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; OMA:ABL1 - orthologs
EC number	2.7.10.2
Gene location (Human)
Chr.	Chromosome 9 (human)
End	130,887,675 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	31,694,239 bp
RNA expression pattern
	Top expressed in
	frontal pole; ; paraflocculus of cerebellum; ; middle frontal gyrus; ; muscle layer of sigmoid colon; ; gastric mucosa; ; stromal cell of endometrium; ; left uterine tube; ; ventricular zone; ; body of uterus; ; ganglionic eminence;
	Top expressed in
	external carotid artery; ; internal carotid artery; ; Gonadal ridge; ; genital tubercle; ; tail of embryo; ; vas deferens; ; condyle; ; endocardial cushion; ; vestibular membrane of cochlear duct; ; ventricular zone;
	More reference expression data
	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; soma; 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
	25
	11350
	ENSG00000097007
	ENSMUSG00000026842
	P00519
	P00520
	NM_007313; NM_005157
	NM_001112703; NM_009594; NM_001283045; NM_001283046; NM_001283047
	NP_005148; NP_009297
	NP_001106174; NP_001269974; NP_001269975; NP_001269976; NP_033724
	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]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000097007 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026842 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D, Gewirtz AM, Calabretta B (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science. 253 (5019): 562–5. Bibcode:1991Sci...253..562S. doi:10.1126/science.1857987. PMID 1857987.
^ Abelson HT, Rabstein LS (August 1970). "Lymphosarcoma: virus-induced thymic-independent disease in mice". Cancer Research. 30 (8): 2213–22. PMID 4318922.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000097007 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026842 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1857987-5] Szczylik C, Skorski T, Nicolaides NC, Manzella L, Malaguarnera L, Venturelli D, Gewirtz AM, Calabretta B (August 1991). "Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides". Science. 253 (5019): 562–5. Bibcode:1991Sci...253..562S. doi:10.1126/science.1857987. PMID 1857987.

[pmid4318922-6] Abelson HT, Rabstein LS (August 1970). "Lymphosarcoma: virus-induced thymic-independent disease in mice". Cancer Research. 30 (8): 2213–22. PMID 4318922.

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