E3 ubiquitin-protein ligase CBL-B (Protein name
), CBLB_HUMAN from NCBI database.
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Gene name:
CBLB(Nbla00127;RNF56);
Protein name:
E3 ubiquitin-protein ligase CBL-B;
Alternative:
RING finger protein 56;Casitas B-lineage lymphoma proto-oncogene b;Signal transduction protein CBL-B;SH3-binding protein CBL-B;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts with SH3 domain-containing proteins LCK, CRK and SORBS1. Interacts with LCP2 and ZAP70. May interact with CBL (By similarity). Interacts with SH3 domain-containing proteins VAV1, FYN, FGR, PLCG1, GRB2, CRKL, PIK3R1 and SH3KBP1/CIN85. Identified in heterotrimeric complexes with SH3KBP1/CIN85, CD2AP and ARHGEF7, where one CBLB peptide binds two copies of the other protein. Interacts with poly-ubiquitinated proteins. Dimerization is required for the binding of poly-ubiquitin, but not for the binding of mono-ubiquitin.
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization.
Subcellular Location:
Cytoplasm
Upon EGF stimulation, associates with endocytic vesicles.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG; TRUNCATED 1 AND TRUNCATED 2)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG);TISSUE SPECIFICITY;INTERACTION WITH VAV1
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG);VARIANT LYS-584
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-982 (ISOFORM LONG)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 857-982 (ISOFORM LONG)
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Cited for: TISSUE SPECIFICITY;MUTAGENESIS OF GLY-298; TYR-665 AND TYR-709;INTERACTION WITH GRB2 AND CRKL;PHOSPHORYLATION AT TYR-665 AND TYR-709;FUNCTION
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Cited for: FUNCTION;PHOSPHORYLATION;INTERACTION WITH GRB2 AND PIK3R1
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Cited for: FUNCTION;INTERACTION WITH PIK3R1;MUTAGENESIS OF GLY-298 AND CYS-373
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Cited for: INTERACTION WITH UBIQUITINATED PROTEINS;MUTAGENESIS OF 943-GLY-TYR-944 AND LEU-967
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-525 AND SER-529;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE;PHOSPHORYLATION AT TYR-363;MUTAGENESIS OF TYR-363
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Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 899-914 IN COMPLEXES WITH SH3KBP1 AND ARHGEF7;MUTAGENESIS OF ARG-904 AND ARG-911;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 902-912 IN COMPLEX WITH CD2AP;MUTAGENESIS OF ARG-904; LYS-907 AND ARG-911;SUBUNIT
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Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 924-973 IN COMPLEX WITH UBIQUITIN;STRUCTURE BY NMR OF 924-973;TYROSINE PHOSPHORYLATION;MUTAGENESIS OF ALA-937; MET-940; PHE-946 AND ILE-966
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Cited for: STRUCTURE BY NMR OF 931-970
26.
"Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide." Structural genomics consortium (SGC)
Submitted (2010-10) to the PDB data bank
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Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-344 IN COMPLEX WITH PHOSPHO-EGFR PEPTIDE;INTERACTION WITH EGFR;HETERODIMER