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P00519 (ABL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 204. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase ABL1

EC=2.7.10.2
Alternative name(s):
Abelson murine leukemia viral oncogene homolog 1
Abelson tyrosine-protein kinase 1
Proto-oncogene c-Abl
p150
Gene names
Name:ABL1
Synonyms:ABL, JTK7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1130 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-receptor tyrosine-protein kinase that plays a role in many key processes linked to cell growth and survival such as cytoskeleton remodeling in response to extracellular stimuli, cell motility and adhesion, receptor endocytosis, autophagy, DNA damage response and apoptosis. Coordinates actin remodeling through tyrosine phosphorylation of proteins controlling cytoskeleton dynamics like WASF3 (involved in branch formation); ANXA1 (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH (involved in signaling); or MAPT and PXN (microtubule-binding proteins). Phosphorylation of WASF3 is critical for the stimulation of lamellipodia formation and cell migration. Involved in the regulation of cell adhesion and motility through phosphorylation of key regulators of these processes such as BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple receptor tyrosine kinases and more particularly promotes endocytosis of EGFR, facilitates the formation of neuromuscular synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and modulates the endocytosis of activated B-cell receptor complexes. Other substrates which are involved in endocytosis regulation are the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL family of ubiquitin ligases that drive receptor down-regulation and actin remodeling. Phosphorylation of CBL leads to increased EGFR stability. Involved in late-stage autophagy by regulating positively the trafficking and function of lysosomal components. ABL1 targets to mitochondria in response to oxidative stress and thereby mediates mitochondrial dysfunction and cell death. ABL1 is also translocated in the nucleus where it has DNA-binding activity and is involved in DNA-damage response and apoptosis. Many substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic pathway when the DNA damage is too severe to be repaired. Phosphorylates TP73, a primary regulator for this type of damage-induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' and regulates its processing in the apoptotic response to DNA damage. Phosphorylates PSMA7 that leads to an inhibition of proteasomal activity and cell cycle transition blocks. ABL1 acts also as a regulator of multiple pathological signaling cascades during infection. Several known tyrosine-phosphorylated microbial proteins have been identified as ABL1 substrates. This is the case of A36R of Vaccinia virus, Tir (translocated intimin receptor) of pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin-associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing protein A) of A.phagocytophilum. Pathogens can highjack ABL1 kinase signaling to reorganize the host actin cytoskeleton for multiple purposes, like facilitating intracellular movement and host cell exit. Finally, functions as its own regulator through autocatalytic activity as well as through phosphorylation of its inhibitor, ABI1. Ref.13 Ref.14 Ref.15 Ref.17 Ref.21 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29 Ref.31 Ref.32 Ref.37 Ref.38 Ref.39 Ref.40 Ref.42 Ref.43 Ref.49 Ref.52 Ref.64 Ref.70

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.70

Cofactor

Magnesium or manganese.

Enzyme regulation

Stabilized in the inactive form by an association between the SH3 domain and the SH2-TK linker region, interactions of the N-terminal cap, and contributions from an N-terminal myristoyl group and phospholipids. Activated by autophosphorylation as well as by SRC-family kinase-mediated phosphorylation. Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage. Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity By similarity. Inhibited by ABI1, whose activity is controlled by ABL1 itself through tyrosine phosphorylation. Also inhibited by imatinib mesylate (Gleevec) which is used for the treatment of chronic myeloid leukemia (CML), and by VX-680, an inhibitor that acts also on imatinib-resistant mutants. Ref.17 Ref.42 Ref.63 Ref.64 Ref.65

Subunit structure

Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16, ITGB1 and HCK By similarity. Interacts with STX17; probably phosphorylates STX17. Interacts with INPPL1/SHIP2. Interacts with the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3 proteins requires phosphorylation on Thr-735 and, sequesters ABL1 into the cytoplasm. Interacts with ABI1, ABI2, BCR, CRK, FGR, FYN, HCK, LYN, PSMA7 RAD9A, RAD51, RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement. Interacts (via SH3 domain) with CASP9; the interaction is direct and increases in the response of cells to genotoxic stress and ABL1/c-Abl activation. Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.21 Ref.22 Ref.27 Ref.32 Ref.33 Ref.36 Ref.38 Ref.40 Ref.41 Ref.44 Ref.53 Ref.56

Subcellular location

Cytoplasmcytoskeleton. Nucleus. Mitochondrion By similarity. Note: Shuttles between the nucleus and cytoplasm depending on environmental signals. Sequestered into the cytoplasm through interaction with 14-3-3 proteins. Localizes to mitochondria in response to oxidative stress By similarity. Ref.33 Ref.35 Ref.40

Isoform IB: Nucleus membrane; Lipid-anchor. Note: The myristoylated c-ABL protein is reported to be nuclear. Ref.33 Ref.35 Ref.40

Tissue specificity

Widely expressed.

Post-translational modification

Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation. Ref.35

Phosphorylation at Tyr-70 by members of the SRC family of kinases disrupts SH3 domain-based autoinhibitory interactions and intermolecular associations, such as that with ABI1, and also enhances kinase activity. Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity. DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation By similarity. Phosphorylation at Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division By similarity. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1. Phosphorylation on Thr-735 is required for binding 14-3-3 proteins for cytoplasmic translocation. Phosphorylated by PRKDC By similarity. Ref.33 Ref.36 Ref.41 Ref.44 Ref.65

Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation.

Isoform IB is myristoylated on Gly-2.

Involvement in disease

Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal myeloproliferative disorder of a pluripotent stem cell with a specific cytogenetic abnormality, the Philadelphia chromosome (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, and sometimes T-lymphoid cells, but not marrow fibroblasts.
Note: The gene represented in this entry is involved in disease pathogenesis.

A chromosomal aberration involving ABL1 has been found in patients with chronic myeloid leukemia. Translocation t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL found also in acute myeloid leukemia (AML) and acute lymphoblastic leukemia (ALL).

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Cell adhesion
DNA damage
DNA repair
Endocytosis
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
DNA-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Lipoprotein
Myristate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage induced protein phosphorylation

Inferred from direct assay PubMed 18280240. Source: UniProtKB

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

actin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein modification process

Non-traceable author statement PubMed 8242749. Source: UniProtKB

cellular response to DNA damage stimulus

Inferred from direct assay Ref.32. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Traceable author statement Ref.54. Source: UniProtKB

mismatch repair

Traceable author statement PubMed 10391249. Source: ProtInc

muscle cell differentiation

Traceable author statement. Source: Reactome

negative regulation of protein serine/threonine kinase activity

Inferred from direct assay PubMed 11121037. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7590236Ref.14. Source: UniProtKB

platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from direct assay Ref.13. Source: UniProtKB

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of oxidoreductase activity

Inferred from direct assay PubMed 12893824. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.32. Source: UniProtKB

regulation of actin cytoskeleton reorganization

Traceable author statement Ref.54. Source: UniProtKB

regulation of autophagy

Traceable author statement Ref.54. Source: UniProtKB

regulation of cell adhesion

Traceable author statement Ref.54. Source: UniProtKB

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of cell motility

Traceable author statement Ref.54. Source: UniProtKB

regulation of endocytosis

Traceable author statement Ref.54. Source: UniProtKB

regulation of response to DNA damage stimulus

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement PubMed 8242749. Source: ProtInc

signal transduction in response to DNA damage

Inferred from direct assay Ref.32Ref.13. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.54. Source: UniProtKB

cell leading edge

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement Ref.54. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay PubMed 12944467. Source: MGI

nucleus

Inferred from direct assay PubMed 17888034. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17888034. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.14. Source: UniProtKB

DNA binding

Non-traceable author statement PubMed 8242749. Source: UniProtKB

SH3 domain binding

Inferred from physical interaction PubMed 7590236. Source: UniProtKB

actin monomer binding

Traceable author statement Ref.54. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.14. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.14. Source: UniProtKB

mitogen-activated protein kinase binding

Inferred from physical interaction PubMed 11121037. Source: BHF-UCL

nicotinate-nucleotide adenylyltransferase activity

Traceable author statement Ref.54. Source: UniProtKB

non-membrane spanning protein tyrosine kinase activity

Inferred from direct assay Ref.15. Source: UniProtKB

proline-rich region binding

Inferred from direct assay Ref.32. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.22. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20PubMed 11375976Ref.32PubMed 17888034PubMed 7590236Ref.15. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.32PubMed 17888034PubMed 7590236Ref.14. Source: UniProtKB

syntaxin binding

Inferred from physical interaction Ref.56. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform IA (identifier: P00519-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform IB (identifier: P00519-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MGQQPGKVLGDQRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEH
Note: Contains a N-myristoyl glycine at position 2.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11301130Tyrosine-protein kinase ABL1
PRO_0000088050

Regions

Domain61 – 12161SH3
Domain127 – 21791SH2
Domain242 – 493252Protein kinase
Nucleotide binding248 – 2569ATP
Nucleotide binding316 – 3227ATP
Region1 – 6060CAP
Region869 – 968100DNA-binding By similarity
Region953 – 1130178F-actin-binding
Motif381 – 40525Kinase activation loop
Motif605 – 6095Nuclear localization signal 1 Potential
Motif709 – 7157Nuclear localization signal 2 Potential
Motif762 – 7698Nuclear localization signal 3 Potential
Motif1090 – 110011Nuclear export signal By similarity
Compositional bias18 – 225Poly-Ser
Compositional bias605 – 6095Poly-Lys
Compositional bias782 – 1019238Pro-rich
Compositional bias897 – 9037Poly-Pro

Sites

Active site3631Proton acceptor By similarity
Binding site2711ATP
Site26 – 272Breakpoint for translocation to form BCR-ABL oncogene

Amino acid modifications

Modified residue501Phosphoserine Ref.45 Ref.51 Ref.65
Modified residue701Phosphotyrosine; by autocatalysis Ref.36 Ref.44
Modified residue1151Phosphotyrosine Ref.36
Modified residue1281Phosphotyrosine Ref.36
Modified residue1391Phosphotyrosine Ref.36
Modified residue1721Phosphotyrosine Ref.36
Modified residue1851Phosphotyrosine Ref.36
Modified residue2151Phosphotyrosine Ref.36
Modified residue2261Phosphotyrosine; by autocatalysis Ref.36
Modified residue2531Phosphotyrosine
Modified residue2571Phosphotyrosine
Modified residue2641Phosphotyrosine
Modified residue3921Phosphothreonine
Modified residue3931Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases Ref.36
Modified residue3941Phosphothreonine
Modified residue4461Phosphoserine By similarity
Modified residue4691Phosphotyrosine
Modified residue5691Phosphoserine Ref.34 Ref.45 Ref.46 Ref.50 Ref.51
Modified residue6131Phosphothreonine
Modified residue6181Phosphoserine; by PAK2 Ref.41
Modified residue6191Phosphoserine; by PAK2 Ref.41
Modified residue6201Phosphoserine
Modified residue6591Phosphoserine Ref.45
Modified residue6831Phosphoserine
Modified residue7111N6-acetyllysine; by EP300 Ref.35
Modified residue7181Phosphoserine
Modified residue7351Phosphothreonine Ref.33
Modified residue7811Phosphothreonine
Modified residue8051Phosphoserine
Modified residue8091Phosphoserine
Modified residue8141Phosphothreonine Ref.45
Modified residue8441Phosphothreonine Ref.45
Modified residue8521Phosphothreonine Ref.46
Modified residue8551Phosphoserine
Modified residue9171Phosphoserine Ref.46
Modified residue9191Phosphoserine
Modified residue9361Phosphoserine
Modified residue9491Phosphoserine
Modified residue9771Phosphoserine Ref.45

Natural variations

Alternative sequence1 – 2626MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKKESSRHGGPHCN VFVEH in isoform IB.
VSP_004957
Natural variant471R → G in a lung large cell carcinoma sample; somatic mutation. Ref.71
VAR_032676
Natural variant1401L → P. Ref.1
Corresponds to variant rs1064152 [ dbSNP | Ensembl ].
VAR_051692
Natural variant1661R → K in a melanoma sample; somatic mutation. Ref.71
VAR_032677
Natural variant2471K → R.
Corresponds to variant rs34549764 [ dbSNP | Ensembl ].
VAR_051693
Natural variant7061G → V. Ref.4 Ref.71
Corresponds to variant rs34634745 [ dbSNP | Ensembl ].
VAR_025043
Natural variant8101P → L. Ref.71
Corresponds to variant rs2229071 [ dbSNP | Ensembl ].
VAR_032678
Natural variant8521T → P. Ref.4
VAR_025044
Natural variant9001P → S. Ref.4
Corresponds to variant rs35266696 [ dbSNP | Ensembl ].
VAR_025045
Natural variant9681S → P.
Corresponds to variant rs1064165 [ dbSNP | Ensembl ].
VAR_051694
Natural variant9721S → L. Ref.4 Ref.71
Corresponds to variant rs2229067 [ dbSNP | Ensembl ].
VAR_025046

Experimental info

Mutagenesis7351T → A: Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity. Ref.33
Sequence conflict1591G → S in AAA51561. Ref.1
Sequence conflict424 – 4252AF → GK Ref.9
Sequence conflict4451L → R in AAA51561. Ref.1
Sequence conflict4591E → K in AAA51561. Ref.1
Sequence conflict5201S → T in AAA51561. Ref.1
Sequence conflict7191A → V in AAA51561. Ref.1
Sequence conflict8371G → E in CAA34438. Ref.2
Sequence conflict8371G → W in AAA51561. Ref.1
Sequence conflict8631G → R in AAA51561. Ref.1
Sequence conflict8941R → K in AAA51561. Ref.1
Sequence conflict917 – 9193SPS → RPG in AAA51561. Ref.1
Sequence conflict9521G → A in AAA51561. Ref.1
Sequence conflict967 – 9682QS → HP in AAA51561. Ref.1
Sequence conflict9821P → PL in AAA51561. Ref.1
Sequence conflict10221Missing in AAA51561. Ref.1
Sequence conflict10451R → G in AAA51561. Ref.1
Sequence conflict11031T → S in AAA51561. Ref.1

Secondary structure

....................................................................................................................... 1130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform IA [UniParc].

Last modified January 24, 2006. Version 4.
Checksum: 85FE6C1C0E483EA2

FASTA1,130122,873
        10         20         30         40         50         60 
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE 

        70         80         90        100        110        120 
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN 

       130        140        150        160        170        180 
SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS 

       190        200        210        220        230        240 
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTVYGVSP NYDKWEMERT 

       250        260        270        280        290        300 
DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 

       310        320        330        340        350        360 
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL LYMATQISSA MEYLEKKNFI 

       370        380        390        400        410        420 
HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS 

       430        440        450        460        470        480 
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP 

       490        500        510        520        530        540 
SDRPSFAEIH QAFETMFQES SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE 

       550        560        570        580        590        600 
HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF 

       610        620        630        640        650        660 
SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP 

       670        680        690        700        710        720 
KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT GEEEGGGSSS KRFLRSCSAS 

       730        740        750        760        770        780 
CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV 

       790        800        810        820        830        840 
TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS 

       850        860        870        880        890        900 
ALGTPAAAEP VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP 

       910        920        930        940        950        960 
PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ PGEGLKKPVL 

       970        980        990       1000       1010       1020 
PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE 

      1030       1040       1050       1060       1070       1080 
RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK 

      1090       1100       1110       1120       1130 
FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS VKEISDIVQR 

« Hide

Isoform IB [UniParc].

Checksum: DF9D4512F78FFE52
Show »

FASTA1,149124,955

References

« Hide 'large scale' references
[1]"Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene."
Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E.
Cell 47:277-284(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, VARIANT PRO-140.
[2]"Nucleotide sequence analysis of human abl and bcr-abl cDNAs."
Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P., Canaani E.
Oncogene 4:1477-1481(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA).
Tissue: Fibroblast.
[3]"Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation."
Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., Heisterkamp N., Groffen J., Roe B.A.
Genomics 27:67-82(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA AND IB).
Tissue: Lung.
[4]NIEHS SNPs program
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-706; PRO-852; SER-900 AND LEU-972.
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IB).
Tissue: Cerebellum.
[8]"A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia."
Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., Dreazen O., Smith S.D., Croce C.M.
Nature 330:386-388(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, SUBCELLULAR COMPONENT.
[9]"Homology between phosphotyrosine acceptor site of human c-abl and viral oncogene products."
Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R.
Nature 304:167-169(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 360-426.
[10]"Sequence analysis of the mutation at codon 834 and the sequence variation of codon 837 of c-abl gene."
Inokuchi K., Futaki M., Dan K., Nomura T.
Leukemia 8:343-344(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845.
[11]"N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl."
Jackson P., Baltimore D.
EMBO J. 8:449-456(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MYRISTOYLATION (ISOFORM IB).
[12]"Differential phosphorylation of c-Abl in cell cycle determined by cdc2 kinase and phosphatase activity."
Kipreos E.T., Wang J.Y.
Science 248:217-220(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, DNA-BINDING.
[13]"Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase."
Yuan Z.M., Huang Y., Ishiko T., Kharbanda S., Weichselbaum R., Kufe D.
Proc. Natl. Acad. Sci. U.S.A. 94:1437-1440(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Protein binding and signaling properties of RIN1 suggest a unique effector function."
Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., Herschman H., Witte O., Colicelli J.
Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RIN1, FUNCTION.
[15]"Regulation of Rad51 function by c-Abl in response to DNA damage."
Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T., Kharbanda S., Wang R., Sung P., Shinohara A., Weichselbaum R., Kufe D.
J. Biol. Chem. 273:3799-3802(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD51.
[16]"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."
Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.
Blood 93:2707-2720(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH INPPL1.
[17]"Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis."
Agami R., Blandino G., Oren M., Shaul Y.
Nature 399:809-813(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH TP73.
[18]"The DNA-binding domain of human c-Abl tyrosine kinase promotes the interaction of a HMG chromosomal protein with DNA."
David-Cordonnier M.H., Payet D., D'Halluin J.C., Waring M.J., Travers A.A., Bailly C.
Nucleic Acids Res. 27:2265-2270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING.
[19]"Regulation of cell death by the Abl tyrosine kinase."
Wang J.Y.
Oncogene 19:5643-5650(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[20]"Cloning, mapping, and characterization of the human sorbin and SH3 domain containing 1 (SORBS1) gene: a protein associated with c-Abl during insulin signaling in the hepatoma cell line Hep3B."
Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., Chuang L.-M.
Genomics 74:12-20(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORBS1.
[21]"Regulation of ionizing radiation-induced Rad52 nuclear foci formation by c-Abl-mediated phosphorylation."
Kitao H., Yuan Z.M.
J. Biol. Chem. 277:48944-48948(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD52.
[22]"c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in response to DNA damage."
Yoshida K., Komatsu K., Wang H.-G., Kufe D.
Mol. Cell. Biol. 22:3292-3300(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAD9A.
[23]"Cbl-ArgBP2 complex mediates ubiquitination and degradation of c-Abl."
Soubeyran P., Barac A., Szymkiewicz I., Dikic I.
Biochem. J. 370:29-34(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[24]"c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14."
Sanguinetti A.R., Mastick C.C.
Cell. Signal. 15:289-298(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase."
Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., Shishido T.
J. Biol. Chem. 278:21685-21692(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[26]"Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases."
Woodring P.J., Hunter T., Wang J.Y.
J. Cell Sci. 116:2613-2626(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[27]"The c-Fes tyrosine kinase cooperates with the breakpoint cluster region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-dependent manner."
Laurent C.E., Smithgall T.E.
Exp. Cell Res. 299:188-198(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCR.
[28]"Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl."
Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S., Deininger M.W., Druker B.J.
FEBS Lett. 577:555-562(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to stimulate Fe65/amyloid precursor protein nuclear signaling."
Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L., Ward M., McLoughlin D.M., Miller C.C.
J. Biol. Chem. 279:22084-22091(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[30]"Role of c-Abl in the DNA damage stress response."
Shaul Y., Ben-Yehoyada M.
Cell Res. 15:33-35(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[31]"RIN1 is an ABL tyrosine kinase activator and a regulator of epithelial-cell adhesion and migration."
Hu H., Bliss J.M., Wang Y., Colicelli J.
Curr. Biol. 15:815-823(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"c-Abl tyrosine kinase regulates caspase-9 autocleavage in the apoptotic response to DNA damage."
Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S., Weichselbaum R., Kufe D.
J. Biol. Chem. 280:11147-11151(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CASP9.
[33]"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damage."
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.
Nat. Cell Biol. 7:278-285(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ, PHOSPHORYLATION AT THR-735, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-735.
[34]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"c-Abl acetylation by histone acetyltransferases regulates its nuclear-cytoplasmic localization."
di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barila D.
EMBO Rep. 7:727-733(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-711, SUBCELLULAR LOCATION.
[36]"Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity."
Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P., Wu J., Hochrein J.M., Engen J.R., Smithgall T.E.
J. Biol. Chem. 281:30907-30916(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-70; TYR-115; TYR-128; TYR-139; TYR-172; TYR-185 TYR-215; TYR-226 AND TYR-393, INTERACTION WITH HCK; LYN AND FYN, IDENTIFICATION BY MASS SPECTROMETRY.
[37]"Abl tyrosine kinase regulates endocytosis of the epidermal growth factor receptor."
Tanos B., Pendergast A.M.
J. Biol. Chem. 281:32714-32723(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit PSMA7 regulates proteasome degradation."
Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C.
Mol. Cell 22:317-327(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PSMA7.
[39]"A critical role for cortactin phosphorylation by Abl-family kinases in PDGF-induced dorsal-wave formation."
Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.
Curr. Biol. 17:445-451(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[40]"c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia formation and cell migration."
Sossey-Alaoui K., Li X., Cowell J.K.
J. Biol. Chem. 282:26257-26265(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH WASF3.
[41]"Phosphorylation of c-Abl by protein kinase Pak2 regulates differential binding of ABI2 and CRK."
Jung J.H., Pendergast A.M., Zipfel P.A., Traugh J.A.
Biochemistry 47:1094-1104(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-618 AND SER-619, INTERACTION WITH ABI2 AND CRK.
[42]"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase by phosphopeptides derived from Abi1/Hssh3bp1."
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X., Debnath A.K., Cowburn D., Kotula L.
Biochim. Biophys. Acta 1783:737-747(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[43]"Abl kinases regulate autophagy by promoting the trafficking and function of lysosomal components."
Yogalingam G., Pendergast A.M.
J. Biol. Chem. 283:35941-35953(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[44]"Tyrosine phosphorylation in the SH3 domain disrupts negative regulatory interactions within the c-Abl kinase core."
Chen S., O'Reilly L.P., Smithgall T.E., Engen J.R.
J. Mol. Biol. 383:414-423(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-70, INTERACTION WITH ABI1.
[45]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-569; SER-659; THR-814; THR-844 AND SER-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[46]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-852 AND SER-917, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[47]"Emerging roles of Abl family tyrosine kinases in microbial pathogenesis."
Backert S., Feller S.M., Wessler S.
Trends Biochem. Sci. 33:80-90(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[48]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]"Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src kinases."
Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.
BMC Cell Biol. 10:80-80(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[50]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[51]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[52]"c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal ruffling of fibroblasts and axonal morphogenesis."
Michael M., Vehlow A., Navarro C., Krause M.
Curr. Biol. 20:783-791(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[53]"Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain kinase to regulate endothelial barrier function."
Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., Imam S.Z., Garcia J.G.N.
Mol. Biol. Cell 21:4042-4056(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYLK AND CTTN.
[54]"ABL tyrosine kinases: evolution of function, regulation, and specificity."
Colicelli J.
Sci. Signal. 3:RE6-RE6(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION, DOMAIN.
[55]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[56]"Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway."
Muppirala M., Gupta V., Swarup G.
Biochim. Biophys. Acta 1823:2109-2119(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STX17.
[57]"Three-dimensional solution structure of the src homology 2 domain of c-abl."
Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D.
Cell 70:697-704(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
[58]"Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution."
Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D.
Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.
[59]"Homology modeling of the Abl-SH3 domain."
Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C.
Proteins 20:203-215(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF SH3 DOMAIN.
[60]"The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct."
Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D.
Structure 3:1075-1086(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF SH3 DOMAIN.
[61]"Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions."
Pisabarro M.T., Serrano L., Wilmanns M.
J. Mol. Biol. 281:513-521(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
[62]"Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide."
Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.
Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK.
[63]"Structural basis for the autoinhibition of c-Abl tyrosine kinase."
Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.
Cell 112:859-871(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 27-512, MYRISTOYLATION (ISOFORM IB), ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
[64]"Structure of the kinase domain of an imatinib-resistant Abl mutant in complex with the Aurora kinase inhibitor VX-680."
Young M.A., Shah N.P., Chao L.H., Seeliger M., Milanov Z.V., Biggs W.H. III, Treiber D.K., Patel H.K., Zarrinkar P.P., Lockhart D.J., Sawyers C.L., Kuriyan J.
Cancer Res. 66:1007-1014(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 229-513 OF MUTANT PRO-396 IN COMPLEX WITH INHIBITOR VX-680, FUNCTION, ENZYME REGULATION.
[65]"Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase."
Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I., Superti-Furga G., Kuriyan J.
Mol. Cell 21:787-798(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, IDENTIFICATION BY MASS SPECTROMETRY, MYRISTOYLATION OF N-TERMINUS (ISOFORM IB), PHOSPHORYLATION AT SER-50, AUTOINHIBITORY MECHANISM, ENZYME REGULATION.
[66]"A Src-like inactive conformation in the abl tyrosine kinase domain."
Levinson N.M., Kuchment O., Shen K., Young M.A., Koldobskiy M., Karplus M., Cole P.A., Kuriyan J.
PLoS Biol. 4:E144-E144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 229-512 IN COMPLEXES WITH ATP-PEPTIDE CONJUGATE, CONFORMATION CHANGES DURING ACTIVATION.
[67]"Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia."
Cowan-Jacob S.W., Fendrich G., Floersheimer A., Furet P., Liebetanz J., Rummel G., Rheinberger P., Centeleghe M., Fabbro D., Manley P.W.
Acta Crystallogr. D 63:80-93(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 229-500 IN COMPLEXES WITH IMATINIB AND WITH THE INHIBITORS NVP-AEG082; NVP-AFN941; NVP-AFG210 AND PD180970.
[68]"Crystallization by capillary counter-diffusion and structure determination of the N114A mutant of the SH3 domain of Abl tyrosine kinase complexed with a high-affinity peptide ligand."
Camara-Artigas A., Palencia A., Martinez J.C., Luque I., Gavira J.A., Garcia-Ruiz J.M.
Acta Crystallogr. D 63:646-652(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-121 OF MUTANT ALA-114 IN COMPLEX WITH PROLINE-RICH PEPTIDE.
[69]"Role of interfacial water molecules in proline-rich ligand recognition by the Src homology 3 domain of Abl."
Palencia A., Camara-Artigas A., Pisabarro M.T., Martinez J.C., Luque I.
J. Biol. Chem. 285:2823-2833(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 60-121 IN COMPLEX WITH PROLINE-RICH PEPTIDE P41.
[70]"A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain."
Wojcik J., Hantschel O., Grebien F., Kaupe I., Bennett K.L., Barkinge J., Jones R.B., Koide A., Superti-Furga G., Koide S.
Nat. Struct. Mol. Biol. 17:519-527(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 121-232 IN COMPLEX WITH ANTIBODY MIMIC HA4, FUNCTION, CATALYTIC ACTIVITY.
[71]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14752 mRNA. Translation: AAA51561.1.
X16416 mRNA. Translation: CAA34438.1.
U07563 Genomic DNA. Translation: AAB60394.1.
U07563, U07561 Genomic DNA. Translation: AAB60393.1.
DQ145721 Genomic DNA. Translation: AAZ38718.1.
AL359092, AL161733 Genomic DNA. Translation: CAM45752.1.
AL161733 Genomic DNA. Translation: CAM45754.1.
AL161733, AL359092 Genomic DNA. Translation: CAM45756.1.
CH471090 Genomic DNA. Translation: EAW87948.1.
BC117451 mRNA. Translation: AAI17452.1.
S69223 Genomic DNA. Translation: AAD14034.1.
CCDSCCDS35165.1. [P00519-2]
CCDS35166.1. [P00519-1]
PIRTVHUA. S08519.
RefSeqNP_005148.2. NM_005157.4. [P00519-1]
NP_009297.2. NM_007313.2. [P00519-2]
UniGeneHs.431048.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB2NMR-A120-220[»]
1ABLmodel-A65-121[»]
1AWONMR-A65-119[»]
1BBZX-ray1.65A/C/E/G64-121[»]
1JU5NMR-C62-122[»]
1OPLX-ray3.42A/B27-512[»]
1ZZPNMR-A1007-1130[»]
2ABLX-ray2.50A57-218[»]
2E2BX-ray2.20A/B229-515[»]
2F4JX-ray1.91A229-513[»]
2FO0X-ray2.27A38-512[»]
2G1TX-ray1.80A/B/C/D229-512[»]
2G2FX-ray2.70A/B229-512[»]
2G2HX-ray2.00A/B229-512[»]
2G2IX-ray3.12A/B229-512[»]
2GQGX-ray2.40A/B229-500[»]
2HIWX-ray2.20A/B230-512[»]
2HYYX-ray2.40A/B/C/D228-500[»]
2HZ0X-ray2.10A/B228-497[»]
2HZ4X-ray2.80A/B/C228-500[»]
2HZIX-ray1.70A/B229-500[»]
2O88X-ray1.75A/B64-121[»]
2V7AX-ray2.50A/B229-512[»]
3CS9X-ray2.21A/B/C/D229-500[»]
3EG0X-ray2.30A60-121[»]
3EG1X-ray1.85A/B60-121[»]
3EG2X-ray1.80A60-121[»]
3EG3X-ray1.40A60-121[»]
3EGUX-ray2.25A60-121[»]
3K2MX-ray1.75A/B121-232[»]
3PYYX-ray1.85A/B229-512[»]
3QRIX-ray2.10A/B229-499[»]
3QRJX-ray1.82A/B229-499[»]
3QRKX-ray2.30A229-499[»]
3T04X-ray2.10A112-232[»]
3UE4X-ray2.42A/B229-512[»]
3UYOX-ray1.83A112-232[»]
4J9BX-ray1.70A60-121[»]
4J9CX-ray1.05A60-121[»]
4J9DX-ray1.50A/C/E60-121[»]
4J9EX-ray1.40A/C/E60-121[»]
4J9FX-ray1.09A/C/E60-121[»]
4J9GX-ray1.80A/C/E60-121[»]
4J9HX-ray1.70A/B/C/D/E/F60-121[»]
4J9IX-ray2.20A/C/E60-121[»]
4JJBX-ray1.65A60-121[»]
4JJCX-ray1.60A60-121[»]
4JJDX-ray1.60A60-121[»]
ProteinModelPortalP00519.
SMRP00519. Positions 46-528, 1024-1130.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106543. 138 interactions.
DIPDIP-1042N.
IntActP00519. 198 interactions.
MINTMINT-7236141.
STRING9606.ENSP00000361423.

Chemistry

BindingDBP00519.
ChEMBLCHEMBL1862.
DrugBankDB00171. Adenosine triphosphate.
DB01254. Dasatinib.
DB00619. Imatinib.
GuidetoPHARMACOLOGY1923.

PTM databases

PhosphoSiteP00519.

Polymorphism databases

DMDM85681908.

Proteomic databases

MaxQBP00519.
PaxDbP00519.
PRIDEP00519.

Protocols and materials databases

DNASU25.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318560; ENSP00000323315; ENSG00000097007. [P00519-1]
ENST00000372348; ENSP00000361423; ENSG00000097007. [P00519-2]
GeneID25.
KEGGhsa:25.
UCSCuc004bzv.3. human. [P00519-2]
uc004bzw.3. human. [P00519-1]

Organism-specific databases

CTD25.
GeneCardsGC09P133589.
HGNCHGNC:76. ABL1.
HPACAB002686.
HPA027251.
HPA027280.
HPA028409.
MIM189980. gene.
608232. phenotype.
neXtProtNX_P00519.
Orphanet521. Chronic myeloid leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBPA24413.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG004162.
KOK06619.
OMAGAFRESG.
OrthoDBEOG7GTT2V.
PhylomeDBP00519.
TreeFamTF105081.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP00519.

Gene expression databases

ArrayExpressP00519.
BgeeP00519.
CleanExHS_ABL1.
GenevestigatorP00519.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR015015. F-actin_binding.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABL1. human.
EvolutionaryTraceP00519.
GeneWikiABL_(gene).
GenomeRNAi25.
NextBio79.
PMAP-CutDBP00519.
PROP00519.
SOURCESearch...

Entry information

Entry nameABL1_HUMAN
AccessionPrimary (citable) accession number: P00519
Secondary accession number(s): A3KFJ3 expand/collapse secondary AC list , Q13869, Q13870, Q16133, Q17R61, Q45F09
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: July 9, 2014
This is version 204 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM