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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC51506
Cbl-type phosphotyrosine-binding (Cbl-PTB) domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC51506

Description

Cbl (Casitas B-lineage lymphoma) is an adaptor protein that functions as a negative regulator of many signalling pathways that start from receptors at the cell surface. The evolutionarily conserved amino-terminal region of Cbl (Cbl-N) binds to phosphorylated tyrosine residues and has cell-transforming activity. The N-terminal Cbl-type phosphotyrosine-binding (Cbl-PTB) domain is composed of three interacting domains: a four-helix bundle (4H), an EF-hand-like calcium-binding domain (see <PDOC00018>), and a divergent SH2-like domain (see <PDOC50001>). The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The three domains together form an integrated phosphoprotein-recognition module. The Cbl-PTB has also been named Cbl N-terminal (Cbl-N) or tyrosine kinase binding (TKB) domain [1,2].

The N-terminal 4H domain contains four long α-helices. The C and D helices in this domain pack against the adjacent EF-hand-like domain, and a highly conserved loop connecting the A and B helices contacts the SH2-like domain. The EF-hand motif is similar to classical EF-hand proteins. The SH2-like domain in Cbl-N retains the general helix-sheet-helix architecture of the SH2 fold, but lacks the secondary β-sheet, comprising β-strands D', E and F, and also a prominent BG loop (see <PDB:2CBL>) [1].

The profile we developed covers the entire Cbl-PTB domain.

Last update:

August 2010 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CBL_PTB, PS51506; Cbl-type phosphotyrosine-binding (Cbl-PTB) domain profile  (MATRIX)


References

1AuthorsMeng W. Sawasdikosol S. Burakoff S.J. Eck M.J.
TitleStructure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase.
SourceNature 398:84-90(1999).
PubMed ID10078535
DOI10.1038/18050

2AuthorsLangenick J. Araki T. Yamada Y. Williams J.G.
TitleA Dictyostelium homologue of the metazoan Cbl proteins regulates STAT signalling.
SourceJ. Cell. Sci. 121:3524-3530(2008).
PubMed ID18840649
DOI10.1242/jcs.036798



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