HCK

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HCK proto-oncogene, Src family tyrosine kinase
Protein HCK PDB 1ad5.png
PDB rendering based on 1ad5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HCK ; JTK9; p59Hck; p61Hck
External IDs OMIM142370 MGI96052 HomoloGene20489 ChEMBL: 3234 GeneCards: HCK Gene
EC number 2.7.10.2
RNA expression pattern
PBB GE HCK 208018 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3055 15162
Ensembl ENSG00000101336 ENSMUSG00000003283
UniProt P08631 P08103
RefSeq (mRNA) NM_001172129 NM_001172117
RefSeq (protein) NP_001165600 NP_001165588
Location (UCSC) Chr 20:
32.05 – 32.1 Mb
Chr 2:
153.11 – 153.15 Mb
PubMed search [1] [2]

Tyrosine-protein kinase HCK is an enzyme that in humans is encoded by the HCK gene.[1]

Function[edit]

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[edit]

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[edit]

  1. ^ 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): 2267–75. PMC 365351. PMID 3496523. 
  2. ^ "Entrez Gene: HCK hemopoietic cell kinase". 
  3. ^ 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): 283–9. doi:10.1038/sj.leu.2402778. PMID 12592324. 
  4. ^ 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): 18581–5. doi:10.1074/jbc.C000126200. PMID 10849448. 
  5. ^ 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): 28238–46. doi:10.1074/jbc.M202783200. PMID 12029088. 
  6. ^ Howlett CJ, Robbins SM (March 2002). "Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated cellular transformation". Oncogene 21 (11): 1707–16. doi:10.1038/sj.onc.1205228. PMID 11896602. 
  7. ^ 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): 129–38. doi:10.1006/bbrc.1999.0427. PMID 10092522. 
  8. ^ a b 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): 14718–24. doi:10.1074/jbc.270.24.14718. PMID 7782336. 
  9. ^ 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): 117–23. doi:10.1006/bbrc.1998.9441. PMID 9790917. 
  10. ^ 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): 4999–5007. doi:10.1074/jbc.M107430200. PMID 11741929. 
  11. ^ 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): 52188–94. doi:10.1074/jbc.M310656200. PMID 14551197. 

Further reading[edit]