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Search results 1 to 2 out of 2 for Dazap1

Category restricted to ProteinDomain (x)

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Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 2 of DAZAP1.DAZAP1, initially identified as a binding partner of Deleted in Azoospermia (DAZ), is a multi-functional ubiquitous RNA-binding protein expressed most abundantly in the testis and is essential for normal cell growth, development, and spermatogenesis [, ]. DAZAP1 is a shuttling protein whose acetylated form is predominantly nuclear and the nonacetylated form is in cytoplasm []. DAZAP1 also functions as a translational regulator that activates translation in an mRNA-specific manner []. It also interacts with numerous hnRNPs, including hnRNP U, hnRNP U like-1, hnRNPA1, hnRNPA/B, and hnRNP D, suggesting DAZAP1 might associate and cooperate with hnRNP particles to regulate adenylate-uridylate-rich elements (AU-rich element or ARE)-containing mRNAs [, ]. DAZAP1 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal proline-rich domain [].
Protein Domain
Type: Domain
Description: This entry represents the RNA recognition motif 1 of DAZAP1.DAZAP1, initially identified as a binding partner of Deleted in Azoospermia (DAZ), is a multi-functional ubiquitous RNA-binding protein expressed most abundantly in the testis and is essential for normal cell growth, development, and spermatogenesis [, ]. DAZAP1 is a shuttling protein whose acetylated form is predominantly nuclear and the nonacetylated form is in cytoplasm []. DAZAP1 also functions as a translational regulator that activates translation in an mRNA-specific manner []. It also interacts with numerous hnRNPs, including hnRNP U, hnRNP U like-1, hnRNPA1, hnRNPA/B, and hnRNP D, suggesting DAZAP1 might associate and cooperate with hnRNP particles to regulate adenylate-uridylate-rich elements (AU-rich element or ARE)-containing mRNAs [, ]. DAZAP1 contains two N-terminal RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a C-terminal proline-rich domain [].