TNK2

Tyrosine kinase, non-receptor, 2
File:PBB Protein TNK2 image.jpg PDB rendering based on 1cf4.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1cf4​, 1u46​, 1u4d​, 1u54​
Identifiers
Symbols	TNK2 ; ACK; ACK1; FLJ44758; FLJ45547; p21cdc42Hs
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4224
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE TNK2 203838 s at tn.png
File:PBB GE TNK2 203839 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Tyrosine kinase, non-receptor, 2, also known as TNK2, is a human gene.

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.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
• Manser E, Leung T, Salihuddin H; et al. (1993). "A non-receptor tyrosine kinase that inhibits the GTPase activity of p21cdc42". Nature. 363 (6427): 364–7. doi:10.1038/363364a0. PMID 8497321.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Satoh T, Kato J, Nishida K, Kaziro Y (1996). "Tyrosine phosphorylation of ACK in response to temperature shift-down, hyperosmotic shock, and epidermal growth factor stimulation". FEBS Lett. 386 (2–3): 230–4. PMID 8647288.CS1 maint: Multiple names: authors list (link)
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mott HR, Owen D, Nietlispach D; et al. (1999). "Structure of the small G protein Cdc42 bound to the GTPase-binding domain of ACK". Nature. 399 (6734): 384–8. doi:10.1038/20732. PMID 10360579.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Eisenmann KM, McCarthy JB, Simpson MA; et al. (2000). "Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas". Nat. Cell Biol. 1 (8): 507–13. doi:10.1038/70302. PMID 10587647.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kato J, Kaziro Y, Satoh T (2000). "Activation of the guanine nucleotide exchange factor Dbl following ACK1-dependent tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 268 (1): 141–7. doi:10.1006/bbrc.2000.2106. PMID 10652228.CS1 maint: Multiple names: authors list (link)
• Owen D, Mott HR, Laue ED, Lowe PN (2000). "Residues in Cdc42 that specify binding to individual CRIB effector proteins". Biochemistry. 39 (6): 1243–50. PMID 10684602.CS1 maint: Multiple names: authors list (link)
• Kiyono M, Kato J, Kataoka T; et al. (2000). "Stimulation of Ras guanine nucleotide exchange activity of Ras-GRF1/CDC25(Mm) upon tyrosine phosphorylation by the Cdc42-regulated kinase ACK1". J. Biol. Chem. 275 (38): 29788–93. doi:10.1074/jbc.M001378200. PMID 10882715.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Linseman DA, Heidenreich KA, Fisher SK (2001). "Stimulation of M3 muscarinic receptors induces phosphorylation of the Cdc42 effector activated Cdc42Hs-associated kinase-1 via a Fyn tyrosine kinase signaling pathway". J. Biol. Chem. 276 (8): 5622–8. doi:10.1074/jbc.M006812200. PMID 11087735.CS1 maint: Multiple names: authors list (link)
• Teo M, Tan L, Lim L, Manser E (2001). "The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors". J. Biol. Chem. 276 (21): 18392–8. doi:10.1074/jbc.M008795200. PMID 11278436.CS1 maint: Multiple names: authors list (link)
• Kato-Stankiewicz J, Ueda S, Kataoka T; et al. (2001). "Epidermal growth factor stimulation of the ACK1/Dbl pathway in a Cdc42 and Grb2-dependent manner". Biochem. Biophys. Res. Commun. 284 (2): 470–7. doi:10.1006/bbrc.2001.5004. PMID 11394904.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Oda T, Muramatsu MA, Isogai T; et al. (2001). "HSH2: a novel SH2 domain-containing adapter protein involved in tyrosine kinase signaling in hematopoietic cells". Biochem. Biophys. Res. Commun. 288 (5): 1078–86. doi:10.1006/bbrc.2001.5890. PMID 11700021.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Salomon AR, Ficarro SB, Brill LM; et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. doi:10.1073/pnas.2436191100. PMID 12522270.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yokoyama N, Miller WT (2004). "Biochemical properties of the Cdc42-associated tyrosine kinase ACK1. Substrate specificity, authphosphorylation, and interaction with Hck". J. Biol. Chem. 278 (48): 47713–23. doi:10.1074/jbc.M306716200. PMID 14506255.
• Ahmed I, Calle Y, Sayed MA; et al. (2004). "Cdc42-dependent nuclear translocation of non-receptor tyrosine kinase, ACK". Biochem. Biophys. Res. Commun. 314 (2): 571–9. PMID 14733946.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gu Y, Lin Q, Childress C, Yang W (2004). "Identification of the region in Cdc42 that confers the binding specificity to activated Cdc42-associated kinase". J. Biol. Chem. 279 (29): 30507–13. doi:10.1074/jbc.M313518200. PMID 15123659.CS1 maint: Multiple names: authors list (link)
• Brandenberger R, Wei H, Zhang S; et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lougheed JC, Chen RH, Mak P, Stout TJ (2004). "Crystal structures of the phosphorylated and unphosphorylated kinase domains of the Cdc42-associated tyrosine kinase ACK1". J. Biol. Chem. 279 (42): 44039–45. doi:10.1074/jbc.M406703200. PMID 15308621.CS1 maint: Multiple names: authors list (link)