Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277384	Thr293	TLNSDGYtPEPARIT	Homo sapiens	T-lymphocyte
pmid	sentence
29440413	We have found that T cell p38 MAP kinase (MAPK), which is directly phosphorylated and activated by ZAP-70 downstream of the TCR, in turn phosphorylates Thr-293 in the interdomain B region of ZAP-70. These results identify a tight negative feedback loop in which ZAP-70-activated p38 reciprocally phosphorylates ZAP-70 and destabilizes the signaling complex.

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-42956	Tyr113	SSFEEDDyESPNDDQ	Homo sapiens
pmid	sentence
8702662	A fourth peptide derived from slp-76 encompassing tyr residues 423 and 426 was also phosphorylated by zap-70 but with a 10-15-fold lesser efficiency compared to tyr-113, _128, and _145. Phosphorylation of slp-76 by the zap-70 protein-tyrosine kinase is required for t-cell receptor function

Identifier	Residue	Sequence	Organism
SIGNOR-46855	Tyr113	SSFEEDDyESPNDDQ	Homo sapiens
pmid	sentence
9047237	Zap-70 phosphorylates slp-76 at specific sites that allow vav sh2 domain bindingwe also show by in vitro and in vivo analysis that two slp-76 pyesp motifs (y113 and y128) mediate binding, the first being more efficient.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-42960	Tyr128	DGEDDGDyESPNEEE	Homo sapiens	T-lymphocyte
pmid	sentence
8702662	A fourth peptide derived from slp-76 encompassing tyr residues 423 and 426 was also phosphorylated by zap-70 but with a 10-15-fold lesser efficiency compared to tyr-113, _128, and _145. Phosphorylation of slp-76 by the zap-70 protein-tyrosine kinase is required for t-cell receptor function

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-46859	Tyr128	DGEDDGDyESPNEEE	Homo sapiens	T-lymphocyte
pmid	sentence
9047237	Zap-70 phosphorylates slp-76 at specific sites that allow vav sh2 domain bindingwe also show by in vitro and in vivo analysis that two slp-76 pyesp motifs (y113 and y128) mediate binding, the first being more efficient.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-42968	Tyr145	PVEDDADyEPPPSND	Homo sapiens	T-lymphocyte
pmid	sentence
8702662	A fourth peptide derived from slp-76 encompassing tyr residues 423 and 426 was also phosphorylated by zap-70 but with a 10-15-fold lesser efficiency compared to tyr-113, _128, and _145. Phosphorylation of slp-76 by the zap-70 protein-tyrosine kinase is required for t-cell receptor function

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-42972	Tyr423	NSLNEEWyVSYITRP	Homo sapiens	T-lymphocyte
pmid	sentence
8702662	A fourth peptide derived from slp-76 encompassing tyr residues 423 and 426 was also phosphorylated by zap-70 but with a 10-15-fold lesser efficiency compared to tyr-113, _128, and _145. Phosphorylation of slp-76 by the zap-70 protein-tyrosine kinase is required for t-cell receptor function

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-42976	Tyr426	NEEWYVSyITRPEAE	Homo sapiens	T-lymphocyte
pmid	sentence
8702662	A fourth peptide derived from slp-76 encompassing tyr residues 423 and 426 was also phosphorylated by zap-70 but with a 10-15-fold lesser efficiency compared to tyr-113, _128, and _145. Phosphorylation of slp-76 by the zap-70 protein-tyrosine kinase is required for t-cell receptor function

Publications:

7

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-102507	Tyr113	SSFEEDDyESPNDDQ	Homo sapiens	T-lymphocyte
pmid	sentence
12817019	Phosphorylation of slp-76 is required for prolonged erk activation in response to sdf-1_ cr signal transduction results in slp-76 tyrosine phosphorylation at the amino-terminal tyrosines 113, 128, and 145 via a mechanism requiring the zap-70 tyrosine kinase.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-102511	Tyr128	DGEDDGDyESPNEEE	Homo sapiens	T-lymphocyte
pmid	sentence
12817019	Phosphorylation of slp-76 is required for prolonged erk activation in response to sdf-1_ cr signal transduction results in slp-76 tyrosine phosphorylation at the amino-terminal tyrosines 113, 128, and 145 via a mechanism requiring the zap-70 tyrosine kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-102515	Tyr145	PVEDDADyEPPPSND	Homo sapiens
pmid	sentence
12817019	Phosphorylation of slp-76 is required for prolonged erk activation in response to sdf-1_ cr signal transduction results in slp-76 tyrosine phosphorylation at the amino-terminal tyrosines 113, 128, and 145 via a mechanism requiring the zap-70 tyrosine kinase.

Publications:

3

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247039	Tyr1203	IFPARDTyHPMSEYP	Homo sapiens	JURKAT Cell
pmid	sentence
14766232	Indeed, the present results demonstrate that ZAP-70 phosphorylates MUC1-CD and that the MUC1-CD Y-20 site functions, at least in part, as a ZAP-70 substrate (Fig. 4C). In this regard, the in vivo phosphorylation data indicate that ZAP-70 may also contribute to phosphorylation of MUC1-CD Y-46.The results further show that ZAP-70 phosphorylation of MUC1-CD stimulates the interaction of MUC1 andBeta-catenin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247044	Tyr126	RDAMVRDyVRQTWKL	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. By comparative two-dimensional phosphopeptide mapping, we show that ZAP-70 isolated from Jurkat T cells also autophosphorylates at Tyr-292 and Tyr-126

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-43324	Tyr292	DTLNSDGyTPEPARI	Homo sapiens	T-lymphocyte, B-lymphocyte
pmid	sentence
8756661	The data further support a model in which ZAP-70 is first phosphorylated by Lck at Tyr-493 to upregulate the catalytic activity of ZAP-70. This in turn per- mits additional phosphorylation of ZAP-70 mediated, in part, by autophosphorylation at sites including Tyr-292 and -492

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247048	Tyr315	MPMDTSVyESPYSDP	Homo sapiens	JURKAT Cell
pmid	sentence
11828374	We show here that Tyr315 and Tyr319 in the interdomain B of ZAP-70 are autophosphorylated in vitro and become phosphorylated in vivo upon TCR triggering. Moreover, by mutational analysis, we demonstrate that phosphorylation of Tyr319 is required for the positive regulation of ZAP-70 function.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247053	Tyr319	TSVYESPySDPEELK	Homo sapiens	JURKAT Cell
pmid	sentence
10037717	We show here that Tyr315 and Tyr319 in the interdomain B of ZAP-70 are autophosphorylated in vitro and become phosphorylated in vivo upon TCR triggering. Moreover, by mutational analysis, we demonstrate that phosphorylation of Tyr319 is required for the positive regulation of ZAP-70 function.

Identifier	Residue	Sequence	Organism
SIGNOR-226624	Tyr492	ALGADDSyYTARSAG	Homo sapiens
pmid	sentence
8756661	The data further support a model in which ZAP-70 is first phosphorylated by Lck at Tyr-493 to upregulate the catalytic activity of ZAP-70. This in turn per- mits additional phosphorylation of ZAP-70 mediated, in part, by autophosphorylation at sites including Tyr-292 and -492

Identifier	Residue	Sequence	Organism
SIGNOR-139098	Tyr493	LGADDSYyTARSAGK	Homo sapiens
pmid	sentence
16049944	Zap-70 is modified by auto-phosphorylation of various tyrosine residues and is activated by specific phosphorylation of the tyrosine residue y-493

Publications:

6

Organism:

Homo Sapiens

Pathways:

P38 Signaling, T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-274561	Tyr 132	DYHNPGyLVVLPD	Homo sapiens
pmid	sentence
29915297	In the presence of the catalytically inactive LckK273R, the phosphorylation of LAT Y132 and Y191 residues by Zap70K362E were considerably increased

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247018	Tyr156	ADEDEDDyHNPGYLV	Homo sapiens	T-lymphocyte
pmid	sentence
11368773	In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127.

Identifier	Residue	Sequence	Organism
SIGNOR-247022	Tyr161	DDYHNPGyLVVLPDS	Homo sapiens
pmid	sentence
11368773	In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127.

Identifier	Residue	Sequence	Organism
SIGNOR-274562	Tyr191	LDGSREyVNVSQE	Homo sapiens
pmid	sentence
29915297	In the presence of the catalytically inactive LckK273R, the phosphorylation of LAT Y132 and Y191 residues by Zap70K362E were considerably increased

Identifier	Residue	Sequence	Organism
SIGNOR-247026	Tyr200	SMESIDDyVNVPESG	Homo sapiens
pmid	sentence
11368773	In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127.

Identifier	Residue	Sequence	Organism
SIGNOR-247030	Tyr220	SLDGSREyVNVSQEL	Homo sapiens
pmid	sentence
11368773	In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127.

Identifier	Residue	Sequence	Organism
SIGNOR-247034	Tyr255	EEEGAPDyENLQELN	Homo sapiens
pmid	sentence
11368773	In the present study we reconstituted the LAT signalling pathway by demonstrating that a direct tyrosine phosphorylation of LAT with activated protein-tyrosine kinase Zap70 is necessary and sufficient for the association and activation of signalling proteins. Zap-70 efficiently phosphorylates LAT on tyrosine residues at positions 226, 191, 171, 132 and 127.

Publications:

7

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276000	Tyr138	SPTLVIAyLMMRQKM	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12447358	ZAP-70 and Syk also tyrosine-phosphorylated VHR in COS-1 cells (Fig. 2d), whereas other kinases (Csk, Lck, Fyn, Jak2, Bcr-Abl and Itk) had little effect. Finally, recombinant ZAP-70 readily phosphorylated VHR in vitro (Fig. 2f).

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-95877	Tyr138	SPTLVIAyLMMRQKM	Homo sapiens
pmid	sentence
12447358	We report here that vhr, a vaccinia virus vh1-related dual-specific protein phosphatase that inactivates the mitogen-activated kinases erk2 and jnk, is phosphorylated at y138 by zap-70. Tyr138 phosphorylation was required for vhr to inhibit the erk2-elk-1 pathway

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-48854	Tyr273	LEMPDNLyTFVLKVK	Homo sapiens	T-lymphocyte
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
SIGNOR-254732	Tyr292	DTLNSDGyTPEPARI	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Identifier	Residue	Sequence	Organism
SIGNOR-254733	Tyr315	MPMDTSVyESPYSDP	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Identifier	Residue	Sequence	Organism
SIGNOR-254734	Tyr319	TSVYESPySDPEELK	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Publications:

3

Organism:

In Vitro

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-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

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

Publications:

8

Organism:

Mus Musculus, In Vitro, Homo Sapiens

Pathways:

P38 Signaling, T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-134329	Tyr323	DEPVADPyDQSFESR	Homo sapiens	T-lymphocyte
pmid	sentence
15735648	Thus, phosphorylation of tyr323 dependent on the tyrosine kinase lck and mediated by zap70 serves as an important mechanism for tcr activation of p38 in t cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276030	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.

Identifier	Residue	Organism	Cell Line
SIGNOR-277385		Homo sapiens	T-lymphocyte
pmid	sentence
29440413	We have found that T cell p38 MAP kinase (MAPK), which is directly phosphorylated and activated by ZAP-70 downstream of the TCR, in turn phosphorylates Thr-293 in the interdomain B region of ZAP-70. These results identify a tight negative feedback loop in which ZAP-70-activated p38 reciprocally phosphorylates ZAP-70 and destabilizes the signaling complex.

Publications:

3

Organism:

Homo Sapiens, Mus Musculus

Pathways:

P38 Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118691	Tyr334	QAEEEAVyEEPPEQE	Homo sapiens	T-lymphocyte
pmid	sentence
14557276	We found an interaction between the tyrosine kinase zap-70 and hip-55, which was induced by tcr stimulation. Zap-70 phosphorylated hip-55 at tyr-334 and tyr-344, which were shown to be the tyrosine phosphorylation sites of hip-55 in stimulated t cells.Our results demonstrate for the first time that hip-55 is an important adaptor protein for the jnk kinase cascade in tcr signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-118695	Tyr344	PPEQETFyEQPPLVQ	Homo sapiens	T-lymphocyte
pmid	sentence
14557276	We found an interaction between the tyrosine kinase zap-70 and hip-55, which was induced by tcr stimulation. Zap-70 phosphorylated hip-55 at tyr-334 and tyr-344, which were shown to be the tyrosine phosphorylation sites of hip-55 in stimulated t cells.Our results demonstrate for the first time that hip-55 is an important adaptor protein for the jnk kinase cascade in tcr signaling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59647	Tyr349	EEPPDHQyYNDFPGK	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on shc1 (iso2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59651	Tyr350	EPPDHQYyNDFPGKE	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on shc1 (iso2).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59659	Tyr427	ELFDDPSyVNVQNLD	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	The syk-family kinases (syk and zap-70) were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site on shc1 (iso2).

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274142	Tyr493	LGADDSYyTARSAGK	Homo sapiens	JURKAT Cell
pmid	sentence
34960191	Immunoblot analysis showed that phosphorylation of the activating ZAP70 kinase domain residue Tyr 493 was decreased in the DLG1 KD cells. Similarly, the Tyr 319 residue of ZAP70 and Tyr 83 residue of TCR- ζ also showed reduced phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-144345	Tyr493	LGADDSYyTARSAGK	Homo sapiens	HEK-293 Cell
pmid	sentence
16461343	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).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248838	Tyr493	LGADDSYyTARSAGK	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	Cell Line
SIGNOR-110731	Tyr614	KSTGSVDyLALDFQP	Homo sapiens	T-lymphocyte
pmid	sentence
11572860	In the present study, we found that gab2 is phosphorylated by zap-70, associates with the tcr signaling complex, and acts as an inhibitory adaptor molecule via recruitment of shp-2 following tcr ligation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-274150		Homo sapiens	Hematopoietic Stem Cell
pmid	sentence
9151714	In summary, we demonstrate here that Y315 in ZAP-70 is required to interact with the Vav SH2 domain, and is critical for ZAP-70–mediated gene activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-259084		Homo sapiens	JURKAT Cell
pmid	sentence
17028588	These findings suggest that RhoH is a critical regulator of thymocyte development and TCR signaling by mediating recruitment and activation of Zap70.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278390		Homo sapiens
pmid	sentence
23620790	These results suggest that CBAP may serve as an adaptor or scaffold in the integrin \u03b21/CBAP/ZAP70-containing complex that, upon chemokine treatment, would allow Vav1 or ZAP70 (or both) to adopt an optimal conformation(s) for ZAP70 to phosphorylate Vav1.\|Together, these results suggested that CBAP is an important component in ZAP70 dependent activation of the Vav1 and Rac1 signaling axis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252304		Chlorocebus aethiops
pmid	sentence
1423621	We have recently identified a 70 kd tyrosine phosphoprotein (ZAP-70) that associates with zeta and undergoes tyrosine phosphorylation following TCR stimulation\|Moreover, tyrosine phosphorylation and association of ZAP-70 with zeta require the presence of src family PTKs and provide a potential mechanism by which the src family PTKs and ZAP-70 may interact to mediate TCR signal transduction.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

T cell activation

Identifier	Residue	Organism	Cell Line
SIGNOR-134325		Homo sapiens	T-lymphocyte
pmid	sentence
1717999	Stimulation of the T-cell antigen receptor (TCR) leads to tyrosine phosphorylation of a number of cellular proteins, including phospholipase C (PLC) gamma 1 and the TCR zeta chain. We describe here a 70-kDa tyrosine phosphoprotein (ZAP-70) that associates with zeta within 15 sec following TCR stimulation. The phosphorylation of ZAP-70 and its association with zeta is independent of the other TCR chains

Publications:

1

Organism:

Homo Sapiens

Pathways:

P38 Signaling

Identifier	Residue	Organism
SIGNOR-274012		in vitro
pmid	sentence
12051764	Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-260377		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	Cell Line
SIGNOR-70237		Homo sapiens	T-lymphocyte
pmid	sentence
10458769	We propose that shp1 can dephosphorylate sites in zap-70 and syk that are involved in coupling these kinases to downstream signaling cascades, including erk2 and elements of the il-2 gene.

Publications:

1

Organism:

Homo Sapiens

Name	ZAP70 View Modifications
Full Name	Tyrosine-protein kinase ZAP-70
Synonyms	70 kDa zeta-chain associated protein, Syk-related tyrosine kinase \| SRK
Primary ID	P43403
Links	- -
Type	protein
Relations	61
Pathways	Mitochondrial dynamics in T cell exhaustion, P38 Signaling, T cell activation
Function	Tyrosine kinase that plays an essential role in regulation of the adaptive immune response. Regulates motility, adhesion and cytokine expression of mature T-cells, as well as thymocyte development. Contributes also to the development and activation of primary B-lymphocytes. When antigen presenting cells (APC) activate T-cell receptor (TCR), a serie of phosphorylations lead to the recruitment of ZAP70 to the doubly phosphorylated TCR component CD247/CD3Z through ITAM motif at the plasma membrane. This recruitment serves to localization to the stimulated TCR and to relieve its autoinhibited conformation. Release of ZAP70 active conformation is further stabilized by phosphorylation mediated by LCK. Subsequently, ZAP70 phosphorylates at least 2 essential adapter proteins

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