The ubiquitination of proteins. In the postsynaptic regions of excitatory synapses, a precise AMPAR trafficking is crucial for synaptic transmission. Benzoylaconine AMPARs, which form tetramers, consist of GluR1�C4 subunits. In the adult hippocampus, GluR1/GluR2 and GluR2/GluR3 complexes are predominant. Here, we introduce a transmembrane and ubiquitin-like domain-containing protein as a factor for AMPAR recycling. The protein was screened from in silico research, by its neuronal expression and domain characteristics; UBL domain and transmembrane domains. We found that the protein is related to the recycling pathway of GluR2-containing AMPAR complexes and consequently contributes to the maintenance of the basal synaptic transmission of AMPARs. In order to identify the functionally unknown UBLs in the brain, we performed bioinformatic analyses using the Celera human genome database and found 57 UBLs. Among them, 28 UBLs showed neuronal tissue expression, which was confirmed by the functional annotations of mouse-3 database. Intriguingly, we found that only one of them contained putative transmembrane domains as expected by the SOSUI system, which is a tool for secondary structure prediction from protein sequences. From further in silico search, it was predicted that the hydrophilic region is directed toward the cytoplasm and the first transmembrane domain serves as a signal peptide. The identified protein was “Transmembrane and ubiquitin-like domain-containing protein 1,” which is an official name of the gene, mRNA and protein of NCBI. This protein is also known as “Hepatocyte Odd Protein Shuttling ” in NCBI and was previously reported as the protein related with cellular proliferation in the liver. We refer to this protein as Tmub1/HOPS because it represents well the domain characteristics which used in our identification. Since the Tmub1/HOPS amino acid sequences were highly conserved between the human and mouse genomes, we used mouse brain cDNA libraries for cloning the full-length gene. In this study, we introduced the neuronal function of Tmub1/ HOPS that we screened by in silico analysis. This protein was initially identified as an overexpressed protein during liver regeneration after partial hepatectomy. Its overexpression interferes with protein synthesis and suppresses proliferation, while its depletion generates supernumerary centrosomes, multinucleated cells, and multipolar spindle formation in NIH3T3 cells. This protein is found in cytosolic complexes containing gamma-tubulin and CRM-1 in hepatoma cells and has been implicated as an essential constituent of centrosome assembly. The following findings of our present report are consistent with the findings of previous reports, i.e., the protein expression level of Tmub1/HOPS is low during normal conditions in the liver and that its signals show two bands on western blotting. In contrast, its localization and function appear to be slightly different. Previous reports show that Tmub1/HOPS is localized at the centrosome and is important for the normal proliferation of hepatoma cells, while our present study presents that Tmub1/HOPS exists widely including in cell body/neurites and plays a role in receptor trafficking within the neuron. Gammatubulin, which is localized to the centrosome in cycling cells, is present at the centrosome of neurons just beginning to extend their processes, while it is not associated with centrosomes in neurons in which functional synaptic Ergosterol connections have formed. This suggests that centrosomes exist in different fashions depending upon whether the cell is of the mitotic or postmitotic type.