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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Tripartite motif containing 17

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. 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. The protein localizes to cytoplasmic bodies. The protein is expressed almost exclusively in the testis, but its function is unknown. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Trim, Ubiquitin, ACID, CAN, V1a
Papers on RBCC
The effect of proteins from animal source foods on heme iron bioavailability in humans.
Arredondo et al., Santiago, Chile. In Food Chem, May 2016
Study 1 was focused on heme, red blood cell concentrate (RBCC), hemoglobin (Hb), RBCC+beef meat; study 2 on heme, heme+fish, chicken, and beef; and study 3 on heme and heme+purified animal protein (casein, collagen, albumin).
TRIM4; a novel mitochondrial interacting RING E3 ligase, sensitizes the cells to hydrogen peroxide (H2O2) induced cell death.
Singh et al., India. In Free Radic Biol Med, Dec 2015
In current study, we studied the role of TRIM4, a member of the TRIM/RBCC protein family of RING E3 ligase, in regulation of hydrogen peroxide (H2O2) induced cell death.
Promyelocytic Leukemia Protein Isoform II Promotes Transcription Factor Recruitment To Activate Interferon Beta and Interferon-Responsive Gene Expression.
Leppard et al., Coventry, United Kingdom. In Mol Cell Biol, May 2015
The unique C-terminal domain of PML-II was essential for its activity, while the N-terminal RBCC motif common to all PML isoforms was dispensable.
A zebrafish (Danio rerio) bloodthirsty member 20 with E3 ubiquitin ligase activity involved in immune response against bacterial infection.
Yao et al., Beijing, China. In Biochem Biophys Res Commun, Mar 2015
Deduced btr20 represents a RBCC-B30.2
TRIM family proteins: emerging class of RING E3 ligases as regulator of NF-κB pathway.
Singh et al., India. In Biol Cell, 2015
TRIMs, members of RING family of Ub E3 ligases, are characterised by the presence of three conserved domains, RING, B-Box and coiled-coil (RBCC).
Molecular characterization of a CpTRIM35-like protein and its splice variants from whitespotted bamboo shark (Chiloscyllium plagiosum).
Yao et al., Beijing, China. In Biochem Biophys Res Commun, 2014
Deduced CpTRIM35 has a RBCC-PRY/SPRY structure typical of TRIM proteins, and its splice variants (CpTRIM35-1-3) have different truncations at the C-terminus.
Terf/TRIM17 stimulates degradation of kinetochore protein ZWINT and regulates cell proliferation.
Inoue et al., Saitama, Japan. In J Biochem, 2012
the E3 ubiquitin ligase terf causes protein degradation of ZWINT and negatively regulates cell proliferation
MuRFs: specialized members of the TRIM/RBCC family with roles in the regulation of the trophic state of muscle and its metabolism.
Labeit et al., Liverpool, United Kingdom. In Adv Exp Med Biol, 2011
MuRFs, brief for muscle specific RING finger proteins, correspond to a subfamily of the TRIM/RBCC protein family.
TRIM proteins in cancer.
Pelicci et al., Milano, Italy. In Adv Exp Med Biol, 2011
Some members of the tripartite motif (TRIM/RBCC) protein family are thought to be important regulators of carcinogenesis.
PML nuclear bodies and other TRIM-defined subcellular compartments.
Freemont et al., London, United Kingdom. In Adv Exp Med Biol, 2011
Tripartite motif (TRIM) proteins are defined by their possession of a RING, B-box and predicted coiled coil (RBCC) domain.
TRIM proteins as RING finger E3 ubiquitin ligases.
Inoue et al., Saitama, Japan. In Adv Exp Med Biol, 2011
The tripartite motif(TRIM) proteins harboring the RING finger, B-box and coiled-coil (RBCC) domain motifs form a large protein family.
Arsenic trioxide controls the fate of the PML-RARalpha oncoprotein by directly binding PML.
Chen et al., Shanghai, China. In Science, 2010
Here we show that arsenic binds directly to cysteine residues in zinc fingers located within the RBCC domain of PML-RARalpha and PML.
TRIM44 interacts with and stabilizes terf, a TRIM ubiquitin E3 ligase.
Inoue et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2009
terf interacts with TRIM44;TRIM44 inhibited ubiquitination of terf, and thus stabilized the protein.
The NHL-domain protein Wech is crucial for the integrin-cytoskeleton link.
Hoch et al., Bonn, Germany. In Nat Cell Biol, 2008
The Wech protein contains a B-box zinc-finger and a coiled-coil domain, which is also found in RBCC/TRIM family members, and an NHL domain.
Rhesus monkey TRIM5alpha restricts HIV-1 production through rapid degradation of viral Gag polyproteins.
Ikeda et al., Rochester, United States. In Nat Med, 2007
TRIM5alpha comprises an RBCC (RING, B-box 2 and coiled-coil motifs) domain and a B30.2(SPRY) domain.
Efp targets 14-3-3 sigma for proteolysis and promotes breast tumour growth.
Inoue et al., Tokyo, Japan. In Nature, 2002
Efp, a target gene product of ER alpha, is a member of the RING-finger B-box coiled-coil (RBCC) motif family.
Gene encoding a new RING-B-box-Coiled-coil protein is mutated in mulibrey nanism.
Lehesjoki et al., Helsinki, Finland. In Nat Genet, 2000
MUL is ubiquitously expressed and encodes a new member of the RING-B-box-Coiled-coil (RBCC) family of zinc-finger proteins, whose members are involved in diverse cellular functions such as developmental patterning and oncogenesis.
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