, Activated by Cross-linking the B-cell Antigen Receptor, Localizes to the Cytosol Where It Interacts with and Phosphorylates alpha-Tubulin on Tyrosine |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates activity
phosphorylation
|
BTK |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247586 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
|
| pmid |
sentence |
| 11226282 |
We have demonstrated that BLNK mediates Syk-dependent Btk activation. In a reconstitution cell system, coexpression of BLNK allows Syk to phosphorylate Btk on its tyrosine 551, leading to the enhancement of Btk activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SYK | up-regulates activity
phosphorylation
|
PRKCA |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246581 |
Tyr658 |
SDFEGFSyVNPQFVH |
Homo sapiens |
Mast Cell |
| pmid |
sentence |
| 12881490 |
We present evidence that Tyr-662 and Tyr-658 of PKCbetaI and PKCalpha, respectively, are phosphorylated by Syk in the membrane compartment of FcepsilonRI-stimulated mast cells. These phosphorylations require prior PKC autophosphorylation of the adjacent serine residues (Ser-661 and Ser-657, respectively) and generate a binding site for the SH2 domain of the adaptor protein Grb-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
SYK | up-regulates activity
phosphorylation
|
PLCG1 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246572 |
Tyr771 |
IGTAEPDyGALYEGR |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 8657103 |
Syk isolated from antigen receptor-activated B cells phosphorylated PLC-gamma1 on Tyr-771 and the key regulatory residue Tyr-783 in vitro, whereas Lyn from the same B cells phosphorylated PLC-gamma1 only on Tyr-771. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246576 |
Tyr783 |
EGRNPGFyVEANPMP |
Homo sapiens |
|
| pmid |
sentence |
| 8657103 |
Syk isolated from antigen receptor-activated B cells phosphorylated PLC-gamma1 on Tyr-771 and the key regulatory residue Tyr-783 in vitro, whereas Lyn from the same B cells phosphorylated PLC-gamma1 only on Tyr-771. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
BCR-Ml | up-regulates activity
binding
|
SYK |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268440 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32323266 |
The tyrosine phosphorylation of the ITAM of CD79 promotes the activation of the non-SRC family tyrosine kinase, spleen tyrosine kinase (SYK), which becomes a key part of a signalosome formed by many other kinases and adaptor proteins. The SYK which is recruited to the phosphorylated CD79- ITAM facilitates the complex formation of B-cell linker protein (BLNK), leading to activation of Bruton’s tyrosine kinase (BTK). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
2-[[7-(3,4-dimethoxyphenyl)-5-imidazo[1,2-c]pyrimidinyl]amino]-3-pyridinecarboxamide | down-regulates activity
chemical inhibition
|
SYK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262020 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 30744170 |
The Selective SYK Inhibitor BAY 61-3606 Enhances the Effect of Chemotherapeutic Drugs on Neuroblastoma Cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | down-regulates activity
phosphorylation
|
PAX5 |
0.434 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269084 |
|
|
Homo sapiens |
RAMOS (RA.1) Cell |
| pmid |
sentence |
| 27181361 |
PAX5 tyrosine phosphorylation by SYK co-operatively functions with its serine phosphorylation to cancel the PAX5-dependent repression of BLIMP1: A mechanism for antigen-triggered plasma cell differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | up-regulates
phosphorylation
|
VAV1 |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107046 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331248 |
Vav interacts with the tyrosine kinase syk. inhibition of syk kinase activity prevents tyrosine phosphorylation of vav and its interaction with pi 3-k. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SH2B1 | down-regulates activity
dephosphorylation
|
SYK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268445 |
|
|
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 |
| + |
BCR-Dl | up-regulates activity
binding
|
SYK |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268442 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32323266 |
The tyrosine phosphorylation of the ITAM of CD79 promotes the activation of the non-SRC family tyrosine kinase, spleen tyrosine kinase (SYK), which becomes a key part of a signalosome formed by many other kinases and adaptor proteins. The SYK which is recruited to the phosphorylated CD79- ITAM facilitates the complex formation of B-cell linker protein (BLNK), leading to activation of Bruton’s tyrosine kinase (BTK). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
R406 | down-regulates
chemical inhibition
|
SYK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206340 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Fostamatinib disodium | down-regulates
chemical inhibition
|
SYK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-206373 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
INPP5D | down-regulates activity
dephosphorylation
|
SYK |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268456 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32323266 |
An adaptor protein Dok-3 mediates the suppressive function of LYN. The Dok-3 phosphorylated by LYN upon BCR stimulation forms a complex with GRB2, which allows it to enter into the signalosome and associate with activation of SHIP protein. This translocation facilitates the efficient inhibition of PLCc2 and SYK from activation, subsequently resulting in the suppression of downstream Ca2+ signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-one | down-regulates activity
chemical inhibition
|
SYK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258295 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN6 | down-regulates
dephosphorylation
|
SYK |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70234 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 10458769 |
We propose that shp1 can dephosphorylate sites in zap-70 and syk that are involved in coupling these kinases to downstream signaling cascades, including erk2 and elements of the il-2 gene. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN11 | down-regulates activity
dephosphorylation
|
SYK |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277085 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23182168 |
Another SHP isoform, SHP-2, has been linked to negative regulation of Syk.|Syk and LAT are differentially dephosphorylated by SHP-2 and SHP-1, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCR-Mk | up-regulates activity
binding
|
SYK |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268439 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The tyrosine phosphorylation of the ITAM of CD79 promotes the activation of the non-SRC family tyrosine kinase, spleen tyrosine kinase (SYK), which becomes a key part of a signalosome formed by many other kinases and adaptor proteins. The SYK which is recruited to the phosphorylated CD79- ITAM facilitates the complex formation of B-cell linker protein (BLNK), leading to activation of Bruton’s tyrosine kinase (BTK). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
VAV1 | up-regulates
binding
|
SYK |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107049 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11331248 |
Vav interacts with the tyrosine kinase syk |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCR-Dk | up-regulates activity
binding
|
SYK |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268441 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32323266 |
The tyrosine phosphorylation of the ITAM of CD79 promotes the activation of the non-SRC family tyrosine kinase, spleen tyrosine kinase (SYK), which becomes a key part of a signalosome formed by many other kinases and adaptor proteins. The SYK which is recruited to the phosphorylated CD79- ITAM facilitates the complex formation of B-cell linker protein (BLNK), leading to activation of Bruton’s tyrosine kinase (BTK). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
CBL | down-regulates activity
ubiquitination
|
SYK |
0.808 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272620 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11742985 |
Intact tyrosine kinase-binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for in vitro Syk ubiquitylation. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl-mediated negative regulation of cytoplasmic targets. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FCRL3 | up-regulates activity
binding
|
SYK |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274011 |
|
|
in vitro |
|
| pmid |
sentence |
| 12051764 |
Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEDD4 | down-regulates quantity by destabilization
polyubiquitination
|
SYK |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272581 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11046148 |
The latent membrane protein (LMP) 2A of Epstein-Barr virus (EBV) is implicated in the maintenance of viral latency and appears to function in part by inhibiting B-cell receptor (BCR) signaling. LMP2A enhances Lyn and Syk ubiquitination in vivo in a fashion that depends on the activity of Nedd4 family members and correlates with destabilization of the Lyn tyrosine kinase. These results suggest that LMP2A serves as a molecular scaffold to recruit both B-cell tyrosine kinases and C2/WW/Hect domain E3 protein-ubiquitin ligases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SYK
- 
- 