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:
Vertebrate MID1 and MID2, which associate with microtubules through homo-
Animal TRIM9, which plays a regulatory role in synaptic vesicle exocytosis.
Mammalian TRIM nine-like (TNL).
Mammalian TRIM36, which could play a regulatory role in exocytosis of the
Mammalian tripartite, fibronectin type III and C-terminal B30.2/SPRY
Mammalian muscle-specific RING finger (MURF) family. MURF proteins have an
ability to form both homo- and heterodimers with each other and to
associate with the microtubule cytoskeleton.
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>)
The COS domain is predicted to consist of two α-helical coils .
The profile we developed covers the entire COS domain.
November 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Short K.M. Cox T.C.
Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding.
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