TNK2

Tyrosine kinase, non-receptor, 2, also known as TNK2, is a human gene.cite web | title = Entrez Gene: TNK2 tyrosine kinase, non-receptor, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10188| accessdate = ]

PBB_Summary
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summary_text = This gene encodes a tyrosine kinase that binds Cdc42Hs in its GTP-bound form and inhibits both the intrinsic and GTPase-activating protein (GAP)-stimulated GTPase activity of Cdc42Hs. This binding is mediated by a unique sequence of 47 amino acids C-terminal to an SH3 domain. The protein may be involved in a regulatory mechanism that sustains the GTP-bound active form of Cdc42Hs and which is directly linked to a tyrosine phosphorylation signal transduction pathway. Several alternatively spliced transcript variants have been identified from this gene, but the full-length nature of only two transcript variants has been determined.cite web | title = Entrez Gene: TNK2 tyrosine kinase, non-receptor, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10188| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Manser E, Leung T, Salihuddin H, "et al." |title=A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42. |journal=Nature |volume=363 |issue= 6427 |pages= 364–7 |year= 1993 |pmid= 8497321 |doi= 10.1038/363364a0
*cite journal | author=Satoh T, Kato J, Nishida K, Kaziro Y |title=Tyrosine phosphorylation of ACK in response to temperature shift-down, hyperosmotic shock, and epidermal growth factor stimulation. |journal=FEBS Lett. |volume=386 |issue= 2-3 |pages= 230–4 |year= 1996 |pmid= 8647288 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Mott HR, Owen D, Nietlispach D, "et al." |title=Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK. |journal=Nature |volume=399 |issue= 6734 |pages= 384–8 |year= 1999 |pmid= 10360579 |doi= 10.1038/20732
*cite journal | author=Eisenmann KM, McCarthy JB, Simpson MA, "et al." |title=Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. |journal=Nat. Cell Biol. |volume=1 |issue= 8 |pages= 507–13 |year= 2000 |pmid= 10587647 |doi= 10.1038/70302
*cite journal | author=Kato J, Kaziro Y, Satoh T |title=Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 1 |pages= 141–7 |year= 2000 |pmid= 10652228 |doi= 10.1006/bbrc.2000.2106
*cite journal | author=Owen D, Mott HR, Laue ED, Lowe PN |title=Residues in Cdc42 that specify binding to individual CRIB effector proteins. |journal=Biochemistry |volume=39 |issue= 6 |pages= 1243–50 |year= 2000 |pmid= 10684602 |doi=
*cite journal | author=Kiyono M, Kato J, Kataoka T, "et al." |title=Stimulation of Ras guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29788–93 |year= 2000 |pmid= 10882715 |doi= 10.1074/jbc.M001378200
*cite journal | author=Linseman DA, Heidenreich KA, Fisher SK |title=Stimulation of M3 muscarinic receptors induces phosphorylation of the Cdc42 effector activated Cdc42Hs-associated kinase-1 via a Fyn tyrosine kinase signaling pathway. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5622–8 |year= 2001 |pmid= 11087735 |doi= 10.1074/jbc.M006812200
*cite journal | author=Teo M, Tan L, Lim L, Manser E |title=The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors. |journal=J. Biol. Chem. |volume=276 |issue= 21 |pages= 18392–8 |year= 2001 |pmid= 11278436 |doi= 10.1074/jbc.M008795200
*cite journal | author=Kato-Stankiewicz J, Ueda S, Kataoka T, "et al." |title=Epidermal growth factor stimulation of the ACK1/Dbl pathway in a Cdc42 and Grb2-dependent manner. |journal=Biochem. Biophys. Res. Commun. |volume=284 |issue= 2 |pages= 470–7 |year= 2001 |pmid= 11394904 |doi= 10.1006/bbrc.2001.5004
*cite journal | author=Oda T, Muramatsu MA, Isogai T, "et al." |title=HSH2: a novel SH2 domain-containing adapter protein involved in tyrosine kinase signaling in hematopoietic cells. |journal=Biochem. Biophys. Res. Commun. |volume=288 |issue= 5 |pages= 1078–86 |year= 2001 |pmid= 11700021 |doi= 10.1006/bbrc.2001.5890
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Salomon AR, Ficarro SB, Brill LM, "et al." |title=Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 2 |pages= 443–8 |year= 2003 |pmid= 12522270 |doi= 10.1073/pnas.2436191100
*cite journal | author=Yokoyama N, Miller WT |title=Biochemical properties of the Cdc42-associated tyrosine kinase ACK1. Substrate specificity, authphosphorylation, and interaction with Hck. |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 47713–23 |year= 2004 |pmid= 14506255 |doi= 10.1074/jbc.M306716200
*cite journal | author=Ahmed I, Calle Y, Sayed MA, "et al." |title=Cdc42-dependent nuclear translocation of non-receptor tyrosine kinase, ACK. |journal=Biochem. Biophys. Res. Commun. |volume=314 |issue= 2 |pages= 571–9 |year= 2004 |pmid= 14733946 |doi=
*cite journal | author=Gu Y, Lin Q, Childress C, Yang W |title=Identification of the region in Cdc42 that confers the binding specificity to activated Cdc42-associated kinase. |journal=J. Biol. Chem. |volume=279 |issue= 29 |pages= 30507–13 |year= 2004 |pmid= 15123659 |doi= 10.1074/jbc.M313518200
*cite journal | author=Brandenberger R, Wei H, Zhang S, "et al." |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971
*cite journal | author=Lougheed JC, Chen RH, Mak P, Stout TJ |title=Crystal structures of the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1. |journal=J. Biol. Chem. |volume=279 |issue= 42 |pages= 44039–45 |year= 2004 |pmid= 15308621 |doi= 10.1074/jbc.M406703200

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