Relation Results

Summary

Name BCR-ABL
Primary ID SIGNOR-FP6
Type Fusion Protein
Formed by P00519, P11274
Description The hallmark genetic abnormality of CML is a t(9;22)(q34;q11) translocation, which was first discovered as an abnormal, small chromosome, named the Philadelphia chromosome. . The ABL gene from chromosome 9 joins to the BCR gene on chromosome 22, to form the BCR-ABL fusion gene. The Abl gene expresses a membrane-associated protein, a tyrosine kinase, and the BCR-Abl transcript is also translated into a tyrosine kinase. Since ABL activates a number of cell cycle-controlling proteins and enzymes, the result of the BCR-Abl fusion is to speed up cell division. Moreover, it inhibits DNA repair, causing genomic instability and potentially causing the feared blast crisis in CML. Finally, the BCR-ABL fusion gene is found in most patients with chronic myelogenous leukemia (CML), and in some patients with acute lymphoblastic leukemia (ALL) or acute myelogenous leukemia (AML).
Sequence
        10         20         30         40
MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA
        50         60         70         80
SIRRLEQEVN QERFRMIYLQ TLLAKEKKSY DRQRWGFRRA
        90        100        110        120
AQAPDGASEP RASASRPQPA PADGADPPPA EEPEARPDGE
       130        140        150        160
GSPGKARPGT ARRPGAAASG ERDDRGPPAS VAALRSNFER
       170        180        190        200
IRKGHGQPGA DAEKPFYVNV EFHHERGLVK VNDKEVSDRI
       210        220        230        240
SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC
       250        260        270        280
GVDGDYEDAE LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ
       290        300        310        320
SIYVGGMMEG EGKGPLLRSQ STSEQEKRLT WPRRSYSPRS
       330        340        350        360
FEDCGGGYTP DCSSNENLTS SEEDFSSGQS SRVSPSPTTY
       370        380        390        400
RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS
       410        420        430        440
EATIVGVRKT GQIWPNDGEG AFHGDADGSF GTPPGYGCAA
       450        460        470        480
DRAEEQRRHQ DGLPYIDDSP SSSPHRQLLK DSFMVELVEG
       490        500        510        520
ARKLRHVFLF TDLLLCTKLK KQSGGKTQQY DCKWYIPLTD
       530        540        550        560
LSFQMVDELE AVPNIPLVPD EELDALKIKI SQIKSDIQRE
       570        580        590        600
KRANKGSKAT ERLKKKLSEQ ESLLLLMSPS MAFRVHSRNG
       610        620        630        640
KSYTFLISSD YERAEWRENI REQQKKCFRS FSLTSVELQM
       650        660        670        680
LTNSCVKLQT VHSIPLTINK EDDESPGLYG FLNVIVHSAT
       690        700        710        720
GFKQSSKALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE
       730        740        750        760
NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC
       770        780        790        800
EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL
       810        820        830        840
LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS
       850        860        870        880
DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR
       890        900        910        920
NKPTVYGVSP NYDKWEMERT DITMKHKLGG GQYGEVYEGV
       930        940        950        960
WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
       970        980        990       1000
LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL
      1010       1020       1030       1040
LYMATQISSA MEYLEKKNFI HRDLAARNCL VGENHLVKVA
      1050       1060       1070       1080
DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS
      1090       1100       1110       1120
DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER
      1130       1140       1150       1160
PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES
      1170       1180       1190       1200
SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE
      1210       1220       1230       1240
HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP
      1250       1260       1270       1280
EGGLNEDERL LPKDKKTNLF SALIKKKKKT APTPPKRSSS
      1290       1300       1310       1320
FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP
      1330       1340       1350       1360
KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT
      1370       1380       1390       1400
GEEEGGGSSS KRFLRSCSAS CVPHGAKDTE WRSVTLPRDL
      1410       1420       1430       1440
QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV
      1450       1460       1470       1480
TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR
      1490       1500       1510       1520
QVTVAPASGL PHKEEAGKGS ALGTPAAAEP VTPTSKAGSG
      1530       1540       1550       1560
APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP
      1570       1580       1590       1600
PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA
      1610       1620       1630       1640
VNSDAAKPSQ PGEGLKKPVL PATPKPQSAK PSGTPISPAP
      1650       1660       1670       1680
VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE
      1690       1700       1710       1720
RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG
      1730       1740       1750       1760
KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC
      1770       1780       1790
PATAGSGPAA TQDFSKLLSS VKEISDIVQR
Relations 53
Pathways Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML

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0.20.20.20.20.20.20.20.20.20.20.20.20.20.20.80.80.20.20.80.20.80.80.20.20.20.80.20.2BCR-ABLJAK2RAD52GRB2LASP1HCKBCRCRKLUSP7RAD51RHOACTNNB1CSF2RBPTPN1MYCnilotinibponatinibCSF2RA/CSF2RBCaspase 3 complexbosutinibCASP3Bafetinibdasatinib (anhydrous)VAV1RUNX1PTENimatinib methanesulfonateNRASSTAT5A

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation JAK2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-255812 Tyr1007 VLPQDKEyYKVKEPG Mus musculus
pmid sentence
In this report, we show that Bcr–Abl forms a complex with Jak2, and induces tyrosine phosphorylation of Jak2; full phosphorylation requires the SH2 domain of Bcr–Abl. We found that Y1007 of Jak2 was phosphorylated in Bcr–Abl positive cells; phosphorylation of Jak2 Y1007 is known to be required for Jak2 kinase activation.
Publications: 1 Organism: Mus Musculus
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation RAD52 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262531 Tyr104 DLNNGKFyVGVCAFV Homo sapiens
pmid sentence
Have found that BCR-ABL1 interacts with the C-terminal portion of RAD52, resulting in tyrosine phosphorylation of Y104 located in RAD52 DNA II and enhanced nuclear foci formation
Publications: 1 Organism: Homo Sapiens
+ BCR-ABL img/unknown.png phosphorylation GRB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-247146 Tyr160 QVPQQPTyVQALFDF Homo sapiens HEK-293 Cell
pmid sentence
Our data show that BCR-ABL also phosphorylates Grb2 in Tyr160Previous reports suggested an inhibitory role of Grb2 Tyr7, Tyr37, Tyr52, and Tyr209 phosphorylation in receptor tyrosine kinase signaling (16) (43). Instead, in our system Grb2 Tyr160 mutation was not show to have a role in ALCL proliferation.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ BCR-ABL img/unknown.png phosphorylation LASP1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271703 Tyr171 IPTSAPVyQQPQQQP Homo sapiens K-562 Cell
pmid sentence
LASP1 is a novel BCR-ABL substrate and a phosphorylation-dependent binding partner of CRKL in chronic myeloid leukemia|We demonstrate that LASP1 is specifically phosphorylated by BCR-ABL at tyrosine-171 in CML patients
Publications: 1 Organism: Homo Sapiens
+ HCKup-regulates img/direct-activation.png phosphorylation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-53964 Tyr177 ADAEKPFyVNVEFHH Homo sapiens
pmid sentence
The src family kinase hck interacts with bcr-abl by a kinase-independent mechanism and phosphorylates the grb2-binding site of bcr
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLdown-regulates activity img/direct_inhibition.png phosphorylation BCR 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-40611 Tyr177 ADAEKPFyVNVEFHH Homo sapiens
pmid sentence
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrosine 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260829 Tyr328 YSPRSFEdCGGGYTP Homo sapiens
pmid sentence
Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr ± Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260828 Tyr360 YSPRSFEdCGGGYTP Homo sapiens
pmid sentence
Thus, we propose that the phosphorylation of tyrosine 328 and 360 within Bcr by Bcr-Abl will drastically interfere with Bcr's kinase role in either signal transduction or some other cellular mechanism.
Identifier Residue Sequence Organism Cell Line
SIGNOR-262530 Tyr360 VSPSPTTyRMFRDKS Chlorocebus aethiops
pmid sentence
These results indicate that tyrosine phosphorylation of Bcr by Bcr-Abl inhibits Bcr’s serine/threonine kinase activity.
Publications: 4 Organism: Homo Sapiens, Chlorocebus Aethiops
+ BCR-ABLup-regulates img/direct-activation.png phosphorylation CRKL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-46893 Tyr207 IPEPAHAyAQPQTTT Homo sapiens Leukemia Cell
pmid sentence
Tyrosine 207 in crkl is the bcr/abl phosphorylation sitephosphorylation of y207 provides a binding site for the crkl sh2 domain and potentially for other sh2-containing proteins.
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLdown-regulates img/direct_inhibition.png phosphorylation GRB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-112354 Tyr209 TGMFPRNyVTPVNRN Homo sapiens A-431 Cell
pmid sentence
Phosphorylation of grb2 by bcr/abl or egf receptor reduced its sh3-dependent binding to sos in vivo, but not its sh2-dependent binding to bcr/abl. Tyr209 within the c-terminal sh3 domain of grb2 was identified as one of the tyrosine phosphorylation sites
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ BCR-ABLdown-regulates activity img/direct_inhibition.png phosphorylation GRB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-246281 Tyr209 TGMFPRNyVTPVNRN Homo sapiens HEK-293 Cell
pmid sentence
More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.
Identifier Residue Sequence Organism Cell Line
SIGNOR-246289 Tyr37 EECDQNWyKAELNGK Homo sapiens
pmid sentence
More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.
Identifier Residue Sequence Organism Cell Line
SIGNOR-246293 Tyr52 DGFIPKNyIEMKPHP Homo sapiens HEK-293 Cell
pmid sentence
More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.
Identifier Residue Sequence Organism Cell Line
SIGNOR-246285 Tyr7 yDFKATAD Homo sapiens HEK-293 Cell
pmid sentence
More recently, however, tyrosine phosphorylation of Grb2 in BCR-ABL-transformed cells on residues Tyr7, Tyr37, Tyr52, and Tyr209 in the SH3 domains has been reported and shown to negatively regulate the Ras/MAPK pathway.
Publications: 4 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation USP7 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276532 Tyr243 NQLRKAVyMMPTEGD
pmid sentence
In this study, we show that BCR-ABL enhances HAUSP-induced de-ubiquitination of PTEN in turn favoring its nuclear exclusion. We further demonstrate that BCR-ABL physically interacts with and phosphorylates HAUSP on tyrosine residues to trigger its activity.|The HAUSP Y243F mutant showed significantly reduced BCR-ABL-induced HAUSP phosphorylation, which in turn was completely abrogated by imatinib treatment
Publications: 1
+ BCR-ABLdown-regulates img/direct_inhibition.png phosphorylation BCR 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-40615 Tyr283 YQPYQSIyVGGMMEG Homo sapiens Leukemia Cell
pmid sentence
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.
Identifier Residue Sequence Organism Cell Line
SIGNOR-40619 Tyr360 VSPSPTTyRMFRDKS Homo sapiens Leukemia Cell
pmid sentence
We have previously demonstrated that the bcr protein is tyrosine phosphorylated within first-exon sequences by the bcr-abl oncoprotein. Here we report that in addition to tyrose 177 (y-177), y-360 and y283 are phosphorylated in bcr-abl proteins in vitro. Tyrosine-phosphorylated bcr, phosphorylated in vitro by bcr-abl, was greatly inhibited in its serine/threonine kinase activity, impairing both auto- and transkinase activities of bcr.
Publications: 2 Organism: Homo Sapiens
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation RAD51 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271707 Tyr315 ETRICKIyDSPCLPE Homo sapiens 32D Cell
pmid sentence
RAD51 is one of six mitotic human homologs of the E. coli RecA protein (RAD51-Paralogs) that play a central role in homologous recombination and repair of DNA double-strand breaks (DSBs).|Phosphorylation of the RAD51 Tyr-315 residue by BCR/ABL appears essential for enhanced DSB repair and drug resistance.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia
+ BCR-ABLdown-regulates activity img/direct_inhibition.png phosphorylation RHOA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271700 Tyr34 KDQFPEVyVPTVFEN Homo sapiens HeLa Cell
pmid sentence
When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity
Identifier Residue Sequence Organism Cell Line
SIGNOR-271699 Tyr66 DTAGQEDyDRLRPLS Homo sapiens HeLa Cell
pmid sentence
When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity
Publications: 2 Organism: Homo Sapiens
+ BCR-ABLup-regulates img/direct-activation.png phosphorylation CTNNB1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-153431 Tyr654 RNEGVATyAAAVLFR Homo sapiens Leukemia Cell
pmid sentence
Bcr-abl stabilizes beta-catenin in chronic myeloid leukemia through its tyrosine phosphorylationthe notion that y86 and y654 are located respectively within the n_ and c_terminal transcriptional domains of __catenin suggests that one or both residues might regulate the transactivating function of __catenin. In this regard, phosphorylation of y654 was reported to strengthen __catenin association with the basal transcription factor tata_binding protein (tbp)
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, Onco-fusion proteins in AML
+ HCKup-regulates activity img/direct-activation.png phosphorylation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260810 Tyr730 PNLFVALyDFVASGD Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260811 Tyr775 QGWVPSNyITPVNSL Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260813 Tyr788 SLEKHSWyHGPVSRN Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260812 Tyr798 VSRNAAEyLLSSGIN Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260814 Tyr832 LRYEGRVyHYRINTA Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260815 Tyr845 TASDGKLyVSSESRF Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260816 Tyr875 GLITTLHyPAPKRNK Homo sapiens
pmid sentence
Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity. | Tyrosine phosphorylation of the SH3-SH2 region is essential for full Bcr-Abl biological activity.
Publications: 7 Organism: Homo Sapiens
+ BCR-ABLdown-regulates img/direct_inhibition.png phosphorylation CTNNB1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-153435 Tyr86 VADIDGQyAMTRAQR Homo sapiens Leukemia Cell
pmid sentence
Bcr_abl_mediated phosphorylation of y86 could induce a conformational change of __catenin impairing its binding to axin
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, Onco-fusion proteins in AML
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation CSF2RB 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-255814 Homo sapiens M-07E Cell
pmid sentence
We demonstrated that Bcr-Abl co-immunoprecipitates with, and constitutively phosphorylates, the common βc,subunit of the interleukin 3 and granulocyte/macrophage-colony stimulating factor receptors.We demonstrate that Bcr-Abl interacts with the common βc subunit of the IL-3 family of receptors and phosphorylates it on tyrosine.
Publications: 1 Organism: Homo Sapiens
+ PTPN1down-regulates img/direct_inhibition.png dephosphorylation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-56822 Homo sapiens
pmid sentence
We have observed association and dephosphorylation of p210 bcr-abl, but not v-abl, by ptp1b in vivo.
Publications: 1 Organism: Homo Sapiens
+ MYCup-regulates quantity by expression img/direct-activation.png transcriptional regulation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272143 Homo sapiens K-562 Cell, LAMA-84 Cell
pmid sentence
In the present study we demonstrate that MYC and its partner MAX bind to the BCR promoter, leading to up-regulation of BCR and BCR/ABL1 at both transcriptional and protein levels.|Here we describe a regulatory pathway modulating BCR and BCR/ABL1 expression, showing that the BCR promoter is under the transcriptional control of the MYC/MAX heterodimer.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ BCR-ABLup-regulates activity img/direct-activation.png binding GRB2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-255820 Homo sapiens HEK-293T Cell
pmid sentence
However, direct binding of Grb2 to Bcr/Abl also facilitates its tyrosine phosphorylation, which we propose reflects activation of a physiological negative regulatory mechanism by this oncogenic tyrosine kinase.Direct binding of Grb2 to Bcr/Abl facilitates Grb2 phosphorylation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-248199 Chlorocebus aethiops COS-7 Cell
pmid sentence
BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Mutation of Y177 to phenylalanine (Y177F) abolishes GRB-2 binding and abrogates BCR-ABL-induced Ras activation
Publications: 2 Organism: Homo Sapiens, Chlorocebus Aethiops
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ nilotinibdown-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-255818 Homo sapiens
pmid sentence
Nilotinib is an oral second-generation bcr-abl TKI indicated for the treatment of imatinib resistant or -intolerant Ph+ CML-CP and -AP in adults. Nilotinib binds to inactive configuration of the abl kinase, thus preventing the tyrosine phosphorylation of proteins involved in bcr-abl signal transduction. Nilotinib binds to the inactive (unphosphorylated) configuration of the abl TK, with the P-Ioop folding over, disrupting the ATP binding site and catalytic activity of the enzyme.
Identifier Residue Sequence Organism Cell Line
SIGNOR-259269 Homo sapiens Myeloid Leukemia Cell
pmid sentence
Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.
Publications: 2 Organism: Homo Sapiens
+ ponatinibdown-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259268 Homo sapiens Myeloid Leukemia Cell
pmid sentence
Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation CSF2RA/CSF2RB 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-256123 Mus musculus Bone Marrow Stem Cell
pmid sentence
This up-regulation required BCR-ABL tyrosine kinase activity and led to IL-3Rbetac/beta chain tyrosine phosphorylation in the absence of detectable IL-3 production. These results suggested that cytokine-independent IL-3 receptor activation could be a dominant signaling component in BCR-ABL-induced leukemogenesis. However, the IL-3Rβc/β chain could act as a cofactor in BCR-ABL-induced leukemogenesis by activation of its many known oncogenic signaling pathways.
Identifier Residue Sequence Organism Cell Line
SIGNOR-255999 Homo sapiens M-07E Cell
pmid sentence
We demonstrated that Bcr-Abl co-immunoprecipitates with, and constitutively phosphorylates, the common βc,subunit of the interleukin 3 and granulocyte/macrophage-colony stimulating factor receptors.We demonstrate that Bcr-Abl interacts with the common βc subunit of the IL-3 family of receptors and phosphorylates it on tyrosine.
Publications: 2 Organism: Mus Musculus, Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML
+ BCR-ABLdown-regulates activity img/indirect_inhibition.png Caspase 3 complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271705 Homo sapiens 32D Cell
pmid sentence
BCR/ABL Tyrosine Kinase Enhances Expression of RAD51 by Stimulation of STAT5-Mediated Transactivation and Inhibition of Caspase-3-Dependent Degradation|
Publications: 1 Organism: Homo Sapiens
+ bosutinibdown-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259271 Homo sapiens Myeloid Leukemia Cell
pmid sentence
Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLdown-regulates activity img/indirect_inhibition.png CASP3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271704 Homo sapiens 32D Cell
pmid sentence
BCR/ABL Tyrosine Kinase Enhances Expression of RAD51 by Stimulation of STAT5-Mediated Transactivation and Inhibition of Caspase-3-Dependent Degradation|
Publications: 1 Organism: Homo Sapiens
+ Bafetinibdown-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-255819 Homo sapiens
pmid sentence
Bafetinib (NS-187, INNO-406) is a second-generation tyrosine kinase inhibitor in development by CytRx under license from Nippon Shinyaku for treating Bcr-Abl+ leukemia's, including chronic myelogenous leukemia (CML) and Philadelphia+ acute lymphoblastic leukemia. It is a rationally developed tyrosine kinase inhibitor based on the chemical structure of imatinib, with modifications added to improve binding and potency against Bcr-Abl kinase.
Publications: 1 Organism: Homo Sapiens
+ dasatinib (anhydrous)down-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259270 Homo sapiens Myeloid Leukemia Cell
pmid sentence
Pre-existing BCR-ABL mutations can be detected in a substantial number of chronic-phase CML patients by sensitive allele-specific PCR technique using CD34+ cells. These mutations are associated with imatinib resistance if affecting drug binding directly or indirectly. After the recent approval of nilotinib, dasatinib, bosutinib and ponatinib for treatment of chronic myeloid leukemia along with imatinib, all of which vary in their effectiveness against mutated BCR-ABL forms, detection of pre-existing BCR-ABL mutations can help in selection of appropriate first-line drug therapy.
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLup-regulates img/direct-activation.png phosphorylation VAV1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-114094 Homo sapiens Leukemia Cell
pmid sentence
Thus, the c-terminal tail of vav serves as a direct substrate of bcr-abl in vitro.
Publications: 1 Organism: Homo Sapiens
+ Bafetinibdown-regulates img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-190224 Homo sapiens
pmid sentence
Publications: 1 Organism: Homo Sapiens
+ RUNX1up-regulates quantity by expression img/direct-activation.png transcriptional regulation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272145 Homo sapiens Chronic Myeloid Leukemia Cell Line
pmid sentence
RUNX1 transactivates BCR-ABL1 expression in Philadelphia chromosome positive acute lymphoblastic leukemia.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, Onco-fusion proteins in AML
+ PTENdown-regulates activity img/direct_inhibition.png dephosphorylation BCR-ABL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260080 Homo sapiens Chronic Myeloid Leukemia Cell
pmid sentence
PTEN targets the protein phosphatase activity of BCR-ABL. PTEN has the same function as PTP1B, which can regulate BCR-ABL dephosphorylation [13]. However, whether PTEN can mediate BCR-ABL dephosphorylation remains unknown. We found that under-expression of PTEN significantly upregulated phosphorylation level of BCR-ABL. In order to verify the mechanisms, co-IP assays were applied, demonstrating the ways in which PTEN and BCR-ABL interact with each other.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML
+ imatinib methanesulfonatedown-regulates activity img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-259357 Homo sapiens Myeloid Leukemia Cell Line
pmid sentence
Imatinib mesylate (Gleevec/Glivec, Novartis, Basel, Switzerland), formerly called STI571, is a specific and potent inhibitor of the BCR-ABL tyrosine kinase, the molecular hallmark of chronic myeloid leukaemia.
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLup-regulates activity img/indirect-activation.png NRAS 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-261506 Chlorocebus aethiops
pmid sentence
BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein. Mutation of Y177 to phenylalanine (Y177F) abolishes GRB-2 binding and abrogates BCR-ABL-induced Ras activation.
Publications: 1 Organism: Chlorocebus Aethiops
Pathways:Acute Myeloid Leukemia, Onco-fusion proteins in AML
+ nilotinibdown-regulates img/direct_inhibition.png chemical inhibition BCR-ABL 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-194640 Homo sapiens
pmid sentence
Publications: 1 Organism: Homo Sapiens
+ BCR-ABLup-regulates activity img/direct-activation.png phosphorylation STAT5A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-255813 Mus musculus 32D Cell
pmid sentence
Phosphorylation of STAT1 and STAT5 was directly due to the tyrosine kinase activity of Bcr/Abl since it could be activated or deactivated by temperature shifting of cells expressing the Bcr/Abl ts mutant.These data suggest that STATs can be activated directly by Bcr/Abl, possibly bypassing JAK family kinase activation.
Publications: 1 Organism: Mus Musculus
Pathways:Acute Myeloid Leukemia, BCR-ABL in AML, Onco-fusion proteins in AML
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