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PROSITE documentation PDOC51262 |
N-terminal RING finger (see <PDOC00449>)/B-box (see <PDOC50119>)/coiled coil (RBCC) or tripartite motif (TRIM) proteins, which are found in metazoan, are involved in a vast array of intracellular functions. They appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. The following RBCC proteins contain an ~60-residue COS (C-terminal subgroup one signature) domain, which is also found in a distantly related non-RBCC microtubule-binding protein, GLFND:
In addition to RBCC, the COS domain is also found in association with B30.2/SPRY (see <PDOC50188>) or fibronectin type-III (FN3) (see <PDOC50853>) domains.
The COS domain is predicted to consist of two α-helical coils [1].
The profile we developed covers the entire COS domain.
Last update:November 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Short K.M. Cox T.C. |
Title | Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding. | |
Source | J. Biol. Chem. 281:8970-8980(2006). | |
PubMed ID | 16434393 | |
DOI | 10.1074/jbc.M512755200 |