This entry represents a domain found at the N terminus of nuclear valosin-containing protein (VCP)-like protein 2 (NVL2). This domain adopts a three helix fold resembling part of a winged helix motif and binds to nucleolin, a multifunctional phosphoprotein ubiquitously distributed in the nucleolus, nucleus and cytoplasm of the cell [].
This entry represents the RNA recognition motif 1 (RRM1) of a group of plant nucleolin-like proteins, including nucleolin 1 (also termed protein nucleolin like 1) and nucleolin 2 (also termed protein nucleolin like 2, or protein parallel like 1). They play roles in the regulation of ribosome synthesis and in the growth and development of plants [, ]. Like yeast nucleolin, nucleolin-like proteins possess two RNA recognition motifs (RRMs).
This entry represents the RNA recognition motif 2 (RRM2) of a group of plant nucleolin-like proteins, including nucleolin 1 (also termed protein nucleolin like 1) and nucleolin 2 (also termed protein nucleolin like 2, or protein parallel like 1). They play roles in the regulation of ribosome synthesis and in the growth and development of plants [, ]. Like yeast nucleolin, nucleolin-like proteins possess two RNA recognition motifs (RRMs).
This entry represents the RNA recognition motif 1 (RRM1) of ubiquitously expressed protein nucleolin.Nucleolin is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc [, ]. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities []. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta [, ]. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe []and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG, NG-dimethylarginines. RRM1, together with RRM2, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop [].
This entry represents the RNA recognition motif 2 (RRM2) of ubiquitously expressed protein nucleolin.Nucleolin is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc[, ]. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities []. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta [, ]. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe []and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG, NG-dimethylarginines. RRM1, together with RRM2, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop [].
This entry represents the RNA recognition motif 3 (RRM3) of ubiquitously expressed protein nucleolin.Nucleolin is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc [, ]. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities []. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta [, ]. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe []and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG, NG-dimethylarginines. RRM1, together with RRM2, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop [].
This entry represents the RNA recognition motif 4 (RRM4) of ubiquitously expressed protein nucleolin.Nucleolin is a multifunctional major nucleolar phosphoprotein that has been implicated in various metabolic processes, such as ribosome biogenesis, cytokinesis, nucleogenesis, cell proliferation and growth, cytoplasmic-nucleolar transport of ribosomal components, transcriptional repression, replication, signal transduction, inducing chromatin decondensation, etc [, ]. Nucleolin exhibits intrinsic self-cleaving, DNA helicase, RNA helicase and DNA-dependent ATPase activities []. It can be phosphorylated by many protein kinases, such as the major mitotic kinase Cdc2, casein kinase 2 (CK2), and protein kinase C-zeta [, ]. Nucleolin shares similar domain architecture with gar2 from Schizosaccharomyces pombe []and NSR1 from Saccharomyces cerevisiae. The highly phosphorylated N-terminal domain of nucleolin is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of nucleolin contains four closely adjacent N-terminal RNA recognition motifs (RRMs), which suggests that nucleolin is potentially able to interact with multiple RNA targets. The C-terminal RGG (or GAR) domain of nucleolin is rich in glycine, arginine and phenylalanine residues, and contains high levels of NG, NG-dimethylarginines. RRM1, together with RRM2, binds specifically to RNA stem-loops containing the sequence (U/G)CCCG(A/G) in the loop [].
This entry contains proteins with a BING4-like, C-terminal domain. WD repeat-containing protein 46 (WDR46) is a component of the nuclear scaffold, which is an insoluble structure that contributes to the inner nuclear organization. WDR46 is a fundamental scaffold component of the nucleolar structure, binding nucleolin and DDX21 []. Also in this family is U3 small nucleolar RNA-associated protein 7 (UTP7) from baker's yeast, which is involved in nucleolar processing of pre-18S ribosomal RNA [].
This entry represents the RNA recognition motif 1 (RRM1) of yeast protein Gar2, a novel nucleolar protein required for 18S rRNA and 40S ribosomal subunit accumulation []. It shares similar domain architecture with nucleolin from vertebrates []and Nsr1 from Saccharomyces cerevisiae []. The highly phosphorylated N-terminal domain of Gar2 is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of Gar2 contains two closely adjacent RNA recognition motifs (RRMs). The C-terminal RGG (or GAR) domain of gar2 is rich in glycine, arginine and phenylalanine residues [].
This entry represents the RNA recognition motif 2 (RRM2) of yeast protein Gar2, a novel nucleolar protein required for 18S rRNA and 40S ribosomal subunit accumulation []. It shares similar domain architecture with nucleolin from vertebrates []and Nsr1 from Saccharomyces cerevisiae []. The highly phosphorylated N-terminal domain of Gar2 is made up of highly acidic regions separated from each other by basic sequences, and contains multiple phosphorylation sites. The central domain of Gar2 contains two closely adjacent RNA recognition motifs (RRMs). The C-terminal RGG (or GAR) domain of gar2 is rich in glycine, arginine and phenylalanine residues [].
