A protein that binds RNA. Binding specificity can depend on nucleotide sequence, RNA secondary structure, chemical modification and other partners; recovery in an RNA pull-down alone does not establish direct recognition.
An RNA-binding protein that collaborates with Nanos and other factors in sequence-specific repression of target messenger RNAs.
An RNA-associated regulator of stress-granule assembly. Requirements for assembly depend on stress and partner context.
A Drosophila regulator whose RNA recognition supports sex-specific and autoregulatory splicing. It can act through competition at early recognition or through substrate-specific later spliceosomal interactions.
A common structured RNA-binding domain. Multiple motifs in a protein can recognize separated RNA segments and support geometry-dependent regulation.
A budding-yeast regulator that targets selected AU-rich transcripts for degradation during iron deficiency, reallocating resources away from iron-consuming processes.[ref]
Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation by Sergi Puig and others. Iron-deficiency-dependent target turnover
A family of microRNA-silencing effectors linking Argonaute-associated recognition to downstream repression and RNA-deadenylation machinery.[ref]
GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets by Joerg E. Braun and others. Direct recruitment interactions
A bacteriophage RNA-recognition module used as a complement to MS2 coat protein for experimental RNA recruitment and imaging.
A bacteriophage protein recognizing a defined RNA hairpin, used as a fusion partner in RNA tethering assays and RNA imaging. Hairpin arrays and bound fusion proteins can themselves perturb RNA behaviour.
A member of a repeat-containing protein family with major roles in organellar RNA recognition and regulation. Different members can support distinct processing, editing, stability or translational functions.
A plastid RNA-binding protein that can protect a bound region against exonucleolytic decay from either direction, helping define stable transcript termini.[ref]
Zipcode-binding protein 1, also known as IGF2BP1. It recognizes a localization element in beta-actin messenger RNA and can repress its biological translation during transport.[ref]
An insulin-like growth factor 2 messenger RNA-binding protein family member. Stabilization and enhanced biological translation of modified targets have been reported; this does not identify every modification-dependent stabilizer as an IGF2BP protein.[ref]
A protein that binds a poly(A) tail and can influence messenger RNA stability and biological translation.
A protein family that binds small guide RNAs and participates in sequence-directed regulation. Guide complementarity can identify targets, but cleavage activity varies among family members and pathways.
A germline nuclear Caenorhabditis elegans Argonaute required for maintenance of some inherited small-RNA-dependent silencing states.
Endonucleolytic target cleavage directed by a small-RNA guide and a catalytically competent Argonaute. Cleavage typically falls opposite guide positions 10 and 11; not all Argonautes can slice.
An Argonaute-family branch binding piRNAs. Cytoplasmic cleavage and nuclear transcriptional silencing protect the germline in many animals, with important species and tissue differences.
The Caenorhabditis elegans Piwi-family protein associated with 21U piRNAs and germline surveillance of RNA expression.
A mouse Piwi-family protein associated with fetal male germ-cell transposon repression and de novo DNA methylation.
A Drosophila Piwi-family protein participating in germline piRNA-mediated regulation, including ping-pong amplification.
A heterogeneous nuclear ribonucleoprotein involved in RNA processing. Its binding can respond to modification-dependent accessibility of an RNA motif.[ref]
A polypyrimidine-tract-binding RNA-binding protein family member involved in precursor-RNA processing and other aspects of gene expression.
A polypyrimidine-tract-binding protein with four RNA recognition motifs. Its splicing effects depend on site position, RNA geometry and other proteins; it is not exclusively a repressor.
A member of a family of sequence-selective RNA-binding proteins involved in regulating alternative splicing.
A member of a neural RNA-binding protein family with position-dependent effects on alternative splicing. Binding-site position helps predict activation or repression of exon inclusion.[ref]
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