Tyrosine-protein kinase HCK

NameTyrosine-protein kinase HCK
Synonyms
  • 2.7.10.2
  • Hematopoietic cell kinase
  • Hemopoietic cell kinase
  • p59-HCK/p60-HCK
  • p59Hck
  • p61Hck
Gene NameHCK
OrganismHuman
Amino acid sequence
>lcl|BSEQ0002827|Tyrosine-protein kinase HCK
MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIK
PGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSL
ATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSY
SLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVP
CMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE
AFLAEANVMKTLQHDKLVKLHAVVTKEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLID
FSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAKFP
IKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPE
NCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDFYTATESQYQQQP
Number of residues526
Molecular Weight59599.355
Theoretical pI6.68
GO Classification
Functions
  • receptor binding
  • non-membrane spanning protein tyrosine kinase activity
  • protein tyrosine kinase activity
  • ATP binding
Processes
  • peptidyl-tyrosine autophosphorylation
  • cell adhesion
  • interferon-gamma-mediated signaling pathway
  • peptidyl-tyrosine phosphorylation
  • transmembrane receptor protein tyrosine kinase signaling pathway
  • cellular response to peptide hormone stimulus
  • negative regulation of apoptotic process
  • regulation of defense response to virus by virus
  • protein phosphorylation
  • regulation of sequence-specific DNA binding transcription factor activity
  • positive regulation of cell proliferation
  • positive regulation of actin cytoskeleton reorganization
  • integrin-mediated signaling pathway
  • inflammatory response
  • regulation of podosome assembly
  • regulation of inflammatory response
  • mesoderm development
  • regulation of cell shape
  • innate immune response-activating signal transduction
  • cytokine-mediated signaling pathway
  • leukocyte degranulation
  • lipopolysaccharide-mediated signaling pathway
  • leukocyte migration involved in immune response
  • regulation of phagocytosis
  • respiratory burst after phagocytosis
  • protein autophosphorylation
  • cell differentiation
  • positive regulation of actin filament polymerization
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • innate immune response
  • viral process
Components
  • cytoskeleton
  • nucleus
  • transport vesicle
  • lysosome
  • caveola
  • Golgi apparatus
  • cytosol
  • extrinsic component of cytoplasmic side of plasma membrane
  • focal adhesion
  • cell projection
General FunctionReceptor binding
Specific FunctionNon-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell adhesion and migration. Acts downstream of receptors that bind the Fc region of immunoglobulins, such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During the phagocytic process, mediates mobilization of secretory lysosomes, degranulation, and activation of NADPH oxidase to bring about the respiratory burst. Plays a role in the release of inflammatory molecules. Promotes reorganization of the actin cytoskeleton and actin polymerization, formation of podosomes and cell protrusions. Inhibits TP73-mediated transcription activation and TP73-mediated apoptosis. Phosphorylates CBL in response to activation of immunoglobulin gamma Fc region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1, GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID306832
UniProtKB IDP08631
UniProtKB Entry NameHCK_HUMAN
Cellular LocationLysosome
Gene sequence
>lcl|BSEQ0021845|Tyrosine-protein kinase HCK (HCK)
ATGGGGTGCATGAAGTCCAAGTTCCTCCAGGTCGGAGGCAATACATTCTCAAAAACTGAA
ACCAGCGCCAGCCCACACTGTCCTGTGTACGTGCCGGATCCCACATCCACCATCAAGCCG
GGGCCTAATAGCCACAACAGCAACACACCAGGAATCAGGGAGGCAGGCTCTGAGGACATC
ATCGTGGTTGCCCTGTATGATTACGAGGCCATTCACCACGAAGACCTCAGCTTCCAGAAG
GGGGACCAGATGGTGGTCCTAGAGGAATCCGGGGAGTGGTGGAAGGCTCGATCCCTGGCC
ACCCGGAAGGAGGGCTACATCCCAAGCAACTATGTCGCCCGCGTTGACTCTCTGGAGACA
GAGGAGTGGTTTTTCAAGGGCATCAGCCGGAAGGACGCAGAGCGCCAACTGCTGGCTCCC
GGCAACATGCTGGGCTCCTTCATGATCCGGGATAGCGAGACCACTAAAGGAAGCTACTCT
TTGTCCGTGCGAGACTACGACCCTCGGCAGGGAGATACCGTGAAACATTACAAGATCCGG
ACCCTGGACAACGGGGGCTTCTACATATCCCCCCGAAGCACCTTCAGCACTCTGCAGGAG
CTGGTGGACCACTACAAGAAGGGGAACGACGGGCTCTGCCAGAAACTGTCGGTGCCCTGC
ATGTCTTCCAAGCCCCAGAAGCCTTGGGAGAAAGATGCCTGGGAGATCCCTCGGGAATCC
CTCAAGCTGGAGAAGAAACTTGGAGCTGGGCAGTTTGGGGAAGTCTGGATGGCCACCTAC
AACAAGCACACCAAGGTGGCAGTGAAGACGATGAAGCCAGGGAGCATGTCGGTGGAGGCC
TTCCTGGCAGAGGCCAACGTGATGAAAACTCTGCAGCATGACAAGCTGGTCAAACTTCAT
GCGGTGGTCACCAAGGAGCCCATCTACATCATCACGGAGTTCATGGCCAAAGGAAGCTTG
CTGGACTTTCTGAAAAGTGATGAGGGCAGCAAGCAGCCATTGCCAAAACTCATTGACTTC
TCAGCCCAGATTGCAGAAGGCATGGCCTTCATCGAGCAGAGGAACTACATCCACCGAGAC
CTCCGAGCTGCCAACATCTTGGTCTCTGCATCCCTGGTGTGTAAGATTGCTGACTTTGGC
CTGGCCCGGGTCATTGAGGACAACGAGTACACGGCTCGGGAAGGGGCCAAGTTCCCCATC
AAGTGGACAGCTCCTGAAGCCATCAACTTTGGCTCCTTCACCATCAAGTCAGACGTCTGG
TCCTTTGGTATCCTGCTGATGGAGATCGTCACCTACGGCCGGATCCCTTACCCAGGGATG
TCAAACCCTGAAGTGATCCGAGCTCTGGAGCGTGGATACCGGATGCCTCGCCCAGAGAAC
TGCCCAGAGGAGCTCTACAACATCATGATGCGCTGCTGGAAAAACCGTCCGGAGGAGCGG
CCGACCTTCGAATACATCCAGAGTGTGCTGGATGACTTCTACACGGCCACAGAGAGCCAG
TACCAACAGCAGCCATGA
GenBank Gene IDM16591
GeneCard IDNot Available
GenAtlas IDHCK
HGNC IDHGNC:4840
Chromosome Location20
Locus20q11-q12
References
  1. Quintrell N, Lebo R, Varmus H, Bishop JM, Pettenati MJ, Le Beau MM, Diaz MO, Rowley JD: Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells. Mol Cell Biol. 1987 Jun;7(6):2267-75. 3496523
  2. Ziegler SF, Marth JD, Lewis DB, Perlmutter RM: Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin. Mol Cell Biol. 1987 Jun;7(6):2276-85. 3453117
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. 11780052
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  6. Lock P, Ralph S, Stanley E, Boulet I, Ramsay R, Dunn AR: Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization. Mol Cell Biol. 1991 Sep;11(9):4363-70. 1875927
  7. Hradetzky D, Strebhardt K, Rubsamen-Waigmann H: The genomic locus of the human hemopoietic-specific cell protein tyrosine kinase (PTK)-encoding gene (HCK) confirms conservation of exon-intron structure among human PTKs of the src family. Gene. 1992 Apr 15;113(2):275-80. 1572549
  8. Ghazizadeh S, Bolen JB, Fleit HB: Physical and functional association of Src-related protein tyrosine kinases with Fc gamma RII in monocytic THP-1 cells. J Biol Chem. 1994 Mar 25;269(12):8878-84. 8132624
  9. Wang AV, Scholl PR, Geha RS: Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn. J Exp Med. 1994 Sep 1;180(3):1165-70. 8064233
  10. Durden DL, Kim HM, Calore B, Liu Y: The Fc gamma RI receptor signals through the activation of hck and MAP kinase. J Immunol. 1995 Apr 15;154(8):4039-47. 7535819
  11. Robbins SM, Quintrell NA, Bishop JM: Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol Cell Biol. 1995 Jul;15(7):3507-15. 7791757
  12. Hallek M, Neumann C, Schaffer M, Danhauser-Riedl S, von Bubnoff N, de Vos G, Druker BJ, Yasukawa K, Griffin JD, Emmerich B: Signal transduction of interleukin-6 involves tyrosine phosphorylation of multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck, and Lyn in multiple myeloma cell lines. Exp Hematol. 1997 Dec;25(13):1367-77. 9406996
  13. Welch H, Maridonneau-Parini I: Hck is activated by opsonized zymosan and A23187 in distinct subcellular fractions of human granulocytes. J Biol Chem. 1997 Jan 3;272(1):102-9. 8995234
  14. Briggs SD, Sharkey M, Stevenson M, Smithgall TE: SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. J Biol Chem. 1997 Jul 18;272(29):17899-902. 9218412
  15. Warmuth M, Bergmann M, Priess A, Hauslmann K, Emmerich B, Hallek M: The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr. J Biol Chem. 1997 Dec 26;272(52):33260-70. 9407116
  16. Howlett CJ, Bisson SA, Resek ME, Tigley AW, Robbins SM: The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase. Biochem Biophys Res Commun. 1999 Apr 2;257(1):129-38. 10092522
  17. Bosco MC, Curiel RE, Zea AH, Malabarba MG, Ortaldo JR, Espinoza-Delgado I: IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck. J Immunol. 2000 May 1;164(9):4575-85. 10779760
  18. Porter M, Schindler T, Kuriyan J, Miller WT: Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand. J Biol Chem. 2000 Jan 28;275(4):2721-6. 10644735
  19. Barlic J, Andrews JD, Kelvin AA, Bosinger SE, DeVries ME, Xu L, Dobransky T, Feldman RD, Ferguson SS, Kelvin DJ: Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI. Nat Immunol. 2000 Sep;1(3):227-33. 10973280
  20. Hassaine G, Courcoul M, Bessou G, Barthalay Y, Picard C, Olive D, Collette Y, Vigne R, Decroly E: The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif protein. J Biol Chem. 2001 May 18;276(20):16885-93. Epub 2001 Feb 27. 11278465
  21. Korkaya H, Jameel S, Gupta D, Tyagi S, Kumar R, Zafrullah M, Mazumdar M, Lal SK, Xiaofang L, Sehgal D, Das SR, Sahal D: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK. J Biol Chem. 2001 Nov 9;276(45):42389-400. Epub 2001 Aug 22. 11518702
  22. Klejman A, Schreiner SJ, Nieborowska-Skorska M, Slupianek A, Wilson M, Smithgall TE, Skorski T: The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid leukemia cells. EMBO J. 2002 Nov 1;21(21):5766-74. 12411494
  23. Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR: Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. J Biol Chem. 2002 Feb 15;277(7):4999-5007. Epub 2001 Dec 10. 11741929
  24. Carreno S, Caron E, Cougoule C, Emorine LJ, Maridonneau-Parini I: p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42- and Rac-dependent manner. J Biol Chem. 2002 Jun 7;277(23):21007-16. Epub 2002 Mar 19. 11904303
  25. Howlett CJ, Robbins SM: Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation. Oncogene. 2002 Mar 7;21(11):1707-16. 11896602
  26. Podar K, Mostoslavsky G, Sattler M, Tai YT, Hayashi T, Catley LP, Hideshima T, Mulligan RC, Chauhan D, Anderson KC: Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation and survival of multiple myeloma cells. J Biol Chem. 2004 May 14;279(20):21658-65. Epub 2004 Mar 9. 15010462
  27. Yokoyama N, deBakker CD, Zappacosta F, Huddleston MJ, Annan RS, Ravichandran KS, Miller WT: Identification of tyrosine residues on ELMO1 that are phosphorylated by the Src-family kinase Hck. Biochemistry. 2005 Jun 21;44(24):8841-9. 15952790
  28. Cougoule C, Carreno S, Castandet J, Labrousse A, Astarie-Dequeker C, Poincloux R, Le Cabec V, Maridonneau-Parini I: Activation of the lysosome-associated p61Hck isoform triggers the biogenesis of podosomes. Traffic. 2005 Aug;6(8):682-94. 15998323
  29. Trible RP, Emert-Sedlak L, Smithgall TE: HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction. J Biol Chem. 2006 Sep 15;281(37):27029-38. Epub 2006 Jul 18. 16849330
  30. Paliwal P, Radha V, Swarup G: Regulation of p73 by Hck through kinase-dependent and independent mechanisms. BMC Mol Biol. 2007 May 30;8:45. 17535448
  31. Hausherr A, Tavares R, Schaffer M, Obermeier A, Miksch C, Mitina O, Ellwart J, Hallek M, Krause G: Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases. Oncogene. 2007 Jul 26;26(34):4987-98. Epub 2007 Feb 19. 17310994
  32. Voss M, Lettau M, Janssen O: Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening. BMC Immunol. 2009 Oct 6;10:53. doi: 10.1186/1471-2172-10-53. 19807924
  33. Poincloux R, Al Saati T, Maridonneau-Parini I, Le Cabec V: The oncogenic activity of the Src family kinase Hck requires the cooperative action of the plasma membrane- and lysosome-associated isoforms. Eur J Cancer. 2009 Feb;45(3):321-7. doi: 10.1016/j.ejca.2008.11.020. Epub 2008 Dec 26. 19114024
  34. Kleino I, Ortiz RM, Yritys M, Huovila AP, Saksela K: Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins. J Cell Biochem. 2009 Nov 1;108(4):877-85. doi: 10.1002/jcb.22317. 19718658
  35. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. 19369195
  36. Baruzzi A, Iacobucci I, Soverini S, Lowell CA, Martinelli G, Berton G: c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration. FEBS Lett. 2010 Jan 4;584(1):15-21. doi: 10.1016/j.febslet.2009.11.009. Epub . 19903482
  37. Pene-Dumitrescu T, Smithgall TE: Expression of a Src family kinase in chronic myelogenous leukemia cells induces resistance to imatinib in a kinase-dependent manner. J Biol Chem. 2010 Jul 9;285(28):21446-57. doi: 10.1074/jbc.M109.090043. Epub 2010 May 7. 20452982
  38. Guiet R, Poincloux R, Castandet J, Marois L, Labrousse A, Le Cabec V, Maridonneau-Parini I: Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from signaling and actin reorganization to migration and phagocytosis. Eur J Cell Biol. 2008 Sep;87(8-9):527-42. doi: 10.1016/j.ejcb.2008.03.008. Epub 2008 Jun 5. 18538446
  39. Zarbock A, Ley K: Protein tyrosine kinases in neutrophil activation and recruitment. Arch Biochem Biophys. 2011 Jun 15;510(2):112-9. doi: 10.1016/j.abb.2011.02.009. Epub 2011 Feb 19. 21338576
  40. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  41. Yokoyama N, Miller WT: Molecular characterization of WDCP, a novel fusion partner for the anaplastic lymphoma tyrosine kinase ALK. Biomed Rep. 2015 Jan;3(1):9-13. Epub 2014 Nov 3. 25469238
  42. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. 25944712
  43. Zhang W, Smithgall TE, Gmeiner WH: Sequential assignment and secondary structure determination for the Src homology 2 domain of hematopoietic cellular kinase. FEBS Lett. 1997 Apr 7;406(1-2):131-5. 9109402
  44. Sicheri F, Moarefi I, Kuriyan J: Crystal structure of the Src family tyrosine kinase Hck. Nature. 1997 Feb 13;385(6617):602-9. 9024658
  45. Arold S, O'Brien R, Franken P, Strub MP, Hoh F, Dumas C, Ladbury JE: RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef. Biochemistry. 1998 Oct 20;37(42):14683-91. 9778343
  46. Horita DA, Baldisseri DM, Zhang W, Altieri AS, Smithgall TE, Gmeiner WH, Byrd RA: Solution structure of the human Hck SH3 domain and identification of its ligand binding site. J Mol Biol. 1998 Apr 24;278(1):253-65. 9571048
  47. Schindler T, Sicheri F, Pico A, Gazit A, Levitzki A, Kuriyan J: Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol Cell. 1999 May;3(5):639-48. 10360180
  48. Burchat A, Borhani DW, Calderwood DJ, Hirst GC, Li B, Stachlewitz RF: Discovery of A-770041, a src-family selective orally active lck inhibitor that prevents organ allograft rejection. Bioorg Med Chem Lett. 2006 Jan 1;16(1):118-22. Epub 2005 Oct 10. 16216497
  49. Sabat M, VanRens JC, Laufersweiler MJ, Brugel TA, Maier J, Golebiowski A, De B, Easwaran V, Hsieh LC, Walter RL, Mekel MJ, Evdokimov A, Janusz MJ: The development of 2-benzimidazole substituted pyrimidine based inhibitors of lymphocyte specific kinase (Lck). Bioorg Med Chem Lett. 2006 Dec 1;16(23):5973-7. Epub 2006 Sep 25. 16997556
  50. Schmidt H, Hoffmann S, Tran T, Stoldt M, Stangler T, Wiesehan K, Willbold D: Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes. J Mol Biol. 2007 Feb 2;365(5):1517-32. Epub 2006 Nov 10. 17141806
  51. Alvarado JJ, Betts L, Moroco JA, Smithgall TE, Yeh JI: Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory region supports an SH3-dominant activation mechanism. J Biol Chem. 2010 Nov 12;285(46):35455-61. doi: 10.1074/jbc.M110.145102. Epub 2010 Sep 1. 20810664
  52. Breuer S, Schievink SI, Schulte A, Blankenfeldt W, Fackler OT, Geyer M: Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef. PLoS One. 2011;6(5):e20033. doi: 10.1371/journal.pone.0020033. Epub 2011 May 20. 21625496
  53. Horenkamp FA, Breuer S, Schulte A, Lulf S, Weyand M, Saksela K, Geyer M: Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. Traffic. 2011 Jul;12(7):867-77. doi: 10.1111/j.1600-0854.2011.01205.x. Epub 2011 May 5. 21477083
  54. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. 17344846