[1]
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NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2030914 [NCBI, ExPASy, EBI, Israel, Japan]
Blake T.J.,
Shapiro M.,
Morse H.C. III,
Langdon W.Y.;
"The sequences of the human and mouse c-cbl proto-oncogenes show v-cbl was generated by a large truncation encompassing a proline-rich domain and a leucine zipper-like motif.";
Oncogene 6:653-657(1991).
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[2]
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FUNCTION.
DOI=10.1126/science.286.5438.309; PubMed=10514377 [NCBI, ExPASy, EBI, Israel, Japan]
Joazeiro C.A.,
Wing S.S.,
Huang H.-K.,
Leverson J.D.,
Hunter T.,
Liu Y.-C.;
"The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase.";
Science 286:309-312(1999).
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[3]
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PHOSPHORYLATION BY EGFR.
DOI=10.1074/jbc.270.35.20242; PubMed=7657591 [NCBI, ExPASy, EBI, Israel, Japan]
Galisteo M.L.,
Dikic I.,
Batzer A.G.,
Langdon W.Y.,
Schlessinger J.;
"Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation.";
J. Biol. Chem. 270:20242-20245(1995).
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[4]
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INTERACTION WITH ZAP70.
DOI=10.1074/jbc.272.52.33140; PubMed=9407100 [NCBI, ExPASy, EBI, Israel, Japan]
Lupher M.L. Jr.,
Songyang Z.,
Shoelson S.E.,
Cantley L.C.,
Band H.;
"The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70.";
J. Biol. Chem. 272:33140-33144(1997).
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[5]
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PHOSPHORYLATION BY SYK AND FYN.
DOI=10.1074/jbc.273.15.8867; PubMed=9535867 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert M.,
Elly C.,
Altman A.,
Liu Y.C.;
"Coordinated regulation of the tyrosine phosphorylation of Cbl by Fyn and Syk tyrosine kinases.";
J. Biol. Chem. 273:8867-8874(1998).
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[6]
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INTERACTION WITH LAT2.
DOI=10.1084/jem.20021405; PubMed=12486104 [NCBI, ExPASy, EBI, Israel, Japan]
Brdicka T.,
Imrich M.,
Angelisova P.,
Brdickova N.,
Horvath O.,
Spicka J.,
Hilgert I.,
Luskova P.,
Draber P.,
Novak P.,
Engels N.,
Wienands J.,
Simeoni L.,
Oesterreicher J.,
Aguado E.,
Malissen M.,
Schraven B.,
Horejsi V.;
"Non-T cell activation linker (NTAL): a transmembrane adaptor protein involved in immunoreceptor signaling.";
J. Exp. Med. 196:1617-1626(2002).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669 AND TYR-674, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2436191100; PubMed=12522270 [NCBI, ExPASy, EBI, Israel, Japan]
Salomon A.R.,
Ficarro S.B.,
Brill L.M.,
Brinker A.,
Phung Q.T.,
Ericson C.,
Sauer K.,
Brock A.,
Horn D.M.,
Schultz P.G.,
Peters E.C.;
"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
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[8]
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INTERACTION WITH SH2B2.
DOI=10.1038/sj/leu/2401397; PubMed=10374881 [NCBI, ExPASy, EBI, Israel, Japan]
Wakioka T.,
Sasaki A.,
Mitsui K.,
Yokouchi M.,
Inoue A.,
Komiya S.,
Yoshimura A.;
"APS, an adaptor protein containing pleckstrin homology (PH) and Src homology-2 (SH2) domains inhibits the JAK-STAT pathway in collaboration with c-Cbl.";
Leukemia 13:760-767(1999).
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[9]
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INTERACTION WITH SH2B2.
DOI=10.1038/sj.onc.1202326; PubMed=9989826 [NCBI, ExPASy, EBI, Israel, Japan]
Yokouchi M.,
Wakioka T.,
Sakamoto H.,
Yasukawa H.,
Ohtsuka S.,
Sasaki A.,
Ohtsubo M.,
Valius M.,
Inoue A.,
Komiya S.,
Yoshimura A.;
"APS, an adaptor protein containing PH and SH2 domains, is associated with the PDGF receptor and c-Cbl and inhibits PDGF-induced mitogenesis.";
Oncogene 18:759-767(1999).
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[10]
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INTERACTION WITH SLA AND ZAP70, AND MUTAGENESIS OF GLY-306.
DOI=10.1073/pnas.96.17.9775; PubMed=10449770 [NCBI, ExPASy, EBI, Israel, Japan]
Tang J.,
Sawasdikosol S.,
Chang J.-H.,
Burakoff S.J.;
"SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling.";
Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999).
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[11]
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INTERACTION WITH SLA2.
DOI=10.1084/jem.194.9.1263; PubMed=11696592 [NCBI, ExPASy, EBI, Israel, Japan]
Holland S.J.,
Liao X.C.,
Mendenhall M.K.,
Zhou X.,
Pardo J.,
Chu P.,
Spencer C.,
Fu A.C.,
Sheng N.,
Yu P.,
Pali E.,
Nagin A.,
Shen M.,
Yu S.,
Chan E.,
Wu X.,
Li C.,
Woisetschlager M.,
Aversa G., ![]()
Kolbinger F.,
Bennett M.K.,
Molineaux S.,
Luo Y.,
Payan D.G.,
Mancebo H.S.Y.,
Wu J.;
"Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel inhibitor of antigen receptor signaling.";
J. Exp. Med. 194:1263-1276(2001).
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[12]
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INTERACTION WITH CD2AP.
DOI=10.1074/jbc.M005784200; PubMed=11067845 [NCBI, ExPASy, EBI, Israel, Japan]
Kirsch K.H.,
Georgescu M.M.,
Shishido T.,
Langdon W.Y.,
Birge R.B.,
Hanafusa H.;
"The adapter type protein CMS/CD2AP binds to the proto-oncogenic protein c-Cbl through a tyrosine phosphorylation-regulated Src homology 3 domain interaction.";
J. Biol. Chem. 276:4957-4963(2001).
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[13]
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INTERACTION WITH SH2B2, MUTAGENESIS OF TYR-371; TYR-700; TYR-731 AND TYR-774, AND PHOSPHORYLATION AT TYR-371; TYR-700 AND TYR-774.
DOI=10.1128/MCB.22.11.3599-3609.2002; PubMed=11997497 [NCBI, ExPASy, EBI, Israel, Japan]
Liu J.,
Kimura A.,
Baumann C.A.,
Saltiel A.R.;
"APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes.";
Mol. Cell. Biol. 22:3599-3609(2002).
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[14]
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INTERACTION WITH INPPL1.
DOI=10.1016/S0006-291X(02)02894-2; PubMed=12504111 [NCBI, ExPASy, EBI, Israel, Japan]
Vandenbroere I.,
Paternotte N.,
Dumont J.E.,
Erneux C.,
Pirson I.;
"The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2.";
Biochem. Biophys. Res. Commun. 300:494-500(2003).
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[15]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371 AND TYR-552, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y.,
Wolf-Yadlin A.,
Ross P.L.,
Pappin D.J.,
Rush J.,
Lauffenburger D.A.,
White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
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[16]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-674, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J.,
Moritz A.,
Lee K.A.,
Guo A.,
Goss V.L.,
Spek E.J.,
Zhang H.,
Zha X.-M.,
Polakiewicz R.D.,
Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
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[17]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-675, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A.,
Wollscheid B.,
O'Brien R.,
Eng J.K.,
Li X.-J.,
Bodenmiller B.,
Watts J.D.,
Hood L.,
Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
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[18]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A.,
Villen J.,
Gerber S.A.,
Rush J.,
Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
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[19]
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X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 47-350, CALCIUM-BINDING SITE, AND MUTAGENESIS OF SER-80; PRO-82; ASP-229; GLU-240; ARG-294 AND GLY-306.
DOI=10.1038/18050; PubMed=10078535 [NCBI, ExPASy, EBI, Israel, Japan]
Meng W.,
Sawasdikosol S.,
Burakoff S.J.,
Eck M.J.;
"Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.";
Nature 398:84-90(1999).
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[20]
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X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 47-434 IN COMPLEX WITH ZAP70 AND UBE2L3.
DOI=10.1016/S0092-8674(00)00057-X; PubMed=10966114 [NCBI, ExPASy, EBI, Israel, Japan]
Zheng N.,
Wang P.,
Jeffrey P.D.,
Pavletich N.P.;
"Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases.";
Cell 102:533-539(2000).
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