ABL1

ABL1
PDBに登録されている構造
PDB	オルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧
	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
識別子
記号	ABL1, ABL proto-oncogene 1, non-receptor tyrosine kinase, ABL, JTK7, bcr/abl, c-ABL, c-p150, v-abl, CHDSKM, BCR-ABL, Genes, abl
外部ID	OMIM: 189980 MGI: 87859 HomoloGene: 3783 GeneCards: ABL1
EC番号	2.7.10.2
遺伝子の位置 (ヒト)
染色体	9番染色体 (ヒト)
終点	130,887,675 bp
遺伝子の位置 (マウス)
染色体	2番染色体 (マウス)
終点	31,694,239 bp
RNA発現パターン
	さらなる参照発現データ
遺伝子オントロジー
分子機能	• actin monomer binding; • protein domain specific binding; • SH3 domain binding; • キナーゼ活性; • protein C-terminus binding; • 受容体結合; • ATP binding; • protein kinase activity; • nicotinate-nucleotide adenylyltransferase activity; • non-membrane spanning protein tyrosine kinase activity; • 金属イオン結合; • proline-rich region binding; • magnesium ion binding; • トランスフェラーゼ活性; • actin filament binding; • 血漿タンパク結合; • syntaxin binding; • protein kinase C binding; • DNA結合; • ヌクレオチド結合; • manganese ion binding; • マイトジェン活性化プロテインキナーゼ結合; • 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;
細胞の構成要素	• 細胞質; • 細胞質基質; • 核膜; • 膜; • extrinsic component of cytoplasmic side of plasma membrane; • ミトコンドリア; • actin cytoskeleton; • perinuclear region of cytoplasm; • 細胞骨格; • 細胞核; • 核小体; • 核質; • cell leading edge; • 核内構造体; • 樹状突起; • 高分子複合体; • soma; • postsynapse;
生物学的プロセス	• 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; • タンパク質リン酸化; • 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; • アポトーシス; • 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; • タンパク質局在化の確立; • 胸腺発生; • negative regulation of phospholipase C activity; • positive regulation of mitotic cell cycle; • actin filament branching; • 脾臓発生; • 酸化ストレスへの反応; • 食作用; • 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; • リン酸化; • 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; • 細胞接着; • 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; • 体細胞分裂; • activated T cell proliferation; • エンドサイトーシス; • 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; • オートファジー; • 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ミスマッチ修復; • 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修復; • 自然免疫; • neural tube closure; • post-embryonic development; • neuron differentiation; • cellular response to oxidative stress; • regulation of cell population proliferation; • 自己リン酸化; • neuroepithelial cell differentiation; • integrin-mediated signaling pathway; • positive regulation of endothelial cell migration; • 細胞分化; • 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;
	出典:Amigo / QuickGO
オルソログ
	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
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

ABL1は、ヒトでは9番染色体（英語版）に位置するABL1遺伝子（以前のシンボルはABL）によってコードされているタンパク質である^[5]。哺乳類ゲノムに存在するホモログを表す場合にはc-Abl、ウイルスの場合にはv-Ablという表記が用いられることがあり、当初エーベルソンマウス白血病ウイルス（英語版）（Abelson murine leukemia virus）から単離されたことに由来する^[6]。

概要 PDBに登録されている構造, PDB ...

閉じる

ABL1がん原遺伝子は細胞質と核に位置するチロシンキナーゼ（英語版）をコードし、細胞分化、細胞分裂、細胞接着、そしてDNA修復などのストレス応答といった過程への関与が示唆されている^[7]^[8]^[9]^[10]。ABL1タンパク質の活性はSH3ドメインによって負に調節されており、SH3ドメイン領域が欠失することでABL1はがん遺伝子となる。t(9;22)転座はBCR遺伝子とABL1遺伝子とのhead-to-tail型の融合を引き起こし、慢性骨髄性白血病の多くの症例でみられる融合遺伝子が形成される。普遍的に発現しているABL1チロシンキナーゼのDNA結合活性はCDC2によるリン酸化によって調節され、このことはABL1が細胞周期機能に関与していることを示唆している。ABL1遺伝子は6 kbまたは7 kbのいずれかの長さのmRNA転写産物として発現する。最初のエクソンが選択的エクソンであり、エクソン2–11は共通である^[11]。

ABL1遺伝子の変異は慢性骨髄性白血病（CML）と関係している。CMLでは、この遺伝子が22番染色体上のBCR遺伝子へ転座することによって活性化されている。この染色体異常はCMLに特徴的であり、稀に他の白血病でもみられる。この新たな融合遺伝子BCR-ABLは調節を受けない細胞質型チロシンキナーゼをコードし、細胞周期調節システムの媒介因子を活性化することで、サイトカインによる調節を受けることのない細胞増殖を可能にし、クローン性骨髄増殖性疾患を引き起こす。BCR-ABLタンパク質はさまざまな低分子によって阻害することができる。そうした阻害薬の1つとしてイマチニブがあり、チロシンキナーゼドメインに結合してBCR-ABLの細胞周期への影響を阻害する。イマチニブ耐性を持つBCR-ABL変異体を阻害する、次世代型BCR-ABLチロシンキナーゼ阻害薬（英語版）の開発も行われている^[12]。

ABL1は次に挙げる因子と相互作用することが示されている。

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

ABL1の発現がmiR-203（英語版）によって調節されている証拠も得られている^[61]。

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GRCh38: Ensembl release 89: ENSG00000097007 - Ensembl, May 2017
[2]
GRCm38: Ensembl release 89: ENSMUSG00000026842 - Ensembl, May 2017
[3]
Human PubMed Reference:
[4]
Mouse PubMed Reference:
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[11]
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[19]
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[21]
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[24]
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[25]
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[26]
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[27]
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[28]
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[29]
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[30]
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[31]
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[32]
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[33]
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[34]
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[35]
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[36]
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[37]
“The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene 17 (8): 941–8. (August 1998). doi:10.1038/sj.onc.1202024. PMID 9747873.
[38]
“Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. J. Biol. Chem. 272 (5): 2659–67. (January 1997). doi:10.1074/jbc.272.5.2659. PMID 9006901.
[39]
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[40]
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[41]
“Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation”. EMBO J. 21 (14): 3715–27. (July 2002). doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.
[42]
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[43]
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[44]
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[46]
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[47]
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[48]
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[49]
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[50]
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[54]
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[55]
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[56]
“A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells”. Blood 93 (8): 2707–20. (April 1999). doi:10.1182/blood.V93.8.2707. PMID 10194451.
[57]
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[58]
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[59]
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[60]
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[61]
“Genetic and epigenetic silencing of microRNA-203 enhances ABL1 and BCR-ABL1 oncogene expression”. Cancer Cell 13 (6): 496–506. (June 2008). doi:10.1016/j.ccr.2008.04.018. hdl:10261/7369. PMID 18538733.

“Transforming pathways activated by the v-Abl tyrosine kinase”. Oncogene 21 (56): 8568–76. (December 2002). doi:10.1038/sj.onc.1206084. PMID 12476303.
“c-Abl: activation and nuclear targets”. Cell Death Differ. 7 (1): 10–6. (2000). doi:10.1038/sj.cdd.4400626. PMID 10713716.
“Bcr-Abl is a "molecular switch" for the decision for growth and differentiation in hematopoietic stem cells”. Int. J. Hematol. 76 (1): 35–43. (2002). doi:10.1007/BF02982716. PMID 12138893.
“The Abl family kinases: mechanisms of regulation and signaling”. Advances in Cancer Research Volume 85. Advances in Cancer Research. 85. (2002). 51–100. doi:10.1016/S0065-230X(02)85003-5. ISBN 978-0120066858. PMID 12374288
“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. (2002). doi:10.1016/S0165-4608(02)00609-X. PMID 12505259.
“Abl: the prototype of oncogenic fusion proteins”. Cell. Mol. Life Sci. 61 (23): 2897–911. (2004). doi:10.1007/s00018-004-4271-0. PMID 15583852.
“Role of c-Abl in the DNA damage stress response”. Cell Res. 15 (1): 33–5. (2005). doi:10.1038/sj.cr.7290261. PMID 15686624.
“Regulation for nuclear targeting of the Abl tyrosine kinase in response to DNA damage”. Advances in Molecular Oncology. Advances in Experimental Medicine and Biology. 604. Springer. (2007). 155–65. doi:10.1007/978-0-387-69116-9_15. ISBN 978-0-387-69114-5. PMID 17695727

BCR

Genes, abl - MeSH・アメリカ国立医学図書館・生命科学用語シソーラス（英語）
Online 'Mendelian Inheritance in Man' (OMIM) 189980 (ABL)
Abelson Leukemia Virus - MeSH・アメリカ国立医学図書館・生命科学用語シソーラス（英語）
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.

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

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

[3] [3]
Human PubMed Reference:

[4] [4]
Mouse PubMed Reference:

[pmid1857987-5] [5]
“Selective inhibition of leukemia cell proliferation by BCR-ABL antisense oligodeoxynucleotides”. Science 253 (5019): 562–5. (August 1991). Bibcode: 1991Sci...253..562S. doi:10.1126/science.1857987. PMID 1857987.

[pmid4318922-6] [6]
“Lymphosarcoma: virus-induced thymic-independent disease in mice”. Cancer Research 30 (8): 2213–22. (August 1970). PMID 4318922.

[:0-7] [7]
“Mutational analyses of the human Rad51-Tyr315 residue, a site for phosphorylation in leukaemia cells”. Genes to Cells 9 (9): 781–90. (September 2004). doi:10.1111/j.1365-2443.2004.00772.x. PMID 15330855.

[:1-8] [8]
“BCR-ABL stimulates mutagenic homologous DNA double-strand break repair via the DNA-end-processing factor CtIP”. Carcinogenesis 32 (1): 27–34. (January 2011). doi:10.1093/carcin/bgq216. PMID 20974687.

[:2-9] [9]
“Targeting DNA Homologous Repair Proficiency With Concomitant Topoisomerase II and c-Abl Inhibition”. Frontiers in Oncology 11: 3666. (2021). doi:10.3389/fonc.2021.733700. PMC 8488401. PMID 34616682.

[:3-10] [10]
“UniProtKB - P00519 (ABL1_HUMAN)”. Uniprot. 18 May 2020閲覧。

[:4-11] [11]
“Entrez Gene: ABL1 v-abl Abelson murine leukemia viral oncogene homolog 1”. 2022年8月5日閲覧。

[:5-12] [12]
“Overriding imatinib resistance with a novel ABL kinase inhibitor”. Science 305 (5682): 399–401. (July 2004). Bibcode: 2004Sci...305..399S. doi:10.1126/science.1099480. PMID 15256671.

[pmid12672821-13] [13]
“Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase”. J. Biol. Chem. 278 (24): 21685–92. (June 2003). doi:10.1074/jbc.M301447200. PMID 12672821.

[pmid9010225-14] [14]
“Isolation and characterization of e3B1, an eps8 binding protein that regulates cell growth”. Oncogene 14 (2): 233–41. (January 1997). doi:10.1038/sj.onc.1200822. PMID 9010225.

[pmid11418237-15] [15]
“Isolation of hNap1BP which interacts with human Nap1 (NCKAP1) whose expression is down-regulated in Alzheimer's disease”. Gene 271 (2): 159–69. (June 2001). doi:10.1016/S0378-1119(01)00521-2. PMID 11418237.

[pmid12569093-16] [16]
“Functional interaction between the c-Abl and Arg protein-tyrosine kinases in the oxidative stress response”. J. Biol. Chem. 278 (15): 12961–7. (April 2003). doi:10.1074/jbc.M300058200. PMID 12569093.

[pmid7590236-17] [17]
“Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity”. Genes Dev. 9 (21): 2569–82. (November 1995). doi:10.1101/gad.9.21.2569. PMID 7590236.

[pmid10212258-18] [18]
“Radiation-induced assembly of Rad51 and Rad52 recombination complex requires ATM and c-Abl”. J. Biol. Chem. 274 (18): 12748–52. (April 1999). doi:10.1074/jbc.274.18.12748. PMID 10212258.

[pmid9168117-19] [19]
“Interaction between ATM protein and c-Abl in response to DNA damage”. Nature 387 (6632): 520–3. (May 1997). Bibcode: 1997Natur.387R.520S. doi:10.1038/387520a0. PMID 9168117.

[pmid11375976-20] [20]
“Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks”. J. Biol. Chem. 276 (31): 29282–91. (August 2001). doi:10.1074/jbc.M011534200. PMID 11375976.

[pmid8810278-21] [21]
“p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene”. J. Biol. Chem. 271 (41): 25198–203. (October 1996). doi:10.1074/jbc.271.41.25198. PMID 8810278.

[pmid7780740-22] [22]
“Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases”. Curr. Biol. 5 (3): 296–305. (March 1995). doi:10.1016/S0960-9822(95)00060-1. PMID 7780740.

[pmid8112292-23] [23]
“Bcr-Abl oncoproteins bind directly to activators of the Ras signalling pathway”. EMBO J. 13 (4): 764–73. (February 1994). doi:10.1002/j.1460-2075.1994.tb06319.x. PMC 394874. PMID 8112292.

[pmid12543778-24] [24]
“Bcr and Abl interaction: oncogenic activation of c-Abl by sequestering Bcr”. Cancer Res. 63 (2): 298–303. (January 2003). PMID 12543778.

[pmid1712671-25] [25]
“BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner”. Cell 66 (1): 161–71. (July 1991). doi:10.1016/0092-8674(91)90148-R. PMID 1712671.

[pmid12024016-26] [26]
“Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation”. Mol. Cell. Biol. 22 (12): 4020–32. (June 2002). doi:10.1128/MCB.22.12.4020-4032.2002. PMC 133860. PMID 12024016.

[pmid12777400-27] [27]
“Catalase activity is regulated by c-Abl and Arg in the oxidative stress response”. J. Biol. Chem. 278 (32): 29667–75. (August 2003). doi:10.1074/jbc.M301292200. PMID 12777400.

[pmid11494134-28] [28]
“Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor”. Oncogene 20 (30): 4058–69. (July 2001). doi:10.1038/sj.onc.1204528. PMID 11494134.

[pmid12475393-29] [29]
“Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl”. Biochem. J. 370 (Pt 1): 29–34. (February 2003). doi:10.1042/BJ20021539. PMC 1223168. PMID 12475393.

[pmid7926767-30] [30]
“Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites”. Genes Dev. 8 (7): 783–95. (April 1994). doi:10.1101/gad.8.7.783. PMID 7926767.

[pmid8978305-31] [31]
“Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation”. Blood 89 (1): 297–306. (January 1997). doi:10.1182/blood.V89.1.297. PMID 8978305.

[pmid9820532-32] [32]
“Differential interaction of Crkl with Cbl or C3G, Hef-1, and gamma subunit immunoreceptor tyrosine-based activation motif in signaling of myeloid high affinity Fc receptor for IgG (Fc gamma RI)”. J. Immunol. 161 (10): 5555–63. (November 1998). PMID 9820532.

[pmid11071635-33] [33]
“Stem cell factor induces phosphatidylinositol 3'-kinase-dependent Lyn/Tec/Dok-1 complex formation in hematopoietic cells”. Blood 96 (10): 3406–13. (November 2000). doi:10.1182/blood.V96.10.3406. PMID 11071635.

[pmid9008161-34] [34]
“Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok”. Cell 88 (2): 205–11. (January 1997). doi:10.1016/S0092-8674(00)81841-3. PMID 9008161.

[pmid11494128-35] [35]
“Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor”. Oncogene 20 (30): 3995–4006. (July 2001). doi:10.1038/sj.onc.1204524. PMID 11494128.

[pmid12893824-36] [36]
“Glutathione peroxidase 1 is regulated by the c-Abl and Arg tyrosine kinases”. J. Biol. Chem. 278 (41): 39609–14. (October 2003). doi:10.1074/jbc.M305770200. PMID 12893824.

[pmid9747873-37] [37]
“The SH2-containing adapter protein GRB10 interacts with BCR-ABL”. Oncogene 17 (8): 941–8. (August 1998). doi:10.1038/sj.onc.1202024. PMID 9747873.

[pmid9006901-38] [38]
“Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains”. J. Biol. Chem. 272 (5): 2659–67. (January 1997). doi:10.1074/jbc.272.5.2659. PMID 9006901.

[pmid10753870-39] [39]
“Regulation of the rapamycin and FKBP-target 1/mammalian target of rapamycin and cap-dependent initiation of translation by the c-Abl protein-tyrosine kinase”. J. Biol. Chem. 275 (15): 10779–87. (April 2000). doi:10.1074/jbc.275.15.10779. PMID 10753870.

[pmid9407116-40] [40]
“The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr”. J. Biol. Chem. 272 (52): 33260–70. (December 1997). doi:10.1074/jbc.272.52.33260. PMID 9407116.

[pmid12110584-41] [41]
“Tyrosine phosphorylation of Mdm2 by c-Abl: implications for p53 regulation”. EMBO J. 21 (14): 3715–27. (July 2002). doi:10.1093/emboj/cdf384. PMC 125401. PMID 12110584.

[pmid8879209-42] [42]
“Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes”. J. Exp. Med. 184 (4): 1365–75. (October 1996). doi:10.1084/jem.184.4.1365. PMC 2192828. PMID 8879209.

[pmid8668148-43] [43]
“Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae”. Mol. Cell. Biol. 16 (7): 3327–37. (July 1996). doi:10.1128/mcb.16.7.3327. PMC 231327. PMID 8668148.

[pmid10708759-44] [44]
“Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop”. FEBS Lett. 469 (1): 72–6. (March 2000). doi:10.1016/S0014-5793(00)01242-4. PMID 10708759.

[pmid10679771-45] [45]
“Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor”. J. Neurosci. Res. 59 (3): 356–64. (February 2000). doi:10.1002/(SICI)1097-4547(20000201)59:3<356::AID-JNR9>3.0.CO;2-G. PMID 10679771.

[pmid10391251-46] [46]
“p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage”. Nature 399 (6738): 814–7. (June 1999). Bibcode: 1999Natur.399..814Y. doi:10.1038/21704. PMID 10391251.

[pmid10391250-47] [47]
“Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis”. Nature 399 (6738): 809–13. (June 1999). Bibcode: 1999Natur.399..809A. doi:10.1038/21697. PMID 10391250.

[pmid9334312-48] [48]
“The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity”. Genes Dev. 11 (19): 2456–67. (October 1997). doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.

[pmid11121037-49] [49]
“Functional interaction between c-Abl and the p21-activated protein kinase gamma-PAK”. Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14346–51. (December 2000). Bibcode: 2000PNAS...9714346R. doi:10.1073/pnas.97.26.14346. PMC 18921. PMID 11121037.

[pmid11163214-50] [50]
“Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation”. Mol. Cell 6 (6): 1413–23. (December 2000). doi:10.1016/S1097-2765(00)00138-6. PMID 11163214.

[pmid11971963-51] [51]
“c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage”. Mol. Cell. Biol. 22 (10): 3292–300. (May 2002). doi:10.1128/MCB.22.10.3292-3300.2002. PMC 133797. PMID 11971963.

[pmid9071815-52] [52]
“Interaction of BCR-ABL with the retinoblastoma protein in Philadelphia chromosome-positive cell lines”. Int. J. Hematol. 65 (2): 115–21. (February 1997). doi:10.1016/S0925-5710(96)00539-7. PMID 9071815.

[pmid8242749-53] [53]
“A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear c-Abl tyrosine kinase in the cell cycle”. Cell 75 (4): 779–90. (November 1993). doi:10.1016/0092-8674(93)90497-E. PMID 8242749.

[pmid9583676-54] [54]
“The kinase activity of c-Abl but not v-Abl is potentiated by direct interaction with RFXI, a protein that binds the enhancers of several viruses and cell-cycle regulated genes”. Oncogene 16 (14): 1779–88. (April 1998). doi:10.1038/sj.onc.1201708. PMID 9583676.

[pmid8943360-55] [55]
“c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein”. Mol. Cell. Biol. 16 (12): 7054–62. (December 1996). doi:10.1128/mcb.16.12.7054. PMC 231708. PMID 8943360.

[pmid10194451-56] [56]
“A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells”. Blood 93 (8): 2707–20. (April 1999). doi:10.1182/blood.V93.8.2707. PMID 10194451.

[pmid9211900-57] [57]
“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. (July 1997). doi:10.1074/jbc.272.28.17542. PMID 9211900.

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“Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton”. J. Biol. Chem. 273 (22): 13681–92. (May 1998). doi:10.1074/jbc.273.22.13681. PMID 9593709.

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ABL1

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