Biology:ABL2

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Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Tyrosine-protein kinase ABL2 also known as Abelson-related gene (Arg) is an enzyme that in humans is encoded by the ABL2 gene.[1][2]

Function

ABL2 is a cytoplasmic tyrosine kinase which is closely related to but distinct from ABL1. The similarity of the proteins includes the tyrosine kinase domains and extends amino-terminal to include the SH2 and SH3 domains. ABL2 is expressed in both normal and tumor cells. The expression of ABL2 gene is higher in KRAS mutant non-small cell lung cancer.[3] The ABL2 gene product is expressed as two variants bearing different amino termini, both approximately 12-kb in length.[2]

Interactions

ABL2 has been shown to interact with three proteins: Abl gene,[4] catalase,[5] and SORBS2.[6] The protein Abl gene is also known as abelson murine leukemia viral oncogene homolog 1 and is a protein that is encoded by the human ABL1 gene.[7] Catalase is a common enzyme that catalyzes the decomposition of hydrogen peroxide to water and oxygen.[8] SORBS2 is also known as Sorbin and SH3 domain-containing protein 2 and is a protein encoded by the SORBS2 gene in humans.[2][6][9]

References

  1. ↑ "A novel human gene closely related to the abl proto-oncogene". Science 234 (4783): 1545–1548. December 1986. doi:10.1126/science.3787260. PMID 3787260. Bibcode: 1986Sci...234.1545K. 
  2. ↑ 2.0 2.1 2.2 "Entrez Gene: ABL2 v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene)". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=27. 
  3. ↑ "KRAS driven expression signature has prognostic power superior to mutation status in non-small cell lung cancer". International Journal of Cancer 140 (4): 930–937. February 2017. doi:10.1002/ijc.30509. PMID 27859136. 
  4. ↑ "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". The Journal of Biological Chemistry 278 (15): 12961–12967. April 2003. doi:10.1074/jbc.M300058200. PMID 12569093. 
  5. ↑ "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". The Journal of Biological Chemistry 278 (32): 29667–29675. August 2003. doi:10.1074/jbc.M301292200. PMID 12777400. 
  6. ↑ 6.0 6.1 "ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers and cardiocyte Z-disks". The Journal of Biological Chemistry 272 (28): 17542–17550. July 1997. doi:10.1074/jbc.272.28.17542. PMID 9211900. 
  7. ↑ "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science 253 (5019): 562–565. August 1991. doi:10.1126/science.1857987. PMID 1857987. Bibcode: 1991Sci...253..562S. 
  8. ↑ "Diversity of structures and properties among catalases". Cellular and Molecular Life Sciences 61 (2): 192–208. January 2004. doi:10.1007/s00018-003-3206-5. PMID 14745498. 
  9. ↑ "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research 5 (5): 277–286. October 1998. doi:10.1093/dnares/5.5.277. PMID 9872452. 

Further reading