Post Translational Modifications | Phosphorylation on Ser-309 is induced upon cell muscle differentiation. Phosphorylated. Phosphorylated in vitro on Ser-309 by SRPK1. Phosphorylation on Ser-309 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation. |
Function | RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCGGCA-3' motif in vitro. |
Protein Name | Rna-Binding Protein 4Lark HomologHlarkRna-Binding Motif Protein 4Rna-Binding Motif Protein 4a |
Database Links | Reactome: R-HSA-400253 |
Cellular Localisation | NucleusNucleolusNucleus SpeckleCytoplasmCytoplasmic GranuleUndergoes Continuous Nucleocytoplasmic ShuttlingUpon Nuclear Import Colocalizes With Sr Proteins In Nuclear SpecklesArsenite Stress-Induced Phosphorylation Increases Its Subcellular Relocalization From The Nucleus To The Cytoplasm And To Cytoplasmic Stress Granules (Sg) Via A P38 Mapk Signaling PathwayPrimarily Localized In Nucleus And Nucleoli Under Cell Growth Conditions And Accumulated In The Cytoplasm And Cytoplasm Perinuclear Granules Upon Muscle Cell Differentiation |
Alternative Antibody Names | Anti-Rna-Binding Protein 4 antibodyAnti-Lark Homolog antibodyAnti-Hlark antibodyAnti-Rna-Binding Motif Protein 4 antibodyAnti-Rna-Binding Motif Protein 4a antibodyAnti-RBM4 antibodyAnti-RBM4A antibody |
Information sourced from Uniprot.org