Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-130274	Ser11	TKQTARKsTGGKAPR	Homo sapiens
pmid	sentence
15537652	Here we provide evidence that fyn kinase, a member of the src kinase family, is involved in the uvb-induced phosphorylation of histone h3 at serine 10

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167147	Ser21	LTEERDGsLNQSSGY	Homo sapiens
pmid	sentence
20658524	The serine 21 (s21) residue of fyn is a protein kinase a (pka) recognition site within an rxxs motif of the amino terminal sh4 domain of fyn. In addition, s21 is critical for fyn kinase-linked cellular signaling. Mutation of s21a blocks pka phosphorylation of fyn and alters its tyrosine kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279716	Ser591	DKEKSKGsLKRK	Homo sapiens
pmid	sentence
28811476	By contrast, receptor multivalent aggregation induced a Fyn-dependent SHP-1 S591 phosphorylation (Fig.\u00a0 xref ).\|Fyn simultaneously activates the PI3K-PKC\u03b1 pathway, leading to SHP-1 phosphorylation on serine 591.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-147932	Tyr1038	ESWIRAKyEQLLFLA	Homo sapiens
pmid	sentence
16841086	We demonstrate that fyn is essential for phosphorylating pike-a and protects it from apoptotic cleavage. Active but not kinase-dead fyn interacts with pike-a and phosphorylates it on both y682 and y774 residues. Tyrosine phosphorylation in pike-a is required for its association with active fyn but not for akt. Mutation of d into a in pike-a protects it from caspase cleavage and promotes cell survival.

Identifier	Residue	Sequence	Organism
SIGNOR-147936	Tyr1130	QGRTALFyARQAGSQ	Homo sapiens
pmid	sentence
16841086	We demonstrate that fyn is essential for phosphorylating pike-a and protects it from apoptotic cleavage. Active but not kinase-dead fyn interacts with pike-a and phosphorylates it on both y682 and y774 residues. Tyrosine phosphorylation in pike-a is required for its association with active fyn but not for akt. Mutation of d into a in pike-a protects it from caspase cleavage and promotes cell survival.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251169	Tyr1039	HSQLSDLyGKFSFKS	in vitro
pmid	sentence
11024032	Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-251170	Tyr1070	ISTHTVTyGNIEGNA	in vitro
pmid	sentence
11024032	Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-251171	Tyr1109	FDEIELAyRRRPPRS	in vitro
pmid	sentence
11024032	Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251172	Tyr1252	CKKAGNLyDISEDNS	Homo sapiens	HEK-293 Cell
pmid	sentence
11024032	Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251173	Tyr1336	RFMDGSPyAHMFEMS	Homo sapiens	HEK-293 Cell
pmid	sentence
11024032	Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251175	Tyr1474	GSSNGHVyEKLSSIE	Homo sapiens	HEK-293 Cell
pmid	sentence
11024032	Tyr-1252, Tyr-1336, and Tyr-1472 of GluRε2 are phosphorylated in 293T cells when active Fyn is co-expressed.

Identifier	Residue	Sequence
SIGNOR-249338	Tyr1474	GSSNGHVyEKLSSIE
pmid	sentence
11483655	We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src and Fyn and compared this to phosphorylation by tyrosine kinases associated with the postsynaptic density (PSD)\|Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases

Identifier	Residue	Sequence	Organism
SIGNOR-251174	Tyr932	IRRESSVyDISEHRR	in vitro
pmid	sentence
11024032	Tyr-932, Tyr-1039, Tyr-1070, Tyr-1109, Tyr-1252, Tyr-1336, and Tyr-1472 are Fyn-mediated phosphorylation sites in GluRε2 in vitro.

Publications:

8

Organism:

In Vitro, Homo Sapiens,

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276396	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

Identifier	Residue	Sequence	Organism
SIGNOR-247151	Tyr1105	CSEVERTyLKTKSSS	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247155	Tyr1267	PATGEQVyQQDWAQN	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247159	Tyr1387	GRCPSDPyKHSLPSQ	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268175	Tyr1261	PTLESAQyPGILPSP	Mus musculus	N1E-115 Cell
pmid	sentence
15557120	Fyn tyrosine kinase, but not Src, regulates the phosphorylation of DCC in N1E-115 neuroblastoma cells.Both DCC phosphorylation and Netrin-1-induced axon outgrowth are impaired in Fyn(-/-) CN and spinal cord explants. We propose that DCC is regulated by tyrosine phosphorylation and that Fyn is essential for the response of axons to Netrin-1. these results show that DCC is phosphorylated by Fyn, but not Src, in N1E-115 cells, and that tyrosines 1261 and 1418 are the major phosphorylation sites of Fyn in vivo.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268176	Tyr1420	TEDSANVyEQDDLSE	Mus musculus	N1E-115 Cell
pmid	sentence
15557120	Fyn tyrosine kinase, but not Src, regulates the phosphorylation of DCC in N1E-115 neuroblastoma cells.Both DCC phosphorylation and Netrin-1-induced axon outgrowth are impaired in Fyn(-/-) CN and spinal cord explants. We propose that DCC is regulated by tyrosine phosphorylation and that Fyn is essential for the response of axons to Netrin-1. these results show that DCC is phosphorylated by Fyn, but not Src, in N1E-115 cells, and that tyrosines 1261 and 1418 are the major phosphorylation sites of Fyn in vivo.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276372	Tyr1311	DSKVDLIyQNTTAMT	Homo sapiens	HEK-293 Cell
pmid	sentence
22898603	We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276374	Tyr1320	NTTAMTIyENLAPVT	Homo sapiens	HEK-293 Cell
pmid	sentence
22898603	We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251149	Tyr132	QLIIEDPyYGNDSDF	Chlorocebus aethiops	COS Cell
pmid	sentence
9038134	We identify Tyr-131 as the major phosphorylation site and Tyr-132 as a minor site and the Src family PTKs Lck and Fyn as enzymes capable of phosphorylating these sites in vivo and in vitro. Both Tyr-131 and Tyr-132 are located next to the catalytic pocket of LMPTP, and especially, Tyr-131 seems to be important for the activity of LMPTP. Phosphorylation of Tyr-131 or Tyr-132, particularly the former, caused an increase in the activity of LMPTP.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251150	Tyr133	LIIEDPYyGNDSDFE	Chlorocebus aethiops	COS Cell
pmid	sentence
9038134	We identify Tyr-131 as the major phosphorylation site and Tyr-132 as a minor site and the Src family PTKs Lck and Fyn as enzymes capable of phosphorylating these sites in vivo and in vitro. Both Tyr-131 and Tyr-132 are located next to the catalytic pocket of LMPTP, and especially, Tyr-131 seems to be important for the activity of LMPTP. Phosphorylation of Tyr-131 or Tyr-132, particularly the former, caused an increase in the activity of LMPTP.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-188527	Tyr1325	RLLEGNFyGSLFSVP	Homo sapiens
pmid	sentence
19834457	The nr2a subunit of the nmda receptor is tyrosine-phosphorylated, with tyr 1325 as its one of the major phosphorylation site. Tyr 1325 phosphorylation site is required for src-induced potentiation of the nmda receptor channel in the striatum. Tyr 1325 was most prominently phosphorylated by fyn in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118003	Tyr14	VDSEGHLyTVPIREQ	Homo sapiens
pmid	sentence
12921535	Caveolin-1 is phosphorylated on tyr(14) in response to both oxidative and hyperosmotic stress. In the present paper, we show that this phosphorylation requires activation of the src family kinase fyn.Therefore,

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273999	Tyr140	PVTDWAWyKITDSED	Homo sapiens	Melanoma Cell Line
pmid	sentence
32291412	Our findings demonstrated that Fyn directly phosphorylates CD147 at Y140 and Y183. Moreover, the CD147-FF (Y140F/Y183F) mutation impaired the interaction between CD147 and GnT-V, leading to decreased CD147 glycosylation and membrane recruitment.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274000	Tyr183	MEADPGQyRCNGTSS	Homo sapiens	Melanoma Cell Line
pmid	sentence
32291412	Our findings demonstrated that Fyn directly phosphorylates CD147 at Y140 and Y183. Moreover, the CD147-FF (Y140F/Y183F) mutation impaired the interaction between CD147 and GnT-V, leading to decreased CD147 glycosylation and membrane recruitment.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251162	Tyr142	AVVNLINyQDDAELA	in vitro
pmid	sentence
12640114	Interaction of beta-catenin with alpha-catenin is regulated by the phosphorylation of beta-catenin Tyr-142. This residue can be phosphorylated in vitro by Fer or Fyn tyrosine kinases. Transfection of these kinases to epithelial cells disrupted the association between both catenins.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-247176	Tyr1474	GSSNGHVyEKLSSIE	in vitro
pmid	sentence
11483655	We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-135600	Tyr1495	TEEQKKYyNAMKKLG	Homo sapiens
pmid	sentence
15831816	This study addresses the effects of the src family tyrosine kinase fyn on na(v)1.5 cardiac sodium channels. Sodium currents were acquired by whole cell recording on hek-293 cells transiently expressing na(v)1.5. Acute treatment of cells with insulin caused a depolarizing shift in steady-state inactivation, an effect eliminated by the src-specific tyrosine kinase inhibitor pp2 we provide evidence that this linker is a substrate for fyn in vitro, and that y1495 is a preferred phosphorylation site.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251156	Tyr15	EKIGEGTyGTVFKAK	Homo sapiens
pmid	sentence
14757045	Constitutively active Fyn phosphorylated Tyr15 of Cdk5. Fyn Facilitates Kinase Activity of Cdk5 Via Tyr15 Phosphorylation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-123099	Tyr18	MEDHAGTyGLGDRKD	Homo sapiens
pmid	sentence
14999081	In this study we determined that human tau tyr18 was phosphorylated by the src family tyrosine kinase fyn.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251179	Tyr180	YTLLNENyVEDDDNM	in vitro
pmid	sentence
11594778	Human NMT was found to be phosphorylated by non-receptor tyrosine kinase family members of Lyn, Fyn and Lck. Tyr100 is the principle phosphorylation site on hNMT for Lyn and Fyn. The significance of a phosphorylation-dependent interaction between NMT and a tyrosine kinase is not known at present.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251157	Tyr182	SQQGMTAyGTRRHLY	Chlorocebus aethiops
pmid	sentence
15206927	We identify, for the first time, tyrosine-phosphorylated calponin h3 within COS 7 cells, before and after their transfection with the pSV vector containing cDNA encoding the cytoplasmic, Src-related, tyrosine kinase, Fyn. we have localized the tyrosines phosphorylated without actin to Tyr261 in calponin h3 and to Tyr261 and Tyr182 in calponin h1. Tyrosine phosphorylation of calponins inhibits their binding to F-actin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251158	Tyr261	SQRGMTVyGLPRQVY	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
15206927	We identify, for the first time, tyrosine-phosphorylated calponin h3 within COS 7 cells, before and after their transfection with the pSV vector containing cDNA encoding the cytoplasmic, Src-related, tyrosine kinase, Fyn. we have localized the tyrosines phosphorylated without actin to Tyr261 in calponin h3 and to Tyr261 and Tyr182 in calponin h1. Tyrosine phosphorylation of calponins inhibits their binding to F-actin

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-264771	Tyr188	EPGEQPIyMNFSEPL	Chlorocebus aethiops
pmid	sentence
16920917	As CD300b phosphorylation was occurring only in the presence of both c-Fyn and DAP-12, we addressed whether tyrosine phosphorylation was required for association of CD300b and DAP-12. For this purpose, we generated a set of HA-tagged CD300b mutants affecting the transmembrane lysine (K158L), the cytoplasmic tyrosine (Y188F) or both residues.\|As expected, the CD300b double mutant could neither recruit DAP-12 nor become phosphorylated in the presence of c-Fyn kinase (Fig. 5⇑C). Association between CD300b and DAP-12 was maintained in absence of the c-Fyn kinase, indicating that phosphorylation of the adaptor was not essential for the formation of the complex (data not shown)

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-251154	Tyr196	GMEEDHTyEGLDIDQ	in vitro
pmid	sentence
9531288	CD79b cytoplasmic tail-containing GST fusion proteins were phosphorylated in vitro by baculovirus-produced Fyn, >80% of phosphorylation occurred on the N-terminal ITAM tyrosine. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). pY195 and pY206 in CD79b

Identifier	Residue	Sequence	Organism
SIGNOR-251155	Tyr207	DIDQTATyEDIVTLR	in vitro
pmid	sentence
9531288	CD79b cytoplasmic tail-containing GST fusion proteins were phosphorylated in vitro by baculovirus-produced Fyn, >80% of phosphorylation occurred on the N-terminal ITAM tyrosine. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM). pY195 and pY206 in CD79b

Publications:

2

Organism:

In Vitro

Pathways:

B-cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-251153	Tyr199	NLDDCSMyEDISRGL	in vitro
pmid	sentence
9531288	Lyn and Fyn phosphorylated the CD79a cytoplasmic portion of the fusion proteins well, with >80% of phosphorylation occurring at Y182. CD79a and CD79b function as transducers of B cell antigen receptor signals via a cytoplasmic sequence, termed the immunoreceptor tyrosine-based activation motif (ITAM).

Publications:

1

Organism:

In Vitro

Pathways:

B-cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266304	Tyr20	NSGQPPNyEMLKEEH	Mus musculus	Fibroblast
pmid	sentence
24627473	We determined that both mouse and human IFITM3 are phosphorylated by the protein-tyrosine kinase FYN on tyrosine 20 (Tyr(20)). Phosphorylation of IFITM3 on Tyr20 Leads to Plasma Membrane Accumulation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149174	Tyr200	SMESIDDyVNVPESG	Homo sapiens	T-lymphocyte
pmid	sentence
16938345	Both lck and syk, phosphorylate the itam-like motifs on lat at y171y191, which is essential for induction of the interaction of lat with downstream signaling molecules such as grb2, plc-gamma1 and c-cbl, and for activation of mapk-erk.

Identifier	Residue	Sequence	Organism
SIGNOR-148931	Tyr220	SLDGSREyVNVSQEL	Homo sapiens
pmid	sentence
16938345	Both lck and syk, phosphorylate the itam-like motifs on lat at y171y191, which is essential for induction of the interaction of lat with downstream signaling molecules such as grb2, plc-gamma1 and c-cbl, and for activation of mapk-erk.

Publications:

2

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-251161	Tyr201	SPLTTGVyVKMPPTE	Homo sapiens
pmid	sentence
9973379	CTLA-4 can associate with the Src kinases Fyn and Lck and that transfection of Fyn or Lck, but not the unrelated kinase ZAP70, can induce tyrosine phosphorylation of CTLA-4 on residues Y201 and Y218.¬† Phosphorylation of CTLA-4 Y201 in Jurkat cells correlated with cell surface accumulation of CTLA-4.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-155709	Tyr21	VSSDAEEyQPPIWKS	Homo sapiens
pmid	sentence
17560670	Ere we report that beta2-chimaerin is tyrosine-phosphorylated by src-family kinases (sfks) upon cell stimulation with epidermal growth factor (egf). these results suggest tyr-21 phosphorylation as a novel, sfk-dependent mechanism that negatively regulates beta2-chimaerin rac-gap activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251160	Tyr218	CEKQFQPyFIPIN	Homo sapiens
pmid	sentence
9973379	CTLA-4 can associate with the Src kinases Fyn and Lck and that transfection of Fyn or Lck, but not the unrelated kinase ZAP70, can induce tyrosine phosphorylation of CTLA-4 on residues Y201 and Y218. Phosphorylation of CTLA-4 Y201 in Jurkat cells correlated with cell surface accumulation of CTLA-4.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275619	Tyr236	VDQVEVEyVTMASLP
pmid	sentence
17202342	Y236 (YVTM) and Y263 (YCNM) fit with the consensus motif reported to bind the p85α regulatory subunit of PI3K (16). \|The association between IREM-1 and p85α was only perceived in the presence of c-Fyn, suggesting that tyrosine phosphorylation of IREM-1 cytoplasmic tail of IREM-1 was required for the interaction.

Identifier	Residue	Sequence
SIGNOR-275620	Tyr263	AEDQEPTyCNMGHLS
pmid	sentence
17202342	Y236 (YVTM) and Y263 (YCNM) fit with the consensus motif reported to bind the p85α regulatory subunit of PI3K (16). \|The association between IREM-1 and p85α was only perceived in the presence of c-Fyn, suggesting that tyrosine phosphorylation of IREM-1 cytoplasmic tail of IREM-1 was required for the interaction.

Publications:

2

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251159	Tyr261	SQKGMSVyGLGRQVY	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
15206927	We identify, for the first time, tyrosine-phosphorylated calponin h3 within COS 7 cells, before and after their transfection with the pSV vector containing cDNA encoding the cytoplasmic, Src-related, tyrosine kinase, Fyn. we have localized the tyrosines phosphorylated without actin to Tyr261 in calponin h3 and to Tyr261 and Tyr182 in calponin h1. Tyrosine phosphorylation of calponins inhibits their binding to F-actin

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-278477	Tyr261	PFEGDNIyKLFENIG	Homo sapiens
pmid	sentence
20142099	Moreover, Fyn kinase directly phosphorylated LKB1 on tyrosine 261 and 365 residues and mutations of these sites resulted in LKB1 export into the cytoplasm and increased AMPK phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273855	Tyr2681	LLNPNYIyDVPPEFV	in vitro
pmid	sentence
23230270	Here, we demonstrate that Trio is phosphorylated by Src family kinases in the embryonic rat cortex in response to netrin-1. In vitro, Trio was predominantly phosphorylated at Tyr(2622) by the Src kinase Fyn.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251168	Tyr28	SLNQSSGyRYGTDPT	in vitro
pmid	sentence
9425276	Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. Tyr28 This site is also a Fyn autophosphorylation site When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Identifier	Residue	Sequence	Organism
SIGNOR-251165	Tyr30	NQSSGYRyGTDPTPQ	in vitro
pmid	sentence
9425276	Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. Tyr28 This site is also a Fyn autophosphorylation site When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Identifier	Residue	Sequence	Organism
SIGNOR-251166	Tyr39	TDPTPQHyPSFGVTS	in vitro
pmid	sentence
9425276	Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. Tyr28 This site is also a Fyn autophosphorylation site When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Identifier	Residue	Sequence	Organism
SIGNOR-251167	Tyr420	RLIEDNEyTARQGAK	in vitro
pmid	sentence
9425276	Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. Tyr28 This site is also a Fyn autophosphorylation site When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Publications:

4

Organism:

In Vitro

Pathways:

B-cell activation, T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-250253	Tyr28	SLNQSSGyRYGTDPT	in vitro
pmid	sentence
9425276	PDGF-induced phosphorylation of Tyr28 in the N-terminus of Fyn affects Fyn activation. We show here that Fyn, a member of the Src family, is phosphorylated on Tyr28 in the unique N-terminal part of the molecule after interaction with the intracellular domain of the PDGF beta-receptor. Activated Fyn furthermore undergoes autophosphorylation on Tyr30, Tyr39 and Tyr420. When Fyn mutants with Tyr28, Tyr30 or Tyr39 replaced with phenylalanine residues were transfected into NIH3T3 cells a decreased activation after PDGF stimulation was seen, suggesting a functional importance of the N-terminal tyrosine phosphorylation of Fyn.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251181	Tyr281	EKKSLTIyAQVQKPG	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11806999	All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251182	Tyr307	QDPCTTIyVAATEPV	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11806999	All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251183	Tyr327	ETNSITVyASVTLPE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
11806999	All 3 tyrosines of CD150 (Tyr281, Tyr307, Tyr327) are phosphorylated by the src kinase Fyn. CD150 is unique among its homologues in the immunoglobulin superfamily in that it is able to bind SAP, a floating SH2 domain, in the absence of tyrosine phosphorylation. In this study, using a detailed mutagenesis mapping approach we have shown that SAP binding to CD150 is in fact bimodal. Prior to tyrosine phosphorylation, SAP binds the membrane-proximal motif surrounding Tyr281. Following tyrosine phosphorylation by tyrosine kinases such as Fyn, SAP binds additionally to the distal motif surrounding Tyr327.

Publications:

3

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-249336	Tyr288	YETADGGyMTLNPRA	in vitro
pmid	sentence
8756631	To identify the FcgammaRII-phosphorylating protein tyrosine kinase (PTK), we used the combination of an in vitro and an in vivo approach. In an in vitro assay using recombinant cytoplasmic tails of the different FcgammaRII isoforms as well as tyrosine exchange mutants, we show that each of the BCR-associated PTKs (Lyn, Blk, Fyn, and Syk) shows different phosphorylation patterns with regard to the different FcgammaR isoforms and point\|Fyn and Blk definitely phosphorylate Y-282 in the ITAM of Fc_RIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addi-tion to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-249337	Tyr304	TDDDKNIyLTLPPND	in vitro
pmid	sentence
8756631	To identify the FcgammaRII-phosphorylating protein tyrosine kinase (PTK), we used the combination of an in vitro and an in vivo approach. In an in vitro assay using recombinant cytoplasmic tails of the different FcgammaRII isoforms as well as tyrosine exchange mutants, we show that each of the BCR-associated PTKs (Lyn, Blk, Fyn, and Syk) shows different phosphorylation patterns with regard to the different FcgammaR isoforms and point\|Fyn and Blk definitely phosphorylate Y-282 in the ITAM of Fc_RIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addi-tion to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273960	Tyr291	AETSKLIyDFIEDQG	Mus musculus	Lymphocyte
pmid	sentence
14707117	TCR-induced WASp tyrosine phosphorylation was also disrupted in T cells lacking Fyn, a kinase shown here to bind, colocalize with, and phosphorylate WASp. Although Fyn enhanced WASp-mediated Arp2/3 activation and was required for synapse formation, PTP-PEST combined with PSTPIP1 inhibited WASp-driven actin polymerization and synapse formation.

Identifier	Residue	Organism
SIGNOR-279333		Homo sapiens
pmid	sentence
14707117	As shown in XREF_FIG F, Fyn immunoprecipitates from activated T cells induced the tyrosine phosphorylation of WASp, but neither WASpDeltaPro nor WASpY291F mutant proteins were phosphorylated in this assay.

Publications:

2

Organism:

Mus Musculus, Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-262677	Tyr294	YETADGGyMTLNPRA	in vitro
pmid	sentence
8756631	Fyn and Blk definitely phosphorylate Y-282 in the ITAM of FcgRIIa/c, whereas the non-ITAM tyrosine residue (Y-275) becomes phosphorylated by Syk, as the phosphorylation of double point mutants shows. In addition to these tyrosine residues, Fyn, Blk, and Syk might phosphorylate the most C-terminal tyrosine residue (Y-298) because altering this tyrosine residue together with one of the tyrosine residues clearly shown to be phosphorylated by the respective PTK results in the abrogation of phosphorylation

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-279737	Tyr313	SSEPVGIyQGFEKKT	Homo sapiens
pmid	sentence
33995031	In conclusion, our in vitro data and previous report ( xref ) demonstrate that Fyn phosphorylation of Y311 on PKC\u03b4 activates the apoptotic signaling cascade in DAergic neurons in response to neurotoxic insults.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134293	Tyr323	DEPVADPyDQSFESR	Homo sapiens
pmid	sentence
15735648	T cell src family kinases and zap70 activate p38 by phosphorylating tyr323.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276031	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274006	Tyr33	EENESPHyDDVHEYL	Homo sapiens	HeLa Cell
pmid	sentence
10930415	In this paper, we demonstrate that p64 becomes tyrosine phosphorylated when co-expressed with p59(fyn) in HeLa cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262874	Tyr348	TRPPEPVySTVNKLC	in vitro
pmid	sentence
13129934	Recombinant PSD-93 was phosphorylated by Fyn in vitro, and Tyr-384 was identified as a major phosphorylation site. In COS7 cells, exogenously expressed PSD-93 was phosphorylated, dependent on its membrane localization. In addition, tyrosine-phosphorylated PSD-93 was able to bind to Csk, a negative regulator of Src family kinases, in vitro as well as in a brain lysate.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59623	Tyr349	EEPPDHQyYNDFPGK	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	Syk and zap-70 were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site. Of the two potential grb2 binding sites (y239 and y317), y239 appears to play a greater role in recruiting sos through grb2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59627	Tyr350	EPPDHQYyNDFPGKE	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	Syk and zap-70 were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site. Of the two potential grb2 binding sites (y239 and y317), y239 appears to play a greater role in recruiting sos through grb2.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59631	Tyr427	ELFDDPSyVNVQNLD	Homo sapiens	T-lymphocyte
pmid	sentence
9710204	Syk and zap-70 were able to phosphorylate the y239 and y240 sites, and less efficiently the y317 site. Of the two potential grb2 binding sites (y239 and y317), y239 appears to play a greater role in recruiting sos through grb2.

Identifier	Residue	Sequence	Organism
SIGNOR-60160	Tyr427	ELFDDPSyVNVQNLD	Homo sapiens
pmid	sentence
9741627	Shc is subsequently phosphorylated at tyrosine 317 and recruits grb2

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-121795	Tyr353	NAQEKMVySLVSVPE	Homo sapiens
pmid	sentence
14761954	We have identified tyrosine 353 (tyr353) in the ip3-binding domain of type 1 ip3r (ip3r1) as a phosphorylation site for fyntyrosine phosphorylation of ip3r1 increased ip3 binding at low ip3 concentrations (<10 nm).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276371	Tyr374	PLPPAPAyLSSPLAL	Homo sapiens	HEK-293 Cell
pmid	sentence
23131831	Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278441	Tyr397	SVSETDDyAEIIDEE	Homo sapiens
pmid	sentence
19917775	Because Fyn deletion prevented FAK phosphorylation at tyrosine residues 397 and 576 (XREF_FIG), we generated a phosphorylation mimicking mutant of FAK to test whether restoring FAK phosphorylation in the fyn -/- mouse lung could restore lung vascular permeability responses to PAR1 agonist to the level seen in WT mice.\|Our findings that interaction of activated FAK with p120-catenins subsequent to Fyn activation of FAK facilitates reannealing of AJ leading to reestablishment of the basal endothelial barrier suggest that the Fyn-FAK pathway plays a critical role in restoring endothelial barrier function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-147156	Tyr406	PLLTYQLyGKFSEAM	Homo sapiens
pmid	sentence
16777849	Tcgap interacted with fyn and was phosphorylated by fyn, with tyr-406 in the gap domain as a major fyn-mediated phosphorylation site. Fyn suppressed the gap activity of wild-type tcgap

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-96768	Tyr420	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
12496362	Regulation of lck and fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-177109	Tyr420	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
22080863	Previously, we reported that sfks can serve as bona fide substrates for tcptp and that tcptp dephosphorylates the y418 activation loop autophosphorylation site (corresponding to y394 in lck and y417 in fyn) to inactivate sfks

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-86791	Tyr420	RLIEDNEyTARQGAK	Homo sapiens	Neuron
pmid	sentence
11983687	Wild-type step(61) dephosphorylates fyn at tyr(420) but not at tyr(531). These results suggest that step regulates the activity of fyn by specifically dephosphorylating the regulatory tyr(420) and may be one mechanism by which fyn activity is decreased within psds.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-177113	Tyr420	RLIEDNEyTARQGAK	Homo sapiens	T-lymphocyte
pmid	sentence
22080863	Previously, we reported that sfks can serve as bona fide substrates for tcptp and that tcptp dephosphorylates the y418 activation loop autophosphorylation site (corresponding to y394 in lck and y417 in fyn) to inactivate sfks

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245332	Tyr420	QFNQRFIyGNQDLFA	Mus musculus	Helper T-lymphocyte
pmid	sentence
16387660	Tyrosine phosphorylation of Itch appears to reduce its interaction with its substrate JunB. The turnover of JunB is accelerated in Fyn-deficient T cells, which is further reconstituted by Itch Tyr371 mutation

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence
SIGNOR-249341	Tyr420	RYVLDDEyVSSFGAK
pmid	sentence
11353545	We further demonstrate that Rlk can be phosphorylated and activated by Src kinases, leading to a decrease in its half-life. A specific tyrosine in the activation loop of Rlk, Y420, is required for phosphorylation and activation, as well as for decreased stability, but is not required for lipid RAFT association.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277279	Tyr436	EWKVVNAyHLRVRRK	Mus musculus	NIH-3T3 Cell
pmid	sentence
27626315	Here we identified that Fyn phosphorylates the α subunit of AMPK on Y436 and inhibits AMPK enzymatic activity without altering the assembly state of the AMPK heterotrimeric complex.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-276644	Tyr446	DQSRQMKyQSFNEYR	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

Identifier	Residue	Sequence	Organism
SIGNOR-251151	Tyr453	ASHVDNEySQPPRNS	in vitro
pmid	sentence
11298344	Tyrosine-mutated CD5 molecules have been used to show that residues Y429 and Y463 are targeted in vivo by protein tyrosine kinases following cell stimulation with anti-CD3 mAb or pervanadate. This is in agreement with data from direct in vitro kinase assays using purified recombinant Lck and Fyn protein tyrosine kinases.

Identifier	Residue	Sequence	Organism
SIGNOR-251152	Tyr487	DNSSDSDyDLHGAQR	in vitro
pmid	sentence
11298344	Tyrosine-mutated CD5 molecules have been used to show that residues Y429 and Y463 are targeted in vivo by protein tyrosine kinases following cell stimulation with anti-CD3 mAb or pervanadate. This is in agreement with data from direct in vitro kinase assays using purified recombinant Lck and Fyn protein tyrosine kinases.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-251185	Tyr460	AVTTEAIyEEIDAHQ	in vitro
pmid	sentence
11711534	Tyr-457, located in the presumed Src SH2 binding site, is the predominant tyrosine residue that is phosphorylated by Fyn.Fyn can phosphorylate Srcasm, and association of these molecules relies on cooperative binding between the SH2 and SH3 domains of Fyn and corresponding canonical binding sites in Srcasm. Srcasm is capable of interacting with Grb2 and the regulatory subunit of phosphoinositide 3-kinase, p85, in a phosphorylation-dependent manner. The evidence suggests that Srcasm may help promote Src family kinase signaling in cells.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-265758	Tyr481	GTVSSSSyNA	Homo sapiens
pmid	sentence
30824700	6PGD is phosphorylated at tyrosine (Y) 481 by Src family kinase Fyn. This phosphorylation enhances 6PGD activity by increasing its binding affinity to NADP+ and therefore activates the PPP for NADPH and ribose-5-phosphate, which consequently detoxifies intracellular reactive oxygen species (ROS) and accelerates DNA synthesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-180449	Tyr523	REDSVLSyETVTQME	Homo sapiens	Neuron
pmid	sentence
18721130	Psd-95 is phosphorylated either by purified src/fyn kinases in vitro or by co-expression of constitutively active src/fyn in cos7 cells. psd-95 tyr(523) phosphorylation contributes to the post-ischaemic over-activation of nmda receptors.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-160048	Tyr529	TITKTVEyLHAQGVV	Homo sapiens
pmid	sentence
18156174	Epidermal growth factor stimulates rsk2 activation through activation of the mek/erk pathway and src-dependent tyrosine phosphorylation of rsk2 at tyr-529. By mass spectroscopy-based studies, we identified src tyrosine kinase family members src and fyn as upstream kinases of rsk2 tyr-529.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248352	Tyr531	FTATEPQyQPGENL	Homo sapiens	T-lymphocyte
pmid	sentence
11909961	On the membrane SKAP55, via its phosphorylated Tyr-271, further binds the SH2 domain of Fyn to replace the low-affinity bound inhibitory site of the kinase. Consequently, CD45 may have transiently disassociated with the Tyr-232 residue of SKAP55 through dephosphorylation and simultaneously interacted with the released the phosphorylated inhibitory tyrosine residue of Fyn for dephosphorylation, resulting in activation of the Src family kinase Fyn and initiation of TCR-engaged signal transduction.

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-96764	Tyr531	FTATEPQyQPGENL	Homo sapiens
pmid	sentence
12496362	Regulation of lck and fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248435	Tyr531	FTATEPQyQPGENL	Mus musculus	Brain Cell Line
pmid	sentence
9535845	In a coexpression system, PTPalpha effected a dose-dependent tyrosine dephosphorylation and activation of p59(fyn), where maximal dephosphorylation correlated with a 5-fold increase in kinase activity.\|the increased p59fyn catalytic activity and SH2 availability for binding are consistent with a PTPα-mediated dephosphorylation of the C-terminal Tyr-531 of p59fyn.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-154796	Tyr531	FTATEPQyQPGENL	Homo sapiens	T-lymphocyte
pmid	sentence
17507376	Ptpalpha is a more widely expressed transmembrane ptp that has been shown to regulate the src family kinases, src and fyn, and is also present in t cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279738	Tyr533	REPSPVRyDNLSRHI	Homo sapiens
pmid	sentence
26334723	Our study demonstrates that under basal conditions, PSD-95 and Fyn cooperatively stabilize DHHC5 at the synaptic membrane through Fyn-mediated phosphorylation of DHHC5 at tyrosine residue 533 and the subsequent inhibition of DHHC5 association with endocytic proteins (Fig. 10).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251177	Tyr550	AAGTQQPyTDGVRME	Rattus norvegicus
pmid	sentence
14517306	Phosphorylation of plakoglobin by Fer and Fyn kinases decreases plakoglobin-desmoplakin interaction and increases plakoglobin-α-catenin association. Fyn mainly phosphorylated Tyr549

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-251176	Tyr550	AAGTQQPyTDGVRME	Rattus norvegicus
pmid	sentence
14517306	Phosphorylation of plakoglobin by Fer and Fyn kinases decreases plakoglobin-desmoplakin interaction and increases plakoglobin-α-catenin association. Fyn mainly phosphorylated Tyr549 and that it phosphorylated Tyr133 with a much lower activity

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-273945	Tyr565	KKKTEGTyDLPYWDR	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273941	Tyr621	LQADSAEyAQPLVGG	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273942	Tyr655	GYADLDPyNSPGQEV	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273946	Tyr666	GQEVYHAyAEPLPIT	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273943	Tyr677	LPITGPEyATPIIMD	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273947	Tyr732	CSSAQAQyDTPKAGK	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-273944	Tyr750	PAPDELVyQVPQSTQ	in vitro
pmid	sentence
23770091	Mutagenesis analysis of ESDN's seven intracellular tyrosines in YxxP motifs found several contribute to the binding of ESDN to the SH2 domains of both CrkCT10 regulator of kinase Crk-Like (CrkL) and a representative SFK Fyn. Quantitative mass spectrometry showed that at least three of these (Y565, Y621 and Y750), as well as non-YxxP Y715, are reversibly phosphorylated. SFK activity was shown to be sufficient, but not required for the interaction between ESDN and the CrkL-SH2 domain. Finally, antibody-mediated ESDN clustering induces ESDN tyrosine phosphorylation and CrkL-SH2 binding.

Publications:

7

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277273	Tyr566	LSNQNNSyGTRFEYN	in vitro
pmid	sentence
27525436	We found that direct phosphorylation of tyrosine 566 on NOX4 was critical for this FYN-mediated negative regulation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-278358	Tyr576	RDEDGKPySPSEYSL	Homo sapiens
pmid	sentence
23434765	Fyn phosphorylates Nrf2 Y568, resulting in nuclear export and degradation of Nrf2.\|Fyn phosphorylates Nrf2Y568 resulting in nuclear export and degradation of Nrf2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251163	Tyr595	IEDDQEVyDDVAEQD	Homo sapiens
pmid	sentence
10570256	two tyrosines, Tyr595 and Tyr651, of FYB are major sites of phosphorylation by FYN-T and mediate binding to SLP-76 in Jurkat T cells. We further demonstrate that the loss of SLP-76 binding by mutation of these sites markedly reduced the ability of FYN-T-FYB-SLP-76 to up-regulate IL-2 transcription.

Identifier	Residue	Sequence	Organism
SIGNOR-251164	Tyr651	LDMGDEVyDDVDTSD	Homo sapiens
pmid	sentence
10570256	two tyrosines, Tyr595 and Tyr651, of FYB are major sites of phosphorylation by FYN-T and mediate binding to SLP-76 in Jurkat T cells. We further demonstrate that the loss of SLP-76 binding by mutation of these sites markedly reduced the ability of FYN-T-FYB-SLP-76 to up-regulate IL-2 transcription.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262875	Tyr60	SGDKDHLySTVCKPR	Chlorocebus aethiops
pmid	sentence
10838081	Hic-5 is a CAKbeta-binding protein localized at focal adhesions. Here we show that overexpression of CAKbeta or Fyn, but not FAK, enhanced the tyrosine phosphorylation of coexpressed Hic-5 in COS-7 cells. The Y60F mutant of Hic-5 was not phosphorylated, and Hic-5 phosphorylated on tyrosine 60 was bound specifically to the SH2 domain of Csk. Specific phosphorylation of Hic-5 by CAKbeta and Fyn may activate a signaling pathway mediated by Hic-5.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262745	Tyr605	MKDPTNGyYNVRAHE	Homo sapiens	HEK-293 Cell
pmid	sentence
18258597	Here we have characterized Neph1, another SD component, as a novel substrate of SFK. Fyn interacts with and phosphorylates the cytoplasmic domain of Neph1 in vitro and in intact cells. Both tyrosine 637 and 638 of Neph1 are crucial for Neph1-Grb2 binding.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262746	Tyr606	KDPTNGYyNVRAHED	Homo sapiens	HEK-293 Cell
pmid	sentence
18258597	Here we have characterized Neph1, another SD component, as a novel substrate of SFK. Fyn interacts with and phosphorylates the cytoplasmic domain of Neph1 in vitro and in intact cells. Both tyrosine 637 and 638 of Neph1 are crucial for Neph1-Grb2 binding.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251178	Tyr620	LTEELAEyAEIRVK	Mus musculus	Brain
pmid	sentence
7525550	Fyn constitutively binds to MAG in a latent form. Ligand stimulation of L-MAG would result in activation of Fyn kinase and phosphorylation of Tyr-620. Binding and activation of PLC y through this phosphotyrosine residue would contribute to the signaling pathway involved in the regulation of myelination.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-148700	Tyr64	ASLVSQDyVNGTDQE	Homo sapiens	Leukemia Cell, JURKAT Cell
pmid	sentence
16899217	To unravel the cellular functions of magicin, we used a yeast two-hybrid system and identified fyn tyrosine kinase as a specific binding partner for magicin. Fyn phosphorylates magicin in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78702	Tyr67	NASLESLySACSMQS	Homo sapiens
pmid	sentence
10871840	Grb10 tyrosine phosphorylation was stimulated by expression of constitutively active src or fyn in cells and by incubation with purified src or fyn in vitro. The insulin stimulated or src/fyn-mediated tyrosine phosphorylation in vivo was significantly reduced when grb10 tyrosine 67 was changed to glycine. This mutant form of grb10 bound with higher affinity to the ir in cells than that of the wild-type protein, suggesting that tyrosine phosphorylation of grb10 may normally negatively regulate its binding to the ir.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277410	Tyr70	HKETGNHyAMKILDK	in vitro
pmid	sentence
30274258	We found that the Src family kinase Fyn phosphorylates the catalytic subunit of PKA (PKA-C) at Y69, thereby increasing PKA kinase activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-63968	Tyr731	QQIDSCTyEAMYNIQ	Homo sapiens
pmid	sentence
9890970	Fyn associates with cbl and phosphorylates tyrosine 731 in cbl, a binding site for phosphatidylinositol 3-kinasecbl represents a substrate for src-like kinases that are activated in response to the engagement of cell surface receptors, and that src-like kinases are responsible for the phosphorylation of a tyrosine residue in cbl that may regulate activation of phosphatidylinositol 3-kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249339	Tyr753	ERDINSLyDVSRMYV	in vitro
pmid	sentence
7682059	The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors.

Identifier	Residue	Sequence	Organism
SIGNOR-249340	Tyr759	LYDVSRMyVDPSEIN	in vitro
pmid	sentence
7682059	The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors.

Publications:

2

Organism:

In Vitro

Pathways:

B-cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-278378	Tyr757	SKMQQNGyENPTYKF	Homo sapiens
pmid	sentence
18089558	Fyn induced phosphorylation of APP at Tyr-757 of the (757)YENPTY(762) motif and increased cell surface expression of APP.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275543	Tyr915	Y-->K
pmid	sentence
19816407	Synapse formation by PTPRT was inhibited by phosphorylation of tyrosine 912 within the membrane-proximal catalytic domain of PTPRT by Fyn. This tyrosine phosphorylation reduced phosphatase activity of PTPRT

Publications:

1

Identifier	Residue	Organism
SIGNOR-265330		Homo sapiens
pmid	sentence
15537652	Here we provide evidence that fyn kinase, a member of the src kinase family, is involved in the uvb-induced phosphorylation of histone h3 at serine 10

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279410		Homo sapiens
pmid	sentence
16860569	Here, we demonstrate that Fyn can directly phosphorylate the intracellular domain of TrkA and that its kinase activity towards Trk is increased by GPCR stimulation ( Fig. 4 ).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279523		Homo sapiens
pmid	sentence
12668668	Fyn directly bound Nephrin via its SH3 domain, and Fyn directly phosphorylated Nephrin.\|Similar to Fyn deletion, simultaneous deletion of Fyn and Yes reduced Nephrin phosphorylating activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279614		Homo sapiens
pmid	sentence
29790812	Our results demonstrate Fyn -mediated upregulation of Nav1.7 protein expression and tyrosine phosphorylation and identify two tyrosine residues within the DIII-DIV linker (L3) as Fyn phosphorylation sites.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279715		Homo sapiens
pmid	sentence
26848862	FYN phosphorylates FLT3 on tyrosine residues (A\u2013B) COS1 cells were transfected with plasmids expressing FLT3 wild-type and FYN wild-type or mutants.\|It was not completely unexpected that FYN associates wild-type FLT3 in the absence of ligand stimulation in COS-1 cells, as overexpression of wild-type FLT3 results in ligand independent activation of FLT3 (data not shown).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279717		Homo sapiens
pmid	sentence
21471003	Fyn phosphorylates TRPC6 and increases its diacylglycerol stimulated single channel activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279372		Homo sapiens
pmid	sentence
24586768	Taken together, these results suggest that p130Cas is directly phosphorylated by Fyn kinase in the cytoplasm of oligodendrocytes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-178607		Homo sapiens
pmid	sentence
18455992	Instead, shh rapidly and locally stimulated phosphorylation of the src family kinase (sfk) members src and fyn in a smo-dependent fashion.

Identifier	Residue	Organism
SIGNOR-199156		Homo sapiens
pmid	sentence
23074268	Instead, shh rapidly and locally stimulated phosphorylation of the src family kinase (sfk) members src and fyn in a smo-dependent fashion.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279043		Homo sapiens
pmid	sentence
23150273	Subsequently, Lck and Fyn phosphorylate and activate the Syk family kinase ZAP-70 when it is recruited to the phosphorylated ITAM motifs xref .

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism	Cell Line
SIGNOR-268216		Homo sapiens	B-lymphocyte
pmid	sentence
32323266	The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation

Identifier	Residue	Organism
SIGNOR-82287		Homo sapiens
pmid	sentence
11005864	Study of t cells from a fyn-deficient tcr transgenic mouse also showed that fyn was required for tyrosine phosphorylation and activation of vav induced by both antagonist and agonist peptides.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-100999		Homo sapiens
pmid	sentence
12730241	Insulin receptor-phosphorylated irs5/dok4 associates with rasgap, crk, src, and fyn, but not phosphatidylinositol 3-kinase p85, grb2, shp-2, nck, or phospholipase cgamma src homology 2 domains, and activates mapk in cells.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Kidney

Identifier	Residue	Organism
SIGNOR-278197		Homo sapiens
pmid	sentence
25340851	Fyn phosphorylates ApoER2.\|Together these data demonstrate that Fyn activity is necessary for its effects increasing ApoER2 levels.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-268210		Homo sapiens	B-lymphocyte
pmid	sentence
32323266	The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation

Identifier	Residue	Organism
SIGNOR-278476		Homo sapiens
pmid	sentence
21534960	Tyrosine phosphorylation of Dab1 by Fyn inhibits its interaction with APP, while increasing its interaction with Fyn.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251180		Chlorocebus aethiops
pmid	sentence
12496362	LAR PTPase domain 2 was tyrosine phosphorylated by Fyn tyrosine kinase. we confirmed that LAR dephosphorylated the phosphorylated tyrosine residues of Lck and Fyn, and tyrosine residue(s) in LAR PTPase D2 was phosphorylated by Fyn to supply Fyn SH2 binding site.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Organism	Cell Line
SIGNOR-68798		Homo sapiens	T-lymphocyte
pmid	sentence
10383400	Further indications of direct interaction are that p59fyn potentiates ?PKC Catalytic activity and that ?PKC Is a substrate for tyrosine phosphorylation by p59fyn.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-268213		Homo sapiens	B-lymphocyte
pmid	sentence
32323266	The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation

Identifier	Residue	Organism
SIGNOR-46851		Homo sapiens
pmid	sentence
9047237	P59fyn_phosphorylated slp-76 at intermediate levels but, significantly, this phosphorylation failed to induce vav?SLP-76 complex formation

Publications:

1

Organism:

Homo Sapiens

Pathways:

T cell activation

Identifier	Residue	Organism	Cell Line
SIGNOR-268207		Homo sapiens	B-lymphocyte
pmid	sentence
32323266	The CD79 molecules contain signaling molecules called immunoreceptor tyrosine-based activation motifs (ITAMs) in their intracellular portion. ITAMs are bound by the SRC kinases such as LYN, FYN and B-lymphoid tyrosine kinase (BLK). The crosslinking of BCR by specific antigens induces phosphorylation of ITAM tyrosines by these SRC kinases.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation

Identifier	Residue	Organism	Cell Line
SIGNOR-58424		Homo sapiens	Neuron
pmid	sentence
9648856	All these data suggest the involvement of fyn in the neurotrophin signal transduction pathways downstream of trkb. We investigated whether fyn is involved in the trk-dependent signal transduction pathways of neurotrophin. The fyn-src homology domain 2 (sh2) was observed to associate in vitro with the intracellular domain of trkb (icd-trkb).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279462		Homo sapiens
pmid	sentence
17371836	The tyrosine kinase Fyn modulates Sam68 mediated alternative splicing of Bcl-x mRNA.\|Tyrosine phosphorylation of Sam68 by Fyn inverted this effect and favored the Bcl-x(L) splice site selection.

Publications:

1

Organism:

Homo Sapiens

Name	FYN View Modifications
Full Name	Tyrosine-protein kinase Fyn
Synonyms	Proto-oncogene Syn, Proto-oncogene c-Fyn, Src-like kinase, SLK, p59-Fyn
Primary ID	P06241
Links	- -
Type	protein
Relations	143
Pathways	B-cell activation, Mitochondrial dynamics in T cell exhaustion, T cell activation
Function	Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).

The SIGnaling Network
Open Resource

Summary

Viewer

Search Tools

▶Modifications Tables

Relations