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PTK6 (protein tyrosine kinase 6)

Written2014-09Priya S Mathur, Angela L Tyner
Department of Biochemistry, Molecular Genetics, University of Illinois College of Medicine, Chicago, IL 60607, USA

(Note : for Links provided by Atlas : click)

Identity

Alias_namesPTK6 protein tyrosine kinase 6
Alias_symbol (synonym)BRK
Other alias
HGNC (Hugo) PTK6
LocusID (NCBI) 5753
Atlas_Id 41900
Location 20q13.33  [Link to chromosome band 20q13]
Location_base_pair Starts at 62159776 and ends at 62168723 bp from pter ( according to hg19-Feb_2009)  [Mapping PTK6.png]
Note Chromosome 2 in Mouse.

DNA/RNA

Description The PTK6 gene contains 8948 bp comprising 8 coding exons.
PTK6 belongs to a small family of intracellular tyrosine kinases with conserved functional domain homology that is related to, but distinct from, the SRC family of kinases (Lee et al., 1998); reviewed in (Serfas and Tyner, 2003; Brauer and Tyner, 2010). Members of the PTK6 family are defined by a highly conserved intron-exon structure that is distinct from other major intracellular tyrosine kinase families; other family members include FRK (FYN-related kinase, also known as Rak) and SRMS (SRC-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites). The PTK6 and SRMS genes are tightly linked on human chromosome 20q13.3 (Kohmura et al., 1994; Llor et al., 1999; Serfas and Tyner, 2003).
Transcription Alternative splicing gives rise to an RNA encoding a small protein containing the amino terminus, the SH3 domain, and a unique carboxyl terminus (isoform 2) (Mitchell et al., 1994; Brauer et al., 2011).

Protein

 
Description Isoform 1
Size: 451 amino acids; ~ 52 KDa.
PTK6 contains SH3 and SH2 protein-protein interaction domains, an SH1 kinase domain, and a regulatory carboxy terminus. Phosphorylation of residue Y342 is required for full activation of kinase activity and activity is negatively regulated by tyrosine phosphorylation of its carboxy-terminal tyrosine residue, Y-447 (Qiu and Miller, 2002; Qiu and Miller, 2004; Qiu et al., 2005).
Isoform 2 (also known as ALT-PTK6, delta m5)
Size: 134 aa; ~15 KDa.
ALT-PTK6 is the product of an alternatively-spliced RNA that encodes a truncated protein due to a premature stop codon; alternative splicing deletes exon 2 and causes in a frameshift. The N-terminus and SH3 domain of ALT-PTK6 are identical to the full-length protein, but it has a unique C-terminus lacking the SH2 and SH1 domains and is thus catalytically inactive (Mitchell et al., 1994; Brauer et al., 2011).
Two additional PTK6 sequences, CRA_a (GenBank: EAW75262.1) and CRA_b (GenBank: EAW75263.1) that would encode larger ~59 kDa proteins have been identified by Celera Genomics, but these isoforms have not been characterized and their biological significance is not known.
Expression Normal Epithelium
PTK6 was first identified in cultured human melanocytes (Lee et al., 1993), breast tumor cells (Mitchell et al., 1994), and mouse small intestine (Siyanova et al., 1994). It is primarily an epithelial kinase that is first detectable in the differentiating granular layer of the skin during late embryogenesis of the mouse at E15.5 (Vasioukhin et al., 1995). In adults, PTK6 is predominantly expressed in the epithelial cells of the gastrointestinal tract (Siyanova et al., 1994; Llor et al., 1999), and skin (Vasioukhin et al., 1995; Wang et al., 2005). In regenerating tissues, such as the small intestine, colon, and skin, PTK6 expression is largely restricted to epithelial cells that are exiting the cell cycle and undergoing terminal differentiation, which are located on the villi in the small intestine, surface epithelium in the colon (Haegebarth et al., 2006), and the suprabasal layer of the skin (Vasioukhin et al., 1995; Wang et al., 2005) as well as in the oral mucosa (Petro et al., 2004). PTK6 is also expressed in the nuclei of normal epithelium of the prostate (Derry et al., 2003), and mammary gland (Peng et al., 2014). Although it is largely restricted to epithelia, PTK6 expression was also reported in activated normal T-cells (Kasprzycka et al., 2006).
Cancer
PTK6 is overexpressed in a large majority of human breast tumors and in most breast cancer cell lines (Barker et al., 1997; Harvey and Crompton, 2003; Ostrander et al., 2007). PTK6 expression is also induced in prostate tumors and cell lines (Zheng et al., 2012); relocalization of PTK6 from the nucleus to cytoplasm was reported in prostate cancer cells (Derry et al., 2003). In breast cancer cells, PTK6 expression has been shown to be mediated by hypoxia via multiple mechanisms; PTK6 protein is stabilized by HSP90 (Kang et al., 2012) and is transcriptionally upregulated by HIF-1a and HIF-2a (Regan Anderson et al., 2013), additionally PTK6 protein can be upregulated in a post-translational manner in response to hypoxia (Pires et al., 2014). PTK6 has been identified as a transcriptional target of CREB, and its expression is upregulated by p90RSK2 phosphorylation of CREB (Jin et al., 2013). PTK6 expression is modestly upregulated in primary colon tumors (Llor et al., 1999), and downregulated in metastatic colon cancer (Chen et al., 1999). In squamous cell carcinoma, PTK6 expression is reduced with increasing malignancy (Petro et al., 2004; Wang et al., 2005).
Function PTK6 is an intracellular protein tyrosine kinase that has distinct context-dependent functions in different normal and cancerous tissues based on its intracellular localization and kinase activity. Studies in breast and ovarian cancer cell lines find that PTK6 interacts with growth factor receptors EGFR (Kamalati et al., 2000) and ERBB2 (Ostrander et al., 2007; Xiang et al., 2008) to propagate growth factor-mediated signaling. PTK6 binds and phosphorylates IGF-1R (Fan et al., 2013) and promotes anchorage independent growth via interactions with IRS-4 and IGF1R (Qiu et al., 2005; Irie et al., 2010). PTK6 has also been shown to mediate Met receptor signaling, although a direct interaction has not been demonstrated (Locatelli et al., 2012). PTK6 stabilizes EGFR expression by phosphorylating ARAP1 (Arf-GAP, Rho-GAP, ankyrin repeat, and pleckstrin homology domain-containing protein 1) (Kang et al., 2010); interaction with EGFR mediates PTK6 phosphorylation of paxillin (Chen et al., 2004) and p190RhoGAP (Shen et al., 2008) in breast cancer cells as well as AKT in breast (Zhang et al., 2005) and prostate (Zheng et al., 2010) cancer cell lines to promote proliferation, invasion, and migration. PTK6 has also been shown to promote breast cancer cell migration via phosphorylation of KAP3A (Lukong and Richard, 2008) and Dok1 (Miah et al., 2014). Membrane-targeted active PTK6 in prostate cancer cell lines phosphorylates pro-oncogenic substrates BCAR1 (Zheng et al., 2012) and FAK (Zheng et al., 2013a). PTK6 phosphorylates and activates Signal Transducers and Activators of Transcription STAT3 (Liu et al., 2006) and STAT5a (Weaver and Silva, 2007) as well as the related scaffolding protein STAP2 (Mitchell et al., 2000). β-catenin has also been identified as a PTK6 substrate; when targeted to the cell membrane PTK6 can activate β-catenin, while nuclear PTK6 negatively regulates β-catenin transcriptional activity in a kinase-independent manner (Palka-Hamblin et al., 2010). PTK6 phosphorylation of the nuclear RNA-splicing factors SAM68 (Derry et al., 2000) and related SLM1 and SLM2 proteins (Haegebarth et al., 2004), as well as PSF (Lukong et al., 2009) inhibits their RNA-binding activity to promote differentiation and cell cycle arrest. PTK6 is a substrate of the PTP1B phosphatase (Fan et al., 2013).
PTK6 promotes epithelial differentiation of enterocytes in the small intestine (Haegebarth et al., 2006) and keratinocytes in skin (Vasioukhin and Tyner, 1997; Wang et al., 2005). In cultured human keratinocytes, addition of calcium promotes differentiation, which is accompanied by increased PTK6 expression and activation, and elevated levels of the epidermal differentiation markers (Vasioukhin and Tyner, 1997) dependent on PTK6 kinase activity (Wang et al., 2005). Disruption of the Ptk6 gene led to impaired intestinal differentiation and increased intestinal proliferation in mice (Haegebarth et al., 2006). When ectopically expressed, PTK6 sensitized non-transformed Rat1a fibroblasts to apoptosis (Haegebarth et al., 2005). Induction of PTK6 in intestinal crypts following total body γ-irradiation enhanced apoptosis in the murine intestinal epithelium, including in intestinal crypts, where it promotes DNA damage-induced apoptosis (Haegebarth et al., 2009). In human colon cancer cell lines and in murine colon tissue, PTK6 negatively regulates β-catenin transcriptional activity (Palka-Hamblin et al., 2010). PTK6 has a tumor-promoting role in the colon as disruption of the Ptk6 gene impaired carcinogen-induced tumorigenesis in mice (Gierut et al., 2011) and PTK6 promotes survival of colon cancer cell lines following DNA damaging treatments including γ-irradiation and chemotherapeutic drugs via STAT3 activation (Gierut et al., 2012).
Targeting PTK6 to plasma membrane enhanced proliferation, survival, migration and anchorage-independent growth in HEK293 cells, while nuclear targeting inhibited the invasive phenotype (Kim and Lee, 2009). Targeting active PTK6 to the plasma membrane in SYF (deficient for SRC, YES, and FYN) mouse embryonic fibroblasts was sufficient to transform these cells (Zheng et al., 2013a). In prostate cancer cells, targeting PTK6 to the nucleus inhibits proliferation while cytoplasmic PTK6 promotes proliferation (Brauer et al., 2010). Overexpression of membrane-targeted active PTK6 in prostate cancer cells drives epithelial-mesenchymal transition (Zheng et al., 2012) and anchorage-independent survival (Zheng et al., 2013a) as well as in vivo xenograft metastasis (Zheng et al., 2013b). Recently, PTK6 was detected in nuclei of normal mammary gland epithelium (Peng et al., 2014), and overexpression of PTK6 promotes oncogenic signaling and invasive phenotypes in breast cancer cells (Harvey and Crompton, 2003; Xiang et al., 2008; Irie et al., 2010). In human prostate and breast cancers, PTK6 is activated at the plasma membrane (Zheng et al., 2013b; Peng et al., 2014).

Mutations

Somatic A few PTK6 mutations have been reported in human cancers. A frameshift mutation resulting in the deletion of 58 amino acid residues (W78fsX58) has been identified in a human bladder cancer cell line and NSCLC cell line (Ruhe et al., 2007). Two point mutations have been reported in a small number of melanoma cases; W210X within the tyrosine kinase domain and a -7 intronic C>T mutation within a splice site (Prickett et al., 2009). Additional mutations have been identified by genomic sequencing (cBioPortal).

Implicated in

Note
  
Entity Breast cancer
Note PTK6 is overexpressed in most human breast tumors and breast cancer cell lines (Barker et al., 1997; Born et al., 2005; Ostrander et al., 2007; Irie et al., 2010). Irie and colleagues detected increased levels of PTK6 mRNA expression in HER2/ERBB2, luminal A and luminal B subtypes of breast cancer and found that high PTK6 expression correlated with reduced recurrence-free survival (Irie et al., 2010). PTK6 protein expression has prognostic significance in breast cancer (Born et al., 2005; Aubele et al., 2009), and active PTK6 protein was detected in human breast tumors but not normal human mammary gland (Peng et al., 2014). Overexpression of PTK6 promotes mammary gland cancer tumorigenesis in mouse models (Lofgren et al., 2011; Peng et al., 2013). PTK6 sustains EGFR signaling via transactivation as well as by inhibition of EGFR degradation (Kang et al., 2010; Li et al., 2012). The correlation between PTK6 and ERBB2 overexpression in invasive human ductal breast carcinomas (Born et al., 2005; Aubele et al., 2007; Ostrander et al., 2007; Xiang et al., 2008) raises the possibility that targeting PTK6 along with ERBB receptors might offer a therapeutic advantage (Harvey and Crompton, 2004; Ostrander et al., 2010). In response to HGF stimulation, PTK6 mediates Met signaling to promote breast cancer cell migration (Castro and Lange, 2010). PTK6 binds with IGF-1R to mediate IGF-1 signaling promoting anchorage-independent growth (Irie et al., 2010). PTK6 expression is upregulated by hypoxia and promotes hypoxia-mediated breast cancer progression (Aubele et al., 2009; Kang et al., 2012; Pires et al., 2014).
  
  
Entity Prostate cancer
Note Elevated expression and relocalization of PTK6 have been reported in prostate cancer. Analysis of Oncomine microarray data showed that PTK6 mRNAs levels are higher in metastatic prostate tumors, and patients with high PTK6 have reduced survival (Zheng et al., 2013b). Knockdown of PTK6 in the human PC3 prostate tumor cell line inhibited xenograft tumor growth (Zheng et al., 2013). In normal prostate epithelium, PTK6 expression is nuclear and expression relocalizes to the cytoplasm and membrane in poorly-differentiated prostate tumors (Derry et al., 2003). Targeting PTK6 to the nucleus in prostate cancer cells arrests their growth while cytoplasmic PTK6 promotes proliferation (Brauer et al., 2010). In the cytoplasm, PTK6 may phosphorylate AKT on tyrosine residues to promote activation and downstream signaling (Zheng et al., 2010). Targeting active PTK6 to the plasma membrane in prostate cancer cells drives epithelial-mesenchymal transition via activation of BCAR1 (Zheng et al., 2012) and anchorage-independent survival via activation of FAK (Zheng et al., 2013a). RSK-mediated expression of PTK6 may contribute to metastasis of prostate cancer cells (Yu et al., 2014).
  
  
Entity Colon cancer
Note PTK6 expression is mildly up-regulated in primary colon tumors (Llor et al., 1999), and down-regulated in metastatic colon cancer (Chen et al., 1999). Disruption of Ptk6 impairs carcinogen induced tumorigenesis in mice, suggesting a tumor-promoting role for the kinase in the colon as well (Gierut et al., 2011). In human colon cancer cell lines, PTK6 promotes cell survival following DNA damaging treatments including γ-irradiation and chemotherapeutic drugs via STAT3 activation (Gierut et al., 2012).
  
  
Entity Other cancers
Note PTK6 has been implicated in several different types of human cancer, with distinct context-specific functions. As in breast and prostate cancers, PTK6 has pro-oncogenic roles in some other cancers. The Ptk6 gene is amplified and PTK6 protein is overexpressed in and may promote the development and growth of ovarian tumors (Schmandt et al., 2006). PTK6 signaling via IGF1R in ovarian cancer promotes cell growth and is inhibitted by PTP1B (Fan et al., 2013). PTK6 is also overexpressed in head and neck cancer, where it may play a role in HNSCC development and progression (Lin et al., 2004). High PTK6 expression is associated with poor prognosis and metastasis in nasopharyngeal carcinoma (Liu et al., 2013a). PTK6 expression is increased in non-small cell lung carcinoma (Fan et al., 2011) and is associated with poor prognosis (Zhao et al., 2013); PTK6 has been identified as a potential therapeutic target in NSCLC (Yauch et al., 2005; Li et al., 2010). It has also been demonstrated that knockdown of PTK6 reduces migration and invasion of pancreatic cancer cells (Ono et al., 2014). Constitutive expression of PTK6 has been reported in cutaneous T-cell lymphomas as well as in other transformed T- and B-cell populations (Kasprzycka et al., 2006).
In some cases, PTK6 may have tumor suppressor functions. It is down-regulated in human esophageal squamous cell carcinomas (ESCC); knockdown of PTK6 in human ESCC cells enhanced xenograft tumor growth (Ma et al., 2012). Low PTK6 expression correlates with poor prognosis in patients with laryngeal squamous cell carcinoma (Liu et al., 2013b). PTK6 expression is reduced with increasing malignancy in squamous cell carcinomas of the skin (Wang et al., 2005) and oral mucosa (Petro et al., 2004).
  

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Differential expression of the non-receptor tyrosine kinase BRK in oral squamous cell carcinoma and normal oral epithelium.
Petro BJ, Tan RC, Tyner AL, Lingen MW, Watanabe K.
Oral Oncol. 2004 Nov;40(10):1040-7.
PMID 15509496
 
HIF-1α-independent hypoxia-induced rapid PTK6 stabilization is associated with increased motility and invasion.
Pires IM, Blokland NJ, Broos AW, Poujade FA, Senra JM, Eccles SA, Span PN, Harvey AJ, Hammond EM.
Cancer Biol Ther. 2014 Oct;15(10):1350-7. doi: 10.4161/cbt.29822. Epub 2014 Jul 14.
PMID 25019382
 
Analysis of the tyrosine kinome in melanoma reveals recurrent mutations in ERBB4.
Prickett TD, Agrawal NS, Wei X, Yates KE, Lin JC, Wunderlich JR, Cronin JC, Cruz P, Rosenberg SA, Samuels Y.
Nat Genet. 2009 Oct;41(10):1127-32. doi: 10.1038/ng.438. Epub 2009 Aug 30.
PMID 19718025
 
Role of the Brk SH3 domain in substrate recognition.
Qiu H, Miller WT.
Oncogene. 2004 Mar 18;23(12):2216-23.
PMID 14676834
 
Interaction between Brk kinase and insulin receptor substrate-4.
Qiu H, Zappacosta F, Su W, Annan RS, Miller WT.
Oncogene. 2005 Aug 25;24(36):5656-64.
PMID 15870689
 
Breast tumor kinase (Brk/PTK6) is a mediator of hypoxia-associated breast cancer progression.
Regan Anderson TM, Peacock DL, Daniel AR, Hubbard GK, Lofgren KA, Girard BJ, Schorg A, Hoogewijs D, Wenger RH, Seagroves TN, Lange CA.
Cancer Res. 2013 Sep 15;73(18):5810-20. doi: 10.1158/0008-5472.CAN-13-0523. Epub 2013 Aug 8.
PMID 23928995
 
Genetic alterations in the tyrosine kinase transcriptome of human cancer cell lines.
Ruhe JE, Streit S, Hart S, Wong CH, Specht K, Knyazev P, Knyazeva T, Tay LS, Loo HL, Foo P, Wong W, Pok S, Lim SJ, Ong H, Luo M, Ho HK, Peng K, Lee TC, Bezler M, Mann C, Gaertner S, Hoefler H, Iacobelli S, Peter S, Tay A, Brenner S, Venkatesh B, Ullrich A.
Cancer Res. 2007 Dec 1;67(23):11368-76.
PMID 18056464
 
The BRK tyrosine kinase is expressed in high-grade serous carcinoma of the ovary.
Schmandt RE, Bennett M, Clifford S, Thornton A, Jiang F, Broaddus RR, Sun CC, Lu KH, Sood AK, Gershenson DM.
Cancer Biol Ther. 2006 Sep;5(9):1136-41. Epub 2006 Sep 28.
PMID 16855388
 
Brk, Srm, Frk, and Src42A form a distinct family of intracellular Src-like tyrosine kinases.
Serfas MS, Tyner AL.
Oncol Res. 2003;13(6-10):409-19. (REVIEW)
PMID 12725532
 
Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and promote breast carcinoma growth, migration, and invasion.
Shen CH, Chen HY, Lin MS, Li FY, Chang CC, Kuo ML, Settleman J, Chen RH.
Cancer Res. 2008 Oct 1;68(19):7779-87. doi: 10.1158/0008-5472.CAN-08-0997.
PMID 18829532
 
Tyrosine kinase gene expression in the mouse small intestine.
Siyanova EY, Serfas MS, Mazo IA, Tyner AL.
Oncogene. 1994 Jul;9(7):2053-7.
PMID 8208550
 
A role for the epithelial-cell-specific tyrosine kinase Sik during keratinocyte differentiation.
Vasioukhin V, Tyner AL.
Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14477-82.
PMID 9405638
 
Role of breast tumour kinase in the in vitro differentiation of HaCaT cells.
Wang TC, Jee SH, Tsai TF, Huang YL, Tsai WL, Chen RH.
Br J Dermatol. 2005 Aug;153(2):282-9.
PMID 16086737
 
Signal transducer and activator of transcription 5b: a new target of breast tumor kinase/protein tyrosine kinase 6.
Weaver AM, Silva CM.
Breast Cancer Res. 2007;9(6):R79.
PMID 17997837
 
Brk is coamplified with ErbB2 to promote proliferation in breast cancer.
Xiang B, Chatti K, Qiu H, Lakshmi B, Krasnitz A, Hicks J, Yu M, Miller WT, Muthuswamy SK.
Proc Natl Acad Sci U S A. 2008 Aug 26;105(34):12463-8. doi: 10.1073/pnas.0805009105. Epub 2008 Aug 21.
PMID 18719096
 
Epithelial versus mesenchymal phenotype determines in vitro sensitivity and predicts clinical activity of erlotinib in lung cancer patients.
Yauch RL, Januario T, Eberhard DA, Cavet G, Zhu W, Fu L, Pham TQ, Soriano R, Stinson J, Seshagiri S, Modrusan Z, Lin CY, O'Neill V, Amler LC.
Clin Cancer Res. 2005 Dec 15;11(24 Pt 1):8686-98.
PMID 16361555
 
RSK Promotes Prostate Cancer Progression in Bone through ING3, CKAP2 and PTK6-mediated Cell Survival.
Yu G, Lee YC, Cheng CJ, Wu CF, Song JH, Gallick GE, Yu-Lee LY, Kuang J, Lin SH.
Mol Cancer Res. 2014 Sep 4. pii: molcanres.0384.2014. [Epub ahead of print]
PMID 25189355
 
Regulated association of protein kinase B/Akt with breast tumor kinase.
Zhang P, Ostrander JH, Faivre EJ, Olsen A, Fitzsimmons D, Lange CA.
J Biol Chem. 2005 Jan 21;280(3):1982-91. Epub 2004 Nov 10.
PMID 15539407
 
Expression of protein tyrosine kinase 6 (PTK6) in nonsmall cell lung cancer and their clinical and prognostic significance.
Zhao C, Chen Y, Zhang W, Zhang J, Xu Y, Li W, Chen S, Deng A.
Onco Targets Ther. 2013;6:183-8. doi: 10.2147/OTT.S41283. Epub 2013 Mar 8.
PMID 23525678
 
Protein-tyrosine kinase 6 promotes peripheral adhesion complex formation and cell migration by phosphorylating p130 CRK-associated substrate.
Zheng Y, Asara JM, Tyner AL.
J Biol Chem. 2012 Jan 2;287(1):148-58. doi: 10.1074/jbc.M111.298117. Epub 2011 Nov 14.
PMID 22084245
 
Protein tyrosine kinase 6 protects cells from anoikis by directly phosphorylating focal adhesion kinase and activating AKT.
Zheng Y, Gierut J, Wang Z, Miao J, Asara JM, Tyner AL.
Oncogene. 2013a Sep 5;32(36):4304-12. doi: 10.1038/onc.2012.427. Epub 2012 Oct 1.
PMID 23027128
 
Protein tyrosine kinase 6 directly phosphorylates AKT and promotes AKT activation in response to epidermal growth factor.
Zheng Y, Peng M, Wang Z, Asara JM, Tyner AL.
Mol Cell Biol. 2010 Sep;30(17):4280-92. doi: 10.1128/MCB.00024-10. Epub 2010 Jul 6.
PMID 20606012
 
PTK6 activation at the membrane regulates epithelial-mesenchymal transition in prostate cancer.
Zheng Y, Wang Z, Bie W, Brauer PM, Perez White BE, Li J, Nogueira V, Raychaudhuri P, Hay N, Tonetti DA, Macias V, Kajdacsy-Balla A, Tyner AL.
Cancer Res. 2013b Sep 1;73(17):5426-37. doi: 10.1158/0008-5472.CAN-13-0443. Epub 2013 Jul 15.
PMID 23856248
 

Citation

This paper should be referenced as such :
Mathur PS, Tyner AL
PTK6 (protein tyrosine kinase 6);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version : http://AtlasGeneticsOncology.org/Genes/PTK6ID41900ch20q13.html


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(1;9)(p34;q34) SFPQ/ABL1


External links

Nomenclature
HGNC (Hugo)PTK6   9617
Cards
AtlasPTK6ID41900ch20q13
Entrez_Gene (NCBI)PTK6  5753  protein tyrosine kinase 6
AliasesBRK
GeneCards (Weizmann)PTK6
Ensembl hg19 (Hinxton)ENSG00000101213 [Gene_View]  chr20:62159776-62168723 [Contig_View]  PTK6 [Vega]
Ensembl hg38 (Hinxton)ENSG00000101213 [Gene_View]  chr20:62159776-62168723 [Contig_View]  PTK6 [Vega]
ICGC DataPortalENSG00000101213
TCGA cBioPortalPTK6
AceView (NCBI)PTK6
Genatlas (Paris)PTK6
WikiGenes5753
SOURCE (Princeton)PTK6
Genetics Home Reference (NIH)PTK6
Genomic and cartography
GoldenPath hg19 (UCSC)PTK6  -     chr20:62159776-62168723 -  20q13.3   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)PTK6  -     20q13.3   [Description]    (hg38-Dec_2013)
EnsemblPTK6 - 20q13.3 [CytoView hg19]  PTK6 - 20q13.3 [CytoView hg38]
Mapping of homologs : NCBIPTK6 [Mapview hg19]  PTK6 [Mapview hg38]
OMIM602004   
Gene and transcription
Genbank (Entrez)AK124082 AK301364 AK301691 AK315232 BC035843
RefSeq transcript (Entrez)NM_001256358 NM_005975
RefSeq genomic (Entrez)NC_000020 NC_018931 NT_011362 NW_004929419
Consensus coding sequences : CCDS (NCBI)PTK6
Cluster EST : UnigeneHs.51133 [ NCBI ]
CGAP (NCI)Hs.51133
Alternative Splicing GalleryENSG00000101213
Gene ExpressionPTK6 [ NCBI-GEO ]   PTK6 [ EBI - ARRAY_EXPRESS ]   PTK6 [ SEEK ]   PTK6 [ MEM ]
Gene Expression Viewer (FireBrowse)PTK6 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5753
GTEX Portal (Tissue expression)PTK6
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13882   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ13882  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ13882
Splice isoforms : SwissVarQ13882
Catalytic activity : Enzyme2.7.10.2 [ Enzyme-Expasy ]   2.7.10.22.7.10.2 [ IntEnz-EBI ]   2.7.10.2 [ BRENDA ]   2.7.10.2 [ KEGG ]   
PhosPhoSitePlusQ13882
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    SH2 (PS50001)    SH3 (PS50002)   
Domains : Interpro (EBI)Kinase-like_dom    Prot_kinase_dom    Protein_kinase_ATP_BS    Ser-Thr/Tyr_kinase_cat_dom    SH2    SH3_domain    Tyr_kinase_AS    Tyr_kinase_cat_dom   
Domain families : Pfam (Sanger)Pkinase_Tyr (PF07714)    SH2 (PF00017)    SH3_1 (PF00018)   
Domain families : Pfam (NCBI)pfam07714    pfam00017    pfam00018   
Domain families : Smart (EMBL)SH2 (SM00252)  SH3 (SM00326)  TyrKc (SM00219)  
Conserved Domain (NCBI)PTK6
DMDM Disease mutations5753
Blocks (Seattle)PTK6
PDB (SRS)1RJA    2KGT   
PDB (PDBSum)1RJA    2KGT   
PDB (IMB)1RJA    2KGT   
PDB (RSDB)1RJA    2KGT   
Structural Biology KnowledgeBase1RJA    2KGT   
SCOP (Structural Classification of Proteins)1RJA    2KGT   
CATH (Classification of proteins structures)1RJA    2KGT   
SuperfamilyQ13882
Human Protein AtlasENSG00000101213
Peptide AtlasQ13882
HPRD03594
IPIIPI00015927   IPI01010624   
Protein Interaction databases
DIP (DOE-UCLA)Q13882
IntAct (EBI)Q13882
FunCoupENSG00000101213
BioGRIDPTK6
STRING (EMBL)PTK6
ZODIACPTK6
Ontologies - Pathways
QuickGOQ13882
Ontology : AmiGOruffle  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  receptor binding  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytosol  protein phosphorylation  transmembrane receptor protein tyrosine kinase signaling pathway  negative regulation of signal transduction  positive regulation of neuron projection development  cell migration  extrinsic component of cytoplasmic side of plasma membrane  peptidyl-tyrosine autophosphorylation  ERBB2 signaling pathway  regulation of cell proliferation  tyrosine phosphorylation of Stat3 protein  tyrosine phosphorylation of Stat5 protein  positive regulation of tyrosine phosphorylation of Stat3 protein  identical protein binding  innate immune response  positive regulation of epidermal growth factor receptor signaling pathway  positive regulation of cell cycle  negative regulation of growth  protein autophosphorylation  intestinal epithelial cell differentiation  negative regulation of protein tyrosine kinase activity  cellular response to retinoic acid  
Ontology : EGO-EBIruffle  protein tyrosine kinase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  receptor binding  protein binding  ATP binding  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytosol  protein phosphorylation  transmembrane receptor protein tyrosine kinase signaling pathway  negative regulation of signal transduction  positive regulation of neuron projection development  cell migration  extrinsic component of cytoplasmic side of plasma membrane  peptidyl-tyrosine autophosphorylation  ERBB2 signaling pathway  regulation of cell proliferation  tyrosine phosphorylation of Stat3 protein  tyrosine phosphorylation of Stat5 protein  positive regulation of tyrosine phosphorylation of Stat3 protein  identical protein binding  innate immune response  positive regulation of epidermal growth factor receptor signaling pathway  positive regulation of cell cycle  negative regulation of growth  protein autophosphorylation  intestinal epithelial cell differentiation  negative regulation of protein tyrosine kinase activity  cellular response to retinoic acid  
REACTOMEQ13882 [protein]
REACTOME Pathways187577 [pathway]   8847993 [pathway]   8849468 [pathway]   8849469 [pathway]   8849470 [pathway]   8849471 [pathway]   8849472 [pathway]   8849473 [pathway]   8849474 [pathway]   8857538 [pathway]   
NDEx NetworkPTK6
Atlas of Cancer Signalling NetworkPTK6
Wikipedia pathwaysPTK6
Orthology - Evolution
OrthoDB5753
GeneTree (enSembl)ENSG00000101213
Phylogenetic Trees/Animal Genes : TreeFamPTK6
HOVERGENQ13882
HOGENOMQ13882
Homologs : HomoloGenePTK6
Homology/Alignments : Family Browser (UCSC)PTK6
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPTK6 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PTK6
dbVarPTK6
ClinVarPTK6
1000_GenomesPTK6 
Exome Variant ServerPTK6
ExAC (Exome Aggregation Consortium)PTK6 (select the gene name)
Genetic variants : HAPMAP5753
Genomic Variants (DGV)PTK6 [DGVbeta]
DECIPHER (Syndromes)20:62159776-62168723  ENSG00000101213
CONAN: Copy Number AnalysisPTK6 
Mutations
ICGC Data PortalPTK6 
TCGA Data PortalPTK6 
Broad Tumor PortalPTK6
OASIS PortalPTK6 [ Somatic mutations - Copy number]
Cancer Gene: CensusPTK6 
Somatic Mutations in Cancer : COSMICPTK6  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDPTK6
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch PTK6
DgiDB (Drug Gene Interaction Database)PTK6
DoCM (Curated mutations)PTK6 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PTK6 (select a term)
intoGenPTK6
NCG5 (London)PTK6
Cancer3DPTK6(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM602004   
Orphanet
MedgenPTK6
Genetic Testing Registry PTK6
NextProtQ13882 [Medical]
TSGene5753
GENETestsPTK6
Huge Navigator PTK6 [HugePedia]
snp3D : Map Gene to Disease5753
BioCentury BCIQPTK6
ClinGenPTK6
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5753
Chemical/Pharm GKB GenePA33960
Clinical trialPTK6
Miscellaneous
canSAR (ICR)PTK6 (select the gene name)
Probes
Litterature
PubMed95 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePTK6
EVEXPTK6
GoPubMedPTK6
iHOPPTK6
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Tue Mar 14 13:47:44 CET 2017

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