ABL (gene)

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]

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 31,688,376 bp[2] End 31,804,227 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • actin monomer binding • protein domain specific binding • SH3 domain binding • kinase activity • protein C-terminus binding • 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 • GO:0001948 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 • GO:0001105 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 • cell nucleus • nucleolus • nucleoplasm • cell leading edge • nuclear body • dendrite • macromolecular 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 • cellular protein modification process • positive regulation of interferon-gamma secretion • 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 • GO:0007067 mitotic cell cycle • activated T cell proliferation • endocytosis • negative regulation of cell-cell adhesion • B cell proliferation involved in immune response • positive regulation of interleukin-2 secretion • 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 • cell cycle arrest • 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 • 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 system • neural tube closure • post-embryonic development • neuron differentiation • cellular response to oxidative stress • regulation of cell proliferation • autophosphorylation • neuroepithelial cell differentiation • cardiovascular system development • 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 from RNA polymerase II promoter • 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 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: 31.69 – 31.8 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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[7]. 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.[8]

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.

Interactions

ABL gene has been shown to interact with:

• ABI1,[9][10][11]
• ABI2,[12][13]
• ABL2,[12]
• ATM,[14][15][16]
• BCAR1,[17][18]
• BCR,[19][20][21]
• BRCA1,[22]
• CAT,[23]
• CBL,[24][25]
• CRKL,[26][27][28]
• DOK1,[29][30]
• EPHB2,[31]
• GPX1,[32]
• GRB10,[33][34]
• MTOR,[35]
• GRB2,[26][36]
• MDM2,[37]
• NCK1,[24][26]
• NEDD9,[38][39]
• NTRK1,[40][41]
• P73,[42][43]
• PAG1,[44]
• PAK2,[45]
• PSTPIP1,[46]
• RAD9A,[47]
• RAD51,[14]
• RB1,[48][49]
• RFX1,[50]
• RYBP,[51]
• SHC1,[19][52]
• SORBS2,[25][53]
• SPTA1,[54]
• SPTAN1,[54]
• TERF1,[16]
• VAV1,[55] and
• YTHDC1.[56]

Regulation

There is some evidence that the expression of Abl is regulated by the microRNA miR-203.[57]

See also

• BCR gene

References

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2. GRCm38: Ensembl release 89: ENSMUSG00000026842 - Ensembl, May 2017
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4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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55. Bassermann F, Jahn T, Miething C, Seipel P, Bai RY, Coutinho S, Tybulewicz VL, Peschel C, Duyster J (April 2002). "Association of Bcr-Abl with the proto-oncogene Vav is implicated in activation of the Rac-1 pathway". J. Biol. Chem. 277 (14): 12437–45. doi:10.1074/jbc.M112397200. PMID 11790798.
56. Rafalska I, Zhang Z, Benderska N, Wolff H, Hartmann AM, Brack-Werner R, Stamm S (August 2004). "The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation". Hum. Mol. Genet. 13 (15): 1535–49. doi:10.1093/hmg/ddh167. PMID 15175272.
57. Bueno MJ, Pérez de Castro I, Gómez de Cedrón M, Santos J, Calin GA, Cigudosa JC, Croce CM, Fernández-Piqueras J, Malumbres M (June 2008). "Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression". Cancer Cell. 13 (6): 496–506. doi:10.1016/j.ccr.2008.04.018. hdl:10261/7369. PMID 18538733.

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.
• 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.
• Pendergast AM (2002). The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. Advances in Cancer Research. 85. pp. 51–100. doi:10.1016/S0065-230X(02)85003-5. ISBN 978-0120066858. PMID 12374288.
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External links

• Genes,+abl at the US National Library of Medicine Medical Subject Headings (MeSH)
• Online Mendelian Inheritance in Man (OMIM): 189980 (ABL)
• Abelson+Leukemia+Virus at the US National Library of Medicine Medical Subject Headings (MeSH)
• Drosophila Abl 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.