"mRNA"

Supplier: Bioss

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

Supplier: Bioss

Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.

Supplier: ProSci Inc.

DCP1B may play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It may remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.DCP1B is a core component of the mRNA decapping complex, a key factor in the regulation of mRNA decay (Lykke-Andersen, 2002 [PubMed 12417715]).

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA.

Supplier: Bioss

Heterogeneous nuclear ribonucleoproteins (hnRNPs) constitute a set of polypeptides that contribute to mRNA transcription, pre-mRNA processing as well as mature mRNA transport to the cytoplasm and translation. They also bind heterogeneous nuclear RNA (hnRNA), which are the transcripts produced by RNA polymerase II. There are approximately 20 known hnRNP proteins, and their complexes are the major constituents of the spliceosome. The majority of hnRNP proteins components are localized to the nucleus; however some shuttle between the nucleus and the cytoplasm, such as hnRNP E1 and E2. hnRNP E1 may function in the cytoplasm as a translational regulatory protein, while hnRNP E2 stabilizes mRNA to enhance polioviral mRNA translation. hnRNP M is involved in pre-mRNA splicing and in stress-induced transient splicing arrest.

Supplier: ProSci Inc.

LIN28 acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. The association of LIN28 with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. IT binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. LIN28 is Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.

Supplier: Bioss

The multiprotein exon junction complex (EJC) is deposited on mRNAs upstream of exon–exon junctions as a consequence of pre-mRNA splicing. In mammalian cells, this complex serves as a key modulator of spliced mRNA metabolism. MLN51 is a nucleocytoplasmic shuttling protein that is overexpressed in breast cancer. The function of MLN51 in mammals remains elusive. Its fly homolog, named barentsz, as well as the proteins mago nashi and tsunagi have been shown to be required for proper oskar mRNA localization to the posterior pole of the oocyte. Magoh and Y14, the human homologs of mago nashi and tsunagi, are core components of the exon junction complex (EJC). The EJC is assembled on spliced mRNAs and plays important roles in post-splicing events including mRNA export, nonsense-mediated mRNA decay, and translation. Human MLN51 is an RNA-binding protein present in ribonucleo-protein complexes.