| + |
CSNK1G3 | up-regulates quantity by stabilization 
phosphorylation
|
LYN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275395 |
Ser13 |
SKGKDSLsDDGVDLK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33004926 |
Although there have been more than 40 reports of mass spectrometric studies on phosphorylation at Lyn-S13, the kinase responsible remained unclear. We succeeded in identifying casein kinase 1γ (CK1γ) as the kinase responsible for phosphorylation of Lyn-S13. In HEK293 cells co-expressing Lyn and CK1γ, the phosphorylation level of Lyn-S13 increased significantly. we concluded that S-palmitoylated CK1γ encounters N-myristoylated Lyn and specifically phosphorylates the Ser-13 residue at the Golgi during intracellular protein traffic, as shown schematically in Fig. 8. Phosphorylated dual-lipid-modified Lyn and S-palmitoylated CK1γ are then transported from the Golgi to the plasma membrane. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1G1 | up-regulates quantity by stabilization
phosphorylation
|
LYN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275396 |
Ser13 |
SKGKDSLsDDGVDLK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33004926 |
Although there have been more than 40 reports of mass spectrometric studies on phosphorylation at Lyn-S13, the kinase responsible remained unclear. We succeeded in identifying casein kinase 1γ (CK1γ) as the kinase responsible for phosphorylation of Lyn-S13. In HEK293 cells co-expressing Lyn and CK1γ, the phosphorylation level of Lyn-S13 increased significantly. we concluded that S-palmitoylated CK1γ encounters N-myristoylated Lyn and specifically phosphorylates the Ser-13 residue at the Golgi during intracellular protein traffic, as shown schematically in Fig. 8. Phosphorylated dual-lipid-modified Lyn and S-palmitoylated CK1γ are then transported from the Golgi to the plasma membrane. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1G2 | up-regulates quantity by stabilization
phosphorylation
|
LYN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275397 |
Ser13 |
SKGKDSLsDDGVDLK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 33004926 |
Although there have been more than 40 reports of mass spectrometric studies on phosphorylation at Lyn-S13, the kinase responsible remained unclear. We succeeded in identifying casein kinase 1γ (CK1γ) as the kinase responsible for phosphorylation of Lyn-S13. In HEK293 cells co-expressing Lyn and CK1γ, the phosphorylation level of Lyn-S13 increased significantly. we concluded that S-palmitoylated CK1γ encounters N-myristoylated Lyn and specifically phosphorylates the Ser-13 residue at the Golgi during intracellular protein traffic, as shown schematically in Fig. 8. Phosphorylated dual-lipid-modified Lyn and S-palmitoylated CK1γ are then transported from the Golgi to the plasma membrane. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
GCSAM |
0.247 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273556 |
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-273557 |
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-273559 |
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-273558 |
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-273560 |
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 |
| + |
LYN | up-regulates activity
phosphorylation
|
KCND3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276395 |
Tyr108 |
GKLHYPRyECISAYD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22198508 |
These results indicate that Y108 (for Src-family kinases) and Y136 (for EGFR kinase) are involved in the tyrosine phosphorylation of hKv4.3 channels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PTGS2 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276643 |
Tyr120 |
PPTYNADyGYKSWEA |
in vitro |
|
| pmid |
sentence |
| 24970799 |
We report that FYN phosphorylates human COX2 on Tyr 446, and while corresponding phospho-mimetic COX2 mutation promotes COX2 activity, the phosphorylation blocking mutation prevents FYN-mediated increase in COX2 activity. FYN and LYN kinases phosphorylate COX2 on two distinct residues in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
GLO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276186 |
Tyr136 |
GIAVPDVySACKRFE |
in vitro |
|
| pmid |
sentence |
| 34838714 |
We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of the Src family (Src, Yes1, FGR, and the related Abl1), and of the FAK, EPHA, FGFR, and VEGFR families (Figure 2B), suggesting phosphorylation of Glo1 on Y136 by multiple different kinases. In vitro kinase assays revealed that all the members of the Src family, as well as Epha5 and VEGFR3, can efficiently phosphorylate recombinant Glo1 on Y136 (Figure 2C–D). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
DAPP1 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249378 |
Tyr139 |
KVEEPSIyESVRVHT |
|
B-lymphocyte |
| pmid |
sentence |
| 10880360 |
Src family kinases mediate receptor-stimulated, phosphoinositide 3-kinase-dependent, tyrosine phosphorylation of dual adaptor for phosphotyrosine and 3-phosphoinositides-1 in endothelial and B cell lines|yrosine phosphorylation of DAPP-1 appears important for appropriate intracellular targeting and creates a potential binding site for Src homology 2 domain-containing proteins. |
|
| Publications: |
1 |
| + |
LYN | up-regulates activity
phosphorylation
|
RGS16 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251410 |
Tyr168 |
TLMEKDSyPRFLKSP |
in vitro |
|
| pmid |
sentence |
| 12588871 |
Lyn kinase phosphorylated recombinant RGS16 in vitro. Induction of RGS16 tyrosine phosphorylation was associated with increased RGS16 protein levels and enhanced GAP activity in cell membranes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN |
phosphorylation
|
NMT1 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251404 |
Tyr180 |
YTLLNENyVEDDDNM |
in vitro |
|
| pmid |
sentence |
| 11594778 |
Human NMT was found to be phosphorylated by non-receptor tyrosine kinase family members of Lyn. a site-directed mutagenesis study indicated that substitution of tyrosine 100 with phenylalanine served NMT as a poor substrate for the Lyn kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
CD79A |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251397 |
Tyr188 |
EYEDENLyEGLNLDD |
in vitro |
|
| pmid |
sentence |
| 9531288 |
Y182 of CD79a appears to be the initial and preferred site of Ag receptor phosphorylation by Src family kinases. In vitro, Src family Lyn and Fyn predominantly phosphorylate this residue in CD79a, and Y195 does so in CD79b. phosphorylation of Y182 alone can lead to further kinase activation and/or effector focusing necessary for phosphorylation of certain downstream targets, such as p62, p110, and Shc, but not others, such as Vav. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates activity
phosphorylation
|
CD79B |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251398 |
Tyr196 |
GMEEDHTyEGLDIDQ |
in vitro |
|
| pmid |
sentence |
| 9531288 |
Y182 of CD79a appears to be the initial and preferred site of Ag receptor phosphorylation by Src family kinases. In vitro, Src family Lyn and Fyn predominantly phosphorylate this residue in CD79a, and Y195 does so in CD79b |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
LYN |
phosphorylation
|
HCLS1 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251399 |
Tyr222 |
MEAPTTAyKKTTPIE |
in vitro |
|
| pmid |
sentence |
| 10066823 |
HS1 was shown to undergo a process of sequential phosphorylation both in vitro and in vivo, which is synergistically mediated by Syk and Src family protein-tyrosine kinases and essential for B cell antigen receptor-mediated apoptosis. We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
ACLY |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274104 |
Tyr227 |
KVDATADyICKVKWG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274105 |
Tyr252 |
EAYPEEAyIADLDAK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274103 |
Tyr682 |
SRTTDGVyEGVAIGG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32420483 |
We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
LYN | down-regulates activity 
phosphorylation
|
YY1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276929 |
Tyr254 |
SPPDYSEyMTGKKLP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26198631 |
In the case of Lyn overexpression, single mutations at either tyrosine 8, 254, or 383 severely reduced Lyn-mediated YY1 phosphorylation, suggesting that these three sites may be targets of Lyn in vivo (Fig. 3, A and B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276928 |
Tyr383 |
IHTGDRPyVCPFDGC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26198631 |
In the case of Lyn overexpression, single mutations at either tyrosine 8, 254, or 383 severely reduced Lyn-mediated YY1 phosphorylation, suggesting that these three sites may be targets of Lyn in vivo (Fig. 3, A and B). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276930 |
Tyr8 |
MASGDTLyIATDGSE |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26198631 |
In the case of Lyn overexpression, single mutations at either tyrosine 8, 254, or 383 severely reduced Lyn-mediated YY1 phosphorylation, suggesting that these three sites may be targets of Lyn in vivo (Fig. 3, A and B). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
LYN | down-regulates activity
phosphorylation
|
PPP1R8 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251405 |
Tyr264 |
FAFSGGLyGGLPPTH |
in vitro |
|
| pmid |
sentence |
| 11104670 |
Tyrosine phosphorylation of NIPP1 by Lyn was abolished by the Tyr-264 to Asp mutation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251406 |
Tyr335 |
NEPKKKKyAKEAWPG |
in vitro |
|
| pmid |
sentence |
| 11104670 |
Lyn phosphorylates both Tyr-264 and Tyr-335, but that the phosphorylation of Tyr-335 is dependent on the association of NIPP1 with RNA. The inhibitory potency of the C-terminal site of NIPP1 was decreased by phosphorylation of Tyr-335 and by the addition of RNA. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
WAS |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273959 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 17890224 |
We demonstrated that WASP is phosphorylated on tyrosine 291 in macrophages, and the WASP phosphorylation is important for the phagocytic cup formation. In addition, we showed that WASP and WASP-interacting protein (WIP) form a complex at the phagocytic cup and that the WASP.WIP complex plays a critical role in the phagocytic cup formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
FCGR2B |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249380 |
Tyr292 |
GAENTITySLLMHPD |
in vitro |
|
| pmid |
sentence |
| 8756631 |
Therefore, we conclude that FcgammaRIIb1 phosphorylation upon BCR-FcgammaR coligation is most likely due to BCR-associated Lyn |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
FCGR2A |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249379 |
Tyr304 |
TDDDKNIyLTLPPND |
in vitro |
|
| pmid |
sentence |
| 8756631 |
Phosphorylation of FcgammaRIIa/c by Lyn is clearly dependent on the presence of Y-298, since all mutants lacking this residue are not phosphorylated by this PTK. This result suggests that Y-298 might be the only tyrosine residue of FcgammaRIIa/c phos- phorylated by Lyn. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
FCGR2C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262676 |
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: |
1 |
Organism: |
In Vitro |
| + |
LYN | down-regulates activity
phosphorylation
|
IRF5 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277247 |
Tyr313 |
PSDKQRFyTNQLLDV |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 27521268 |
Lyn Kinase Suppresses the Transcriptional Activity of IRF5. Here, we found that Lyn physically interacted with IRF5 to inhibit ubiquitination and phosphorylation of IRF5 in the TLR-MyD88 pathway, thereby suppressing the transcriptional activity of IRF5 in a manner independent of Lyn's kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277248 |
Tyr335 |
QLQGQDLyAIRLCQC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 27521268 |
Lyn Kinase Suppresses the Transcriptional Activity of IRF5. Here, we found that Lyn physically interacted with IRF5 to inhibit ubiquitination and phosphorylation of IRF5 in the TLR-MyD88 pathway, thereby suppressing the transcriptional activity of IRF5 in a manner independent of Lyn's kinase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PAG1 |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262898 |
Tyr317 |
EEEISAMySSVNKPG |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16920712 |
Here we show that Lyn interacts with C-terminal Src kinase-binding protein (Cbp), an adaptor protein that recruits negative regulators C-terminal Src kinase (Csk)/Csk-like protein-tyrosine kinase (Ctk). Lyn phosphorylated Cbp on several tyrosine residues, including Tyr314, which recruited Csk/Ctk to suppress Lyn kinase activity.Thus, a single phosphotyrosine residue on Cbp coordinates a two-phase process involving distinct negative regulatory pathways to inactivate, then degrade, Lyn. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262893 |
Tyr387 |
SEEPEPDyEAIQTLN |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16920712 |
Here we show that Lyn interacts with C-terminal Src kinase-binding protein (Cbp), an adaptor protein that recruits negative regulators C-terminal Src kinase (Csk)/Csk-like protein-tyrosine kinase (Ctk). Lyn phosphorylated Cbp on several tyrosine residues, including Tyr314, which recruited Csk/Ctk to suppress Lyn kinase activity.Thus, a single phosphotyrosine residue on Cbp coordinates a two-phase process involving distinct negative regulatory pathways to inactivate, then degrade, Lyn. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262899 |
Tyr417 |
LVPKENDyESISDLQ |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16920712 |
Here we show that Lyn interacts with C-terminal Src kinase-binding protein (Cbp), an adaptor protein that recruits negative regulators C-terminal Src kinase (Csk)/Csk-like protein-tyrosine kinase (Ctk). Lyn phosphorylated Cbp on several tyrosine residues, including Tyr314, which recruited Csk/Ctk to suppress Lyn kinase activity.Thus, a single phosphotyrosine residue on Cbp coordinates a two-phase process involving distinct negative regulatory pathways to inactivate, then degrade, Lyn. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
LYN |
phosphorylation
|
SLAMF1 |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127997 |
Tyr327 |
ETNSITVyASVTLPE |
Homo sapiens |
|
| pmid |
sentence |
| 15315965 |
Cd150-mediated akt phosphorylation required syk and sh2d1a, was negatively regulated by lyn and btk, but was ship independent. Lyn directly phosphorylated y327 in cd150, but the akt pathway did not depend on cd150 tyrosine phosphorylation and cd150-shp-2 association. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN |
phosphorylation
|
SLC4A1 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251412 |
Tyr359 |
AKPDSSFyKGLDLNG |
in vitro |
|
| pmid |
sentence |
| 10942405 |
Lyn phosphorylates Y904 and Y359 of band 3. 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 movements, and anion transport. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251414 |
Tyr904 |
EEEGRDEyDEVAMPV |
in vitro |
|
| pmid |
sentence |
| 10942405 |
Lyn phosphorylates Y904 and Y359 of band 3. 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 movements, and anion transport. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
LYN | down-regulates activity
phosphorylation
|
IKBKG |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276369 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
LYN | up-regulates activity
phosphorylation
|
HCLS1 |
0.702 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251400 |
Tyr378 |
EPEPENDyEDVEEMD |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Lyn and Syk synergistically phosphorylate HS1, and that Tyr-378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis. PMID: 9104825 PMCID: PMC2196252 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251401 |
Tyr397 |
EDEPEGDyEEVLEPE |
Homo sapiens |
|
| pmid |
sentence |
| 9104825 |
Lyn and Syk synergistically phosphorylate HS1, and that Tyr-378 and Tyr-397 of HS1 are the critical residues for its BCR-induced phosphorylation. tyrosine phosphorylation of HS1 is required for BCR-induced apoptosis and nuclear translocation of HS1 may be a prerequisite for B cell apoptosis. PMID: 9104825 PMCID: PMC2196252 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN | down-regulates activity
phosphorylation
|
CASP8 |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272979 |
Tyr380 |
TDSEEQPyLEMDLSS |
|
|
| pmid |
sentence |
| 18086677 |
The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272980 |
Tyr448 |
TILTEVNyEVSNKDD |
|
|
| pmid |
sentence |
| 18086677 |
The non-receptor tyrosine kinase, Lyn, can phosphorylate caspase-8 on Tyr-397 and Tyr-465, rendering it resistant to activational cleavage and inhibiting apoptosis. |
|
| Publications: |
2 |
| + |
LYN | up-regulates activity
phosphorylation
|
MAP4K1 |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251403 |
Tyr381 |
SESSDDDyDDVDIPT |
Chlorocebus aethiops |
|
| 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. Tyr-379 within HPK1 is essential for binding to BASH and thus strongly suggest that the DDDYDDV sequence containing the phosphorylated Tyr-379 is the binding site for the BASH SH2 domain. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | EBV infection |
| + |
PTPN6 | down-regulates activity
dephosphorylation
|
LYN |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248471 |
Tyr397 |
RVIEDNEyTAREGAK |
Rattus norvegicus |
|
| pmid |
sentence |
| 15537644 |
SHP-1 efficiently inhibits Lyn autophosphorylation and suppresses FcϵRI stimulation|We found that PTPα and SHP-1 both dephosphorylate Lyn exclusively at Tyr-397 |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
LYN | up-regulates activity
phosphorylation
|
LYN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251402 |
Tyr397 |
RVIEDNEyTAREGAK |
in vitro |
|
| pmid |
sentence |
| 8530369 |
Lyn is a member of the Src family of protein-tyrosine kinases that can readily undergo autophosphorylation in vitro. The site of autophosphorylation is Tyr397. Autophosphorylation results in a 17-fold increase in protein-tyrosine kinase activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | B-cell activation, EBV infection |
| + |
PTPRC | down-regulates activity
dephosphorylation
|
LYN |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248353 |
Tyr397 |
RVIEDNEyTAREGAK |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10415030 |
CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells.| Phosphoamino acid analysis confirmed that Lyn is tyrosine phosphorylated with little serine or threonine phosphorylation. In CD45-negative cells, two bands at 8.2 and 4.1 kDa were phosphorylated in the absence of B cell Ag receptor (BCR) ligation. The 8.2-kDa band corresponded to a fragment containing the positive regulatory site (Tyr397), as assessed by its size and its phosphorylation in an in vitro kinase assay. The 4.1-kDa band was phosphorylated by COOH-terminal Src kinase, suggesting that it contains the COOH-terminal negative regulatory site (Tyr508) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248354 |
Tyr508 |
YTATEGQyQQQP |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10415030 |
CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells.| Phosphoamino acid analysis confirmed that Lyn is tyrosine phosphorylated with little serine or threonine phosphorylation. In CD45-negative cells, two bands at 8.2 and 4.1 kDa were phosphorylated in the absence of B cell Ag receptor (BCR) ligation. The 8.2-kDa band corresponded to a fragment containing the positive regulatory site (Tyr397), as assessed by its size and its phosphorylation in an in vitro kinase assay. The 4.1-kDa band was phosphorylated by COOH-terminal Src kinase, suggesting that it contains the COOH-terminal negative regulatory site (Tyr508) |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PTPRA | down-regulates activity
dephosphorylation
|
LYN |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248436 |
Tyr397 |
RVIEDNEyTAREGAK |
Rattus norvegicus |
|
| pmid |
sentence |
| 15537644 |
We found that PTPα and SHP-1 both dephosphorylate Lyn exclusively at Tyr-397|Lyn expressed in CHO cells has a substantially higher specific activity than Lyn in RBL cells because of high levels of phosphorylation at its active site Tyr-397 (Fig. 1). Enhanced Lyn kinase activity in the CHO cells leads to spontaneous phosphorylation of multiple cellular proteins, including FcϵRI |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
LYN |
phosphorylation
|
PDIA3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262894 |
Tyr445 |
ANDVPSPyEVRGFPT |
in vitro |
|
| pmid |
sentence |
| 8631326 |
Lyn phosphorylates tyrosine residues Y444, Y453 and Y466 which are located in a highly acidic region of the protein at the C-terminus. Upon phosphorylation, p57 forms a complex with Lyn which can be immunoprecipitated with anti-Lyn IgG. The association which occurs between the phosphorylated substrate and the SH2 domain of the kinase is consistent with the suggested 'processive phosphorylation' model, which implies that a primary phosphorylation site of the substrate binds to the SH2 domain of the enzyme and triggers the phosphorylation at secondary site(s). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262895 |
Tyr454 |
VRGFPTIyFSPANKK |
in vitro |
|
| pmid |
sentence |
| 8631326 |
Lyn phosphorylates tyrosine residues Y444, Y453 and Y466 which are located in a highly acidic region of the protein at the C-terminus. Upon phosphorylation, p57 forms a complex with Lyn which can be immunoprecipitated with anti-Lyn IgG. The association which occurs between the phosphorylated substrate and the SH2 domain of the kinase is consistent with the suggested 'processive phosphorylation' model, which implies that a primary phosphorylation site of the substrate binds to the SH2 domain of the enzyme and triggers the phosphorylation at secondary site(s). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262896 |
Tyr467 |
KKLNPKKyEGGRELS |
in vitro |
|
| pmid |
sentence |
| 8631326 |
Lyn phosphorylates tyrosine residues Y444, Y453 and Y466 which are located in a highly acidic region of the protein at the C-terminus. Upon phosphorylation, p57 forms a complex with Lyn which can be immunoprecipitated with anti-Lyn IgG. The association which occurs between the phosphorylated substrate and the SH2 domain of the kinase is consistent with the suggested 'processive phosphorylation' model, which implies that a primary phosphorylation site of the substrate binds to the SH2 domain of the enzyme and triggers the phosphorylation at secondary site(s). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
LYN | up-regulates
phosphorylation
|
CD19 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80290 |
Tyr500 |
TSLGSQSyEDMRGIL |
Homo sapiens |
|
| pmid |
sentence |
| 10933394 |
Experiments with purified proteins demonstrated that cd19-y513 was lyn's initial phosphorylation and binding site. This led to processive phosphorylation of cd19-y482, which recruited a second lyn molecule, allowing for transphosphorylation and amplification of lyn activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80294 |
Tyr531 |
HEEDADSyENMDNPD |
Homo sapiens |
|
| pmid |
sentence |
| 10933394 |
Experiments with purified proteins demonstrated that cd19-y513 was lyn's initial phosphorylation and binding site. This led to processive phosphorylation of cd19-y482, which recruited a second lyn molecule, allowing for transphosphorylation and amplification of lyn activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation, EBV infection |
| + |
LYN | up-regulates activity
phosphorylation
|
CD19 |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249376 |
Tyr500 |
TSLGSQSyEDMRGIL |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10933394 |
Experiments with purified proteins demonstrated that CD19-Y513 was Lyn's initial phosphorylation and binding site. This led to processive phosphorylation of CD19-Y482, which recruited a second Lyn molecule, allowing for transphosphorylation and amplification of Lyn activation|Tyrosine phosphorylation of CD19 following BCR and/or CD19 ligation provides Src homology 2 (SH2) recognition motifs that recruit regulatory molecules to the cell surface. CD19 dually phosphorylated at CD19Y482 and CD19Y513 binds the tandem SH2 domains of phosphatidylinositol 3-kinase (PI 3-kinase) p85 subuni |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249377 |
Tyr531 |
HEEDADSyENMDNPD |
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 10933394 |
Experiments with purified proteins demonstrated that CD19-Y513 was Lyn's initial phosphorylation and binding site. This led to processive phosphorylation of CD19-Y482, which recruited a second Lyn molecule, allowing for transphosphorylation and amplification of Lyn activation|Tyrosine phosphorylation of CD19 following BCR and/or CD19 ligation provides Src homology 2 (SH2) recognition motifs that recruit regulatory molecules to the cell surface. CD19 dually phosphorylated at CD19Y482 and CD19Y513 binds the tandem SH2 domains of phosphatidylinositol 3-kinase (PI 3-kinase) p85 subuni |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242891 |
|
|
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 25673924 |
CD19 has an extracellular region containing two C2-type Ig-like domains and a cytoplasmic region of ~240 amino acids with 9 conserved tyrosine residues24. Lyn, a Src-family protein tyrosine kinase member, is the dominant kinase that phosphorylates CD19 upon stimulation. Once tyrosyl-phosphorylated, CD19 serves as a membrane-bound adaptor protein for Src homology 2-containing signaling molecules such as Lyn, Vav, and phosphatidylinositol 3-kinase, which further mediate downstream activation cascades. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| Pathways: | B-cell activation, EBV infection |
| + |
CSK | down-regulates
phosphorylation
|
LYN |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132912 |
Tyr508 |
YTATEGQyQQQP |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 15626731 |
Lyn tyr507 kinase, csk, is recruited by pag, which targets lipid rafts by palmitoylation.Thus, our data suggest that il-6 treatment induces the translocation of cd45 to lipid rafts sequentially, followed by the association of cd45 with lyn and pag;dephosphorylation of lyn tyr507 and pag tyr314;lyn activation;and csk release from lipid rafts |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
MATK | down-regulates activity
phosphorylation
|
LYN |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250177 |
Tyr508 |
YTATEGQyQQQP |
in vitro |
|
| pmid |
sentence |
| 9171348 |
In vitro phosphorylation assays showed that Chk suppressed Lyn activity by phosphorylating its C-terminal negative regulatory tyrosine. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
PRKCD |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251408 |
Tyr52 |
VQKKPTMyPEWKSTF |
in vitro |
|
| pmid |
sentence |
| 9692543 |
Lyn was found to phosphorylate Lyn-associated and recombinant PKC-delta in vitro and the tyrosine 52 phosphorylated PKC-delta was recruited to associate with the Lyn SH2 domain. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates
phosphorylation
|
BTK |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-41607 |
Tyr551 |
RYVLDDEyTSSVGSK |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 8630736 |
Phosphorylation at y551 requires lyn kinase activity, indicating that y551 is a transphosphorylation site \ this transphosphorylation at y551 is followed by phosphorylation at a second site, which is dependent on btk catalytic activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates activity
phosphorylation
|
PTPN6 |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251409 |
Tyr564 |
SKHKEDVyENLHTKN |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10574931 |
Lyn phosphorylates SHPTP1 at the C-terminal Tyr-564 site. Lyn-mediated phosphorylation of SHPTP1 stimulates SHPTP1 tyrosine phosphatase activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | down-regulates activity
phosphorylation
|
PRKCD |
0.539 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251407 |
Tyr567 |
IRVDTPHyPRWITKE |
in vitro |
|
| pmid |
sentence |
| 11812791 |
Src, Fyn, or Lyn are the essential kinases that tyrosine phosphorylate and inactivate PKC δ. Lyn phosphorylates tyrosine residue 565 in vitro |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | up-regulates activity
phosphorylation
|
LPXN |
0.383 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262892 |
Tyr72 |
NIQELNVySEAQEPK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17640867 |
Of a total of 11 tyrosine sites in LPXN, we mutated Tyr(22), Tyr(72), Tyr(198), and Tyr(257) to phenylalanine and demonstrated that LPXN was phosphorylated by Lyn only at Tyr(72) and that this tyrosine site is proximal to the LD3 domain. We further show that LPXN suppressed the secretion of interleukin-2 by BCR-activated A20 B cells and that this inhibition was abrogated in the Y72F LPXN mutant, indicating that the phosphorylation of Tyr(72) is critical for the biological function of LPXN. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PLCG2 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249383 |
Tyr753 |
ERDINSLyDVSRMYV |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249384 |
Tyr759 |
LYDVSRMyVDPSEIN |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates activity
phosphorylation
|
PLCG1 |
0.642 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249381 |
Tyr771 |
IGTAEPDyGALYEGR |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249382 |
Tyr783 |
EGRNPGFyVEANPMP |
in vitro |
|
| pmid |
sentence |
| 7682059 |
The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | B-cell activation |
| + |
LYN | down-regulates activity
phosphorylation
|
SOCS1 |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277888 |
Tyr80 |
LLDACGFyWGPLSVH |
in vitro |
|
| pmid |
sentence |
| 31101761 |
These findings show that SOCS1 phosphorylation by the SRC family inhibits its tumor-suppressive activity, indicating that patients with increased SOCS1 phosphorylation may benefit from SRC family kinase inhibitors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
LYN | down-regulates
phosphorylation
|
CDKN1B |
0.535 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172904 |
Tyr88 |
KGSLPEFyYRPPRPP |
Homo sapiens |
|
| pmid |
sentence |
| 21423214 |
We previously reported that y88 phosphorylation of p27(kip1) by oncogenic tyrosine kinases impairs p27(kip1)-mediated cdk inhibition, and initiates its ubiquitin-dependent proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
BCR-Ml |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268209 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
CD19 | up-regulates activity
binding
|
LYN |
0.763 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242894 |
|
|
Mus musculus |
B-lymphocyte |
| pmid |
sentence |
| 25673924 |
CD19 has an extracellular region containing two C2-type Ig-like domains and a cytoplasmic region of ~240 amino acids with 9 conserved tyrosine residues24. Lyn, a Src-family protein tyrosine kinase member, is the dominant kinase that phosphorylates CD19 upon stimulation. Once tyrosyl-phosphorylated, CD19 serves as a membrane-bound adaptor protein for Src homology 2-containing signaling molecules such as Lyn, Vav, and phosphatidylinositol 3-kinase, which further mediate downstream activation cascades. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | B-cell activation, EBV infection |
| + |
LYN | up-regulates
phosphorylation
|
PPP1R15A |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109934 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11517336 |
Gadd34 was tyrosine-phosphorylated in vivo in a lyn-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ponatinib | down-regulates activity
chemical inhibition
|
LYN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259273 |
|
|
Homo sapiens |
Mast Cell |
| pmid |
sentence |
| 23539538 |
Ponatinib was found to inhibit the kinase activity of KIT G560V and KIT D816V in the human mast cell leukemia cell line HMC-1. In addition, ponatinib was found to block Lyn- and STAT5 activity in neoplastic mast cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Bafetinib | down-regulates
chemical inhibition
|
LYN |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190227 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRO | down-regulates activity
dephosphorylation
|
LYN |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20564182 |
Both Lyn and ZAP70 were dephosphorylated by wild-type PTPROt, but not by its catalytic site mutant.|Lyn kinase and ZAP70 are substrates of PTPROt in B-cells: Lyn inactivation by PTPROt sensitizes leukemia cells to VEGF-R inhibitor pazopanib. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
BCR-Mk |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268206 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates activity
phosphorylation
|
BCR-Dl |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268215 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
LYN | down-regulates activity
phosphorylation
|
CD22 |
0.733 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268443 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
LYN is a BCR-associated SRC kinase involved in the positive regulation of BCR, but it also functions as a negative regulator by phosphorylating the immunoreceptor tyrosine-based inhibitory motifs (ITIMs) of CD22. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
LYN | up-regulates activity
phosphorylation
|
BCR-Dk |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268212 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 32323266 |
The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | B-cell activation |
| + |
NEDD4 | down-regulates quantity by destabilization
polyubiquitination
|
LYN |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272558 |
|
|
Homo sapiens |
BJAB Cell |
| pmid |
sentence |
| 10683340 |
These findings suggest that LMP2A recruits Nedd4-like ubiquitin-protein ligases and B-cell signal transduction molecules, resulting in the degradation of LMP2A and Lyn by a ubiquitin-dependent mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
DOK3 |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268447 |
|
|
Homo sapiens |
B-lymphocyte |
| 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 |
3.0
LYN
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- 