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P00519

- ABL1_HUMAN

UniProt

P00519 - ABL1_HUMAN

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Protein

Tyrosine-protein kinase ABL1

Gene

ABL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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, ABI1.22 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

Cofactori

Magnesium or manganese.

Enzyme regulationi

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.By similarity5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei26 – 272Breakpoint for translocation to form BCR-ABL oncogene
Binding sitei271 – 2711ATP
Active sitei363 – 3631Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2569ATP
Nucleotide bindingi316 – 3227ATP

GO - Molecular functioni

  1. actin monomer binding Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. magnesium ion binding Source: UniProtKB
  5. manganese ion binding Source: UniProtKB
  6. mitogen-activated protein kinase binding Source: BHF-UCL
  7. nicotinate-nucleotide adenylyltransferase activity Source: UniProtKB
  8. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  9. proline-rich region binding Source: UniProtKB
  10. protein C-terminus binding Source: UniProtKB
  11. protein kinase activity Source: MGI
  12. protein tyrosine kinase activity Source: UniProtKB
  13. SH3 domain binding Source: UniProtKB
  14. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. autophagy Source: UniProtKB-KW
  3. axon guidance Source: Reactome
  4. blood coagulation Source: Reactome
  5. cell adhesion Source: UniProtKB-KW
  6. cell cycle arrest Source: ParkinsonsUK-UCL
  7. cellular protein modification process Source: UniProtKB
  8. cellular response to DNA damage stimulus Source: UniProtKB
  9. cellular response to dopamine Source: ParkinsonsUK-UCL
  10. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  11. DNA damage induced protein phosphorylation Source: UniProtKB
  12. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  13. innate immune response Source: Reactome
  14. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  15. mismatch repair Source: ProtInc
  16. mitochondrial depolarization Source: ParkinsonsUK-UCL
  17. mitotic nuclear division Source: ParkinsonsUK-UCL
  18. muscle cell differentiation Source: Reactome
  19. negative regulation of phospholipase C activity Source: MGI
  20. negative regulation of protein serine/threonine kinase activity Source: BHF-UCL
  21. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  22. peptidyl-tyrosine phosphorylation Source: UniProtKB
  23. platelet-derived growth factor receptor signaling pathway Source: Ensembl
  24. positive regulation of apoptotic process Source: UniProtKB
  25. positive regulation of cytosolic calcium ion concentration Source: MGI
  26. positive regulation of muscle cell differentiation Source: Reactome
  27. positive regulation of oxidoreductase activity Source: BHF-UCL
  28. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  29. regulation of actin cytoskeleton reorganization Source: UniProtKB
  30. regulation of autophagy Source: UniProtKB
  31. regulation of cell adhesion Source: UniProtKB
  32. regulation of cell motility Source: UniProtKB
  33. regulation of endocytosis Source: UniProtKB
  34. regulation of response to DNA damage stimulus Source: UniProtKB
  35. regulation of transcription, DNA-templated Source: ProtInc
  36. response to oxidative stress Source: MGI
  37. signal transduction in response to DNA damage Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Autophagy, Cell adhesion, DNA damage, DNA repair, Endocytosis

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_21402. CDO in myogenesis.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP00519.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ABL1
Synonyms:ABL, JTK7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:76. ABL1.

Subcellular locationi

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).By similarity
Isoform IB : Nucleus membrane; Lipid-anchor
Note: The myristoylated c-ABL protein is reported to be nuclear.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cell leading edge Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: MGI
  5. membrane Source: UniProtKB-KW
  6. mitochondrion Source: ParkinsonsUK-UCL
  7. nucleolus Source: MGI
  8. nucleus Source: UniProtKB
  9. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

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).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi735 – 7351T → A: Abolishes phosphorylation. Loss of binding YWHAS and YWHAZ. Localizes to the nucleus. No effect on kinase activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MIMi608232. phenotype.
Orphaneti521. Chronic myeloid leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA24413.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11301130Tyrosine-protein kinase ABL1PRO_0000088050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501Phosphoserine3 Publications
Modified residuei70 – 701Phosphotyrosine; by autocatalysis2 Publications
Modified residuei115 – 1151Phosphotyrosine1 Publication
Modified residuei128 – 1281Phosphotyrosine1 Publication
Modified residuei139 – 1391Phosphotyrosine1 Publication
Modified residuei172 – 1721Phosphotyrosine1 Publication
Modified residuei185 – 1851Phosphotyrosine1 Publication
Modified residuei215 – 2151Phosphotyrosine1 Publication
Modified residuei226 – 2261Phosphotyrosine; by autocatalysis1 Publication
Modified residuei253 – 2531Phosphotyrosine
Modified residuei257 – 2571Phosphotyrosine
Modified residuei264 – 2641Phosphotyrosine
Modified residuei392 – 3921Phosphothreonine
Modified residuei393 – 3931Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases1 Publication
Modified residuei394 – 3941Phosphothreonine
Modified residuei446 – 4461PhosphoserineBy similarity
Modified residuei469 – 4691Phosphotyrosine
Modified residuei569 – 5691Phosphoserine5 Publications
Modified residuei613 – 6131Phosphothreonine
Modified residuei618 – 6181Phosphoserine; by PAK21 Publication
Modified residuei619 – 6191Phosphoserine; by PAK21 Publication
Modified residuei620 – 6201Phosphoserine
Modified residuei659 – 6591Phosphoserine1 Publication
Modified residuei683 – 6831Phosphoserine
Modified residuei711 – 7111N6-acetyllysine; by EP3001 Publication
Modified residuei718 – 7181Phosphoserine
Modified residuei735 – 7351Phosphothreonine1 Publication
Modified residuei781 – 7811Phosphothreonine
Modified residuei805 – 8051Phosphoserine
Modified residuei809 – 8091Phosphoserine
Modified residuei814 – 8141Phosphothreonine1 Publication
Modified residuei844 – 8441Phosphothreonine1 Publication
Modified residuei852 – 8521Phosphothreonine1 Publication
Modified residuei855 – 8551Phosphoserine
Modified residuei917 – 9171Phosphoserine1 Publication
Modified residuei919 – 9191Phosphoserine
Modified residuei936 – 9361Phosphoserine
Modified residuei949 – 9491Phosphoserine
Modified residuei977 – 9771Phosphoserine1 Publication

Post-translational modificationi

Acetylated at Lys-711 by EP300 which promotes the cytoplasmic translocation.1 Publication
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).By similarity
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation.1 Publication
Isoform IB is myristoylated on Gly-2.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00519.
PaxDbiP00519.
PRIDEiP00519.

PTM databases

PhosphoSiteiP00519.

Miscellaneous databases

PMAP-CutDBP00519.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP00519.
CleanExiHS_ABL1.
ExpressionAtlasiP00519. baseline and differential.
GenevestigatoriP00519.

Organism-specific databases

HPAiCAB002686.
HPA027251.
HPA027280.
HPA028409.

Interactioni

Subunit structurei

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. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases.By similarity23 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP011EBI-375543,EBI-375446
ABI2Q9NYB92EBI-375543,EBI-743598
ARP102752EBI-375543,EBI-608057
CDONQ4KMG02EBI-375543,EBI-7016840
CdonO351584EBI-375543,EBI-7016767From a different organism.
CRKP461082EBI-375543,EBI-886
CRKLP461092EBI-375543,EBI-910
CTNNB1P352222EBI-375543,EBI-491549
EGFRP005332EBI-375543,EBI-297353
ERBB2P046262EBI-375543,EBI-641062
FLNCQ143152EBI-375543,EBI-489954
ITGB2P051074EBI-375543,EBI-300173
KITP107212EBI-375543,EBI-1379503
LRRK1Q38SD23EBI-375543,EBI-1050422
MAP4K1Q929183EBI-375543,EBI-881
MAVSQ7Z4346EBI-375543,EBI-995373
MSH5O4319610EBI-375543,EBI-6092730
MUC1P159418EBI-375543,EBI-2804728
NCK1P163332EBI-375543,EBI-389883
PRICKLE3O439002EBI-375543,EBI-1751761
RAPGEF1Q139054EBI-375543,EBI-976876
RIMS1Q86UR52EBI-375543,EBI-1043236
RIN1Q136714EBI-375543,EBI-366017
SFNP319472EBI-375543,EBI-476295
SHBQ154645EBI-375543,EBI-4402156
SLC22A3O757512EBI-375543,EBI-1752674
SORBS1Q9BX662EBI-375543,EBI-433642
SORBS3O60504-25EBI-375543,EBI-1222956
SOS2Q078902EBI-375543,EBI-298181
SRCP129312EBI-375543,EBI-621482
TLN2Q9Y4G63EBI-375543,EBI-1220811
TOP1P113877EBI-375543,EBI-876302
VAV1P154985EBI-375543,EBI-625518
YWHAZP631042EBI-375543,EBI-347088

Protein-protein interaction databases

BioGridi106543. 139 interactions.
DIPiDIP-1042N.
IntActiP00519. 200 interactions.
MINTiMINT-7236141.
STRINGi9606.ENSP00000361423.

Structurei

Secondary structure

1
1130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi49 – 535
Helixi58 – 603
Beta strandi65 – 706
Beta strandi76 – 794
Beta strandi87 – 937
Beta strandi97 – 1048
Beta strandi107 – 1126
Helixi113 – 1153
Beta strandi116 – 1183
Helixi122 – 1243
Beta strandi128 – 1314
Helixi134 – 1407
Turni141 – 1433
Beta strandi148 – 1536
Beta strandi155 – 1573
Beta strandi161 – 1677
Beta strandi170 – 1789
Beta strandi180 – 1823
Beta strandi184 – 1874
Beta strandi192 – 1943
Helixi195 – 20410
Beta strandi209 – 2113
Beta strandi226 – 2283
Beta strandi229 – 2313
Turni233 – 2353
Helixi239 – 2413
Beta strandi242 – 2487
Helixi249 – 2513
Beta strandi254 – 2618
Helixi262 – 2643
Beta strandi266 – 2727
Beta strandi275 – 2784
Helixi280 – 29011
Beta strandi301 – 3055
Beta strandi307 – 3104
Beta strandi312 – 3165
Beta strandi319 – 3224
Helixi323 – 3297
Turni332 – 3343
Helixi337 – 35620
Beta strandi359 – 3613
Helixi366 – 3683
Beta strandi369 – 3713
Helixi373 – 3753
Beta strandi377 – 3793
Helixi381 – 3833
Helixi384 – 3874
Helixi390 – 3923
Beta strandi395 – 4017
Helixi403 – 4053
Helixi408 – 4136
Helixi418 – 43316
Helixi445 – 4473
Helixi448 – 4536
Helixi466 – 47510
Helixi480 – 4823
Helixi486 – 49914
Turni510 – 5123
Helixi1029 – 104517
Turni1046 – 10483
Helixi1053 – 107018
Helixi1071 – 10733
Helixi1080 – 109718
Beta strandi1101 – 11044
Beta strandi1106 – 11083
Helixi1115 – 112814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00519.
SMRiP00519. Positions 46-528, 1024-1130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12161SH3PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 21791SH2PROSITE-ProRule annotationAdd
BLAST
Domaini242 – 493252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060CAPAdd
BLAST
Regioni869 – 968100DNA-bindingBy similarityAdd
BLAST
Regioni953 – 1130178F-actin-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi381 – 40525Kinase activation loopAdd
BLAST
Motifi605 – 6095Nuclear localization signal 1Sequence Analysis
Motifi709 – 7157Nuclear localization signal 2Sequence Analysis
Motifi762 – 7698Nuclear localization signal 3Sequence Analysis
Motifi1090 – 110011Nuclear export signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 225Poly-Ser
Compositional biasi605 – 6095Poly-Lys
Compositional biasi782 – 1019238Pro-richAdd
BLAST
Compositional biasi897 – 9037Poly-Pro

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118938.
HOVERGENiHBG004162.
InParanoidiP00519.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG7GTT2V.
PhylomeDBiP00519.
TreeFamiTF105081.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR015015. 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]
PfamiPF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform IA (identifier: P00519-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS
60 70 80 90 100
KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC
110 120 130 140 150
EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL
160 170 180 190 200
VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH
210 220 230 240 250
HHSTVADGLI TTLHYPAPKR NKPTVYGVSP NYDKWEMERT DITMKHKLGG
260 270 280 290 300
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
310 320 330 340 350
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL LYMATQISSA
360 370 380 390 400
MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK
410 420 430 440 450
FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE
460 470 480 490 500
LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES
510 520 530 540 550
SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE HRDTTDVPEM
560 570 580 590 600
PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF
610 620 630 640 650
SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP
660 670 680 690 700
LDTADPAKSP KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT
710 720 730 740 750
GEEEGGGSSS KRFLRSCSAS CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS
760 770 780 790 800
TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV TPPPRLVKKN EEAADEVFKD
810 820 830 840 850
IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS ALGTPAAAEP
860 870 880 890 900
VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP
910 920 930 940 950
PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ
960 970 980 990 1000
PGEGLKKPVL PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST
1010 1020 1030 1040 1050
AFIPLISTRV SLRKTRQPPE RIASGAITKG VVLDSTEALC LAISRNSEQM
1060 1070 1080 1090 1100
ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC
1110 1120 1130
PATAGSGPAA TQDFSKLLSS VKEISDIVQR
Length:1,130
Mass (Da):122,873
Last modified:January 24, 2006 - v4
Checksum:i85FE6C1C0E483EA2
GO
Isoform IB (identifier: P00519-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,149
Mass (Da):124,955
Checksum:iDF9D4512F78FFE52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591G → S in AAA51561. (PubMed:3021337)Curated
Sequence conflicti424 – 4252AF → GK(PubMed:6191223)Curated
Sequence conflicti445 – 4451L → R in AAA51561. (PubMed:3021337)Curated
Sequence conflicti459 – 4591E → K in AAA51561. (PubMed:3021337)Curated
Sequence conflicti520 – 5201S → T in AAA51561. (PubMed:3021337)Curated
Sequence conflicti719 – 7191A → V in AAA51561. (PubMed:3021337)Curated
Sequence conflicti837 – 8371G → E in CAA34438. (PubMed:2687768)Curated
Sequence conflicti837 – 8371G → W in AAA51561. (PubMed:3021337)Curated
Sequence conflicti863 – 8631G → R in AAA51561. (PubMed:3021337)Curated
Sequence conflicti894 – 8941R → K in AAA51561. (PubMed:3021337)Curated
Sequence conflicti917 – 9193SPS → RPG in AAA51561. (PubMed:3021337)Curated
Sequence conflicti952 – 9521G → A in AAA51561. (PubMed:3021337)Curated
Sequence conflicti967 – 9682QS → HP in AAA51561. (PubMed:3021337)Curated
Sequence conflicti982 – 9821P → PL in AAA51561. (PubMed:3021337)Curated
Sequence conflicti1022 – 10221Missing in AAA51561. (PubMed:3021337)Curated
Sequence conflicti1045 – 10451R → G in AAA51561. (PubMed:3021337)Curated
Sequence conflicti1103 – 11031T → S in AAA51561. (PubMed:3021337)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471R → G in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_032676
Natural varianti140 – 1401L → P.1 Publication
Corresponds to variant rs1064152 [ dbSNP | Ensembl ].
VAR_051692
Natural varianti166 – 1661R → K in a melanoma sample; somatic mutation. 1 Publication
VAR_032677
Natural varianti247 – 2471K → R.
Corresponds to variant rs34549764 [ dbSNP | Ensembl ].
VAR_051693
Natural varianti706 – 7061G → V.2 Publications
Corresponds to variant rs34634745 [ dbSNP | Ensembl ].
VAR_025043
Natural varianti810 – 8101P → L.1 Publication
Corresponds to variant rs2229071 [ dbSNP | Ensembl ].
VAR_032678
Natural varianti852 – 8521T → P.1 Publication
VAR_025044
Natural varianti900 – 9001P → S.1 Publication
Corresponds to variant rs35266696 [ dbSNP | Ensembl ].
VAR_025045
Natural varianti968 – 9681S → P.
Corresponds to variant rs1064165 [ dbSNP | Ensembl ].
VAR_051694
Natural varianti972 – 9721S → L.2 Publications
Corresponds to variant rs2229067 [ dbSNP | Ensembl ].
VAR_025046

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKKESSRHGGPHCN VFVEH in isoform IB. 1 PublicationVSP_004957Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35165.1. [P00519-2]
CCDS35166.1. [P00519-1]
PIRiS08519. TVHUA.
RefSeqiNP_005148.2. NM_005157.5. [P00519-1]
NP_009297.2. NM_007313.2. [P00519-2]
UniGeneiHs.431048.

Genome annotation databases

EnsembliENST00000318560; ENSP00000323315; ENSG00000097007. [P00519-1]
ENST00000372348; ENSP00000361423; ENSG00000097007. [P00519-2]
GeneIDi25.
KEGGihsa:25.
UCSCiuc004bzv.3. human. [P00519-2]
uc004bzw.3. human. [P00519-1]

Polymorphism databases

DMDMi85681908.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
CGP resequencing studies
NIEHS-SNPs
Wikipedia

Abl entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35165.1. [P00519-2 ]
CCDS35166.1. [P00519-1 ]
PIRi S08519. TVHUA.
RefSeqi NP_005148.2. NM_005157.5. [P00519-1 ]
NP_009297.2. NM_007313.2. [P00519-2 ]
UniGenei Hs.431048.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AB2 NMR - A 120-220 [» ]
1ABL model - A 65-121 [» ]
1AWO NMR - A 65-119 [» ]
1BBZ X-ray 1.65 A/C/E/G 64-121 [» ]
1JU5 NMR - C 62-122 [» ]
1OPL X-ray 3.42 A/B 27-512 [» ]
1ZZP NMR - A 1007-1130 [» ]
2ABL X-ray 2.50 A 57-218 [» ]
2E2B X-ray 2.20 A/B 229-515 [» ]
2F4J X-ray 1.91 A 229-513 [» ]
2FO0 X-ray 2.27 A 38-512 [» ]
2G1T X-ray 1.80 A/B/C/D 229-512 [» ]
2G2F X-ray 2.70 A/B 229-512 [» ]
2G2H X-ray 2.00 A/B 229-512 [» ]
2G2I X-ray 3.12 A/B 229-512 [» ]
2GQG X-ray 2.40 A/B 229-500 [» ]
2HIW X-ray 2.20 A/B 230-512 [» ]
2HYY X-ray 2.40 A/B/C/D 228-500 [» ]
2HZ0 X-ray 2.10 A/B 228-497 [» ]
2HZ4 X-ray 2.80 A/B/C 228-500 [» ]
2HZI X-ray 1.70 A/B 229-500 [» ]
2O88 X-ray 1.75 A/B 64-121 [» ]
2V7A X-ray 2.50 A/B 229-512 [» ]
3CS9 X-ray 2.21 A/B/C/D 229-500 [» ]
3EG0 X-ray 2.30 A 60-121 [» ]
3EG1 X-ray 1.85 A/B 60-121 [» ]
3EG2 X-ray 1.80 A 60-121 [» ]
3EG3 X-ray 1.40 A 60-121 [» ]
3EGU X-ray 2.25 A 60-121 [» ]
3K2M X-ray 1.75 A/B 121-232 [» ]
3PYY X-ray 1.85 A/B 229-512 [» ]
3QRI X-ray 2.10 A/B 229-499 [» ]
3QRJ X-ray 1.82 A/B 229-499 [» ]
3QRK X-ray 2.30 A 229-499 [» ]
3T04 X-ray 2.10 A 112-232 [» ]
3UE4 X-ray 2.42 A/B 229-512 [» ]
3UYO X-ray 1.83 A 112-232 [» ]
4J9B X-ray 1.70 A 60-121 [» ]
4J9C X-ray 1.05 A 60-121 [» ]
4J9D X-ray 1.50 A/C/E 60-121 [» ]
4J9E X-ray 1.40 A/C/E 60-121 [» ]
4J9F X-ray 1.09 A/C/E 60-121 [» ]
4J9G X-ray 1.80 A/C/E 60-121 [» ]
4J9H X-ray 1.70 A/B/C/D/E/F 60-121 [» ]
4J9I X-ray 2.20 A/C/E 60-121 [» ]
4JJB X-ray 1.65 A 60-121 [» ]
4JJC X-ray 1.60 A 60-121 [» ]
4JJD X-ray 1.60 A 60-121 [» ]
ProteinModelPortali P00519.
SMRi P00519. Positions 46-528, 1024-1130.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106543. 139 interactions.
DIPi DIP-1042N.
IntActi P00519. 200 interactions.
MINTi MINT-7236141.
STRINGi 9606.ENSP00000361423.

Chemistry

BindingDBi P00519.
ChEMBLi CHEMBL2111414.
DrugBanki DB00171. Adenosine triphosphate.
DB06616. Bosutinib.
DB01254. Dasatinib.
DB00619. Imatinib.
DB04868. Nilotinib.
DB08901. Ponatinib.
DB08896. Regorafenib.
GuidetoPHARMACOLOGYi 1923.

PTM databases

PhosphoSitei P00519.

Polymorphism databases

DMDMi 85681908.

Proteomic databases

MaxQBi P00519.
PaxDbi P00519.
PRIDEi P00519.

Protocols and materials databases

DNASUi 25.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318560 ; ENSP00000323315 ; ENSG00000097007 . [P00519-1 ]
ENST00000372348 ; ENSP00000361423 ; ENSG00000097007 . [P00519-2 ]
GeneIDi 25.
KEGGi hsa:25.
UCSCi uc004bzv.3. human. [P00519-2 ]
uc004bzw.3. human. [P00519-1 ]

Organism-specific databases

CTDi 25.
GeneCardsi GC09P133589.
HGNCi HGNC:76. ABL1.
HPAi CAB002686.
HPA027251.
HPA027280.
HPA028409.
MIMi 189980. gene.
608232. phenotype.
neXtProti NX_P00519.
Orphaneti 521. Chronic myeloid leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBi PA24413.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOVERGENi HBG004162.
InParanoidi P00519.
KOi K06619.
OMAi GAFRESG.
OrthoDBi EOG7GTT2V.
PhylomeDBi P00519.
TreeFami TF105081.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19230. Role of Abl in Robo-Slit signaling.
REACT_21402. CDO in myogenesis.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinki P00519.

Miscellaneous databases

ChiTaRSi ABL1. human.
EvolutionaryTracei P00519.
GeneWikii ABL_(gene).
GenomeRNAii 25.
NextBioi 79.
PMAP-CutDB P00519.
PROi P00519.
SOURCEi Search...

Gene expression databases

Bgeei P00519.
CleanExi HS_ABL1.
ExpressionAtlasi P00519. baseline and differential.
Genevestigatori P00519.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR015015. 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 ]
Pfami PF08919. F_actin_bind. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00808. FABD. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  51. "Unc119 protects from Shigella infection by inhibiting the Abl family kinases."
    Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.
    PLoS ONE 4:E5211-E5211(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH UNC119; ABL2 AND CRK.
  52. "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.
  53. "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.
  54. "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.
  55. "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.
  56. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  57. "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.
  58. "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.
  59. "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.
  60. Cited for: 3D-STRUCTURE MODELING OF SH3 DOMAIN.
  61. "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.
  62. "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.
  63. "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.
  64. Cited for: X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 27-512, MYRISTOYLATION (ISOFORM IB), ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
  65. "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.
  66. "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.
  67. "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.
  68. "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.
  69. "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.
  70. "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.
  71. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 121-232 IN COMPLEX WITH ANTIBODY MIMIC HA4, FUNCTION, CATALYTIC ACTIVITY.
  72. "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.
    , 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.

Entry informationi

Entry nameiABL1_HUMAN
AccessioniPrimary (citable) accession number: P00519
Secondary accession number(s): A3KFJ3
, Q13869, Q13870, Q16133, Q17R61, Q45F09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 24, 2006
Last modified: October 29, 2014
This is version 207 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3