TRIM67, TNL (Kr.1q42.2) Aivon TRIM, järjestää mikrotubuluksia.

http://www.genecards.org/cgi-bin/carddisp.pl?gene=TRIM67
Tämä TRIM67 on TRIM9-kaltainen proteiini. TRIM9 on sen paralogi.
TRIM67 omaa fibronektiini tyyppi III-domaanin ( aminohappojakso 519-607).
tällä trimillä on myös COS- struktuuri C-terminaalissa (aminohappojakso 448-506).
Lisäksi on B30.4 /SPRY( aminohappojakso 589-780).
Aminohappoja on  783 kpl.

Aivoissa näyttää esiintyvän eniten. Vähän myös lisämunuaisessa.
Joitain artikkeleitakin on PubMed  tarjonnassa: Mikrotubuleille  tämäkin on tärkeä, (ja kuuluu samaan ryhmään sen puolesta kuin  MID1,MID2,TRIM9, TRIM36 ja TRIFIC. Niille on yhteistä COS-rakenne C-terminaalissa) . Ainakin  artikkeli 1. mainitsee TRIM67 eli TNL proteiinin.Siitä ei näytä olevan montaa arikkelia. 

Related articles in PubMed

1. Subclassification of the RBCC/TRIM superfamily reveals a novel motif necessary for microtubule binding. Short KM, et al. J Biol Chem, 2006 Mar 31. PMID 16434393 The biological significance of RBCC (N-terminal RING finger/B-box/coiled coil) proteins is increasingly being appreciated following demonstrated roles in disease pathogenesis, tumorigenesis, and retroviral protective activity. Found in all multicellular eukaryotes, RBCC proteins are involved in a vast array of intracellular functions; but as a general rule, they appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. Those members characterized to date have diverse C-terminal domain compositions and equally diverse subcellular localizations and functions. Using a bioinformatics approach, we have identified some new RBCC proteins that help define a subfamily that shares an identical domain arrangement (MID1, MID2, TRIM9, TNL, TRIM36, and TRIFIC). Significantly, we show that all analyzed members of this subfamily associate with the microtubule cytoskeleton, suggesting that subcellular compartmentalization is determined by the unique domain architecture, which may in turn reflect basic functional similarities. We also report a new motif called the COS box, which is found within these proteins, the MURF family, and a distantly related non-RBCC microtubule-binding protein. Notably, we demonstrate that mutations in the COS box abolish microtubule binding ability, whereas its incorporation into a nonmicrotubule-binding RBCC protein redirects it to microtubule structures. Further bioinformatics investigation permitted subclassification of the entire human RBCC complement into nine subfamilies based on their varied C-terminal domain compositions. This classification schema may aid the understanding of the molecular function of members of each subgroup and their potential involvement in both basic cellular processes and human disease.
2. Novel genetic loci identified for the pathophysiology of childhood obesity in the Hispanic population. Comuzzie AG, et al. PLoS One, 2012. PMID 23251661, Free PMC Article
3. The DNA sequence and biological annotation of human chromosome 1. Gregory SG, et al. Nature, 2006 May 18. PMID 16710414
4. Complete sequencing and characterization of 21,243 full-length human cDNAs. Ota T, et al. Nat Genet, 2004 Jan. PMID 14702039

See citations in PubMed for homologs of this gene provided by HomoloGene