Atlas of Genetics and Cytogenetics in Oncology and Haematology


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ABL1 (v-abl Abelson murine leukemia viral oncogene homolog 1)

Identity

Other namesABL
HGNC (Hugo) ABL1
LocusID (NCBI) 25
Location 9q34.12
Location_base_pair Starts at 133710831 and ends at 133763062 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order CAN is more telomeric, TAN1 even more in 9q34.3.

DNA/RNA

 
  DNA diagram
Description 12 exons; 230 kb.
Transcription Alternate splicing: 1a and 1b are 5' alternative exons; mRNA of 6 and 7 kb (with 1a and 1b respectively), giving rise to 2 protein of 145 kDa.

Protein

 
  Protein diagram
Description 1130-1143 amino acids; 4 domains: of which are SH (SRC homology) domains; NH2-term -- domain 1: SH3 (where can bind the binding protein BP1, to inhibit SH1 activation) and SH2 (with high affinity towards BCR first exon) -- domain 2: SH1 (with a self-phosphorylable tyrosine) -- 'domain' 3: nuclear localization domain (DNA binding, but not during mitosis) -- domain 4: actin binding (cytoskeleton) --COOH-term; note: 1b (but not the 1a alternative) myristylable allowing anchorage to the membrane.
Normal ABL has a tri-dimensional structure which is tightly preserved in a closed, inactive conformation order to prevent oncogenic activation. The maintenance of this inactive conformation is possible by:
  • 1- the "latching" of the myristilated NH2-terminal sequence which is directly linked to a myristilation recognition sequence on the c-lobe of the SH1 kinase domain;
  • 2-The close contact between SH3 and SH2 domain
  • 3- The interactions between SH3 domain and the C-lobe of the kinase domain. These interactions clamp the structure and prevent the kinase to switch to an active conformation, a process which requires the phosphorylation of Tyr 412 residue and the "unlatching" of the myristoyl group from the C-Lobe of the kinase domain. The attachment of proline-rich SH2 and SH3 ligands leads to the complete switch of the protein to an open, active conformation of the kinase. The NH2-terminal myristilation (autoregulatory role) is deleted during the t(9;22) translocation.
  • Expression Ubiquitously expressed, c-ABL K/O phenotype is lethal.
    Localisation c-abl is localized to the nucleus, plasma membrane and actin cytoskeleton.
    Function c-ABL exhibit a permanent nuclear and cytoplasmic shuttling activity, driven by 3 nuclear localisation signals (NLS) and a single nuclear export signal (NES) close to the C-terminal region. Recent data suggest that nuclear and cytoplasmic ABL may have different functions.
  • 1- Nuclear c-ABL plays a major role in the regulation of cell death after DNA damage. All DNA damage inducing agents activate nuclear c-ABL kinase in a ATM-dependent manner and in the presence of the p53-homolog p73 protein. The latter is physically associated with c-ABL after DNA damage through the SH3 domain of c-ABL. DNA damage also activates simultanously p53 pathway, leading to the activation of Rb which induces growth arrest and protects cells from apoptosis. The exacts mechanisms of apoptosis induced by c-ABL are unknown. The translocation of cytoplasmic c-ABL to the nucleus has been shown to be due to its release from 14-3-3 proteins to which c-ABL is associated in the cytoplasm. JNK-dependent phosphorylation of 14-3-3 upon an oxidative stress, allows this release process and translocation of c-ABL to the nucleus. The oncoprotein MUC has also been shown to block nuclear translocation of c-ABL after apoptotic stimuli.The nuclear entrapment of BCR-ABL has also been shown to induce apoptosis in leukemic cells.
  • 2- Cytoplasmic c-ABL : possible function in adhesion signalling as an efflux of c-ABL from nucleus to the cytoplasm is found in fibroblasts after adhesion. Regulation: Experiments using purified c-abl in vitro allowed to elucidate the mechanism of c-abl regulation which is mediated by an intrinsic property of the molecule. This is the 80 amino-acid N terminal "cap" of the protein is able and sufficient its tyrosine kinase activity and the loss of this cap portion activates the oncogenic potential of c-abl. From the structural point of view, this inhibition is generated by the docking of the myristilated N-terminal of c-abl into the kinase domain. The current view is the fact that c-abl localized in the nucleus, plasma membrane and the actin cytoskeleton undergo different types of regulation. In the membrane-associated c-abl, the myristilated N-terminal end of membrane form can not interact with the kinase c-lobe and it has been suggested that phosphadytilinositol 4-5 bi-phosphate could play an inhibitory role. The autoregulatory mechanism remains functional in the cytoplasmic and nuclear form of c-abl. The latter is also negatively regulated by Rb in the G-phase of the cell cycle. Beside the structural auto-inhibition, several cellular proteins have been shown to inhibit c-ABL: Pag (or Peroxiredoxin-I), Rb and F(actin). Regulation of ABL could therefore be due to a dual mechanism, involving an autoinhibition in the presence of co-inhibitors, which can be active on normal ABL-kinase activity but inactive against increased TK activity of BCR-ABL proteins.
    Recent data suggest that pharmacological inhibition of endogenous ABL could lead to a genetic instability, potentially by inhibition of mismatch repair mechanisms. Long-term inhibition of c-ABL by TKI therapies could therefore be responsible of the occurrence of a mutator phenotypes.
    Activation of ABL can also be detected in solid malignant tumors (lung and breast). Similarly , it has been shown that tumor suppression induced by Ephrin receptor EphB4 requires the presence of an active ABL and phosphorylation of the downstream target CRK by ABL.
  • Homology SRC homology; like SRC, ABL is one of the tyrosine kinases which are not membrane receptors.

    Implicated in

    Entity t(9;12)(q34;p12)/acute lymphoblastic leukemia (ALL) --> ETV6-ABL
    Disease Common ALL; yet poorly known.
    Hybrid/Mutated Gene 5' ETV6/TEL from 12p12 - 3' ABL from 9q34.
    Abnormal Protein NH2-term Helix Loop Helix from ETV6(TEL) fused to Tyr Kinase from ABL COOH-term; localised in the cytoskeleton.
    Oncogenesis Forms HLH-dependent oligomers, which may be critical for Tyr kinase activation; oncogenesis may be comparable to that induced by BCR/ABL.
      
    Entity t(9;22)(q34;q11)/chronic myelogenous leukemia (CML) --> BCR/ABL
    Disease All CML have a t(9;22), at least at the molecular level (BCR/ABL); phenotype and stem cell origin: multipotent progenitor: t(9;22) is found in all myeloid and B- lineage progenitors.
    Prognosis The prognosis of CML has changed radically over the last 10 years, due to the development of novel drugs able to target the enhanced tyrosine kinase activity of BCR-ABL. The first of these therapies is Imatinib Mesylate (Gleevec) which has become the first line therapy for all patients with CML (See CML). In the first cohort trial of patients treated with Imatinib mesylate, the rates of complete cytogenetics responses (CCR) were exceptionally high (82 %) as compared to standard IFN-alpha - ARA-C therapy. At the most recent 6-year update, the overall survival is 90 % and most interestingly, the rates of progression towards more aggressive phases have been found to be progressively decreasing in all patients with major molecular responses (MMR). (For definition of MMR see CML). In IM-resistant or relapsing Ph1+ CML patients, second generation tyrosine kinase inhibitor (TKI) therapies such as Dasatinib (a dual SRC and ABL inhibitor) and Nilotinib have also recently become available.
    Cytogenetics Anomalies additional to the t(9;22) may be found either at diagnosis or during course of the disease, or at the time of acute transformation; mainly: +der(22), +8, i(17q), +19; +21, -Y, -7, -17, +17; variant translocations: t(9;22;V) and apparent t(V;22) or t(9;V), where V is a variable chromosome, karyotypes with apparently normal chromosomes 9 and 22, may be found.
     
    Probe 1132H12 on a case of CML with t(9/22). Note the splitting of the probe, evident also on interphase nuclei - Courtesy Mariano Rocchi, Resources for Molecular Cytogenetics
    Hybrid/Mutated Gene see below
    Abnormal Protein see below
    Oncogenesis see below
      
    Entity t(9;22)(q34;q11)/ALL --> BCR/ABL
    Disease Most often CD 10+ B-ALL; frequent CNS involvement.
    Prognosis The prognosis of Ph1+ ALL has changed since the introduction of tyrosine-kinase inhibitor therapies, especially imatinib mesylate which is currently used as a first line therapy associated with either high dose chemotherapy or classical ALL-type induction (steroids+ vincristine) and maintenance. Allogeneic stem cell transplantation is indicated in Ph1+ ALL patients relapsing after Imatinib-based regimens. In IM-resistant or relapsing Ph1+ ALL patients, second generation tyrosine kinase inhibitor (TKI) therapies such as Dasatinib (a dual SRC and ABL inhibitor) and Nilotinib have also recently become available.
    Cytogenetics The chromosome anomaly t(9;22) disappear during remission, in contrast with BC-CML cases (CML in blast crisis); additional anomalies: +der(22), -7, del(7q) most often, +8, but not an i(17q), in contrast with CML and AML cases; complex karyotypes, often hyperploid; variants and complex translocations may be found as in CML.
    Hybrid/Mutated Gene see below. In Both CML and Ph1+ ALL, detection and quantification of p210 BCR-ABL and p190 BCR-ABL have become the cornerstones of monitoring targeted therapies.
    Abnormal Protein see below
    Oncogenesis see below
      
    Entity t(9;22)(q34;q11)/acute myeloid leukemia (AML) --> BCR/ABL
    Disease AML mostly M1 or M2 AML.
    Prognosis High rates of hematologic , cytogenetic and molecular responses have been reported in de novo PH1+ AML, which is a rare entity.
    Cytogenetics The chromosome anomaly t(9;22) disappear during remission, in contrast with BC-CML cases (CML in blast crisis); additional anomalies: similar to what is found in CML.
    Hybrid/Mutated Gene see below
    Abnormal Protein see below
    Oncogenesis see below
      
    Hybrid/Mutated Gene BCR/ABL the crucial event lies on der(22), id est 5' BCR - 3' ABL hybrid gene is the crucial one, while ABL/BCR may or may not be expressed; breakpoint in ABL is variable over a region of 200 kb, often between the two alternative exons 1b and 1a, sometimes 5' of 1b or 3' of 1a, but always 5' of exon 2; breakpoint in BCR is either:
  • 1- in a region called M-bcr (for major breakpoint cluster region), a cluster of 5.8 kb, between exons 12 and 16, also called b1 to b5 of M-bcr; most breakpoints being either between b2 and b3, or between b3 and b4; transcript is 8.5 kb long; this results in a 210 KDa chimeric protein (P210); this is found in (most cases of) CML, and in half cases of ALL or AML.
  • 2- in a 35 kb region between exons 1 and 2, called m-bcr (minor breakpoint cluster region), -> 7 kb mRNA, resulting in a 190 KDa protein (P190); this is found in half of the cases of ALL or AML.
  • 3- A breakpoint in the exon 19 of BCR (designed as micro-bcr) with fusion to abl sequences (a2) has been in neutrophilic CML, with presence of a larger protein (P230).
  • Abnormal Protein BCR/ABL P210 comprises the first 902 or 927 amino acids from BCR, P190 only the 427 N-term from BCR; BCR/ABL has a cytoplasmic localization, in contrast with ABL, mostly nuclear.
    Oncogenesis BCR/ABL has a cytoplasmic localization role and all three BCR-ABL fusion proteins have been shown to exhibit oncogenic potential. All three hybrid proteins have increased protein kinase activity compared to ABL: 3BP1 (binding protein) binds normal ABL on SH3 domain,which prevents SH1 activation; with BCR/ABL, the first (N-terminal) exon of BCR binds to SH2, hidding SH3 which, as a consequence, cannot be bound to 3BP1; thereof, SH1 is activated; oncogenesis
    1- proliferation is induced through activation by BCR/ABL of RAS signal transduction pathway, PI3-K (phosphatidyl inositol 3' kinase) pathway, and MYC;
    2- BCR/ABL inhibits apoptosis (via activation of STAT5 and BclXL)
    3- BCR/ABL provokes cell adhesive abnormalities (via CRK-L, FAK) as well as abnormalities of cell migration (via CXCR-4 whose expression is downregulated in CML cells expressing high levels of BCR-ABL).
    In experimental settings CD44 has been shown to play a major role in homing of BCR-ABL expressing cells.
    4- BCR-ABL induces a major genetic instability: Molecular pathways involved in this phenomenon have recently been elucidated (See BCR-ABL).
    5-BCR-ABL and endogenous ABL have been shown to be the target of miR 203 which is heavily methylated in CML cell lines expressing BCR-ABL. Restoration of miR 203 expression leads to reduction of BCR-ABL levels, suggesting a potential use of this strategy for therapeutic purposes.
      

    Breakpoints

     

    Other Leukemias implicated (Data extracted from papers in the Atlas)

    Leukemias 11q23ChildAMLID1615 11q23ID1030 11q23secondLeukID1131 t1119ELLID1029 t0812q24q22ID2057
    t0814ID1050 8p11inMPDID1091 inv8p11q13ID1189 PrimarCutanALCLID2118 t0708q34p11ID1409
    t0809p12q33ID1129 t0811p11p15ID1200 t0811p12p15ID1521 t0812p12p11ID1330 t0812p12q15ID1201
    t0817p12q23ID1387

    Other Solid tumors implicated (Data extracted from papers in the Atlas)

    Solid Tumors AmeloblastomID5945 MedulloblastomaID5065

    External links

    Nomenclature
    HGNC (Hugo)ABL1   76
    Cards
    AtlasABL
    Entrez_Gene (NCBI)ABL1  25  ABL proto-oncogene 1, non-receptor tyrosine kinase
    GeneCards (Weizmann)ABL1
    Ensembl (Hinxton)ENSG00000097007 [Gene_View]  chr9:133710831-133763062 [Contig_View]  ABL1 [Vega]
    ICGC DataPortalENSG00000097007
    cBioPortalABL1
    AceView (NCBI)ABL1
    Genatlas (Paris)ABL1
    WikiGenes25
    SOURCE (Princeton)NM_005157 NM_007313
    Genomic and cartography
    GoldenPath (UCSC)ABL1  -  9q34.12   chr9:133710831-133763062 +  9q34.1   [Description]    (hg19-Feb_2009)
    EnsemblABL1 - 9q34.1 [CytoView]
    Mapping of homologs : NCBIABL1 [Mapview]
    OMIM189980   
    Gene and transcription
    Genbank (Entrez)AA524892 AB209456 AB209642 AK294983 AL707819
    RefSeq transcript (Entrez)NM_005157 NM_007313
    RefSeq genomic (Entrez)AC_000141 NC_000009 NC_018920 NG_012034 NT_008470 NW_001839240 NW_004929367
    Consensus coding sequences : CCDS (NCBI)ABL1
    Cluster EST : UnigeneHs.431048 [ NCBI ]
    CGAP (NCI)Hs.431048
    Alternative Splicing : Fast-db (Paris)GSHG0030522
    Alternative Splicing GalleryENSG00000097007
    Gene ExpressionABL1 [ NCBI-GEO ]     ABL1 [ SEEK ]   ABL1 [ MEM ]
    Protein : pattern, domain, 3D structure
    UniProt/SwissProtP00519 (Uniprot)
    NextProtP00519  [Medical]
    With graphics : InterProP00519
    Splice isoforms : SwissVarP00519 (Swissvar)
    Catalytic activity : Enzyme2.7.10.2 [ Enzyme-Expasy ]   2.7.10.22.7.10.2 [ IntEnz-EBI ]   2.7.10.2 [ BRENDA ]   2.7.10.2 [ KEGG ]   
    Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_TYR (PS00109)    SH2 (PS50001)    SH3 (PS50002)   
    Domains : Interpro (EBI)F-actin_binding [organisation]   Kinase-like_dom [organisation]   Prot_kinase_dom [organisation]   Protein_kinase_ATP_BS [organisation]   Ser-Thr/Tyr_kinase_cat_dom [organisation]   SH2 [organisation]   SH3_domain [organisation]   Tyr_kinase_AS [organisation]   Tyr_kinase_cat_dom [organisation]  
    Related proteins : CluSTrP00519
    Domain families : Pfam (Sanger)F_actin_bind (PF08919)    Pkinase_Tyr (PF07714)    SH2 (PF00017)    SH3_1 (PF00018)   
    Domain families : Pfam (NCBI)pfam08919    pfam07714    pfam00017    pfam00018   
    Domain families : Smart (EMBL)FABD (SM00808)  SH2 (SM00252)  SH3 (SM00326)  TyrKc (SM00219)  
    DMDM Disease mutations25
    Blocks (Seattle)P00519
    PDB (SRS)1AB2    1ABL    1AWO    1BBZ    1JU5    1OPL    1ZZP    2ABL    2E2B    2F4J    2FO0    2G1T    2G2F    2G2H    2G2I    2GQG    2HIW    2HYY    2HZ0    2HZ4    2HZI    2O88    2V7A    3CS9    3EG0    3EG1    3EG2    3EG3    3EGU    3K2M    3PYY    3QRI    3QRJ    3QRK    3T04    3UE4    3UYO    4J9B    4J9C    4J9D    4J9E    4J9F    4J9G    4J9H    4J9I    4JJB    4JJC    4JJD   
    PDB (PDBSum)1AB2    1ABL    1AWO    1BBZ    1JU5    1OPL    1ZZP    2ABL    2E2B    2F4J    2FO0    2G1T    2G2F    2G2H    2G2I    2GQG    2HIW    2HYY    2HZ0    2HZ4    2HZI    2O88    2V7A    3CS9    3EG0    3EG1    3EG2    3EG3    3EGU    3K2M    3PYY    3QRI    3QRJ    3QRK    3T04    3UE4    3UYO    4J9B    4J9C    4J9D    4J9E    4J9F    4J9G    4J9H    4J9I    4JJB    4JJC    4JJD   
    PDB (IMB)1AB2    1ABL    1AWO    1BBZ    1JU5    1OPL    1ZZP    2ABL    2E2B    2F4J    2FO0    2G1T    2G2F    2G2H    2G2I    2GQG    2HIW    2HYY    2HZ0    2HZ4    2HZI    2O88    2V7A    3CS9    3EG0    3EG1    3EG2    3EG3    3EGU    3K2M    3PYY    3QRI    3QRJ    3QRK    3T04    3UE4    3UYO    4J9B    4J9C    4J9D    4J9E    4J9F    4J9G    4J9H    4J9I    4JJB    4JJC    4JJD   
    PDB (RSDB)1AB2    1ABL    1AWO    1BBZ    1JU5    1OPL    1ZZP    2ABL    2E2B    2F4J    2FO0    2G1T    2G2F    2G2H    2G2I    2GQG    2HIW    2HYY    2HZ0    2HZ4    2HZI    2O88    2V7A    3CS9    3EG0    3EG1    3EG2    3EG3    3EGU    3K2M    3PYY    3QRI    3QRJ    3QRK    3T04    3UE4    3UYO    4J9B    4J9C    4J9D    4J9E    4J9F    4J9G    4J9H    4J9I    4JJB    4JJC    4JJD   
    Human Protein AtlasENSG00000097007 [gene] [tissue] [antibody] [cell] [cancer]
    Peptide AtlasP00519
    HPRD01809
    IPIIPI00216969   IPI00221171   IPI01015130   IPI01010675   IPI00385144   IPI00642669   
    Protein Interaction databases
    DIP (DOE-UCLA)P00519
    IntAct (EBI)P00519
    FunCoupENSG00000097007
    BioGRIDABL1
    InParanoidP00519
    Interologous Interaction database P00519
    IntegromeDBABL1
    STRING (EMBL)ABL1
    Ontologies - Pathways
    Ontology : AmiGOmagnesium ion binding  DNA binding  actin monomer binding  nicotinate-nucleotide adenylyltransferase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  nucleus  nucleus  nucleus  nucleolus  nucleolus  cytoplasm  mitochondrion  cytosol  mismatch repair  regulation of transcription, DNA-templated  cellular protein modification process  autophagy  cellular response to DNA damage stimulus  DNA damage induced protein phosphorylation  cell adhesion  axon guidance  blood coagulation  protein C-terminus binding  intrinsic apoptotic signaling pathway in response to DNA damage  regulation of autophagy  actin cytoskeleton  SH3 domain binding  peptidyl-tyrosine phosphorylation  syntaxin binding  actin cytoskeleton organization  regulation of endocytosis  manganese ion binding  regulation of cell adhesion  cell leading edge  nuclear membrane  Fc-gamma receptor signaling pathway involved in phagocytosis  muscle cell differentiation  signal transduction in response to DNA damage  positive regulation of apoptotic process  innate immune response  platelet-derived growth factor receptor signaling pathway  perinuclear region of cytoplasm  positive regulation of peptidyl-tyrosine phosphorylation  mitogen-activated protein kinase binding  positive regulation of muscle cell differentiation  positive regulation of oxidoreductase activity  regulation of cell cycle  proline-rich region binding  proline-rich region binding  negative regulation of protein serine/threonine kinase activity  regulation of cell motility  regulation of actin cytoskeleton reorganization  regulation of response to DNA damage stimulus  
    Ontology : EGO-EBImagnesium ion binding  DNA binding  actin monomer binding  nicotinate-nucleotide adenylyltransferase activity  protein tyrosine kinase activity  non-membrane spanning protein tyrosine kinase activity  protein binding  ATP binding  nucleus  nucleus  nucleus  nucleolus  nucleolus  cytoplasm  mitochondrion  cytosol  mismatch repair  regulation of transcription, DNA-templated  cellular protein modification process  autophagy  cellular response to DNA damage stimulus  DNA damage induced protein phosphorylation  cell adhesion  axon guidance  blood coagulation  protein C-terminus binding  intrinsic apoptotic signaling pathway in response to DNA damage  regulation of autophagy  actin cytoskeleton  SH3 domain binding  peptidyl-tyrosine phosphorylation  syntaxin binding  actin cytoskeleton organization  regulation of endocytosis  manganese ion binding  regulation of cell adhesion  cell leading edge  nuclear membrane  Fc-gamma receptor signaling pathway involved in phagocytosis  muscle cell differentiation  signal transduction in response to DNA damage  positive regulation of apoptotic process  innate immune response  platelet-derived growth factor receptor signaling pathway  perinuclear region of cytoplasm  positive regulation of peptidyl-tyrosine phosphorylation  mitogen-activated protein kinase binding  positive regulation of muscle cell differentiation  positive regulation of oxidoreductase activity  regulation of cell cycle  proline-rich region binding  proline-rich region binding  negative regulation of protein serine/threonine kinase activity  regulation of cell motility  regulation of actin cytoskeleton reorganization  regulation of response to DNA damage stimulus  
    Pathways : BIOCARTACell Cycle: G1/S Check Point [Genes]    Tumor Suppressor Arf Inhibits Ribosomal Biogenesis [Genes]    ATM Signaling Pathway [Genes]    Lissencephaly gene (LIS1) in neuronal migration and development [Genes]   
    Pathways : KEGGErbB signaling pathway    Ras signaling pathway    Cell cycle    Axon guidance    Neurotrophin signaling pathway    Pathogenic Escherichia coli infection    Shigellosis    Pathways in cancer    MicroRNAs in cancer    Chronic myeloid leukemia    Viral myocarditis   
    Protein Interaction DatabaseABL1
    Wikipedia pathwaysABL1
    Gene fusion - rearrangments
    Rearrangement : TICdbBCR [22q11.23]  -  ABL1 [8q12.1]
    Rearrangement : TICdbEML1 [14q32.2]  -  ABL1 [6q22.31]
    Rearrangement : TICdbETV6 [12p13.2]  -  ABL1 [21q22.12]
    Rearrangement : TICdbFOXP1 [3p13]  -  ABL1 [3q28]
    Rearrangement : TICdbINPP5D [2q37.1]  -  ABL1 [6p21.32]
    Rearrangement : TICdbNUP214 [9q34.13]  -  ABL1 [9q34.11]
    Rearrangement : TICdbRCSD1 [1q24.2]  -  ABL1 [Xp11.23]
    Rearrangement : TICdbSFPQ [1p34.3]  -  ABL1 [8q12.1]
    Rearrangement : TICdbSNX2 [5q23.2]  -  ABL1 [19q13.42]
    Rearrangement : TICdbZMIZ1 [10q22.3]  -  ABL1 []
    Polymorphisms : SNP, mutations, diseases
    SNP Single Nucleotide Polymorphism (NCBI)ABL1
    snp3D : Map Gene to Disease25
    SNP (GeneSNP Utah)ABL1
    SNP : HGBaseABL1
    Genetic variants : HAPMAPABL1
    Exome VariantABL1
    1000_GenomesABL1 
    ICGC programENSG00000097007 
    Cancer Gene: CensusABL1 
    Somatic Mutations in Cancer : COSMICABL1 
    CONAN: Copy Number AnalysisABL1 
    Mutations and Diseases : HGMDABL1
    Mutations and Diseases : intOGenABL1
    Genomic VariantsABL1  ABL1 [DGVbeta]
    dbVarABL1
    ClinVarABL1
    Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
    Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
    Diseases
    OMIM189980   
    MedgenABL1
    GENETestsABL1
    Disease Genetic AssociationABL1
    Huge Navigator ABL1 [HugePedia]  ABL1 [HugeCancerGEM]
    General knowledge
    Homologs : HomoloGeneABL1
    Homology/Alignments : Family Browser (UCSC)ABL1
    Phylogenetic Trees/Animal Genes : TreeFamABL1
    Chemical/Protein Interactions : CTD25
    Chemical/Pharm GKB GenePA24413
    Clinical trialABL1
    Cancer Resource (Charite)ENSG00000097007
    Other databases
    Probes
    Litterature
    PubMed499 Pubmed reference(s) in Entrez
    CoreMineABL1
    iHOPABL1
    OncoSearchABL1

    Bibliography

    The molecular biology of chronic myeloid leukemia.
    Deininger MW, Goldman JM, Melo JV.
    Blood. 2000 Nov 15;96(10):3343-56.
    PMID 11071626
     
    Regulation of cell death by the Abl tyrosine kinase.
    Wang JY.
    Oncogene. 2000 Nov 20;19(49):5643-50.
    PMID 11114745
     
    BCR-ABL suppresses C/EBPalpha expression through inhibitory action of hnRNP E2.
    Perrotti D, Cesi V, Trotta R, Guerzoni C, Santilli G, Campbell K, Iervolino A, Condorelli F, Gambacorti-Passerini C, Caligiuri MA, Calabretta B.
    Nat Genet. 2002 Jan;30(1):48-58. Epub 2001 Dec 20.
    PMID 11753385
     
    Autoinhibition of c-Abl.
    Pluk H, Dorey K, Superti-Furga G.
    Cell. 2002 Jan 25;108(2):247-59.
    PMID 11832214
     
    Structural basis for the autoinhibition of c-Abl tyrosine kinase.
    Nagar B, Hantschel O, Young MA, Scheffzek K, Veach D, Bornmann W, Clarkson B, Superti-Furga G, Kuriyan J.
    Cell. 2003 Mar 21;112(6):859-71.
    PMID 12654251
     
    c-Abl regulation: a tail of two lipids.
    Van Etten RA.
    Curr Biol. 2003 Aug 5;13(15):R608-10.
    PMID 12906815
     
    The biology of CML blast crisis.
    Calabretta B, Perrotti D.
    Blood. 2004 Jun 1;103(11):4010-22. Epub 2004 Feb 24.
    PMID 14982876
     
    Abl-dependent tyrosine phosphorylation of Sos-1 mediates growth-factor-induced Rac activation.
    Sini P, Cannas A, Koleske AJ, Di Fiore PP, Scita G.
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    Contributor(s)

    Written10-1997Jean-Loup Huret
    Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France
    Updated04-2001Ali G Turhan
    Translational Research - Cell Therapy, Laboratory, Institut Gustave Roussy, INSERM U. 362, 1 - 39, rue Camille Desmoulins, 94805 Villejuif Cedex, France
    Updated08-2008Ali G Turhan
    Pole de Biologie-Sante - 40 avenue du Recteur Pineau - 86022 Poitiers Cedex, France

    Citation

    This paper should be referenced as such :
    Turhan, AG
    ABL1 (v-abl Abelson murine leukemia viral oncogene homolog 1)
    Atlas Genet Cytogenet Oncol Haematol. 2009;13(7):462-466.
    Free online version   Free pdf version   [Bibliographic record ]
    History of this paper:
    Turhan, AG. ABL1 (v-abl Abelson murine leukemia viral oncogene homolog 1). Atlas Genet Cytogenet Oncol Haematol. 2009;13(7):462-466.
    http://documents.irevues.inist.fr/bitstream/2042/44507/1/08-2008-ABL.pdf
    Atlas Genet Cytogenet Oncol Haematol. April 2001
    http://documents.irevues.inist.fr/bitstream/handle/2042/32041/10-1997-ABL.pdf
    URL : http://AtlasGeneticsOncology.org/Genes/ABL.html

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