Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-249999	Ser42	TLLIRNGsEVRDPLV	in vitro
pmid	sentence
8506364	Ser-42 can be phosphorylated by either protein kinase A or protein kinase C

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248936	Ser42	TLLIRNGsEVRDPLV	in vitro
pmid	sentence
8506364	In vitro kinase assays show that Ser-59 can be uniquely phosphorylated by mitogen-activated protein kinase and that Ser-42 can be phosphorylated by either protein kinase A or protein kinase C.

Publications:

1

Organism:

In Vitro

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249469	Ser59	EGSNPPAsPLQDNLV	Homo sapiens	HeLa Cell
pmid	sentence
8618896	Phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62.\|phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p56lck signaling that is regulated by Ser-59 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249412	Ser59	EGSNPPAsPLQDNLV	Homo sapiens	HeLa Cell
pmid	sentence
8618896	Phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62.\|phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p56lck signaling that is regulated by Ser-59 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-247058	Tyr1229	SSTDRSPyEKVSAGN	Homo sapiens
pmid	sentence
14766232	The present results demonstrate that Lck phosphorylation of MUC1 on Y-46 also increases binding of MUC1 and _-catenin. The results further show that ZAP-70 phosphorylation of MUC1-CD stimulates the interaction of MUC1 and _-catenin

Identifier	Residue	Sequence	Cell Line
SIGNOR-249358	Tyr1229	SSTDRSPyEKVSAGN	JURKAT Cell
pmid	sentence
14766232	The present results demonstrate that Lck phosphorylation of MUC1 on Y-46 also increases binding of MUC1 and beta-catenin. The results further show that ZAP-70 phosphorylation of MUC1-CD stimulates the interaction of MUC1 and beta-catenin

Publications:

2

Organism:

Homo Sapiens,

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251366	Tyr132	QLIIEDPyYGNDSDF	Chlorocebus aethiops	COS Cell
pmid	sentence
9038134	In co-transfected COS cells, Lck and Fyn caused phosphorylation of LMPTP. Most of the phosphate was located at Tyr-131, and some was also located at Tyr-132. Site-directed mutagenesis showed that Tyr-131 is important for the catalytic activity of LMPTP, and that thiophosphorylation of Tyr-131, and to a lesser degree Tyr-132, is responsible for the activation.

Identifier	Residue	Sequence	Organism
SIGNOR-251367	Tyr133	LIIEDPYyGNDSDFE	Chlorocebus aethiops
pmid	sentence
9038134	In co-transfected COS cells, Lck and Fyn caused phosphorylation of LMPTP. Most of the phosphate was located at Tyr-131, and some was also located at Tyr-132. Site-directed mutagenesis showed that Tyr-131 is important for the catalytic activity of LMPTP, and that thiophosphorylation of Tyr-131, and to a lesser degree Tyr-132, is responsible for the activation.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-253367	Tyr133	NFLSEDKyPLIMVPD	Homo sapiens
pmid	sentence
18976935	Here, we report that the T cell receptor (TCR)-induced translocation of SLAT to the immunological synapse required Lck-mediated phosphorylation of two tyrosine residues located in an immunoreceptor tyrosine-based activation motif-like sequence but was independent of the SLAT PH domain. This subcellular relocalization was coupled to, and necessary for, activation of the NFAT pathway\|These results indicate that SLAT undergoes Lck-dependent phosphorylation on Tyr-144 and Tyr-133 upon TCR and CD28 stimulation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-253368	Tyr144	MVPDEVEyLLKKVLS	Homo sapiens	JURKAT Cell
pmid	sentence
18976935	Here, we report that the T cell receptor (TCR)-induced translocation of SLAT to the immunological synapse required Lck-mediated phosphorylation of two tyrosine residues located in an immunoreceptor tyrosine-based activation motif-like sequence but was independent of the SLAT PH domain. This subcellular relocalization was coupled to, and necessary for, activation of the NFAT pathway\|These results indicate that SLAT undergoes Lck-dependent phosphorylation on Tyr-144 and Tyr-133 upon TCR and CD28 stimulation.

Identifier	Residue	Sequence	Organism
SIGNOR-251372	Tyr210	SMAIHEVyQELIQDV	in vitro
pmid	sentence
12923183	In vitro kinase assays indeed demonstrated that Lck can phosphorylate wild-type IBP but not the Y210F mutant. IBP Binds PI(3,4,5)P3 upon Phosphorylation by Lck

Publications:

3

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence
SIGNOR-249373	Tyr139	KVEEPSIyESVRVHT
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

Identifier	Residue	Sequence	Organism
SIGNOR-251389	Tyr142	SVGDEDIySGLSDQI	in vitro
pmid	sentence
10669745	Lck recognizes preferentially the tyrosine residue of Vav located at position 174 and, with significantly less affinity, those present at positions 142 and 160. It is now clear that this posttranslational modification will be involved in the activation of Vav, in the regulation of the strength of the signals emanating from this molecule, and also in the negative regulation of its function.

Identifier	Residue	Sequence	Organism
SIGNOR-251390	Tyr160	VEEDEDLyDCVENEE	in vitro
pmid	sentence
10669745	Lck recognizes preferentially the tyrosine residue of Vav located at position 174 and, with significantly less affinity, those present at positions 142 and 160. It is now clear that this posttranslational modification will be involved in the activation of Vav, in the regulation of the strength of the signals emanating from this molecule, and also in the negative regulation of its function.

Identifier	Residue	Sequence	Organism
SIGNOR-251391	Tyr174	EAEGDEIyEDLMRSE	in vitro
pmid	sentence
10669745	Lck recognizes preferentially the tyrosine residue of Vav located at position 174 and, with significantly less affinity, those present at positions 142 and 160. It is now clear that this posttranslational modification will be involved in the activation of Vav, in the regulation of the strength of the signals emanating from this molecule, and also in the negative regulation of its function.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251374	Tyr146	KEVHKSGyLSSERLI	in vitro
pmid	sentence
12560083	Lck phosphorylated ezrin in vitro, and the major phosphotyrosine was identified as Y145. Whether tyrosine phosphorylation of ezrin is an alternative mechanism to regulate dynamic changes of the actin cytoskeleton, as has been suggested in EGF-, PDGF- or HGF-treated epithelial cells, is still unclear. Alternatively, Lck-induced tyrosine phosphorylation of ezrin may be linked to its other functions, including participation in signaling pathways that control proliferation and apoptosis

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276240	Tyr153	KMTTNPIyEHIGYAT	Homo sapiens	JURKAT Cell
pmid	sentence
19201754	We now demonstrate Lck-dependent phosphorylation of beta2-chimaerin in response to TCR triggering. We identify Tyr-153 as the Lck-dependent phosphorylation residue and show that its phosphorylation negatively regulates membrane stabilization of beta2-chimaerin, decreasing its GAP activity to Rac.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251392	Tyr178	EEAERKLySGAQTDG	Homo sapiens	JURKAT Cell
pmid	sentence
7961936	We show that ZAP-70 has a primary autophosphorylation site at Tyr-292, with a secondary site at Tyr-126. We also show additional phosphorylation at Tyr-69, Tyr-178, Tyr-492, and Tyr-493 upon the addition of the protein tyrosine kinase, p56lck.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251396	Tyr69	ERQLNGTyAIAGGKA	Homo sapiens	JURKAT Cell
pmid	sentence
7961936	We show that ZAP-70 has a primary autophosphorylation site at Tyr-292, with a secondary site at Tyr-126. We also show additional phosphorylation at Tyr-69, Tyr-178, Tyr-492, and Tyr-493 upon the addition of the protein tyrosine kinase, p56lck.

Publications:

2

Organism:

Homo Sapiens

Pathways:

P38 Signaling, T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251368	Tyr188	PPVPNPDyEPIRKGQ	Chlorocebus aethiops	COS Cell
pmid	sentence
11855827	Tyrosine Phosphorylation of CD8- Chimeras by Lck and ZAP-70 in COS Cells. both Y170F and Y181F chimeric proteins could be efficiently phosphorylated by Lck in vivo. phosphorylation of Y170 and Y181 within CD3- –ITAM provides to CD3- the potential to interact with multiple downstream effectors and signaling pathways.

Identifier	Residue	Sequence	Organism
SIGNOR-251369	Tyr199	RKGQRDLySGLNQRR	Chlorocebus aethiops
pmid	sentence
11855827	Tyrosine Phosphorylation of CD8- Chimeras by Lck and ZAP-70 in COS Cells. both Y170F and Y181F chimeric proteins could be efficiently phosphorylated by Lck in vivo. phosphorylation of Y170 and Y181 within CD3- –ITAM provides to CD3- the potential to interact with multiple downstream effectors and signaling pathways.

Identifier	Residue	Organism
SIGNOR-259930		Mus musculus
pmid	sentence
2470098	Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex.

Publications:

3

Organism:

Chlorocebus Aethiops, Mus Musculus

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-198755	Tyr191	SRLLHSDyMNMTPRR	Homo sapiens
pmid	sentence
22936936	We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-45524	Tyr191	SRLLHSDyMNMTPRR	Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
8992971	We demonstrate that emt can phosphorylate all four tyrosines of the cd28 tail, in contrast to lck, which phosphorylates only tyrosine 173. Together with evidence that in vivo, tyrosines other than tyrosine 173 become phosphorylated following cd28 stimulation, this finding suggests that, like lck, one function of emt during cd28 signaling is phosphorylation of the receptor

Publications:

2

Organism:

Homo Sapiens

Pathways:

T cell activation

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

Identifier	Residue	Sequence	Organism
SIGNOR-276279	Tyr193	NVDDSKEyFSKHN	in vitro
pmid	sentence
20178744	Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273525	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-273526	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-273527	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-273528	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

Identifier	Residue	Sequence	Organism
SIGNOR-276277	Tyr194	DVQKSKEyFSKQK	in vitro
pmid	sentence
20178744	Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. To determine whether Prxs are phosphorylated, we subjected recombinant human PrxI and II to an in vitro kinase assay with two nonreceptor PTKs, Lck and Abl, in the presence of [γ-32P]ATP. Both PTKs phosphorylated PrxI and PrxII. Phosphorylation of the wild-type protein was detected, whereas that of the Y194F mutant was not (Figure 1B), indicating that Tyr194 is the only site of tyrosine phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149182	Tyr200	SMESIDDyVNVPESG	Homo sapiens	T-lymphocyte
pmid	sentence
16938345	Evidence of lat as a dual substrate for lck and syk in t lymphocytes.Lat is a linker protein essential for activation of t lymphocytes. Its rapid tyrosine-phosphorylation upon t cell receptor (tcr) stimulation recruits downstream signaling molecules for membrane targeting and activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149186	Tyr220	SLDGSREyVNVSQEL	Homo sapiens	T-lymphocyte
pmid	sentence
16938345	Evidence of lat as a dual substrate for lck and syk in t lymphocytes.Lat is a linker protein essential for activation of t lymphocytes. Its rapid tyrosine-phosphorylation upon t cell receptor (tcr) stimulation recruits downstream signaling molecules for membrane targeting and activation.

Publications:

2

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-251370	Tyr201	SPLTTGVyVKMPPTE	Homo sapiens
pmid	sentence
9973379	Lck and Fyn, but not ZAP70, induce tyrosine phosphorylation of CTLA-4 in the cell line HEK293. Phosphorylation of CTLA-4 occurs on both Y201 and Y218. Phosphorylation of Y201 correlated with accumulation of CTLA-4 on the cell surface.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-159168	Tyr204	HTGFLTEyVATRWYR	Homo sapiens
pmid	sentence
17998336	The sh3 domain of lck modulates t-cell receptor-dependent activation of extracellular signal-regulated kinase through activation of raf-1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-262853	Tyr217	MAEEKKAyKKAKERE	Homo sapiens
pmid	sentence
19059208	We found that Ymer was considerably phosphorylated on tyrosine residues also via Src family kinases such as Lck. A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262854	Tyr279	TDGEDADyTHFTNQQ	Homo sapiens	HeLa Cell
pmid	sentence
19059208	We found that Ymer was considerably phosphorylated on tyrosine residues also via Src family kinases such as Lck. A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262855	Tyr304	SSHKGFHyKH	Homo sapiens	HeLa Cell
pmid	sentence
19059208	We found that Ymer was considerably phosphorylated on tyrosine residues also via Src family kinases such as Lck. A luciferase reporter assay showed that mutation of tyrosines on Ymer (YmerY217/279/304F) results in loss of the inhibitory activity for NF-kappaB signaling.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251371	Tyr218	CEKQFQPyFIPIN	Homo sapiens	HEK-293 Cell
pmid	sentence
9973379	Lck and Fyn, but not ZAP70, induce tyrosine phosphorylation of CTLA-4 in the cell line HEK293. Phosphorylation of CTLA-4 occurs on both Y201 and Y218.the role of Y218 in CTLA-4 biology is not known at the present

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273649	Tyr23	AREKLALyVYEYLLH	Homo sapiens	HEK-293 Cell
pmid	sentence
18080319	The Src tyrosine kinase inhibitor PP2 blocked the nuclear translocation of Ssdp1. Western blot analysis showed that co-expression of Ssdp1 and Lck in 293T cells induces Ssdp1 phosphorylation. Mutation of the Ssdp1 N terminal tyrosine residues 23 and 25 markedly reduced both the phosphorylation and the nuclear localization of Ssdp1. Lck enhanced the transcriptional activity of Ssdp1 in the context of known components of a LIM-homeodomain (LIM-HD)/cofactor complex.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273648	Tyr25	EKLALYVyEYLLHVG	Homo sapiens	HEK-293 Cell
pmid	sentence
18080319	The Src tyrosine kinase inhibitor PP2 blocked the nuclear translocation of Ssdp1. Western blot analysis showed that co-expression of Ssdp1 and Lck in 293T cells induces Ssdp1 phosphorylation. Mutation of the Ssdp1 N terminal tyrosine residues 23 and 25 markedly reduced both the phosphorylation and the nuclear localization of Ssdp1. Lck enhanced the transcriptional activity of Ssdp1 in the context of known components of a LIM-homeodomain (LIM-HD)/cofactor complex.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275984	Tyr240	RREDKFMyFEFPQPL	Homo sapiens	U-251MG Cell
pmid	sentence
11948419	MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275983	Tyr315	RADNDKEyLVLTLTK	Homo sapiens	U-251MG Cell
pmid	sentence
11948419	MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-48850	Tyr273	LEMPDNLyTFVLKVK	Homo sapiens
pmid	sentence
9169414	In vitro tyrosine phosphorylation of lnk by lck and zap-70. Tyrosine 297 would appear to be an attractive target for phosphorylation within the c-terminal domain. Our studies suggest that although lnk may participate in tcr signaling, its functions are in no way limiting during t cell development or activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262888	Tyr280	PKPSNPIyNEPDEPI	Homo sapiens	T-lymphocyte
pmid	sentence
18541536	Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262889	Tyr290	PDEPIAFyAMGRGSP	Homo sapiens	T-lymphocyte
pmid	sentence
18541536	Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition.

Identifier	Residue	Sequence	Organism
SIGNOR-262890	Tyr305	GEAPSNIyVEVEDEG	Homo sapiens
pmid	sentence
18541536	Here we mapped Lck phosphorylation and interaction sites on TSAd and evaluated their functional importance. The three C-terminal TSAd tyrosines Tyr(280), Tyr(290), and Tyr(305) were phosphorylated by Lck and functioned as docking sites for the Lck Src homology 2 (SH2) domain. Lck binds to TSAd prolines and phosphorylates and interacts with the three C-terminal TSAd tyrosines. We propose that through multivalent interactions with Lck, TSAd diverts Lck from phosphorylating other substrates, thus modulating its functional activity through substrate competition.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251384	Tyr313	SSEPVGIyQGFEKKT	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11381116	The tyrosine phosphorylation sites of PKC delta in the H(2)O(2)-treated cells were identified as Tyr-311, Tyr-332, and Tyr-512 by mass spectrometric analysis with the use of the precursor-scan method and by immunoblot analysis with the use of phosphorylation site-specific antibodies. Tyr-311 was the predominant modification site among them. In an in vitro study, phosphorylation at this site by Lck, a non-receptor-type tyrosine kinase, enhanced the basal enzymatic activity and elevated its maximal velocity in the presence of diacylglycerol. phosphorylation at Tyr-311 between the regulatory and catalytic domains is a critical step for generation of the active PKC delta in response to H(2)O(2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251385	Tyr334	MQDNSGTyGKIWEGS	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11381116	The tyrosine phosphorylation sites of PKC delta in the H(2)O(2)-treated cells were identified as Tyr-311, Tyr-332, and Tyr-512 by mass spectrometric analysis with the use of the precursor-scan method and by immunoblot analysis with the use of phosphorylation site-specific antibodies. Tyr-311 was the predominant modification site among them. In an in vitro study, phosphorylation at this site by Lck, a non-receptor-type tyrosine kinase, enhanced the basal enzymatic activity and elevated its maximal velocity in the presence of diacylglycerol. phosphorylation at Tyr-311 between the regulatory and catalytic domains is a critical step for generation of the active PKC delta in response to H(2)O(2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251386	Tyr514	TFCGTPDyIAPEILQ	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11381116	The tyrosine phosphorylation sites of PKC delta in the H(2)O(2)-treated cells were identified as Tyr-311, Tyr-332, and Tyr-512 by mass spectrometric analysis with the use of the precursor-scan method and by immunoblot analysis with the use of phosphorylation site-specific antibodies. Tyr-311 was the predominant modification site among them. In an in vitro study, phosphorylation at this site by Lck, a non-receptor-type tyrosine kinase, enhanced the basal enzymatic activity and elevated its maximal velocity in the presence of diacylglycerol. phosphorylation at Tyr-311 between the regulatory and catalytic domains is a critical step for generation of the active PKC delta in response to H(2)O(2).

Publications:

3

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-116499	Tyr315	RADNDKEyLVLTLTK	Homo sapiens
pmid	sentence
11948419	Thus, y240a and y315a are involved in the ability of mmac/pten to dephosphorylate ptdins and regulate tumor cell growth in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251393	Tyr319	TSVYESPySDPEELK	Mus musculus	T-lymphocyte
pmid	sentence
10037717	the protein tyrosine kinase (PTK) ZAP-70 is rapidly phosphorylated on several tyrosine residues, presumably by two mechanisms: an autophosphorylation and a trans-phosphorylation by the Src-family PTK Lck. we demonstrate that phosphorylation of Tyr319 is required for the positive regulation of ZAP-70 function

Identifier	Residue	Sequence	Organism
SIGNOR-273948	Tyr319	TSVYESPySDPEELK	in vitro
pmid	sentence
10202147	In this report, we identify Tyr319 as a functionally important phosphorylation site in the ZAP-70 interdomain B region. Phosphorylation of Tyr319 promoted the association of ZAP-70 with the SH2 domains of two key signaling molecules, Lck and PLC-gamma1. These studies suggest that Tyr319 phosphorylation is required for the assembly of a ZAP-70-containing signaling complex that leads to the activation of the PLC-gamma1- and Ras-dependent signaling cascades in antigen-stimulated T cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249375	Tyr474	VLLVNRHyAKISDFG	Homo sapiens	JURKAT Cell
pmid	sentence
9685404	We show that ZAP-70 has a primary autophosphorylation site at Tyr-292, with a secondary site at Tyr-126. We also show additional phosphorylation at Tyr-69, Tyr-178, Tyr-492, and Tyr-493 upon the addition of the protein tyrosine kinase, p56lck

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-30429	Tyr492	ALGADDSyYTARSAG	Homo sapiens	T-lymphocyte
pmid	sentence
7642520	When expressed in COS cells, Y493F-mutated ZAP-70 demonstrated normal basal kinase activity, but, unlike wild type ZAP-70, could not be activated by tyrosine phosphorylation induced by incubation with pervanadate or by co-expression of constitutively activated Lck

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251395	Tyr493	LGADDSYyTARSAGK	Homo sapiens	JURKAT Cell
pmid	sentence
7961936	We show that ZAP-70 has a primary autophosphorylation site at Tyr-292, with a secondary site at Tyr-126. We also show additional phosphorylation at Tyr-69, Tyr-178, Tyr-492, and Tyr-493 upon the addition of the protein tyrosine kinase, p56lck.

Identifier	Residue	Sequence	Organism
SIGNOR-226628	Tyr493	LGADDSYyTARSAGK	in vitro
pmid	sentence
8756661	these data suggest that phosphorylation of ZAP-70 is initiated by a heterologous trans-phosphorylation of ZAP-70 by Lck on Tyr- 493.

Identifier	Residue	Organism
SIGNOR-67443		Homo sapiens
pmid	sentence
10318843	Phosphopeptide encompassing the motif harboring tyr319, ysdp, interacted with lcksh2;tyr319-mediated binding of the sh2 domain of lck is crucial for zap-70 activation and consequently for the propagation of the signaling cascade leading to t-cell activation

Identifier	Residue	Organism
SIGNOR-43659		Homo sapiens
pmid	sentence
8798643	Phosphopeptide encompassing the motif harboring tyr319, ysdp, interacted with lcksh2;tyr319-mediated binding of the sh2 domain of lck is crucial for zap-70 activation and consequently for the propagation of the signaling cascade leading to t-cell activation

Publications:

8

Organism:

Mus Musculus, In Vitro, Homo Sapiens

Pathways:

P38 Signaling, T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276029	Tyr323	DEPVADPyDQSFESR	Mus musculus	T-lymphocyte
pmid	sentence
15735648	Lck, Fyn, and Zap70 activate p38 even in the absence of Tyr182 phosphorylation.p38 is a substrate for Fyn, Lck and Zap70.Thus, T cell Src family kinases and Zap70 activate p38 by phosphorylating Tyr323.

Publications:

1

Organism:

Mus Musculus

Pathways:

Glucocorticoid receptor Signaling, P38 Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-78960	Tyr340	EMDEELHyASLNFHG	Homo sapiens
pmid	sentence
10887109	Human cd33 has two tyrosine residues in its cytoplasmic domain (y340 and y358). When phosphorylated, these tyrosines could function as docking sites for the phosphatases, shp-1 and/or shp-2, enabling cd33 to function as an inhibitory receptor. Lck is effective at phosphorylating y340

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-203089	Tyr342	NMRPPFTyATLIRWA	Homo sapiens
pmid	sentence
24155921	Lck phosphorylated tyr-342 of foxp3 by immunoprecipitation and in vitro kinase assay, and the replacement of tyr-342 with phenylalanine (y342f) abolished the ability to suppress mmp9 expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251375	Tyr381	EIEACQVyFTYDPYS	in vitro
pmid	sentence
10214954	Recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510.

Identifier	Residue	Sequence	Organism
SIGNOR-251376	Tyr384	ACQVYFTyDPYSEED	in vitro
pmid	sentence
10214954	Recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510.

Identifier	Residue	Sequence	Organism
SIGNOR-251377	Tyr387	VYFTYDPySEEDPDE	in vitro
pmid	sentence
10214954	Recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510.

Identifier	Residue	Sequence	Organism
SIGNOR-251378	Tyr418	LSGEDDAyCTFPSRD	in vitro
pmid	sentence
10214954	Recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510.

Identifier	Residue	Sequence	Organism
SIGNOR-251379	Tyr536	LPLNTDAyLSLQELQ	in vitro
pmid	sentence
10214954	Recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248836	Tyr394	RLIEDNEyTAREGAK	Homo sapiens
pmid	sentence
16461343	In vitro experiments with purified recombinant proteins demonstrated that PTPN22-D195A/C227S interacted directly with activated Lck, Zap70, and TCRzeta, confirming the initial substrate trap results. Native PTPN22 dephosphorylated Lck and Zap70 at their activating tyrosine residues Tyr-394 and Tyr-493, respectively, but not at the regulatory tyrosines Tyr-505 (Lck) or Tyr-319 (Zap70). Native PTPN22 also dephosphorylated TCRzeta in vitro and in cells, and its substrate trap variant co-immunoprecipitated with TCRzeta when both were coexpressed in 293T cells, establishing TCRzeta as a direct substrate of PTPN22.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248351	Tyr394	RLIEDNEyTAREGAK	Homo sapiens
pmid	sentence
11259588	Importantly, and in disagreement with the model that CD45 only activates Lck in vivo, the kinase activity of Lck from cells lacking CD45 was substantially increased. These results support a model in which CD45 dephosphorylates both Tyr505 and Tyr394, the net effect in normal thymocytes being a decrease in enzymatic activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-106604	Tyr394	RLIEDNEyTAREGAK	Homo sapiens
pmid	sentence
11294838	We demonstrate that shp-1 dephosphorylates the lymphoid-specific src family kinase lck at tyr-394. Because phosphorylation of tyr-394 activates lck, the fact that shp-1 specifically dephosphorylates this site suggests that shp-1 is a negative regulator of lck.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-144341	Tyr394	RLIEDNEyTAREGAK	Homo sapiens	HEK-293 Cell
pmid	sentence
16461343	Native ptpn22 dephosphorylated lck at its activating tyrosine residues tyr-394.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-81372	Tyr394	RLIEDNEyTAREGAK	Homo sapiens
pmid	sentence
2250907	They also demonstrate that replacement of the major site of autophosphorylation of p56lck (tyrosine 394) by a phenylalanine residue abolishes the ability to activate p56lck by CD4 cross-linking, implying that this residue is critical for the positive regulation of the Lck tyrosine kinase activity by CD4.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling, P38 Signaling, T cell activation

Identifier	Residue	Sequence
SIGNOR-249374	Tyr42	DSMKDEEyEQMVKEL
pmid	sentence
14534291	Loss of tyrosine kinase p56lck in Jurkat cells abolished NFkappaB activation and partially suppressed and delayed phosphorylation of Tyr-42 of IkappaB upon pervanadate treatment. \|Transfection of these cells with wild type Lck but not with mutant Lck F394 followed by H/R induces the tyrosine phosphorylation of inhibitor of nuclear factor kappaB (IkappaBalpha) and transcriptional activation of NFkappaB, and these are inhibited by Lck inhibitors

Publications:

1

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-251381	Tyr423	NSLNEEWyVSYITRP	in vitro
pmid	sentence
8702662	Ability of p56lck to phosphorylate Tyr-423/426 within SLP-76 in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251382	Tyr426	NEEWYVSyITRPEAE	in vitro
pmid	sentence
8702662	Ability of p56lck to phosphorylate Tyr-423/426 within SLP-76 in vitro

Publications:

2

Organism:

In Vitro

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251388	Tyr427	ELFDDPSyVNVQNLD	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	We show that during TCR signaling, the tyrosines Y239, Y240 and Y317 of Shc are the primary sites of tyrosine phosphorylation. CD4/Lck-dependent tyrosine phosphorylation on Shc was markedly diminished when Y317 was mutated, suggesting a preference of Lck for the Y317 site. tyrosine phosphorylation of Shc may play a key role in T lymphocyte proliferation via interaction of phosphorylated Shc with downstream molecules involved in activation of Ras and Myc proteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-106799	Tyr453	ASHVDNEySQPPRNS	Homo sapiens	T-lymphocyte
pmid	sentence
11298344	Tyrosine phosphorylation of cd5 requires lck activity. We propose that t cell activation mediates cd5 tyrosine phosphorylation at residues y429 and y463 mainly through the activation of lck

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-106803	Tyr487	DNSSDSDyDLHGAQR	Homo sapiens	T-lymphocyte
pmid	sentence
11298344	Tyrosine phosphorylation of cd5 requires lck activity. We propose that t cell activation mediates cd5 tyrosine phosphorylation at residues y429 and y463 mainly through the activation of lck

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248350	Tyr505	FTATEGQyQPQP	Homo sapiens
pmid	sentence
11259588	Importantly, and in disagreement with the model that CD45 only activates Lck in vivo, the kinase activity of Lck from cells lacking CD45 was substantially increased. These results support a model in which CD45 dephosphorylates both Tyr505 and Tyr394, the net effect in normal thymocytes being a decrease in enzymatic activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259933	Tyr505	FTATEGQyQPQP	Mus musculus	T-lymphocyte
pmid	sentence
17719247	CD45 differentially regulates the negatively acting pTyr-505 and positively acting pTyr-394 p56(lck) tyrosine kinase phosphorylation sites. We propose that high wild-type CD45 expression is necessary to dephosphorylate p56(lck) pTyr-394, suppressing CD4 T+ cell lineage commitment and hyperactivity.

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-20371	Tyr505	FTATEGQyQPQP	Homo sapiens	T-lymphocyte
pmid	sentence
1639064	P50csk tyrosine kinase phosphorylates p56lck at tyr-505 and down regulates its catalytic activity.

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-251380	Tyr512	RFVLDDQyTSSTGTK	in vitro
pmid	sentence
9312162	Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity. The major site of Lck phosphorylation on Itk was mapped to the conserved tyrosine (Tyr511) in the activation loop of the Itk kinase domain.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251387	Tyr536	QKGQESEyGNITYPP	Mus musculus	T-lymphocyte
pmid	sentence
8114715	Two sites (Y-536 and Y-564) which are directly phosphorylated by Lck in vitro are also phosphorylated in vivo in LSTRA cells. .

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-55853	Tyr537	CKNVVPLyDLLLEML	Homo sapiens	Breast Cancer Cell, HeLa Cell
pmid	sentence
9500442	On the basis of these data and other reports describing the structure and activity of y537 mutations, as well as knowledge of the three-dimensional structure of the her ligand binding domain, we propose an alternate model wherein y537f mutation favors an open pocket conformation, affecting the estrogen binding kinetics and stability of the hormone-bound, transcriptionally active closed pocket conformation.

Identifier	Residue	Sequence	Organism
SIGNOR-72373	Tyr537	CKNVVPLyDLLLEML	Homo sapiens
pmid	sentence
10571988	On the basis of these data and other reports describing the structure and activity of y537 mutations, as well as knowledge of the three-dimensional structure of the her ligand binding domain, we propose an alternate model wherein y537f mutation favors an open pocket conformation, affecting the estrogen binding kinetics and stability of the hormone-bound, transcriptionally active closed pocket conformation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-36121	Tyr564	SKHKEDVyENLHTKN	Homo sapiens	T-lymphocyte
pmid	sentence
8114715	The two sites (y-536 and y-564) which are directly phosphorylated by lck in vitro are also phosphorylated in vivo in lstra cells. One of these sites (y-564) is phosphorylated in t cells in response to lck activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-112491	Tyr597	RHSTILDyINVVPTA	Homo sapiens
pmid	sentence
11733002	These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. Y597 and y667 are likely involved in intracellular signaling

Identifier	Residue	Sequence	Organism
SIGNOR-112495	Tyr667	ESQEELHyATLNFPG	Homo sapiens
pmid	sentence
11733002	These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. Phosphorylation of the tyrosine located at position 667 in an itim motif appears to be necessary for the recruitment of shp-1 and partial recruitment of shp-2

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-148704	Tyr64	ASLVSQDyVNGTDQE	Homo sapiens
pmid	sentence
16899217	Y64 of magicin is phosphorylated by lck creating a sh2-grb2 binding motif

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252699	Tyr688	FAEPYNLySSLKELV	Chlorocebus aethiops	COS Cell
pmid	sentence
9461588	The regulatory p85 subunit of phosphatidylinositol 3-kinase is phosphorylated on tyrosine residues. We report that this phosphorylation event is readily catalyzed by the Abl and Lck protein-tyrosine kinases in vitro, by Bcr-Abl or a catalytically activated Lck-Y505F in co-transfected COS cells. we have mapped a major phosphorylation site to Tyr-688 in the C-terminal SH2 domain of p85. Tyrosine phosphorylation of p85 in vitro or in vivo was not associated with detectable change in the enzymatic activity of the phosphatidylinositol 3-kinase heterodimer, but correlated with a strong reduction in the binding of some, but not all, phosphoproteins to the SH2 domains of p85.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251383	Tyr688	FAEPYNLySSLKELV	Chlorocebus aethiops	COS Cell
pmid	sentence
9461588	the regulatory p85 subunit of phosphatidylinositol 3-kinase is phosphorylated on tyrosine residues. We report that this phosphorylation event is readily catalyzed by the Abl and Lck protein-tyrosine kinases in vitro, by Bcr-Abl or a catalytically activated Lck-Y505F in co-transfected COS cells. we have mapped a major phosphorylation site to Tyr-688 in the C-terminal SH2 domain of p85. Tyrosine phosphorylation of p85 in vitro or in vivo was not associated with detectable change in the enzymatic activity of the phosphatidylinositol 3-kinase heterodimer, but correlated with a strong reduction in the binding of some, but not all, phosphoproteins to the SH2 domains of p85.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-112499	Tyr691	PKGTQADyAEVKFQ	Homo sapiens
pmid	sentence
11733002	These results suggest that the tyrosines at positions 597 and 667, contained within itim-like motifs, are likely targets of phosphorylation by several classes of signaling molecules, including lck, jak3, and emt. The tyrosine located at position y691 was also contributing to the phosphorylation of the wild-type siglec tail by lck and jak3 kinases. however, it is not clear whether y691 is capable of binding sap or a similar protein. Future studies will attempt to elucidate the signaling activities associated with y691

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262742	Tyr713	KKDTETVySEVRKAV	Chlorocebus aethiops
pmid	sentence
9624175	We demonstrated that phosphorylation of PECAM-1 by Src or Csk family kinases was sufficient to trigger its association with SHP-2. Moreover, it was able to promote binding of PECAM-1 to SHP-1, a SHP-2-related protein-tyrosine phosphatase expressed in hemopoietic cells. Taken together, these findings indicated that the Src and Csk families of kinases are strong candidates for mediating tyrosine phosphorylation of PECAM-1 and triggering its association with SH2 domain-containing phosphatases under physiological circumstances.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-112931	Tyr715	LVMLGASyWYRARLH	Homo sapiens	JURKAT Cell
pmid	sentence
11741929	Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-112935	Tyr735	LKGPTCQyRAAQSGP	Homo sapiens
pmid	sentence
11741929	Hck, and to a lesser extent lck, phosphorylated the adam15. Deletion and point mutation analysis of the adam15 cytoplasmic domain confirmed the importance of the proline-rich motifs for grb2 and lck binding and indicated the regulatory nature of tyr(715) and tyr(735). These data demonstrate selective, phosphorylation-dependent interactions of adam15 with src family ptks and grb2, which highlight the potential for integration of adam functions and cellular signaling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-91473	Tyr753	ERDINSLyDVSRMYV	Homo sapiens
pmid	sentence
12181444	In vitro phosphorylation experiments with recombinant plcgamma2 and recombinant lck, fyn, and lyn tyrosine kinases showed that phosphorylation of plcgamma2 led to activation of the recombinant enzyme.

Identifier	Residue	Sequence	Organism
SIGNOR-91477	Tyr759	LYDVSRMyVDPSEIN	Homo sapiens
pmid	sentence
12181444	In vitro phosphorylation experiments with recombinant plcgamma2 and recombinant lck, fyn, and lyn tyrosine kinases showed that phosphorylation of plcgamma2 led to activation of the recombinant enzyme.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-74574	Tyr90	SETTVELySLAERCR	Homo sapiens
pmid	sentence
10652356	Tyrosine 90 (tyr-90) in the regulatory domain of pkctheta was identified as the major phosphorylation site by lck.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-269899		Homo sapiens	T-lymphocyte
pmid	sentence
17998336	The sh3 domain of lck modulates t-cell receptor-dependent activation of extracellular signal-regulated kinase through activation of raf-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252305		Homo sapiens
pmid	sentence
8626561	The binding of Lck to the tyrosine-phosphorylated zeta chain of the TcR would serve to strengthen the interaction of the associated CD4 and the TcR complex, leading to increased avidity for the antigen-major histocompatibility protein complex

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism	Cell Line
SIGNOR-269921		Homo sapiens	T-lymphocyte
pmid	sentence
17998336	The sh3 domain of lck modulates t-cell receptor-dependent activation of extracellular signal-regulated kinase through activation of raf-1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism
SIGNOR-259928		Mus musculus
pmid	sentence
2470098	Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex.

Identifier	Residue	Organism	Cell Line
SIGNOR-259931		Mus musculus	T-lymphocyte
pmid	sentence
2470098	Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex.

Publications:

2

Organism:

Mus Musculus

Pathways:

T cell activation

Identifier	Residue	Organism
SIGNOR-159164		Homo sapiens
pmid	sentence
17998336	The sh3 domain of lck modulates t-cell receptor-dependent activation of extracellular signal-regulated kinase through activation of raf-1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism
SIGNOR-96771		Homo sapiens
pmid	sentence
12496362	We confirmed that lar dephosphorylated the phosphorylated tyrosine residues of lck..Activation Of lck and fyn involves tyrosine dephosphorylation of the cooh-terminal regulatory domain of kinases, followed by autophosphorylation of the kinase domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-259929		Mus musculus	T-lymphocyte
pmid	sentence
2470098	Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism	Cell Line
SIGNOR-270074		Homo sapiens	HeLa Cell
pmid	sentence
8618896	Phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62.\|phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p56lck signaling that is regulated by Ser-59 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-118902		Homo sapiens	T-lymphocyte
pmid	sentence
14583609	Endogenous notch-1 associates with p56(lck) and pi3k. p56(lck) is required for the notch-1-mediated activation of akt/pkb function

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-259932		Mus musculus
pmid	sentence
2470098	Last, we demonstrate directly that members of the CD3 complex, including the gamma, delta, and epsilon chains, as well as a putative zeta subunit, can be phosphorylated at tyrosine residues by the CD4/CD8.p56lck complex.

Publications:

1

Organism:

Mus Musculus

Pathways:

T cell activation

Identifier	Residue	Organism
SIGNOR-251373		Homo sapiens
pmid	sentence
10799545	Phosphorylation of p56 dok and p62 dok is increased following CD2 stimulation and requires Lck. Phosphorylation of Dok proteins by Lck might provide a mechanism by which SH2-containing proteins can be recruited and co-localized with their substrates.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-270177		Homo sapiens	HeLa Cell
pmid	sentence
8618896	Phosphorylation at Ser-59 (or alternatively, its mutation to Glu) reverses the inhibition and allows interaction of the p56lck SH2 domain with p62.\|phosphotyrosine-independent binding of p62 to the p56lck SH2 domain appears to provide an alternative pathway for p56lck signaling that is regulated by Ser-59 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism
SIGNOR-166658		Homo sapiens
pmid	sentence
20626350	However, non-canonical mechanisms of p38alfa activation have been also described. One is apparently specific to antigen receptor stimulated t-lymphocytes. This involves phosphorylation of p38alfa on tyr323 by the tcr-proximal tyrosine kinase zap70 and p56lck.

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling

Identifier	Residue	Organism	Cell Line
SIGNOR-272614		Homo sapiens	HEK-293 Cell
pmid	sentence
11904433	Coexpression in 293T cells demonstrated that Lck kinase activity and Cbl ubiquitin ligase activity were essential for Lck ubiquitination and negative regulation of Lck-dependent serum response element-luciferase reporter activity. The Lck SH3 domain was pivotal for Cbl-Lck association and Cbl-mediated Lck degradation, with a smaller role for interactions mediated by the Cbl tyrosine kinase-binding domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-41361		Homo sapiens	T-lymphocyte
pmid	sentence
8626561	During tcr signaling, lck interacts with numerous molecules, including tcr-zeta. The binding of lck to the tyrosine-phosphorylated zeta chain of the tcr would serve to strengthen the interaction of the associated cd4 and the tcr complex, leading to increased avidity for the antigen-major histocompatibility protein complex.

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism
SIGNOR-260376		Homo sapiens
pmid	sentence
18641330	In these studies, we also found that SLP-2 interacted with Lck, ZAP70, LAT, and PLC-gamma1 during the 30-min period following stimulation in vitro\|The SLP-2-associated pool of these molecules became phosphorylated/activated in a sequential manner, a profile compatible with their temporal involvement in early TCR signalling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251685		Homo sapiens
pmid	sentence
16888650	The present study shows that the GC receptor is part of a TCR-linked multiprotein complex containing heat-shock protein (HSP)90, LCK and FYN, which is essential for TCR-dependent LCK/FYN activation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glucocorticoid receptor Signaling

Identifier	Residue	Organism
SIGNOR-190910		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Name	LCK View Modifications
Full Name	Tyrosine-protein kinase Lck
Synonyms	Leukocyte C-terminal Src kinase, LSK, Lymphocyte cell-specific protein-tyrosine kinase, Protein YT16, Proto-oncogene Lck, T cell-specific protein-tyrosine kinase, p56-LCK
Primary ID	P06239
Links	- -
Type	protein
Relations	117
Pathways	Mitochondrial dynamics in T cell exhaustion, P38 Signaling, T cell activation
Inhibitors	CCT239065
Function	Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2 (PubMed:27335501).

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