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P00520

- ABL1_MOUSE

UniProt

P00520 - ABL1_MOUSE

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Protein

Tyrosine-protein kinase ABL1

Gene

Abl1

Organism
Mus musculus (Mouse)
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-191' 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.11 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.3 PublicationsPROSITE-ProRule annotation

Cofactori

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 (By similarity). Activated by RIN1 binding to the SH2 and SH3 domains. Also stimulated by cell death inducers and DNA-damage (By similarity). Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant phosphoinositide known to regulate cytoskeletal and membrane proteins, inhibits also the tyrosine kinase activity. Inhibited by imatinib mesylate (Gleevec).By similarity6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei271 – 2711ATPPROSITE-ProRule annotation
Active sitei363 – 3631Proton acceptorPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. actin filament binding Source: MGI
  2. ATP binding Source: UniProtKB
  3. DNA binding Source: UniProtKB-KW
  4. kinase activity Source: MGI
  5. magnesium ion binding Source: UniProtKB
  6. manganese ion binding Source: UniProtKB
  7. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  8. proline-rich region binding Source: UniProtKB
  9. protein domain specific binding Source: MGI
  10. protein kinase activity Source: MGI
  11. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: UniProtKB
  2. actin filament branching Source: MGI
  3. activated T cell proliferation Source: MGI
  4. alpha-beta T cell differentiation Source: MGI
  5. apoptotic process Source: UniProtKB-KW
  6. autophagy Source: UniProtKB-KW
  7. B-1 B cell homeostasis Source: MGI
  8. B cell proliferation Source: MGI
  9. B cell proliferation involved in immune response Source: MGI
  10. B cell receptor signaling pathway Source: MGI
  11. Bergmann glial cell differentiation Source: MGI
  12. cellular response to DNA damage stimulus Source: UniProtKB
  13. cellular response to lipopolysaccharide Source: MGI
  14. cerebellum morphogenesis Source: MGI
  15. collateral sprouting Source: MGI
  16. DNA damage induced protein phosphorylation Source: Ensembl
  17. DNA repair Source: UniProtKB-KW
  18. epidermal growth factor receptor signaling pathway Source: MGI
  19. microspike assembly Source: MGI
  20. negative regulation of BMP signaling pathway Source: MGI
  21. negative regulation of cell-cell adhesion Source: MGI
  22. negative regulation of cellular senescence Source: MGI
  23. negative regulation of endothelial cell apoptotic process Source: MGI
  24. negative regulation of ERK1 and ERK2 cascade Source: MGI
  25. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  26. negative regulation of mitotic cell cycle Source: MGI
  27. negative regulation of protein serine/threonine kinase activity Source: Ensembl
  28. neuromuscular process controlling balance Source: MGI
  29. peptidyl-tyrosine phosphorylation Source: UniProtKB
  30. phagocytosis Source: MGI
  31. platelet-derived growth factor receptor signaling pathway Source: MGI
  32. positive regulation of apoptotic process Source: MGI
  33. positive regulation of ERK1 and ERK2 cascade Source: MGI
  34. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  35. positive regulation of interferon-gamma secretion Source: MGI
  36. positive regulation of interleukin-2 secretion Source: MGI
  37. positive regulation of mitotic cell cycle Source: MGI
  38. positive regulation of neuron death Source: MGI
  39. positive regulation of osteoblast proliferation Source: MGI
  40. positive regulation of oxidoreductase activity Source: Ensembl
  41. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  42. positive regulation of release of sequestered calcium ion into cytosol Source: MGI
  43. positive regulation of Wnt signaling pathway, planar cell polarity pathway Source: MGI
  44. regulation of actin cytoskeleton organization Source: MGI
  45. regulation of cell cycle Source: MGI
  46. regulation of cellular senescence Source: MGI
  47. regulation of extracellular matrix organization Source: MGI
  48. regulation of response to DNA damage stimulus Source: Ensembl
  49. response to oxidative stress Source: MGI
  50. signal transduction in response to DNA damage Source: UniProtKB
  51. spleen development Source: MGI
  52. substrate adhesion-dependent cell spreading Source: MGI
  53. thymus development Source: MGI
  54. transitional one stage B cell differentiation Source: MGI
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. 3474.
ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_254504. Role of Abl in Robo-Slit signaling.
REACT_258600. CDO in myogenesis.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:87859. Abl1.

Subcellular locationi

Cytoplasmcytoskeleton. Nucleus. Mitochondrion
Note: The myristoylated c-ABL protein is reported to be nuclear. Sequestered into the cytoplasm through interaction with 14-3-3 proteins (By similarity). Localizes to mitochondria in response to oxidative stress.By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutants are born with the expected Mendelian frequency, but fail to thrive and most die within three weeks after birth. Most mutants are runted, and have atrophied thymuses with severe thymocyte deficiency. Mutants that survive to weaning age are most often runted, and about half of them show lymphopenia. They display a major reduction in the number of pre-B and immature B-cell classes in bone marrow with a wide variation between individuals, but essentially normal mature B-cell levels. Mutants are highly susceptible to infections.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121P → S: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi128 – 1281Y → D: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi139 – 1391Y → C: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi226 – 2261Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication
Mutagenesisi229 – 2291S → P: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi271 – 2711K → M: Loss of kinase activity. 1 Publication
Mutagenesisi315 – 3151T → I: Loss of inhibition by imatinib. Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi393 – 3931Y → F: Minimal reduction in ability to autophosphorylate. 1 Publication
Mutagenesisi446 – 4461S → A: No effect on basal activity, but abolishes ionizing radiation-induced activation. 1 Publication
Mutagenesisi464 – 4641C → Y: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi465 – 4651P → S: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi497 – 4971F → L: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi505 – 5051E → K: Loss of inhibition by GNF-2. 1 Publication
Mutagenesisi506 – 5061V → L: Strongly reduced inhibition by GNF-2. 1 Publication
Mutagenesisi1083 – 10831L → A: Loss of nuclear export.

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11231123Tyrosine-protein kinase ABL1PRO_0000088051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei70 – 701Phosphotyrosine; by autocatalysisBy similarity
Modified residuei185 – 1851PhosphotyrosineBy similarity
Modified residuei226 – 2261Phosphotyrosine; by autocatalysis1 Publication
Modified residuei253 – 2531PhosphotyrosineBy similarity
Modified residuei257 – 2571PhosphotyrosineBy similarity
Modified residuei264 – 2641PhosphotyrosineBy similarity
Modified residuei392 – 3921PhosphothreonineBy similarity
Modified residuei393 – 3931Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases2 Publications
Modified residuei394 – 3941PhosphothreonineBy similarity
Modified residuei446 – 4461Phosphoserine1 Publication
Modified residuei469 – 4691PhosphotyrosineBy similarity
Modified residuei547 – 5471Phosphothreonine1 Publication
Modified residuei569 – 5691Phosphoserine1 Publication
Modified residuei613 – 6131PhosphothreonineBy similarity
Modified residuei618 – 6181Phosphoserine; by PAK2By similarity
Modified residuei619 – 6191Phosphoserine; by PAK2By similarity
Modified residuei620 – 6201PhosphoserineBy similarity
Modified residuei658 – 6581PhosphoserineBy similarity
Modified residuei682 – 6821PhosphoserineBy similarity
Modified residuei710 – 7101N6-acetyllysine; by EP300By similarity
Modified residuei717 – 7171PhosphoserineBy similarity
Modified residuei734 – 7341PhosphothreonineBy similarity
Modified residuei803 – 8031PhosphoserineBy similarity
Modified residuei807 – 8071PhosphoserineBy similarity
Modified residuei812 – 8121PhosphothreonineBy similarity
Modified residuei844 – 8441PhosphothreonineBy similarity
Modified residuei909 – 9091PhosphoserineBy similarity
Modified residuei911 – 9111PhosphoserineBy similarity
Modified residuei927 – 9271PhosphoserineBy similarity
Modified residuei970 – 9701PhosphoserineBy similarity

Post-translational modificationi

Acetylated at Lys-710 by EP300 which promotes the cytoplasmic translocation.By similarity
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 (By similarity). Phosphorylation at Tyr-226 and Tyr-393 correlate with increased activity (By similarity). DNA damage-induced activation of ABL1 requires the function of ATM and Ser-446 phosphorylation. Phosphorylation at Thr-547 and Ser-569 has been attributed to a CDC2-associated kinase and is coupled to cell division. Phosphorylation at Ser-618 and Ser-619 by PAK2 increases binding to CRK and reduces binding to ABI1 (By similarity). Phosphorylation on Thr-734 is required for binding 14-3-3 proteins for cytoplasmic translocation (By similarity). Phosphorylated by PDGFRB and PRKDC.By similarity7 Publications
Polyubiquitinated. Polyubiquitination of ABL1 leads to degradation (By similarity).By similarity
Isoform IV is myristoylated on Gly-2.

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP00520.
PaxDbiP00520.
PRIDEiP00520.

PTM databases

PhosphoSiteiP00520.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiP00520.
CleanExiMM_ABL1.
ExpressionAtlasiP00520. baseline and differential.
GenevestigatoriP00520.

Interactioni

Subunit structurei

Interacts with INPPL1/SHIP2. Interacts with SORBS1 following insulin stimulation. Found in a trimolecular complex containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16. 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-734 and sequesters ABL1 into the cytoplasm. 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 (By similarity). Interacts with ABI1, ABI2, BCR, CRK, FYN, 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 with STX17; probably phosphorylates STX17 (By similarity). Interacts with ITGB1, HCK and FGR. Found in a complex with ABL1, ABL2, CRK and UNC119; leading to the inhibition of CRK phosphorylation by ABL kinases (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI1Q8IZP0-45EBI-8593082,EBI-8593095From a different organism.
CDKN1BP465272EBI-914519,EBI-519280From a different organism.
CdonQ32MD92EBI-914519,EBI-7017034
Dok1P974654EBI-914519,EBI-914917
EPHB2P28693-25EBI-914519,EBI-6725926From a different organism.
Nck1Q99M512EBI-914519,EBI-642202
Pstpip1P978145EBI-914519,EBI-7484574
Ptpn18P706022EBI-914519,EBI-7484661From a different organism.

Protein-protein interaction databases

BioGridi197906. 19 interactions.
IntActiP00520. 20 interactions.
MINTiMINT-85127.

Structurei

Secondary structure

1
1123
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi65 – 706Combined sources
Beta strandi76 – 794Combined sources
Beta strandi87 – 937Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi108 – 1125Combined sources
Helixi113 – 1153Combined sources
Beta strandi116 – 1216Combined sources
Helixi122 – 1243Combined sources
Beta strandi128 – 1314Combined sources
Helixi134 – 1407Combined sources
Helixi141 – 1433Combined sources
Beta strandi148 – 1536Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi170 – 1756Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 2028Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi230 – 2334Combined sources
Helixi239 – 2413Combined sources
Beta strandi242 – 2487Combined sources
Helixi249 – 2513Combined sources
Beta strandi255 – 2617Combined sources
Helixi262 – 2643Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi275 – 2784Combined sources
Helixi280 – 29213Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi307 – 31610Combined sources
Helixi323 – 3297Combined sources
Turni332 – 3343Combined sources
Helixi337 – 35721Combined sources
Beta strandi359 – 3624Combined sources
Helixi366 – 3683Combined sources
Beta strandi369 – 3713Combined sources
Helixi373 – 3753Combined sources
Beta strandi377 – 3793Combined sources
Helixi384 – 3863Combined sources
Beta strandi390 – 3967Combined sources
Beta strandi399 – 4013Combined sources
Helixi403 – 4053Combined sources
Helixi408 – 4136Combined sources
Helixi418 – 43316Combined sources
Beta strandi439 – 4424Combined sources
Helixi445 – 4473Combined sources
Helixi448 – 4536Combined sources
Helixi466 – 47510Combined sources
Helixi480 – 4823Combined sources
Helixi486 – 50924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ABOX-ray2.00A/B61-121[»]
1ABQX-ray2.80A61-121[»]
1FPUX-ray2.40A/B229-515[»]
1IEPX-ray2.10A/B229-515[»]
1M52X-ray2.60A/B229-515[»]
1OPJX-ray1.75A/B229-515[»]
1OPKX-ray1.80A27-515[»]
2HZNX-ray2.70A229-515[»]
2QOHX-ray1.95A/B229-515[»]
2Z60X-ray1.95A229-515[»]
3DK3X-ray2.02A/B233-514[»]
3DK6X-ray2.02A/B233-514[»]
3DK7X-ray2.01A/B233-505[»]
3IK3X-ray1.90A/B229-513[»]
3K5VX-ray1.74A/B229-515[»]
3KF4X-ray1.90A/B229-515[»]
3KFAX-ray1.22A/B229-515[»]
3MS9X-ray1.80A/B229-515[»]
3MSSX-ray1.95A/B/C/D229-515[»]
3OXZX-ray2.20A229-511[»]
3OY3X-ray1.95A/B229-511[»]
ProteinModelPortaliP00520.
SMRiP00520. Positions 46-511, 1017-1123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00520.

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
Regioni863 – 96199DNA-bindingAdd
BLAST
Regioni945 – 1123179F-actin-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi381 – 40525Kinase activation loopAdd
BLAST
Motifi605 – 6095Nuclear localization signal 1Sequence Analysis
Motifi708 – 7147Nuclear localization signal 2Sequence Analysis
Motifi761 – 7688Nuclear localization signal 3Sequence Analysis
Motifi1083 – 109311Nuclear export signalAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 225Poly-Ser
Compositional biasi605 – 6095Poly-Lys
Compositional biasi804 – 1012209Pro-richAdd
BLAST
Compositional biasi891 – 8977Poly-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.
InParanoidiP00520.
KOiK06619.
OMAiGAFRESG.
OrthoDBiEOG7GTT2V.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform I (identifier: P00520-1) [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 NKPTIYGVSP NYDKWEMERT DITMKHKLGG
260 270 280 290 300
GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
310 320 330 340 350
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL 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 GKRGTRGGAG SMLQAPELPT KTRTCRRAAE QKDAPDTPEL
560 570 580 590 600
LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
610 620 630 640 650
SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS
660 670 680 690 700
DAAEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA
710 720 730 740 750
EEESGMSSSK RFLRSCSASC MPHGARDTEW RSVTLPRDLP SAGKQFDSST
760 770 780 790 800
FGGHKSEKPA LPRKRTSESR SEQVAKSTAM PPPRLVKKNE EAAEEGFKDT
810 820 830 840 850
ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS GMGTPATAEP
860 870 880 890 900
APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
910 920 930 940 950
GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP
960 970 980 990 1000
VPPSVPKPQS TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS
1010 1020 1030 1040 1050
TRVSLRKTRQ PPERIASGTI TKGVVLDSTE ALCLAISRNS EQMASHSAVL
1060 1070 1080 1090 1100
EAGKNLYTFC VSYVDSIQQM RNKFAFREAI NKLESNLREL QICPATASSG
1110 1120
PAATQDFSKL LSSVKEISDI VRR
Length:1,123
Mass (Da):122,673
Last modified:February 15, 2005 - v3
Checksum:iBD48ADE8557AE95C
GO
Isoform II (identifier: P00520-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MISFDLLSDELHLKLLVLDV

Show »
Length:1,117
Mass (Da):122,179
Checksum:i002F9D346307028A
GO
Isoform III (identifier: P00520-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MSQRWTYTKCRVQRDPALPFM

Show »
Length:1,118
Mass (Da):122,480
Checksum:iAB3B4510AE8C5C38
GO
Isoform IV (identifier: P00520-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MLEICLKLVGCKSKKGLSSSSSCYLE → MGQQPGKVLGDQRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH

Show »
Length:1,142
Mass (Da):124,769
Checksum:i7A9DB9E772EAF05F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1874LYVS → VGDW in AAB60451. (PubMed:7665185)Curated
Sequence conflicti184 – 1874LYVS → VGDW in AAB60450. (PubMed:7665185)Curated
Sequence conflicti782 – 7865PPRLV → LPGWL in AAA88241. (PubMed:3317402)Curated
Sequence conflicti987 – 9871D → G in BAC41088. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MLEIC…SCYLE → MISFDLLSDELHLKLLVLDV in isoform II. CuratedVSP_004959Add
BLAST
Alternative sequencei1 – 2626MLEIC…SCYLE → MSQRWTYTKCRVQRDPALPF M in isoform III. CuratedVSP_004958Add
BLAST
Alternative sequencei1 – 2626MLEIC…SCYLE → MGQQPGKVLGDQRRPSLPAL HFIKGAGKRDSSRHGGPHCN VFVEH in isoform IV. 1 PublicationVSP_004960Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02995 mRNA. Translation: AAA88241.1.
AK090095 mRNA. Translation: BAC41088.1.
BC059260 mRNA. Translation: AAH59260.1.
U14721, U14720 Genomic DNA. Translation: AAB60451.1.
U14721, U14720 Genomic DNA. Translation: AAB60450.1.
U14721, U13835 Genomic DNA. Translation: AAB60448.1.
U14721, U13835 Genomic DNA. Translation: AAB60449.1.
X07539 Genomic DNA. Translation: CAA30411.1.
X07539 Genomic DNA. Translation: CAA30412.1.
X07540 Genomic DNA. Translation: CAA30413.1.
X07541 Genomic DNA. Translation: CAA30414.1.
M12263 mRNA. Translation: AAA37136.1.
M12264 mRNA. Translation: AAA37137.1.
M12265 mRNA. Translation: AAA37138.1.
M12266 Genomic DNA. Translation: AAA37134.1.
K03228 mRNA. Translation: AAA37135.1.
CCDSiCCDS15901.1. [P00520-1]
CCDS50563.1. [P00520-4]
PIRiA39962.
S00774.
RefSeqiNP_001106174.1. NM_001112703.2. [P00520-4]
NP_001269974.1. NM_001283045.1. [P00520-3]
NP_001269975.1. NM_001283046.1. [P00520-2]
NP_033724.2. NM_009594.4. [P00520-1]
UniGeneiMm.1318.

Genome annotation databases

EnsembliENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842. [P00520-1]
ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842. [P00520-4]
GeneIDi11350.
KEGGimmu:11350.
UCSCiuc008jdz.2. mouse. [P00520-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02995 mRNA. Translation: AAA88241.1 .
AK090095 mRNA. Translation: BAC41088.1 .
BC059260 mRNA. Translation: AAH59260.1 .
U14721 , U14720 Genomic DNA. Translation: AAB60451.1 .
U14721 , U14720 Genomic DNA. Translation: AAB60450.1 .
U14721 , U13835 Genomic DNA. Translation: AAB60448.1 .
U14721 , U13835 Genomic DNA. Translation: AAB60449.1 .
X07539 Genomic DNA. Translation: CAA30411.1 .
X07539 Genomic DNA. Translation: CAA30412.1 .
X07540 Genomic DNA. Translation: CAA30413.1 .
X07541 Genomic DNA. Translation: CAA30414.1 .
M12263 mRNA. Translation: AAA37136.1 .
M12264 mRNA. Translation: AAA37137.1 .
M12265 mRNA. Translation: AAA37138.1 .
M12266 Genomic DNA. Translation: AAA37134.1 .
K03228 mRNA. Translation: AAA37135.1 .
CCDSi CCDS15901.1. [P00520-1 ]
CCDS50563.1. [P00520-4 ]
PIRi A39962.
S00774.
RefSeqi NP_001106174.1. NM_001112703.2. [P00520-4 ]
NP_001269974.1. NM_001283045.1. [P00520-3 ]
NP_001269975.1. NM_001283046.1. [P00520-2 ]
NP_033724.2. NM_009594.4. [P00520-1 ]
UniGenei Mm.1318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ABO X-ray 2.00 A/B 61-121 [» ]
1ABQ X-ray 2.80 A 61-121 [» ]
1FPU X-ray 2.40 A/B 229-515 [» ]
1IEP X-ray 2.10 A/B 229-515 [» ]
1M52 X-ray 2.60 A/B 229-515 [» ]
1OPJ X-ray 1.75 A/B 229-515 [» ]
1OPK X-ray 1.80 A 27-515 [» ]
2HZN X-ray 2.70 A 229-515 [» ]
2QOH X-ray 1.95 A/B 229-515 [» ]
2Z60 X-ray 1.95 A 229-515 [» ]
3DK3 X-ray 2.02 A/B 233-514 [» ]
3DK6 X-ray 2.02 A/B 233-514 [» ]
3DK7 X-ray 2.01 A/B 233-505 [» ]
3IK3 X-ray 1.90 A/B 229-513 [» ]
3K5V X-ray 1.74 A/B 229-515 [» ]
3KF4 X-ray 1.90 A/B 229-515 [» ]
3KFA X-ray 1.22 A/B 229-515 [» ]
3MS9 X-ray 1.80 A/B 229-515 [» ]
3MSS X-ray 1.95 A/B/C/D 229-515 [» ]
3OXZ X-ray 2.20 A 229-511 [» ]
3OY3 X-ray 1.95 A/B 229-511 [» ]
ProteinModelPortali P00520.
SMRi P00520. Positions 46-511, 1017-1123.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197906. 19 interactions.
IntActi P00520. 20 interactions.
MINTi MINT-85127.

Chemistry

BindingDBi P00520.
ChEMBLi CHEMBL3099.

PTM databases

PhosphoSitei P00520.

Proteomic databases

MaxQBi P00520.
PaxDbi P00520.
PRIDEi P00520.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028190 ; ENSMUSP00000028190 ; ENSMUSG00000026842 . [P00520-1 ]
ENSMUST00000075759 ; ENSMUSP00000075167 ; ENSMUSG00000026842 . [P00520-4 ]
GeneIDi 11350.
KEGGi mmu:11350.
UCSCi uc008jdz.2. mouse. [P00520-1 ]

Organism-specific databases

CTDi 25.
MGIi MGI:87859. Abl1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118938.
HOVERGENi HBG004162.
InParanoidi P00520.
KOi K06619.
OMAi GAFRESG.
OrthoDBi EOG7GTT2V.
TreeFami TF105081.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 3474.
Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_254504. Role of Abl in Robo-Slit signaling.
REACT_258600. CDO in myogenesis.

Miscellaneous databases

EvolutionaryTracei P00520.
NextBioi 278620.
PROi P00520.
SOURCEi Search...

Gene expression databases

Bgeei P00520.
CleanExi MM_ABL1.
ExpressionAtlasi P00520. baseline and differential.
Genevestigatori P00520.

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. "Nucleotide sequence of testis-derived c-abl cDNAs: implications for testis-specific transcription and abl oncogene activation."
    Oppi C., Shore S.K., Reddy E.P.
    Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
    Strain: ICR.
    Tissue: Embryo.
  3. "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 IV).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "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] OF 1-187 (ISOFORMS I; II; III AND IV).
  5. "The mouse c-abl locus: molecular cloning and characterization."
    Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.
    Cell 36:349-356(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-182.
  6. "Four murine c-abl mRNAs arise by usage of two transcriptional promoters and alternative splicing."
    Bernards A., Paskind M., Baltimore D.
    Oncogene 2:297-304(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "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: PHOSPHORYLATION AT THR-547 AND SER-569.
  8. "Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene."
    Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C.
    Cell 65:1153-1163(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Mice homozygous for the ablm1 mutation show poor viability and depletion of selected B and T cell populations."
    Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T., Boast S., Harbison M.L., Robertson E.J., Goff S.P.
    Cell 65:1165-1175(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Cell cycle-regulated binding of c-Abl tyrosine kinase to DNA."
    Kipreos E.T., Wang J.Y.
    Science 256:382-385(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, DOMAIN, PHOSPHORYLATION.
  11. "c-Abl kinase regulates the protein binding activity of c-Crk."
    Feller S.M., Knudsen B., Hanafusa H.
    EMBO J. 13:2341-2351(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases."
    Mayer B.J., Hirai H., Sakai R.
    Curr. Biol. 5:296-305(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Functional interaction between DNA-PK and c-Abl in response to DNA damage."
    Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M., Weichselbaum R., Weaver D., Kufe D.
    Nature 386:732-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-446, MUTAGENESIS OF SER-446.
  14. Cited for: SUBCELLULAR LOCATION.
  15. "Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine phosphorylation, kinase upregulation, and neurite outgrowth."
    Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L., Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.
    Neuron 26:633-646(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, INTERACTION WITH CABLES1.
    Tissue: Brain.
  16. "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation."
    Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P.
    Mol. Cell 6:1413-1423(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSTPIP1.
  17. "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.
  18. "Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes."
    Kain K.H., Klemke R.L.
    J. Biol. Chem. 276:16185-16192(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRK, FUNCTION.
  19. "Targeting of the c-Abl tyrosine kinase to mitochondria in the necrotic cell death response to oxidative stress."
    Kumar S., Bharti A., Mishra N.C., Raina D., Kharbanda S., Saxena S., Kufe D.
    J. Biol. Chem. 276:17281-17285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. "The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene."
    Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T.
    J. Biol. Chem. 276:19787-19792(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-apoptotic activity."
    Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.
    J. Biol. Chem. 277:28870-28876(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZDHHC16.
  22. "Interaction between UV-damaged DNA binding activity proteins and the c-Abl tyrosine kinase."
    Cong F., Tang J., Hwang B.J., Vuong B.Q., Chu G., Goff S.P.
    J. Biol. Chem. 277:34870-34878(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "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.
  24. "Two distinct phosphorylation pathways have additive effects on Abl family kinase activation."
    Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.
    Mol. Cell. Biol. 23:3884-3896(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, PHOSPHORYLATION AT TYR-226 AND TYR-393, MUTAGENESIS OF TYR-226; LYS-271 AND TYR-393.
  25. "Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor."
    Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.
    Mol. Cell. Biol. 24:2573-2583(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION.
  26. "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.
  27. "c-Abl and Src-family kinases cross-talk in regulation of myeloid cell migration."
    Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G., Berton G.
    FEBS Lett. 584:15-21(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF CELL MIGRATION, PHOSPHORYLATION, INTERACTION WITH ITGB1; HCK AND FGR.
  28. "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.
  29. "High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides."
    Musacchio A., Saraste M., Wilmanns M.
    Nat. Struct. Biol. 1:546-551(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
  30. "Structural mechanism for STI-571 inhibition of Abelson tyrosine kinase."
    Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B., Kuriyan J.
    Science 289:1938-1942(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH INHIBITOR STI-571, CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-393, ACTIVATION LOOP.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION (ISOFORM IV), ENZYME REGULATION.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND MUTANT ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
  33. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, FUNCTION.
  34. "Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors sharing a common vinyl purine template."
    Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K., Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C.
    Chem. Biol. Drug Des. 75:18-28(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH INHIBITORS AP24283 AND AP24163.
  35. Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF PRO-112; TYR-128; TYR-139; SER-229; THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.

Entry informationi

Entry nameiABL1_MOUSE
AccessioniPrimary (citable) accession number: P00520
Secondary accession number(s): P97896
, Q61252, Q61253, Q61254, Q61255, Q61256, Q61257, Q61258, Q61259, Q61260, Q61261, Q6PCM5, Q8C1X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 15, 2005
Last modified: November 26, 2014
This is version 193 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

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