| V-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene) |
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| PDB rendering based on 1ab2. |
| Available structures |
| 1ab2, 1abo, 1abq, 1bbz, 1fpu, 1iep, 1ju5, 1m52, 1opj, 2e2b, 2f4j, 2g1t, 2g2f, 2g2h, 2g2i, 2gqg, 2hiw, 2hyy, 2hz0, 2hz4, 2hzi, 2hzn |
| Identifiers |
| Symbols |
ABL2; ABLL; ARG |
| External IDs |
OMIM: 164690 MGI: 87860 HomoloGene: 5278 |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
| Entrez |
27 |
11352 |
| Ensembl |
ENSG00000143322 |
ENSMUSG00000026596 |
| UniProt |
P42684 |
Q61055 |
| RefSeq |
NM_005158 (mRNA) |
NM_009595 (mRNA) |
| NP_005149 (protein) |
NP_033725 (protein) |
| Location |
Chr 1:
177.34 - 177.47 Mb |
Chr 1:
158.4 - 158.48 Mb |
| PubMed search |
[1] |
[2] |
Tyrosine-protein kinase ABL2 is an enzyme that in humans is encoded by the ABL2 gene.[1][2]
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 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 Catalase,[3] SORBS2[4] and Abl gene.[5]
References
- ^ Kruh GD, King CR, Kraus MH, Popescu NC, Amsbaugh SC, McBride WO, Aaronson SA (Jan 1987). "A novel human gene closely related to the abl proto-oncogene". Science 234 (4783): 1545–8. PMID 3787260.
- ^ a b "Entrez Gene: ABL2 v-abl Abelson murine leukemia viral oncogene homolog 2 (arg, Abelson-related gene)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27.
- ^ Cao, Cheng; Leng Yumei, Kufe Donald (Aug. 2003). "Catalase activity is regulated by c-Abl and Arg in the oxidative stress response". J. Biol. Chem. (United States) 278 (32): 29667–75. doi:10.1074/jbc.M301292200. ISSN 0021-9258. PMID 12777400.
- ^ Wang, B; Golemis E A, Kruh G D (Jul. 1997). "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". J. Biol. Chem. (UNITED STATES) 272 (28): 17542–50. ISSN 0021-9258. PMID 9211900.
- ^ Cao, Cheng; Leng Yumei, Li Chufang, Kufe Donald (Apr. 2003). "Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response". J. Biol. Chem. (United States) 278 (15): 12961–7. doi:10.1074/jbc.M300058200. ISSN 0021-9258. PMID 12569093.
Further reading
- Pendergast AM (2003). "The Abl family kinases: mechanisms of regulation and signaling.". Adv. Cancer Res. 85: 51–100. doi:10.1016/S0065-230X(02)85003-5. PMID 12374288.
- Muller AJ, Pendergast AM, Havlik MH, et al. (1992). "A limited set of SH2 domains binds BCR through a high-affinity phosphotyrosine-independent interaction.". Mol. Cell. Biol. 12 (11): 5087–93. PMID 1383690.
- Kruh GD, Perego R, Miki T, Aaronson SA (1990). "The complete coding sequence of arg defines the Abelson subfamily of cytoplasmic tyrosine kinases.". Proc. Natl. Acad. Sci. U.S.A. 87 (15): 5802–6. doi:10.1073/pnas.87.15.5802. PMID 2198571.
- Kruh GD, King CR, Kraus MH, et al. (1987). "A novel human gene closely related to the abl proto-oncogene.". Science 234 (4783): 1545–8. doi:10.1126/science.3787260. PMID 3787260.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Wang B, Kruh GD (1996). "Subcellular localization of the Arg protein tyrosine kinase.". Oncogene 13 (1): 193–7. PMID 8700546.
- Wang B, Mysliwiec T, Feller SM, et al. (1996). "Proline-rich sequences mediate the interaction of the Arg protein tyrosine kinase with Crk.". Oncogene 13 (7): 1379–85. PMID 8875975.
- Wang B, Golemis EA, Kruh GD (1997). "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.". J. Biol. Chem. 272 (28): 17542–50. doi:10.1074/jbc.272.28.17542. PMID 9211900.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Koval AP, Blakesley VA, Roberts CT, et al. (1998). "Interaction in vitro of the product of the c-Crk-II proto-oncogene with the insulin-like growth factor I receptor.". Biochem. J. 330 ( Pt 2): 923–32. PMID 9480911.
- Hashimoto Y, Katayama H, Kiyokawa E, et al. (1998). "Phosphorylation of CrkII adaptor protein at tyrosine 221 by epidermal growth factor receptor.". J. Biol. Chem. 273 (27): 17186–91. doi:10.1074/jbc.273.27.17186. PMID 9642287.
- Danial NN, Losman JA, Lu T, et al. (1998). "Direct interaction of Jak1 and v-Abl is required for v-Abl-induced activation of STATs and proliferation.". Mol. Cell. Biol. 18 (11): 6795–804. PMID 9774693.
- Cao C, Ren X, Kharbanda S, et al. (2001). "The ARG tyrosine kinase interacts with Siva-1 in the apoptotic response to oxidative stress.". J. Biol. Chem. 276 (15): 11465–8. doi:10.1074/jbc.C100050200. PMID 11278261.
- Yu HH, Zisch AH, Dodelet VC, Pasquale EB (2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor.". Oncogene 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. PMID 11494128.
- Endo A, Nagashima K, Kurose H, et al. (2002). "Sphingosine 1-phosphate induces membrane ruffling and increases motility of human umbilical vein endothelial cells via vascular endothelial growth factor receptor and CrkII.". J. Biol. Chem. 277 (26): 23747–54. doi:10.1074/jbc.M111794200. PMID 11956190.
- Abassi YA, Vuori K (2002). "Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling.". Embo J. 21 (17): 4571–82. doi:10.1093/emboj/cdf446. PMID 12198159.
- Bianchi C, Muradore I, Corizzato M, et al. (2002). "The expression of the non-receptor tyrosine kinases Arg and c-abl is differently modulated in B lymphoid cells at different stages of differentiation.". FEBS Lett. 527 (1-3): 216–222. doi:10.1016/S0014-5793(02)03233-7. PMID 12220663.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
- Salomon AR, Ficarro SB, Brill LM, et al. (2003). "Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.". Proc. Natl. Acad. Sci. U.S.A. 100 (2): 443–8. doi:10.1073/pnas.2436191100. PMID 12522270.
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PDB Gallery |
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1ab2: THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE SRC HOMOLOGY 2 DOMAIN OF C-ABL
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1abo: CRYSTAL STRUCTURE OF THE COMPLEX OF THE ABL TYROSINE KINASE SH3 DOMAIN WITH 3BP-1 SYNTHETIC PEPTIDE
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1abq: CRYSTAL STRUCTURE OF THE UNLIGANDED ABL TYROSINE KINASE SH3 DOMAIN
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1bbz: CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS
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1fpu: CRYSTAL STRUCTURE OF ABL KINASE DOMAIN IN COMPLEX WITH A SMALL MOLECULE INHIBITOR
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1iep: CRYSTAL STRUCTURE OF THE C-ABL KINASE DOMAIN IN COMPLEX WITH STI-571.
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1ju5: Ternary complex of an Crk SH2 domain, Crk-derived phophopeptide, and Abl SH3 domain by NMR spectroscopy
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1m52: Crystal Structure of the c-Abl Kinase domain in complex with PD173955
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1opj: Structural basis for the auto-inhibition of c-Abl tyrosine kinase
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2e2b: Crystal structure of the c-Abl kinase domain in complex with INNO-406
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2f4j: Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680
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2g1t: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
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2g2f: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
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2g2h: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
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2g2i: A Src-like Inactive Conformation in the Abl Tyrosine Kinase Domain
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2gqg: X-ray Crystal Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain
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2hiw: Crystal Structure of Inactive Conformation Abl Kinase Catalytic Domain Complexed with Type II Inhibitor
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2hyy: Human Abl kinase domain in complex with imatinib (STI571, Glivec)
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2hz0: Abl kinase domain in complex with NVP-AEG082
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2hz4: Abl kinase domain unligated and in complex with tetrahydrostaurosporine
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2hzi: Abl kinase domain in complex with PD180970
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2hzn: Abl kinase domain in complex with NVP-AFG210
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