Relation Results

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-181452	Tyr1109	KGYSDEIyVVPDDSQ	Homo sapiens	Breast Cancer Cell
pmid	sentence
18829532	Breast tumor kinase phosphorylates p190rhogap to regulate rho and ras and promote breast carcinoma growth, migration, and invasion. Brk phosphorylates p190 at the y(1105) residue both in vitro and in vivo, thereby promoting the association of p190 with p120rasgap (p120). As a consequence, brk stimulates p190 and attenuates p120 functions, leading to rhoa inactivation and ras activation, respectively.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278286	Tyr142	AVVNLINyQDDAELA	Homo sapiens
pmid	sentence
20026641	PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.\|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-278287	Tyr331	LVNIMRTyTYEKLLW	Homo sapiens
pmid	sentence
20026641	PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.\|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-278289	Tyr333	NIMRTYTyEKLLWTT	Homo sapiens
pmid	sentence
20026641	PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.\|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-278288	Tyr64	VDTSQVLyEWEQGFS	Homo sapiens
pmid	sentence
20026641	PTK6 directly phosphorylates beta-catenin on Tyr64, Tyr142, Tyr331 and/or Tyr333, with the predominant site being Tyr64.\|The ability of PTK6 to negatively regulate beta-catenin and TCF transcription by modulating levels of TCF4 and TLE and Groucho could contribute to its growth-inhibitory activities in vivo.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-177238	Tyr165	PSPATDLyQVPPGPG	Homo sapiens
pmid	sentence
22084245	Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 crk-associated substrate. Tyrosine residues 165 and 664 of p130cas were both phosphorylated by ptk6 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263188	Tyr231	PEFDDSDyDEVPEEG	Homo sapiens	HEK-293 Cell
pmid	sentence
20554524	ARAP1 associated with PTK6 in an EGF/EGF receptor (EGFR)-dependent manner. In addition, the SH2 domain of PTK6, particularly the Arg(105) residue that contacts the phosphate group of the tyrosine residue, was essential for the association. Moreover, PTK6 phosphorylated residue Tyr(231) in the N-terminal domain of ARAP1. Expression of ARAP1, but not of the Y231F mutant, inhibited the down-regulation of EGFR in HEK293 cells expressing PTK6. These results demonstrate that PTK6 enhances EGFR signaling by inhibition of EGFR down-regulation through phosphorylation of ARAP1 in breast cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247067	Tyr250	PFLLDEDyEKVLGYV	Homo sapiens
pmid	sentence
19393627	Our previous studies revealed that STAP-2 binds to signal transducer and activator of transcription 3 (STAT3) and STAT5, and regulates the signaling pathways downstream of them. In the present study, we identified tyrosine-250 (Tyr250) in STAP-2 as a major site of phosphorylation by Brk, using a series of STAP-2 YF mutants and anti-phospho-STAP-2 Tyr250 antibody. Furthermore, overexpression of the STAP-2 Y250F mutant protein affected Brk-mediated STAT3 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-138437	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens
pmid	sentence
15994200	These observations suggest that RET/PTC is able to phosphorylate the Y315 residue of PKB, an event that results in maximal activation of PKB for RET/PTC-induced thyroid tumorigenesis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-166506	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-166510	Tyr326	EVLEDNDyGRAVDWW	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Prostate Gland

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252618	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Identifier	Residue	Sequence	Organism
SIGNOR-252617	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens
pmid	sentence
15994200	These observations suggest that RET/PTC is able to phosphorylate the Y315 residue of PKB, an event that results in maximal activation of PKB for RET/PTC-induced thyroid tumorigenesis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252622	Tyr326	EVLEDNDyGRAVDWW	Homo sapiens	Breast Cancer Cell
pmid	sentence
20606012	Here we demonstrate that AKT is a direct substrate of PTK6 and that AKT tyrosine residues 315 and 326 are phosphorylated by PTK6.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Prostate Gland

Identifier	Residue	Sequence	Organism
SIGNOR-276975	Tyr342	RLIKEDVyLSHDHNI	in vitro
pmid	sentence
29142193	PTEN inhibits PTK6 activity and downstream signaling in prostate cancer cells.\|Using an in vitro phosphatase assay, we observed that PTEN was able to dephosphorylate PTK6 at tyrosine residue 342 in a dose dependent manner.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277082	Tyr342	RLIKEDVyLSHDHNI	Homo sapiens
pmid	sentence
29142193	Using a variety of PTEN mutant constructs, we show that protein phosphatase activity of PTEN targets PTK6, with efficiency similar to PTP1B, a phosphatase that directly dephosphorylates PTK6 Y342.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-90604	Tyr342	RLIKEDVyLSHDHNI	Homo sapiens	Breast Cancer Cell
pmid	sentence
12121988	Autophosphorylation increases enzyme activity of wild-type brk but not of a y342a mutant form of brk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278301	Tyr362	DPKEDPIyDEPEGLA	Homo sapiens
pmid	sentence
24523872	BRK downregulates Dok1 via proteasomal degradation.\|BRK phosphorylates Dok1 at tyrosine 362.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249293	Tyr435	ARPVKGAyREHPYGR	Homo sapiens
pmid	sentence
16179349	We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249294	Tyr440	GAYREHPyGRY	Homo sapiens	HeLa Cell
pmid	sentence
16179349	We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal. \|Tyrosine 440 was identified as a principal modulator of Sam68 localization and this site was phosphorylated in response to EGF treatment in human breast tumor cell lines.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249292	Tyr443	REHPYGRy	Homo sapiens	HeLa Cell
pmid	sentence
16179349	We show that BRK phosphorylates Sam68 on all three tyrosines in the nuclear localization signal.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249152	Tyr447	RLSSFTSyENPT	Homo sapiens
pmid	sentence
12121988	Mutation of a C-terminal tyrosine (Tyr-447) increases enzyme activity and SH2 domain accessibility, consistent with a role for this residue in autoinhibition. \| These results suggest that the Y447F and W44A mutations disrupt the normal intramolecular regulation of Brk and increase the catalytic activity of Brk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263189	Tyr498	YAFSSNIyTRGSHLD	Homo sapiens	HEK-293 Cell
pmid	sentence
27738316	Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis.

Identifier	Residue	Sequence	Organism
SIGNOR-263190	Tyr525	NRHIDRNyEPLKTQP	Homo sapiens
pmid	sentence
28214294	Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263191	Tyr535	LKTQPKKyAKSKYDF	Homo sapiens	HEK-293 Cell
pmid	sentence
28214294	Eps8 which was identified by this method is phosphorylated by Myr-PTK6 in HEK293 cells. Mouse Eps8 expressed in HEK293 cells is phosphorylated by Myr-PTK6 at residues Tyr497, Tyr524, and Tyr534. These results indicate that plasma-membrane-associated PTK6 phosphorylates Eps8, which promotes cell proliferation, adhesion, and migration and, thus, tumorigenesis.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-177242	Tyr664	EGGWMEDyDYVHLQG	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
22084245	Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 crk-associated substrate. Tyrosine residues 165 and 664 of p130cas were both phosphorylated by ptk6 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-159066	Tyr699	TAKAVDGyVKPQIKQ	Homo sapiens	Breast Cancer Cell
pmid	sentence
17997837	Phosphospecific antibodies, mutational analysis, and in vitro kinase assays demonstrated that brk specifically mediated stat5b phosphorylation at the activating tyrosine, y699.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278346	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens
pmid	sentence
26247733	29 PTK6 promotes activating phosphorylation of STAT3 at tyrosine residue 705.\|STAT3 has been shown to promote tumor initiation of different tumor types, including those of the gastrointestinal tract and skin, and PTK6 was previously shown to promote STAT3 activation and tumorigenesis in mouse models of colon and skin cancer.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278428	Tyr861	PIGNQHIyQPVGKPD	Homo sapiens
pmid	sentence
23027128	B. PTK6 phosphorylates FAK at tyrosine residue 861.\|Knockdown of PTK6 in the PC3 human prostate cancer cell line disrupts FAK and AKT activation and promotes anoikis, which can be rescued by exogenous expression of FAK.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-80020		Homo sapiens	Breast Cancer Cell
pmid	sentence
10913193	Sik/brk is the first identified tyrosine kinase that can phosphorylate sam68 and regulate its activity within the nucleus, where it resides during most of the cell cycle

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-81489		Homo sapiens	Breast Cancer Cell
pmid	sentence
10980601	The phosphorylation of and association with bks by brk was also dependent on the sh2-like domain present within bks.bks is a substrate for the kinase activity of brk and has the characteristics of an adaptor protein.

Publications:

1

Organism:

Homo Sapiens

Name	PTK6 View Modifications
Full Name	Protein-tyrosine kinase 6
Synonyms	Breast tumor kinase, Tyrosine-protein kinase BRK \| BRK
Primary ID	Q13882
Links	- -
Type	protein
Relations	31
Function	Non-receptor tyrosine-protein kinase implicated in the regulation of a variety of signaling pathways that control the differentiation and maintenance of normal epithelia, as well as tumor growth. Function seems to be context dependent and differ depending on cell type, as well as its intracellular localization. A number of potential nuclear and cytoplasmic substrates have been identified. These include the RNA-binding proteins

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