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PROSITE documentation PDOC51262COS domain profile
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PURL: https://purl.expasy.org/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:
- Vertebrate MID1 and MID2, which associate with microtubules through homo- and heterodimerization.
- 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 sperm vesicle.
- Mammalian tripartite, fibronectin type III and C-terminal B30.2/SPRY (TRIFIC).
- 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>) 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 |
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