Relation Results

Summary

Name CBL
Full Name E3 ubiquitin-protein ligase CBL
Synonyms Casitas B-lineage lymphoma proto-oncogene, Proto-oncogene c-Cbl, RING finger protein 55, Signal transduction protein CBL | CBL2, RNF55
Primary ID P22681
Links - -
Type protein
Relations 55
Pathways Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, Glioblastoma Multiforme
Function Adapter protein that functions as a negative regulator of many signaling pathways that are triggered by activation of cell surface receptors. Acts as ...
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Type: Score: Layout: SPV 
0.5770.3250.3920.5140.8070.7250.8840.3860.5210.6280.5650.6850.3730.4430.5140.6120.4710.5820.8840.9020.7310.8190.6350.8110.7030.3760.6190.5780.680.6580.6110.5780.5950.20.6070.450.20.6370.6010.6850.3590.30.7410.327CBLJAK2PRKCAPTPN22INSRFYNMETEGFRSH3GLB1SORBS2EPHA2FRS2VAV1LTKFLT3ERBB2PDGFRAERBB4GRB2SRCCRKNCK1SYKLCKABI1PDGFRBLRIG1SORBS1HCKABL1PIK3R2Ub:E2KITUBASH3BCFLARSH2B2PI3KPIK3R1PRKCQMYCBPAPSH3KBP1PTPRJ

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination JAK2 0.577
Identifier Residue Sequence Organism Cell Line
SIGNOR-278538 Lys970 GMEYLGTkRYIHRDL Homo sapiens
pmid sentence
K63 linked poly-ubiquitination on K970 of JAK2 kinase domain is promoted by Cbl.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, FLT3 in AML, KIT in AML
+ PRKCAdown-regulates quantity img/direct_inhibition.png phosphorylation CBL 0.325
Identifier Residue Sequence Organism Cell Line
SIGNOR-249054 Ser619 RELTNRHsLPFSLPS Homo sapiens T-lymphocyte
pmid sentence
However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-249055 Ser623 NRHSLPFsLPSQMEP Homo sapiens T-lymphocyte
pmid sentence
However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-249056 Ser639 PDVPRLGsTFSLDTS Homo sapiens T-lymphocyte
pmid sentence
However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-249057 Ser642 PRLGSTFsLDTSMSM Homo sapiens T-lymphocyte
pmid sentence
However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway. 
Publications: 4 Organism: Homo Sapiens
+ PTPN22down-regulates img/direct_inhibition.png dephosphorylation CBL 0.392
Identifier Residue Sequence Organism Cell Line
SIGNOR-65405 Ser798 SDISNASsSFGWLSL Homo sapiens T-lymphocyte
pmid sentence
The tyrosine phosphatase lyp1 was found to be constitutively associated with the proto-oncogene c-cbl in thymocytes and t cells. Overexpression of lyp1 reduces cbl tyrosine phosphorylation. It is known that cbl is heavily tyrosine phosphorylated after tcr stimulation and can associate with the syk and zap tyrosine kinases, negatively regulating their activities. Tyrosine phosphatases keep cbl in a basally dephosphorylated state.
Publications: 1 Organism: Homo Sapiens
+ INSRup-regulates activity img/direct-activation.png phosphorylation CBL 0.514
Identifier Residue Sequence Organism Cell Line
SIGNOR-251304 Tyr371 TQEQYELyCEMGSTF Mus musculus NIH-3T3 Cell
pmid sentence
Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-251305 Tyr700 EGEEDTEyMTPSSRP Mus musculus
pmid sentence
Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-251306 Tyr774 SENEDDGyDVPKPPV Mus musculus NIH-3T3 Cell
pmid sentence
Insulin receptor phosphorylates Cbl on tyrosines 371, 700, and 774 in the presence of APS. This phosphorylation event is required for the recruitment of Crk to the CAP/Cbl complex and for the subsequent activation of GLUT4 translocation.
Publications: 3 Organism: Mus Musculus
+ FYNup-regulates activity img/direct-activation.png phosphorylation CBL 0.807
Identifier Residue Sequence Organism Cell Line
SIGNOR-63968 Tyr731 QQIDSCTyEAMYNIQ Homo sapiens
pmid sentence
Fyn associates with cbl and phosphorylates tyrosine 731 in cbl, a binding site for phosphatidylinositol 3-kinasecbl represents a substrate for src-like kinases that are activated in response to the engagement of cell surface receptors, and that src-like kinases are responsible for the phosphorylation of a tyrosine residue in cbl that may regulate activation of phosphatidylinositol 3-kinase
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination MET 0.725
Identifier Residue Sequence Organism Cell Line
SIGNOR-185680 Homo sapiens
pmid sentence
Tyrosine y1001, which when phosphorylated upon met activation, is involved in cbl recruitment, allowing receptor ubiquitination and down regulation
Publications: 1 Organism: Homo Sapiens
+ EGFRup-regulates img/direct-activation.png relocalization CBL 0.884
Identifier Residue Sequence Organism Cell Line
SIGNOR-114701 Homo sapiens
pmid sentence
Consistent with a negative role for c-Cbl, here we report that defective Tyr1045 of EGFR, an inducible c-Cbl docking site, enhances the mitogenic response to EGF
Identifier Residue Sequence Organism Cell Line
SIGNOR-147826 Homo sapiens
pmid sentence
Likewise, cbl is recruited to erbb1 either directly (tyr1045), or indirectly, trough grb2
Publications: 2 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, Glioblastoma Multiforme
+ SH3GLB1up-regulates img/direct-activation.png binding CBL 0.386
Identifier Residue Sequence Organism Cell Line
SIGNOR-115826 Homo sapiens
pmid sentence
Cbl rapidly recruits cin85 (cbl-interacting protein of 85k;ref. 6) and endophilins (regulatory components of clathrin-coated vesicles) to form a complex with activated egf receptors, thus controlling receptor internalization.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates img/direct_inhibition.png ubiquitination SORBS2 0.521
Identifier Residue Sequence Organism Cell Line
SIGNOR-96325 Homo sapiens
pmid sentence
Cbl-argbp2 complex mediates ubiquitination and degradation of c-abl
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png binding EPHA2 0.628
Identifier Residue Sequence Organism Cell Line
SIGNOR-272590 Homo sapiens
pmid sentence
In our present study, we demonstrate that ligand-mediated stimulation causes EphA2 to be internalized and degraded. The mechanism of this response involves ligand-mediated autophosphorylation of EphA2, which promotes an association between EphA2 and the c-Cbl adaptor protein. We also show that c-Cbl promotes stimulation-dependent EphA2 degradation. 
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates img/direct_inhibition.png ubiquitination FRS2 0.565
Identifier Residue Sequence Organism Cell Line
SIGNOR-87166 Homo sapiens
pmid sentence
The experiments presented in this report illustrate that in response to fgf stimulation, cbl is recruited by grb2 binding to the frs2_ multiprotein complex, resulting in ubiquitination of frs2_ and fgfr. grb2 functions as a link between frs2_ and cbl;grb2 is bound to tyrosine-phosphorylated frs2_ by means of its sh2 domain and to a proline-rich region in the c terminus of cbl by means of its sh3 domains.
Publications: 1 Organism: Homo Sapiens
+ VAV1up-regulates img/direct-activation.png binding CBL 0.685
Identifier Residue Sequence Organism Cell Line
SIGNOR-49188 Homo sapiens T-lymphocyte
pmid sentence
Hese data imply that c-cbl is a molecular adapter that regulates the function of vav
Publications: 1 Organism: Homo Sapiens
+ LTKup-regulates img/direct-activation.png phosphorylation CBL 0.373
Identifier Residue Sequence Organism Cell Line
SIGNOR-49528 Homo sapiens Neuron
pmid sentence
Although c-cbl is found to be phosphorylated by ltk and therefore is a second candidate linking ltk with the pi3-kinase pathway along with irs-1, we found that the p85 subunit of pi3 kinase directly binds to tyrosine 753 of ltk, which is located within a yxxm motif, a consensus binding amino acid sequence for the sh2 domain of p85.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates activity img/direct_inhibition.png binding FLT3 0.443
Identifier Residue Sequence Organism Cell Line
SIGNOR-255739 Mus musculus BA/F3 Cell
pmid sentence
Functionally, CBL negatively regulated FMS-like tyrosine kinase 3 (FLT3) activity and interacted with human FLT3 via the autophosphorylation sites Y589 and Y599 and colocalized in vivo.
Publications: 1 Organism: Mus Musculus
Pathways:Acute Myeloid Leukemia, FLT3 in AML
+ CBLdown-regulates img/direct_inhibition.png ubiquitination INSR 0.514
Identifier Residue Sequence Organism Cell Line
SIGNOR-109688 Homo sapiens
pmid sentence
Aps couples c-cbl to theinsulinreceptor, resulting in ubiquitination of theinsulinreceptor
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination ERBB2 0.612
Identifier Residue Sequence Organism Cell Line
SIGNOR-30794 Homo sapiens
pmid sentence
Ligand binding to EGFR also leads to rapid internalization and proteosomal/lysosomal degradation of the receptors. This process results in a dramatic downregulation of both total and cell surface receptors. EGF-induced degradation of EGFR is thought to be initiated by phosphorylation of tyrosine 1045 of the receptor followed by binding of Cbl adaptor proteins and ubiquitination of the receptor. Internalized EGFR is transported to early endosomes where receptor-ligand complexes are sorted for either degradation or recycling to the cell surface.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination PDGFRA 0.471
Identifier Residue Sequence Organism Cell Line
SIGNOR-68024 Homo sapiens
pmid sentence
Cbl overexpression in nih3t3 cells enhanced the ubiquitination and degradation of the platelet-derived growth factor receptor-alpha (pdgfralpha)
Publications: 1 Organism: Homo Sapiens
+ ERBB4up-regulates img/direct-activation.png binding CBL 0.582
Identifier Residue Sequence Organism Cell Line
SIGNOR-180895 Homo sapiens
pmid sentence
Erbb4 might not be able to directly recruit cbl, and therefore downregulation of this receptor is slow.
Identifier Residue Sequence Organism Cell Line
SIGNOR-147841 Homo sapiens
pmid sentence
Erbb4 might not be able to directly recruit cbl, and therefore downregulation of this receptor is slow.
Publications: 2 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination EGFR 0.884
Identifier Residue Sequence Organism Cell Line
SIGNOR-65642 Homo sapiens
pmid sentence
Ligand binding to EGFR also leads to rapid internalization and proteosomal/lysosomal degradation of the receptors. This process results in a dramatic downregulation of both total and cell surface receptors. EGF-induced degradation of EGFR is thought to be initiated by phosphorylation of tyrosine 1045 of the receptor followed by binding of Cbl adaptor proteins and ubiquitination of the receptor. Internalized EGFR is transported to early endosomes where receptor-ligand complexes are sorted for either degradation or recycling to the cell surface.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, Glioblastoma Multiforme
+ GRB2up-regulates img/direct-activation.png relocalization CBL 0.902
Identifier Residue Sequence Organism Cell Line
SIGNOR-114704 Homo sapiens
pmid sentence
The underlying mechanism seems to involve recruitment of a grb2 c-cbl complex to grb2-specific docking sites of egfr, and concurrent acceleration of receptor ubiquitylation and desensitization.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, FLT3 in AML, KIT in AML, Glioblastoma Multiforme
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination SRC 0.731
Identifier Residue Sequence Organism Cell Line
SIGNOR-278539 Homo sapiens
pmid sentence
Cbl-b also targets active Src for degradation in cells, and Nedd4 similarly reverses Cbl mediated Src degradation.|Cbl-b also targets active Src for degradation in cells, and Nedd4 similarly reverses Cbl-mediated Src degradation
Publications: 1 Organism: Homo Sapiens
+ CRKup-regulates img/direct-activation.png binding CBL 0.819
Identifier Residue Sequence Organism Cell Line
SIGNOR-39241 Homo sapiens T-lymphocyte, Leukemia Cell
pmid sentence
These results indicate that crk binds to c-cbl in a tyrosine phosphorylation-dependent manner.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination NCK1 0.635
Identifier Residue Sequence Organism Cell Line
SIGNOR-278606 Homo sapiens
pmid sentence
Taken together, these results show that lysine 178 in Nck1 is the acceptor site for ubiquitin transferred by c-Cbl, and that the ubiquitination of Nck1 by c-Cbl is blocked in the presence of synaptopodin.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity img/direct_inhibition.png ubiquitination SYK 0.811
Identifier Residue Sequence Organism Cell Line
SIGNOR-278689 Homo sapiens
pmid sentence
Thus, c-Cbl specifically downregulates Syk levels in the presence of LMP2A.|c-Cbl promoted LMP2A degradation through ubiquitination, specifically degraded the Syk protein tyrosine kinase in the presence of LMP2A, and inhibited LMP2A induction of the EBV lytic cycle
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity img/direct_inhibition.png ubiquitination LCK 0.703
Identifier Residue Sequence Organism Cell Line
SIGNOR-278804 Homo sapiens
pmid sentence
One study indicated that loss of CBL expression increases the constitutive level of LCK 80, but other studies have not shown this - .|The ubiquitylation of LCK by CBL (Casitas B-lineage lymphoma) is known to be a negative mechanism that regulates the signalling function of LCK xref .
Publications: 1 Organism: Homo Sapiens
+ ABI1up-regulates img/direct-activation.png binding CBL 0.376
Identifier Residue Sequence Organism Cell Line
SIGNOR-154162 Homo sapiens
pmid sentence
Here we uncover a novel interaction between abi-1 and the cbl ubiquitin ligase and show that abi-1 mediates cbl accumulation to the plasma membrane upon stimulation by egf.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination LCK 0.703
Identifier Residue Sequence Organism Cell Line
SIGNOR-272614 Homo sapiens HEK-293 Cell
pmid sentence
Coexpression in 293T cells demonstrated that Lck kinase activity and Cbl ubiquitin ligase activity were essential for Lck ubiquitination and negative regulation of Lck-dependent serum response element-luciferase reporter activity. The Lck SH3 domain was pivotal for Cbl-Lck association and Cbl-mediated Lck degradation, with a smaller role for interactions mediated by the Cbl tyrosine kinase-binding domain.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png polyubiquitination PDGFRB 0.619
Identifier Residue Sequence Organism Cell Line
SIGNOR-272553 Homo sapiens
pmid sentence
Ubiquitination of the PDGF β-receptor (Rβ) by the c-Cbl RING in an SH2-dependent manner.
Identifier Residue Sequence Organism Cell Line
SIGNOR-272549 Mus musculus NIH-3T3 Cell
pmid sentence
 Overexpression of wild type Cbl in NIH3T3 cells led to an enhancement of the ligand-dependent ubiquitination and subsequent degradation of the PDGFRbeta, as observed with PDGFRalpha.
Publications: 2 Organism: Homo Sapiens, Mus Musculus
+ LRIG1up-regulates img/direct-activation.png binding CBL 0.578
Identifier Residue Sequence Organism Cell Line
SIGNOR-127298 Homo sapiens
pmid sentence
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation.
Publications: 1 Organism: Homo Sapiens
Tissue: Skin
+ SORBS1up-regulates img/direct-activation.png binding CBL 0.68
Identifier Residue Sequence Organism Cell Line
SIGNOR-82283 Homo sapiens
pmid sentence
Cbl is recruited to the insulin receptor by interaction with the adapter protein cap, through one of three adjacent sh3 domains in the carboxy terminus of cap
Publications: 1 Organism: Homo Sapiens
Tissue: Muscle
+ HCK img/unknown.png phosphorylation CBL 0.658
Identifier Residue Sequence Organism Cell Line
SIGNOR-251262 Mus musculus
pmid sentence
Hck is one member of the Src-family PTKs that is able to phosphorylate Cbl. Upon enzymatic activation of Hck either by pharmacological agents or genetic mutation, Cbl becomes tyrosine phosphorylated.
Publications: 1 Organism: Mus Musculus
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination ABL1 0.611
Identifier Residue Sequence Organism Cell Line
SIGNOR-167194 Homo sapiens Leukemia Cell
pmid sentence
We found that while c-cbl e3 ligase induced ubiquitin-dependent degradation of mature and phosphorylated bcr-abl proteins
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates img/direct_inhibition.png ubiquitination LRIG1 0.578
Identifier Residue Sequence Organism Cell Line
SIGNOR-127289 Homo sapiens
pmid sentence
We report upregulation of lrig1 transcript and protein upon egf stimulation, and physical association of the encoded protein with the four egfr orthologs of mammals. Upregulation of lrig1 is followed by enhanced ubiquitylation and degradation of egfr. The underlying mechanism involves recruitment of c-cbl, an e3 ubiquitin ligase that simultaneously ubiquitylates egfr and lrig1 and sorts them for degradation.
Publications: 1 Organism: Homo Sapiens
Tissue: Skin
+ CBLdown-regulates img/direct_inhibition.png ubiquitination PIK3R2 0.595
Identifier Residue Sequence Organism Cell Line
SIGNOR-110063 Homo sapiens
pmid sentence
Cbl-b, a ring-type e3 ubiquitin protein ligase, is implicated in setting the threshold of t lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (pi3k) was identified as a substrate for cbl-b. We have shown that cbl-b negatively regulated p85 in a proteolysis-independent manner.
Publications: 1 Organism: Homo Sapiens
+ Ub:E2up-regulates activity img/direct-activation.png ubiquitination CBL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271100 Homo sapiens
pmid sentence
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates activity img/direct_inhibition.png ubiquitination KIT 0.607
Identifier Residue Sequence Organism Cell Line
SIGNOR-260104 Homo sapiens
pmid sentence
KIT binds to and induces the phosphorylation of Cbl proteins, which in turn act as E3 ligases, mediating the ubiquitination and degradation of KIT and themselves. Tyrosine kinase binding and RING finger domains of Cbl are essential for Cbl-mediated ubiquitination and degradation of KIT.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, KIT in AML
+ UBASH3Bdown-regulates img/direct_inhibition.png binding CBL 0.45
Identifier Residue Sequence Organism Cell Line
SIGNOR-124897 Homo sapiens
pmid sentence
Sts-1 and sts-2 contain sh3 domains that interacted with cbl, ub-associated domains, which bound directly to mono-ub or to the egfr/ub chimera as well as phosphoglycerate mutase domains that mediated oligomerization of sts-1/2. Ligand-induced recruitment of sts-1/sts-2 into activated egfr complexes led to inhibition of receptor internalization, reduction in the number of egfr-containing endocytic vesicles, and subsequent block of receptor degradation followed by prolonged activation of mitogenic signaling pathways.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates quantity by destabilization img/direct_inhibition.png ubiquitination CFLAR 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-186998 Homo sapiens
pmid sentence
We therefore conclude that c-cbl is a e3 ubiquitin ligase for flips and that the interaction of flips with c-cbl requires phosphorylation of both ser4 and tyr211 of flips.This interaction triggered proteasomal degradation of FLIP(S), which promoted activation of caspase-8 and apoptosis.
Publications: 1 Organism: Homo Sapiens
+ CBLdown-regulates activity img/direct_inhibition.png ubiquitination SYK 0.811
Identifier Residue Sequence Organism Cell Line
SIGNOR-272620 Homo sapiens HEK-293 Cell
pmid sentence
Intact tyrosine kinase-binding and RING finger domains of Cbl were found to be essential for Syk ubiquitylation in 293T cells and for in vitro Syk ubiquitylation. Altogether, our results support an essential role for Cbl ubiquitin ligase activity in the negative regulation of Syk, and establish that ubiquitylation provides a mechanism of Cbl-mediated negative regulation of cytoplasmic targets.
Publications: 1 Organism: Homo Sapiens
+ SH2B2up-regulates img/direct-activation.png binding CBL 0.637
Identifier Residue Sequence Organism Cell Line
SIGNOR-78337 Cricetulus griseus Ovary Cell Line
pmid sentence
APS-mediated recruitment of c-Cbl to the insulin receptor led to rapid ubiquitination of the insulin receptor beta-subunit in CHO. T-APS but not in parental CHO.T cells. These results suggest that the function of APS is to facilitate coupling of the insulin receptor to c-Cbl in order to catalyse the ubiquitination of the receptor and initiation of internalisation or degradation.
Identifier Residue Sequence Organism Cell Line
SIGNOR-109691 Homo sapiens
pmid sentence
Aps couples c-cbl to theinsulinreceptor, resulting in ubiquitination of theinsulinreceptor. The aps adapter protein couples theinsulinreceptor to the phosphorylation of c-cbl and facilitates ligand-stimulated ubiquitination of theinsulinreceptor.
Publications: 2 Organism: Cricetulus Griseus, Homo Sapiens
Tissue: Ovary
+ CBLdown-regulates img/direct_inhibition.png ubiquitination PI3K 0.601
Identifier Residue Sequence Organism Cell Line
SIGNOR-252668 Homo sapiens T-lymphocyte
pmid sentence
Cbl-b, a ring-type e3 ubiquitin protein ligase, is implicated in setting the threshold of t lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (pi3k) was identified as a substrate for cbl-b. We have shown that cbl-b negatively regulated p85 in a proteolysis-independent manner.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia, FLT3 in AML, KIT in AML
+ CBLdown-regulates img/direct_inhibition.png ubiquitination PIK3R1 0.685
Identifier Residue Sequence Organism Cell Line
SIGNOR-110060 Homo sapiens T-lymphocyte
pmid sentence
Cbl-b, a ring-type e3 ubiquitin protein ligase, is implicated in setting the threshold of t lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (pi3k) was identified as a substrate for cbl-b. We have shown that cbl-b negatively regulated p85 in a proteolysis-independent manner.
Publications: 1 Organism: Homo Sapiens
Pathways:Glioblastoma Multiforme
+ PRKCQup-regulates activity img/direct-activation.png phosphorylation CBL 0.359
Identifier Residue Sequence Organism Cell Line
SIGNOR-274144 Mus musculus T-lymphocyte
pmid sentence
PKC-θ-mediated phosphorylation of serine and tyrosine residues of c-Cbl prevents its inhibitory effect. Phosphorylation of c-Cbl by PKC-θ inhibits the recruitment of Sh2-containing proteins and subsequent association of cbl E3 ubiquitin ligase with its target proteins
Publications: 1 Organism: Mus Musculus
+ CBLup-regulates activity img/direct-activation.png monoubiquitination MYCBPAP 0.3
Identifier Residue Sequence Organism Cell Line
SIGNOR-272627 Homo sapiens HEK-293 Cell
pmid sentence
We moreover found that AMAP1 is monoubiquitinated, rather than polyubiquitinated, by virtue of Cbl and provide evidence that the ability of AMAP1 to be monoubiquitinated is important for its involvement in invasion. 
Publications: 1 Organism: Homo Sapiens
+ SH3KBP1up-regulates img/direct-activation.png binding CBL 0.741
Identifier Residue Sequence Organism Cell Line
SIGNOR-203139 Homo sapiens
pmid sentence
The cin85 sh3 domains interact with c-cbl, an e3 ubiquitin ligase, via an unconventional pxxxpr ligand sequence, with the highest affinity displayed by the sh3-b domain. Interaction with cin85 recruits c-cbl to the amap1 complex where its ubiquitination activity is necessary for cancer cells to develop an invasive phenotype and to degrade the matrix.
Publications: 1 Organism: Homo Sapiens
+ PTPRJdown-regulates activity img/indirect_inhibition.png CBL 0.327
Identifier Residue Sequence Organism Cell Line
SIGNOR-248839 Homo sapiens
pmid sentence
Because c-CBL’s activation is achieved via tyrosine phosphorylation, we tested the effect of DEP-1 on modification of a major site of phosphorylation, namely tyro- sine 731. Upon DEP-1 overexpression, c-CBL displayed reduced phosphorylation on this site compared to control cells (Figure 7B). This result offers a mechanism by which DEP-1 affects EGFR trafficking: by dephosphorylating EGFR, and possibly also SRC family kinases involved in phosphoryla- tion of c-CBL [31, 32], DEP-1 reduces activation of c-CBL and its recruitment to the activated EGFR, hence inhibiting subsequent receptor internalization and degradation.
Publications: 1 Organism: Homo Sapiens
Pathways:Acute Myeloid Leukemia
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