ABL (gene)

ABL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1AB2, 1AWO, 1BBZ, 1JU5, 1OPL, 1ZZP, 2ABL, 2E2B, 2FO0, 2G1T, 2G2F, 2G2H, 2G2I, 2GQG, 2HIW, 2HYY, 2HZ0, 2HZ4, 2HZI, 2V7A, 3CS9, 3EG0, 3EG1, 3EG2, 3EG3, 3EGU, 3K2M, 3QRI, 3QRJ, 3QRK, 3T04, 3UE4, 3UYO, 3PYY, 4J9B, 4J9C, 4J9D, 4J9E, 4J9F, 4J9G, 4J9H, 4J9I, 4JJB, 4JJC, 4JJD, 4TWP, 4WA9, 4XEY, 4YC8, 5DC9, 5DC4, 5DC0, 2O88, 5HU9
Identifiers
Aliases	ABL1 , ABL proto-oncogene 1, non-receptor tyrosine kinase, ABL, JTK7, bcr/abl, c-ABL, c-p150, v-abl, CHDSKM, BCR-ABL, Genes, abl
External IDs	OMIM: 189980 MGI: 87859 HomoloGene: 3783 GeneCards: ABL1
EC number	2.7.10.2
Gene location (Human) Chr. Chromosome 9 (human) [1] Band 9q34.12 Start 130,713,016 bp [1] End 130,887,675 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 21.86 cM|2 B Start 31,578,388 bp [2] End 31,694,239 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in frontal pole middle frontal gyrus gastric mucosa stromal cell of endometrium left uterine tube ganglionic eminence popliteal artery canal of the cervix saphenous vein fundus Top expressed in external carotid artery internal carotid artery vas deferens condyle endocardial cushion atrium maxillary prominence dermis molar body of femur More reference expression data BioGPS More reference expression data
Gene ontology Molecular function actin monomer binding protein domain specific binding SH3 domain binding kinase activity protein C-terminus binding signaling receptor binding ATP binding protein kinase activity nicotinate-nucleotide adenylyltransferase activity non-membrane spanning protein tyrosine kinase activity metal ion binding proline-rich region binding magnesium ion binding transferase activity actin filament binding protein binding syntaxin binding protein kinase C binding DNA binding nucleotide binding manganese ion binding mitogen-activated protein kinase binding protein tyrosine kinase activity four-way junction DNA binding bubble DNA binding phosphotyrosine residue binding transcription coactivator activity neuropilin binding SH2 domain binding ephrin receptor binding supercoiled DNA binding sequence-specific double-stranded DNA binding Cellular component cytoplasm cytosol nuclear membrane membrane extrinsic component of cytoplasmic side of plasma membrane mitochondrion actin cytoskeleton perinuclear region of cytoplasm cytoskeleton nucleus nucleolus nucleoplasm cell leading edge nuclear body dendrite protein-containing complex neuronal cell body postsynapse Biological process positive regulation of protein phosphorylation B-1 B cell homeostasis regulation of axon extension neuromuscular process controlling balance positive regulation of muscle cell differentiation cellular response to DNA damage stimulus protein phosphorylation regulation of cell adhesion regulation of microtubule polymerization DNA damage induced protein phosphorylation intrinsic apoptotic signaling pathway in response to DNA damage positive regulation of ERK1 and ERK2 cascade substrate adhesion-dependent cell spreading platelet-derived growth factor receptor-beta signaling pathway positive regulation of actin filament binding B cell receptor signaling pathway apoptotic process negative regulation of endothelial cell apoptotic process cerebellum morphogenesis regulation of actin cytoskeleton reorganization regulation of transcription, DNA-templated epidermal growth factor receptor signaling pathway Fc-gamma receptor signaling pathway involved in phagocytosis establishment of protein localization thymus development negative regulation of phospholipase C activity positive regulation of mitotic cell cycle actin filament branching spleen development response to oxidative stress phagocytosis positive regulation of peptidyl-tyrosine phosphorylation regulation of response to DNA damage stimulus mitochondrial depolarization positive regulation of Wnt signaling pathway, planar cell polarity pathway platelet-derived growth factor receptor signaling pathway regulation of endocytosis activation of protein kinase C activity regulation of actin cytoskeleton organization phosphorylation signal transduction in response to DNA damage positive regulation of oxidoreductase activity positive regulation of release of sequestered calcium ion into cytosol negative regulation of I-kappaB kinase/NF-kappaB signaling regulation of cell motility positive regulation of microtubule binding cell adhesion regulation of autophagy peptidyl-tyrosine autophosphorylation alpha-beta T cell differentiation regulation of cellular senescence negative regulation of protein serine/threonine kinase activity actin cytoskeleton organization negative regulation of cellular senescence positive regulation of osteoblast proliferation mitotic cell cycle activated T cell proliferation endocytosis negative regulation of cell-cell adhesion B cell proliferation involved in immune response cellular response to dopamine positive regulation of cytosolic calcium ion concentration positive regulation of neuron death regulation of cell cycle negative regulation of BMP signaling pathway autophagy B cell proliferation negative regulation of ubiquitin-protein transferase activity microspike assembly positive regulation of apoptotic process regulation of extracellular matrix organization positive regulation of I-kappaB kinase/NF-kappaB signaling negative regulation of ERK1 and ERK2 cascade transitional one stage B cell differentiation DNA mismatch repair Bergmann glial cell differentiation peptidyl-tyrosine phosphorylation collateral sprouting cellular response to lipopolysaccharide negative regulation of mitotic cell cycle cellular response to hydrogen peroxide DNA repair innate immune response neural tube closure post-embryonic development neuron differentiation cellular response to oxidative stress regulation of cell population proliferation protein autophosphorylation neuroepithelial cell differentiation integrin-mediated signaling pathway positive regulation of endothelial cell migration cell differentiation regulation of Cdc42 protein signal transduction neuropilin signaling pathway endothelial cell migration regulation of T cell differentiation positive regulation of transcription by RNA polymerase II T cell receptor signaling pathway positive regulation of stress fiber assembly positive regulation of focal adhesion assembly DNA conformation change positive regulation of cell migration involved in sprouting angiogenesis positive regulation of substrate adhesion-dependent cell spreading negative regulation of long-term synaptic potentiation regulation of hematopoietic stem cell differentiation regulation of modification of synaptic structure positive regulation of blood vessel branching positive regulation of actin cytoskeleton reorganization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 25 11350 Ensembl ENSG00000097007 ENSMUSG00000026842 UniProt P00519 P00520 RefSeq (mRNA) NM_007313 NM_005157 NM_001112703 NM_009594 NM_001283045 NM_001283046 NM_001283047 RefSeq (protein) NP_005148 NP_009297 NP_001106174 NP_001269974 NP_001269975 NP_001269976 NP_033724 Location (UCSC) Chr 9: 130.71 – 130.89 Mb Chr 2: 31.58 – 31.69 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Tyrosine-protein kinase ABL1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9. ^[5] c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene, which was initially isolated from the Abelson murine leukemia virus. ^[6]

Function

The ABL1 proto-oncogene encodes a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response such as DNA repair. ^{[7] [8] [9] [10]} Activity of ABL1 protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR and ABL1 genes, leading to a fusion gene present in many cases of chronic myelogenous leukemia. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for ABL1. The ABL1 gene is expressed as either a 6- or a 7-kb mRNA transcript, with alternatively spliced first exons spliced to the common exons 2–11. ^[11]

Clinical significance

ABL1 kinase domain (blue) in complex with the second-generation Bcr-Abl tyrosine-kinase inhibitor nilotinib (red)

Mutations in the ABL1 gene are associated with chronic myelogenous leukemia (CML). In CML, the gene is activated by being translocated within the BCR (breakpoint cluster region) gene on chromosome 22. This new fusion gene, BCR-ABL, encodes an unregulated, cytoplasm-targeted tyrosine kinase that allows the cells to proliferate without being regulated by cytokines. This, in turn, allows the cell to become cancerous.

This gene is a partner in a fusion gene with the BCR gene in the Philadelphia chromosome, a characteristic abnormality in chronic myelogenous leukemia (CML) and rarely in some other leukemia forms. The BCR-ABL transcript encodes a tyrosine kinase, which activates mediators of the cell cycle regulation system, leading to a clonal myeloproliferative disorder. The BCR-ABL protein can be inhibited by various small molecules. One such inhibitor is imatinib mesylate, which occupies the tyrosine kinase domain and inhibits BCR-ABL's influence on the cell cycle. Second generation BCR-ABL tyrosine-kinase inhibitors are also under development to inhibit BCR-ABL mutants resistant to imatinib. ^[12]

Interactions

ABL gene has been shown to interact with:

• ABI1, ^{[13] [14] [15]}
• ABI2, ^{[16] [17]}
• ABL2, ^[16]
• ATM, ^{[18] [19] [20]}
• BCAR1, ^{[21] [22]}
• BCR, ^{[23] [24] [25]}
• BRCA1, ^[26]
• CAT, ^[27]
• CBL, ^{[28] [29]}
• CRKL, ^{[30] [31] [32]}
• DOK1, ^{[33] [34]}
• EPHB2, ^[35]
• GPX1, ^[36]
• GRB10, ^{[37] [38]}
• MTOR, ^[39]
• GRB2, ^{[30] [40]}
• MDM2, ^[41]
• NCK1, ^{[28] [30]}
• NEDD9, ^{[42] [43]}
• NTRK1, ^{[44] [45]}
• P73, ^{[46] [47]}
• PAG1, ^[48]
• PAK2, ^[49]
• PSTPIP1, ^[50]
• RAD9A, ^[51]
• RAD51, ^[18]
• RB1, ^{[52] [53]}
• RFX1, ^[54]
• RYBP, ^[55]
• SHC1, ^{[23] [56]}
• SORBS2, ^{[29] [57]}
• SPTA1, ^[58]
• SPTAN1, ^[58]
• TERF1, ^[20]
• VAV1, ^[59] and
• YTHDC1. ^[60]

Regulation

There is some evidence that the expression of Abl is regulated by the microRNA miR-203. ^[61]

See also

• BCR gene

References

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2. GRCm38: Ensembl release 89: ENSMUSG00000026842 - Ensembl, May 2017
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Further reading

• Shore SK, Tantravahi RV, Reddy EP (December 2002). "Transforming pathways activated by the v-Abl tyrosine kinase". Oncogene. 21 (56): 8568–76. doi:10.1038/sj.onc.1206084. PMID   12476303. S2CID   42502628.
• Shaul Y (2000). "c-Abl: activation and nuclear targets". Cell Death Differ. 7 (1): 10–6. doi: 10.1038/sj.cdd.4400626 . PMID   10713716.
• Era T (2002). "Bcr-Abl is a "molecular switch" for the decision for growth and differentiation in hematopoietic stem cells". Int. J. Hematol. 76 (1): 35–43. doi:10.1007/BF02982716. PMID   12138893. S2CID   10269867.
• Pendergast AM (2002). "The Abl family kinases: mechanisms of regulation and signaling". Advances in Cancer Research Volume 85. Vol. 85. pp. 51–100. doi:10.1016/S0065-230X(02)85003-5. ISBN   978-0-12-006685-8. PMID   12374288.{{cite book}}: |journal= ignored (help)
• Keung YK, Beaty M, Steward W, Jackle B, Pettnati M (2002). "Chronic myelocytic leukemia with eosinophilia, t(9;12)(q34;p13), and ETV6-ABL gene rearrangement: case report and review of the literature". Cancer Genet. Cytogenet. 138 (2): 139–42. doi:10.1016/S0165-4608(02)00609-X. PMID   12505259.
• Saglio G, Cilloni D (2004). "Abl: the prototype of oncogenic fusion proteins". Cell. Mol. Life Sci. 61 (23): 2897–911. doi:10.1007/s00018-004-4271-0. PMID   15583852. S2CID   35998018.
• Shaul Y, Ben-Yehoyada M (2005). "Role of c-Abl in the DNA damage stress response". Cell Res. 15 (1): 33–5. doi: 10.1038/sj.cr.7290261 . PMID   15686624.
• Yoshida K (2007). "Regulation for Nuclear Targeting of the Abl Tyrosine Kinase in Response to DNA Damage" . Advances in Molecular Oncology. Advances in Experimental Medicine and Biology. Vol. 604. Springer. pp.  155–65. doi:10.1007/978-0-387-69116-9_15. ISBN   978-0-387-69114-5. PMID   17695727.

External links

• Genes,+abl at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• Online Mendelian Inheritance in Man (OMIM): 189980 (ABL)
• Abelson+Leukemia+Virus at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
• DrosophilaAbl tyrosine kinase - The Interactive Fly
• ABL1 Info with links in the Cell Migration Gateway
• ABL1 on the Atlas of Genetics and Oncology
• Human ABL1 genome location and ABL1 gene details page in the UCSC Genome Browser .
• Overview of all the structural information available in the PDB for UniProt : P00519 (Human Tyrosine-protein kinase ABL1) at the PDBe-KB .
• Overview of all the structural information available in the PDB for UniProt : P00520 (Mouse Tyrosine-protein kinase ABL1) at the PDBe-KB .