COS domain
IPR017903
Definition
N-terminal RING finger/B-box/coiled coil (RBCC) or tripartite motif (TRIM) proteins, which are found in metazoa, 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 or fibronectin type-III (FN3) domains. The COS domain is predicted to consist of two α-helical coils PMID:16434393.
12 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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