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P00520

- ABL1_MOUSE

UniProt

P00520 - ABL1_MOUSE

Protein

Tyrosine-protein kinase ABL1

Gene

Abl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 191 (01 Oct 2014)
      Sequence version 3 (15 Feb 2005)
      Previous versions | rss
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    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

    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 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. ATP binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. kinase activity Source: MGI
    4. magnesium ion binding Source: UniProtKB
    5. manganese ion binding Source: UniProtKB
    6. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    7. proline-rich region binding Source: UniProtKB
    8. protein binding Source: IntAct
    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. apoptotic process Source: UniProtKB-KW
    3. autophagy Source: UniProtKB-KW
    4. cell adhesion Source: UniProtKB-KW
    5. cellular response to DNA damage stimulus Source: UniProtKB
    6. DNA damage induced protein phosphorylation Source: Ensembl
    7. DNA repair Source: UniProtKB-KW
    8. endocytosis Source: UniProtKB-KW
    9. negative regulation of protein serine/threonine kinase activity Source: Ensembl
    10. peptidyl-tyrosine phosphorylation Source: UniProtKB
    11. platelet-derived growth factor receptor signaling pathway Source: MGI
    12. positive regulation of apoptotic process Source: Ensembl
    13. positive regulation of oxidoreductase activity Source: Ensembl
    14. positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    15. regulation of cell cycle Source: MGI
    16. regulation of response to DNA damage stimulus Source: Ensembl
    17. signal transduction in response to DNA damage Source: UniProtKB

    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.

    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. cell leading edge Source: MGI
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: MGI
    5. mitochondrion Source: UniProtKB-SubCell
    6. nucleolus Source: Ensembl
    7. nucleus Source: UniProtKB
    8. perinuclear region of cytoplasm Source: Ensembl

    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

    PaxDbiP00520.
    PRIDEiP00520.

    PTM databases

    PhosphoSiteiP00520.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    ArrayExpressiP00520.
    BgeeiP00520.
    CleanExiMM_ABL1.
    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 – 706
    Beta strandi76 – 794
    Beta strandi87 – 937
    Beta strandi97 – 1037
    Beta strandi108 – 1125
    Helixi113 – 1153
    Beta strandi116 – 1216
    Helixi122 – 1243
    Beta strandi128 – 1314
    Helixi134 – 1407
    Helixi141 – 1433
    Beta strandi148 – 1536
    Beta strandi155 – 1573
    Beta strandi161 – 1677
    Beta strandi170 – 1756
    Beta strandi184 – 1874
    Beta strandi192 – 1943
    Helixi195 – 2028
    Beta strandi209 – 2113
    Beta strandi226 – 2283
    Beta strandi230 – 2334
    Helixi239 – 2413
    Beta strandi242 – 2487
    Helixi249 – 2513
    Beta strandi255 – 2617
    Helixi262 – 2643
    Beta strandi266 – 2738
    Beta strandi275 – 2784
    Helixi280 – 29213
    Beta strandi301 – 3055
    Beta strandi307 – 31610
    Helixi323 – 3297
    Turni332 – 3343
    Helixi337 – 35721
    Beta strandi359 – 3624
    Helixi366 – 3683
    Beta strandi369 – 3713
    Helixi373 – 3753
    Beta strandi377 – 3793
    Helixi384 – 3863
    Beta strandi390 – 3967
    Beta strandi399 – 4013
    Helixi403 – 4053
    Helixi408 – 4136
    Helixi418 – 43316
    Beta strandi439 – 4424
    Helixi445 – 4473
    Helixi448 – 4536
    Helixi466 – 47510
    Helixi480 – 4823
    Helixi486 – 50924

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00640000091347.
    HOVERGENiHBG004162.
    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

    MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS     50
    KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC 100
    EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL 150
    VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH 200
    HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT DITMKHKLGG 250
    GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ 300
    LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA 350
    MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK 400
    FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE 450
    LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES 500
    SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE QKDAPDTPEL 550
    LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF 600
    SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS 650
    DAAEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA 700
    EEESGMSSSK RFLRSCSASC MPHGARDTEW RSVTLPRDLP SAGKQFDSST 750
    FGGHKSEKPA LPRKRTSESR SEQVAKSTAM PPPRLVKKNE EAAEEGFKDT 800
    ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS GMGTPATAEP 850
    APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT 900
    GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP 950
    VPPSVPKPQS TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS 1000
    TRVSLRKTRQ PPERIASGTI TKGVVLDSTE ALCLAISRNS EQMASHSAVL 1050
    EAGKNLYTFC VSYVDSIQQM RNKFAFREAI NKLESNLREL QICPATASSG 1100
    PAATQDFSKL LSSVKEISDI VRR 1123
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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 ENSGT00640000091347.
    HOVERGENi HBG004162.
    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.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P00520.
    Bgeei P00520.
    CleanExi MM_ABL1.
    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

    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: October 1, 2014
    This is version 191 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

    Dasty 3