HCK

From Wikipedia, the free encyclopedia

Hemopoietic cell kinase

PDB rendering based on 1ad5.

Available structures: 1ad5, 1bu1, 1qcf, 2c0i, 2c0o, 2c0t, 2hck, 2hk5, 2oi3, 2oj2, 3hck, 4hck, 5hck

Identifiers

Symbol(s)

HCK; JTK9

External IDs

OMIM: 142370 MGI: 96052 HomoloGene: 20489

Gene ontology
Molecular Function:	• nucleotide binding • protein-tyrosine kinase activity • protein binding • ATP binding • transferase activity
Cellular Component:	• membrane
Biological Process:	• protein amino acid phosphorylation • intracellular signaling cascade • mesoderm development

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002110 (mRNA)
NP_002101 (protein)

NM_010407 (mRNA)
NP_034537 (protein)

Location

Chr 20: 30.1 - 30.15 Mb

Chr 2: 152.8 - 152.84 Mb

Pubmed search

[1]

[2]

Hemopoietic cell kinase, also known as HCK, is a human gene.

The protein encoded by this gene is a protein-tyrosine kinase that is predominantly expressed in hemopoietic cell types. 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.^[1]

[edit] References

^ Entrez Gene: HCK hemopoietic cell kinase.

[edit] Further reading

Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef.". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMID 11463741.
Lake JA, Carr J, Feng F, et al. (2003). "The role of Vif during HIV-1 infection: interaction with novel host cellular factors.". J. Clin. Virol. 26 (2): 143–52. PMID 12600646.
Greenway AL, Holloway G, McPhee DA, et al. (2004). "HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication.". J. Biosci. 28 (3): 323–35. PMID 12734410.
Tolstrup M, Ostergaard L, Laursen AL, et al. (2004). "HIV/SIV escape from immune surveillance: focus on Nef.". Curr. HIV Res. 2 (2): 141–51. PMID 15078178.
Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection.". Curr. HIV Res. 3 (1): 87–94. PMID 15638726.
Stove V, Verhasselt B (2006). "Modelling thymic HIV-1 Nef effects.". Curr. HIV Res. 4 (1): 57–64. 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): 849–58. PMID 1373873.
Hradetzky D, Strebhardt K, Rübsamen-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): 275–80. PMID 1572549.
Kim JW, Sim SS, Kim UH, et al. (1990). "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro.". J. Biol. Chem. 265 (7): 3940–3. PMID 1689310.
Holtrich U, Bräuninger A, Strebhardt K, Rübsamen-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): 10411–5. PMID 1720539.
Lock P, Ralph S, Stanley E, et al. (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): 4363–70. 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): 2276–85. PMID 3453117.
Quintrell N, Lebo R, Varmus H, et al. (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. PMID 3496523.
Lee CH, Leung B, Lemmon MA, 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): 5006–15. 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): 1028–33. doi:10.1006/bbrc.1993.1320. PMID 7682059.
Briggs SD, Bryant SS, Jove R, et al. (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. 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): 3507–15. 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): 484–91. 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): 8152–5. 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): 1165–70. PMID 8064233.