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Search results 1 to 6 out of 6 for Rbm15

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of RBM15.RNA-binding motif protein 15 (RBM15), also termed one-twenty two protein 1 (OTT1), is a novel mRNA export factor and component of the NXF1 pathway. It binds to NXF1 and serves as receptor for the RNA export element RTE []. It also possesses mRNA export activity and can facilitate the access of DEAD-box protein DBP5 to mRNA at the nuclear pore complex (NPC) []. RBM15 belongs to the Spen (split end) protein family, which contains three N-terminal RNA recognition motifs (RRMs), and a C-terminal SPOC (Spen paralogue and orthologue C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 (RRM1) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of RBM15B.RNA binding motif protein 15B (RBM15B, also known as OTT3) is a paralogue of RBM15. Like RBM15, RBM15B has post-transcriptional regulatory activity. It is a nuclear protein sharing with RBM15 the association with the splicing factor compartment and the nuclear envelope as well as the binding to mRNA export factors NXF1 and Aly/REF [].RBM15B belongs to the Spen (split end) protein family, which shares a domain architecture comprising three N-terminal RNA recognition motifs (RRMs) and a C-terminal SPOC (Spen paralog and ortholog C-terminal) domain.