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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 (68) and Tripartite Motif Containing 3 Kits (5) and many more products for this protein.
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Studies indicate most-studied TRIpartite Motif (TRIM (show TRAT1 Proteins))-NHL proteins TRIM2 (show TRIM2 Proteins), TRIM3, TRIM32 (show TRIM32 Proteins) and TRIM71 (show TRIM71 Proteins), 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 (show CDKN1A Proteins) interact in cells.
TRIM63 (show TRIM63 Proteins) 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 (show TP53 Proteins)-dependent manner
the endosome-associated protein hrs is a subunit of a protein complex containing actinin-4 (show ACTN4 Proteins), BERP, and myosin V (show MYO5A Proteins) that is necessary for efficient TfR (show TFRC Proteins) recycling but not for EGFR (show EGFR Proteins) degradation
Loss of heterozygosity of chromosome segment 11p15.5 in malignant gliomas suggests TRIM3 as a candidate brain tumor suppressor gene.
Temporal control of gamma-actin (show ACTG1 Proteins) levels by TRIM3 is required to regulate the timing of hippocampal plasticity.
TRIM3, also known as BERP, interacts with KIF21B via its RBCC (show TRIM17 Proteins) domain.
the RING domain is required for TRIM3-induced growth suppression.
Data indicate TRIM3 and p21 interact in cells.
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.
tripartite motif-containing 3
, RING finger protein 97
, brain expressed ring finger
, brain-expressed RING finger protein
, ring finger protein 22
, tripartite motif protein TRIM3
, tripartite motif-containing protein 3
, RING finger protein HAC1
, tripartite motif protein 3