HCK
HCK proto-oncogene, Src family tyrosine kinase |
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PDB rendering based on 1ad5. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1AD5, 1BU1, 1QCF, 2C0I, 2C0O, 2C0T, 2HCK, 2HK5, 2OI3, 2OJ2, 3HCK, 3NHN, 3RBB, 3REA, 3REB, 3VRY, 3VRZ, 3VS0, 3VS1, 3VS2, 3VS3, 3VS4, 3VS5, 3VS6, 3VS7, 4HCK, 4LUD, 4LUE, 4ORZ, 5HCK
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Identifiers |
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Symbols | HCK ; JTK9; p59Hck; p61Hck |
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External IDs | OMIM: 142370 MGI: 96052 HomoloGene: 20489 IUPHAR: 2032 ChEMBL: 3234 GeneCards: HCK Gene |
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EC number | 2.7.10.2 |
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RNA expression pattern |
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More reference expression data |
Orthologs |
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Species | Human | Mouse | |
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Entrez | 3055 | 15162 | |
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Ensembl | ENSG00000101336 | ENSMUSG00000003283 | |
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UniProt | P08631 | P08103 | |
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RefSeq (mRNA) | NM_001172129 | NM_001172117 | |
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RefSeq (protein) | NP_001165600 | NP_001165588 | |
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Location (UCSC) | Chr 20: 30.64 β 30.69 Mb | Chr 2: 153.11 β 153.15 Mb | |
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PubMed search | | | |
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Tyrosine-protein kinase HCK is an enzyme that in humans is encoded by the HCK gene.[1]
Function
The protein encoded by this gene is a protein-tyrosine kinase that is predominantly expressed in hemopoietic cell types, and belongs to the Src family of tyrosine kinases. The encoded protein may help couple the Fc receptor to the activation of the respiratory burst. In addition, it may play a role in neutrophil migration and in the degranulation of neutrophils. Alternate translation initiation site usage, including a non-AUG (CUG) codon, results in the production of two different isoforms, that have different subcellular localization.[2]
Interactions
HCK has been shown to interact with BCR gene,[3][4] ELMO1,[5] Cbl gene,[6][7] RAS p21 protein activator 1,[8] RASA3,[8] Granulocyte colony-stimulating factor receptor,[9] ADAM15[10] and RAPGEF1.[11]
References
- β Quintrell N, Lebo R, Varmus H, Bishop JM, Pettenati MJ, Le Beau MM et al. (August 1987). "Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells". Mol Cell Biol 7 (6): 2267β75. PMC 365351. PMID 3496523.
- β "Entrez Gene: HCK hemopoietic cell kinase".
- β Stanglmaier M, Warmuth M, Kleinlein I, Reis S, Hallek M (February 2003). "The interaction of the Bcr-Abl tyrosine kinase with the Src kinase Hck is mediated by multiple binding domains". Leukemia 17 (2): 283β9. doi:10.1038/sj.leu.2402778. PMID 12592324.
- β Lionberger JM, Wilson MB, Smithgall TE (June 2000). "Transformation of myeloid leukemia cells to cytokine independence by Bcr-Abl is suppressed by kinase-defective Hck". J. Biol. Chem. 275 (24): 18581β5. doi:10.1074/jbc.C000126200. PMID 10849448.
- β Scott MP, Zappacosta F, Kim EY, Annan RS, Miller WT (August 2002). "Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1". J. Biol. Chem. 277 (31): 28238β46. doi:10.1074/jbc.M202783200. PMID 12029088.
- β Howlett CJ, Robbins SM (March 2002). "Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation". Oncogene 21 (11): 1707β16. doi:10.1038/sj.onc.1205228. PMID 11896602.
- β Howlett CJ, Bisson SA, Resek ME, Tigley AW, Robbins SM (April 1999). "The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase". Biochem. Biophys. Res. Commun. 257 (1): 129β38. doi:10.1006/bbrc.1999.0427. PMID 10092522.
- β 8.0 8.1 Briggs SD, Bryant SS, Jove R, Sanderson SD, Smithgall TE (June 1995). "The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck". J. Biol. Chem. 270 (24): 14718β24. doi:10.1074/jbc.270.24.14718. PMID 7782336.
- β Ward AC, Monkhouse JL, Csar XF, Touw IP, Bello PA (October 1998). "The Src-like tyrosine kinase Hck is activated by granulocyte colony-stimulating factor (G-CSF) and docks to the activated G-CSF receptor". Biochem. Biophys. Res. Commun. 251 (1): 117β23. doi:10.1006/bbrc.1998.9441. PMID 9790917.
- β Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR (February 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". J. Biol. Chem. 277 (7): 4999β5007. doi:10.1074/jbc.M107430200. PMID 11741929.
- β Shivakrupa R, Radha V, Sudhakar C, Swarup G (December 2003). "Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain". J. Biol. Chem. 278 (52): 52188β94. doi:10.1074/jbc.M310656200. PMID 14551197.
Further reading
- Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580β5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
- Lake JA, Carr J, Feng F, Mundy L, Burrell C, Li P (2003). "The role of Vif during HIV-1 infection: interaction with novel host cellular factors.". J. Clin. Virol. 26 (2): 143β52. doi:10.1016/S1386-6532(02)00113-0. PMID 12600646.
- Greenway AL, Holloway G, McPhee DA, Ellis P, Cornall A, Lidman M (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323β35. doi:10.1007/BF02970151. PMID 12734410.
- Tolstrup M, Ostergaard L, Laursen AL, Pedersen SF, Duch M (2004). "HIV/SIV escape from immune surveillance: focus on Nef.". Curr. HIV Res. 2 (2): 141β51. doi:10.2174/1570162043484924. PMID 15078178.
- Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87β94. doi:10.2174/1570162052773013. PMID 15638726.
- Stove V, Verhasselt B (2006). "Modelling thymic HIV-1 Nef effects.". Curr. HIV Res. 4 (1): 57β64. doi:10.2174/157016206775197583. PMID 16454711.
- Lichtenberg U, Quintrell N, Bishop JM (1992). "Human protein-tyrosine kinase gene HCK: expression and structural analysis of the promoter region.". Oncogene 7 (5): 849β58. PMID 1373873.
- Hradetzky D, Strebhardt K, RΓΌbsamen-Waigmann H (1992). "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 113 (2): 275β80. doi:10.1016/0378-1119(92)90407-G. PMID 1572549.
- Kim JW, Sim SS, Kim UH, Nishibe S, Wahl MI, Carpenter G et al. (1990). "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro.". J. Biol. Chem. 265 (7): 3940β3. PMID 1689310.
- Holtrich U, BrΓ€uninger A, Strebhardt K, RΓΌbsamen-Waigmann H (1992). "Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase.". Proc. Natl. Acad. Sci. U.S.A. 88 (23): 10411β5. doi:10.1073/pnas.88.23.10411. PMC 52938. PMID 1720539.
- Lock P, Ralph S, Stanley E, Boulet I, Ramsay R, Dunn AR (1991). "Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization.". Mol. Cell. Biol. 11 (9): 4363β70. PMC 361298. PMID 1875927.
- Ziegler SF, Marth JD, Lewis DB, Perlmutter RM (1987). "Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin.". Mol. Cell. Biol. 7 (6): 2276β85. PMC 365352. PMID 3453117.
- Lee CH, Leung B, Lemmon MA, Zheng J, Cowburn D, Kuriyan J et al. (1995). "A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein.". EMBO J. 14 (20): 5006β15. PMC 394604. PMID 7588629.
- Liao F, Shin HS, Rhee SG (1993). "In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases.". Biochem. Biophys. Res. Commun. 191 (3): 1028β33. doi:10.1006/bbrc.1993.1320. PMID 7682059.
- Briggs SD, Bryant SS, Jove R, Sanderson SD, Smithgall TE (1995). "The Ras GTPase-activating protein (GAP) is an SH3 domain-binding protein and substrate for the Src-related tyrosine kinase, Hck.". J. Biol. Chem. 270 (24): 14718β24. doi:10.1074/jbc.270.24.14718. PMID 7782336.
- Robbins SM, Quintrell NA, Bishop JM (1995). "Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae.". Mol. Cell. Biol. 15 (7): 3507β15. PMC 230587. PMID 7791757.
- Saksela K, Cheng G, Baltimore D (1995). "Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4.". EMBO J. 14 (3): 484β91. PMC 398106. PMID 7859737.
- Cheng G, Ye ZS, Baltimore D (1994). "Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction.". Proc. Natl. Acad. Sci. U.S.A. 91 (17): 8152β5. doi:10.1073/pnas.91.17.8152. PMC 44563. PMID 8058772.
- Wang AV, Scholl PR, Geha RS (1994). "Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn.". J. Exp. Med. 180 (3): 1165β70. doi:10.1084/jem.180.3.1165. PMC 2191633. PMID 8064233.
PDB gallery |
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| | 1ad5: SRC FAMILY KINASE HCK-AMP-PNP COMPLEX |
| 1bu1: SRC FAMILY KINASE HCK SH3 DOMAIN |
| 1qcf: CRYSTAL STRUCTURE OF HCK IN COMPLEX WITH A SRC FAMILY-SELECTIVE TYROSINE KINASE INHIBITOR |
| 2c0i: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-420983 |
| 2c0o: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-770041 |
| 2c0t: SRC FAMILY KINASE HCK WITH BOUND INHIBITOR A-641359 |
| 2hck: SRC FAMILY KINASE HCK-QUERCETIN COMPLEX |
| 2hk5: Hck Kinase in Complex with Lck targetted Inhibitor PG-1009247 |
| 2oi3: NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) |
| 2oj2: NMR Structure Analysis of the Hematopoetic Cell Kinase SH3 Domain complexed with an artificial high affinity ligand (PD1) |
| 3hck: NMR ensemble of the uncomplexed human HCK SH2 domain, 20 structures |
| 4hck: HUMAN HCK SH3 DOMAIN, NMR, 25 STRUCTURES |
| 5hck: HUMAN HCK SH3 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE |
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| ABL family | |
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| ACK family | |
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| CSK family | |
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| FAK family | |
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| FES family | |
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| FRK family | |
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| JAK family | |
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| SRC-A family | |
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| SRC-B family | |
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| TEC family | |
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| SYK family | |
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