| + |
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 |
0.244 |
| 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
|
EGFR |
0.602 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279205 |
Tyr1125 |
APSRDPHyQDPHSTA |
Homo sapiens |
|
| pmid |
sentence |
| 22430206 |
Taken together, our findings demonstrate that Yes and Lyn phosphorylate EGFR at Y1101 which influences EGFR nuclear translocation in this model of cetuximab resistance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
PTGS2 |
0.381 |
| 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 |
0.641 |
| 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 | down-regulates activity 
phosphorylation
|
CDK2 |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279204 |
Tyr15 |
EKIGEGTyGVVYKAR |
Homo sapiens |
|
| pmid |
sentence |
| 8806683 |
We also show that Lyn phosphorylates Tyr15 of Cdk2 and that incubation of Lyn with Cdk2 results in inhibition of Cdk2 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
RGS16 |
0.338 |
| 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 |
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4.0
LYN
- 
- 