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The protein encoded by TRIM3 is a member of the tripartite motif (TRIM) family, also called the 'RING-B-box-coiled-coil' (RBCC) subgroup of RING finger proteins. Additionally we are shipping Tripartite Motif Containing 3 Antibodies (81) and Tripartite Motif Containing 3 Kits (10) and many more products for this protein.
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TRIM3 plays a tumor-suppressing role in the regulation of liver cancer development by reducing cell proliferation through cell cycle arrest at the G0/G1 phase.
The results of quantitative real-time RT-PCR and western blotting showed that the TRIM3 expression was very low in five cervical cancer cell lines. The TRIM3 overexpression weakened cell viability, and promote apoptosis of C-33A and SiHa cells in vitro, and inhibit tumor growth in vivo, which suggested that TRIM3 could reduce proliferation of cervical cancer cells.
TRIM3 exerted an anti-proliferation role in rheumatoid arthritis fibroblast-like synoviocytes via p38 signaling pathway.
results support a novel role for Brat/TRIM3 in maintaining stem cell equilibrium and suppressing tumor growth by regulating NICD nuclear transport
TRIM3 functions as a tumour suppressor in CRC progression. This tumour-suppressive function is exerted partially through regulation of p53 protein.
Studies indicate most-studied TRIpartite Motif (TRIM)-NHL proteins TRIM2, TRIM3, TRIM32 and TRIM71, and their mutations have been linked to diseases.
TRIM3 may play a significant role in hepatocellular carcinoma progression.TRIM3 is downregulated in hepatocellular carcinoma at both the mRNA and protein levels and that low TRIM3 expression is correlated with an unfavorable prognosis.
TRIM3 acts as a tumor suppressor in GBM by restoring asymmetric cell division.
Data indicate TRIM3 and p21 interact in cells.
TRIM63 is a candidate for genes mediating the glucocorticoid-induced promotion of osteoblastic differentiation.
brain-expressed RING finger protein (BERP) is a gene whose expression is up-regulated in a p53-dependent manner
the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4, BERP, and myosin V that is necessary for efficient TfR recycling but not for EGFR degradation
Loss of heterozygosity of chromosome segment 11p15.5 in malignant gliomas suggests TRIM3 as a candidate brain tumor suppressor gene.
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also called the 'RING-B-box-coiled-coil' (RBCC) subgroup of RING finger proteins. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to cytoplasmic filaments. It is similar to a rat protein which is a specific partner for the tail domain of myosin V, a class of myosins which are involved in the targeted transport of organelles. The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin V-mediated cargo transport. Alternatively spliced transcript variants encoding the same isoform have been identified.
RING finger protein 97
, brain expressed ring finger
, brain-expressed RING finger protein
, ring finger protein 22
, tripartite motif protein TRIM3
, tripartite motif-containing 3
, tripartite motif-containing protein 3
, RING finger protein HAC1
, tripartite motif protein 3
, NHL repeat-containing protein 3