CIRBP (cold-inducible RNA-binding protein; also known as A18 hnRNP / CIRP) is a small (172 aa) stress-responsive RNA-binding protein built from an N-terminal canonical RRM domain and a C-terminal intrinsically disordered, arginine/glycine-rich (RGG/RG) region that also contains an arginine-serine-tyrosine (RSY) motif. It is induced by mild hypothermia (cold shock) as well as UV irradiation, hypoxia and other cellular stresses. CIRBP binds primarily the 3'-untranslated regions of target transcripts and acts post- transcriptionally to stabilize stress- and survival-related mRNAs (e.g. RPA2, thioredoxin/TXN) and to modulate their translation; it associates with ribosomes and the translation initiation factor eIF4G1 and can enhance translation of its stabilized targets while acting as a translational repressor when sequestered in cytoplasmic stress granules. CIRBP is predominantly nuclear (nucleoplasm) at steady state and shuttles to the cytoplasm and into stress granules upon stress; nuclear import is mediated by Transportin-1 (recognizing the RG/RGG region) and Transportin-3 (recognizing the RSY motif), and its localization and phase behavior are tuned by arginine methylation (PRMT1) and phosphorylation (CK2, GSK3B, SRPK1). Functionally it contributes to cold-induced suppression of cell proliferation and to protection against genotoxic/oxidative stress. A distinct, extensively studied moonlighting activity is that of extracellular CIRP (eCIRP): when released from stressed or dying cells it acts as a damage-associated molecular pattern that engages receptors such as TLR4/MD2, TREM-1 and IL-6R to promote inflammation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003729 mRNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic (IBA) annotation that CIRBP binds mRNA. This is well supported by direct experimental evidence for binding the 3'-UTRs of specific mRNAs and by unbiased mRNA- interactome capture studies, and reflects the core molecular function of the protein. Reason: CIRBP is a bona fide mRNA-binding protein; the IBA term is at an appropriate level of generality and is corroborated by IDA/HDA evidence (mRNA 3'-UTR binding; RNA-binding atlases). Supporting Evidence: PMID:11574538 A18 hnRNP binds specifically to the 3'-untranslated region of RPA2 transcript independently of its poly(A) tail |
| GO:0000398 mRNA splicing, via spliceosome | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetic (IBA) propagation of a splicing role from the broader hnRNP/RBM family. There is no direct experimental evidence that CIRBP functions in pre-mRNA splicing; its characterized activities are 3'-UTR binding, mRNA stabilization and translational control. CIRBP co-purifies with the spliceosome in high-throughput interaction maps, but copurification is not evidence of a splicing function. Reason: The defining and experimentally supported functions of CIRBP are post-transcriptional (mRNA stability and translation), not splicing. The comprehensive literature review of CIRBP does not attribute a splicing function to it. PANTHER PAINT analysis (see file:interpro/panther/PTHR48034/PTHR48034-review.md) shows this IBA descends from internal node PTN000391532, whose splicing IBD is seeded only by transformer-2/RBMX splicing factors (TRA2A Q13595, TRA2B P62995, RBMX P38159, Drosophila tra2 FBgn0003742, rat Tra2 RGD:1306751/RGD:1565256). CIRBP's own subfamily node (PTN008729690) carries only the generic, correct 'mRNA binding' term. The splicing annotation is therefore an over-propagation across a functional-divergence boundary (splicing-factor branch vs. cold-inducible mRNA-stability branch). Supporting Evidence: PMID:22365833 More than 200 proteins copurify with spliceosomes |
| GO:0005681 spliceosomal complex | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Phylogenetic (IBA) localization to the spliceosomal complex, inherited from spliceosome-associated paralogs. CIRBP appears in spliceosome protein-interaction maps, but it is not a recognized core spliceosomal component and the primary literature does not describe it acting within the spliceosome. Reason: As with the splicing process term, there is no direct evidence CIRBP is a functional part of the spliceosome; the annotation reflects family-level propagation rather than CIRBP-specific data. Per PANTHER PAINT (file:interpro/panther/PTHR48034/PTHR48034-review.md), the spliceosomal-complex IBD at node PTN000391532 is seeded only by the splicing factors TRA2B (P62995), RBMX (P38159) and rat Tra2 (RGD:1306751); it was propagated to the diverged cold-inducible CIRBP/RBM3 branch, whose subfamily node carries only 'mRNA binding'. Supporting Evidence: PMID:22365833 More than 200 proteins copurify with spliceosomes |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro-based electronic annotation of generic nucleic acid binding, derived from the RRM domain. Correct but very general; the more specific RNA-binding / mRNA 3'-UTR binding terms better capture the function. Reason: The term is accurate (CIRBP has an RRM and binds nucleic acid) and a broad IEA parent is acceptable; more specific terms are present elsewhere in the annotation set. |
| GO:0003723 RNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro-based electronic annotation of RNA binding from the RRM domain. Strongly supported by direct and high-throughput evidence. Reason: CIRBP is an RRM-containing RNA-binding protein; the term is correct and well supported. |
| GO:0005654 nucleoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Electronic annotation (UniProt subcellular location mapping) placing CIRBP in the nucleoplasm. Consistent with immunofluorescence showing nucleoplasmic localization at steady state and with the IDA HPA annotation. Reason: Nucleoplasmic localization is well established for CIRBP under unstressed conditions. Supporting Evidence: PMID:9151692 CIRP was localized in the nucleoplasm of BALB/3T3 mouse fibroblasts |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Electronic annotation of cytoplasmic localization. CIRBP translocates from the nucleus to the cytoplasm upon UV and other stresses, where it carries out much of its mRNA- stabilizing/translational function; supported by IDA (PMID:11574538). Reason: Stress-induced cytoplasmic localization is experimentally documented. Supporting Evidence: PMID:11574538 is induced and translocated from the nuclei to the cytoplasm after exposure to UV radiation |
| GO:0009409 response to cold | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA machine-learning electronic annotation of response to cold. This is the defining property of CIRBP (cold-inducible) and is independently supported by the founding study and a TAS annotation. Reason: Cold-inducibility and a role in the cold-stress response are the hallmark features of CIRBP. Supporting Evidence: PMID:9151692 CIRP plays an essential role in cold-induced growth suppression of mouse fibroblasts |
| GO:0017148 negative regulation of translation | IEA GO_REF:0000108 | ACCEPT | Summary: Inferred electronically from the translation repressor activity (GO:0030371) annotation. Consistent with CIRBP acting as a translational repressor when recruited into stress granules and via its RGG domain. Reason: CIRBP can repress translation (notably in stress granules), so this process term is appropriate; it is context-dependent and complementary to its positive regulation of translation of stabilized targets. Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md under severe stress, CIRBP is recruited to stress granules |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | ACCEPT | Summary: Protein-protein interaction (high-throughput interactome) annotation. Uninformative as a molecular function; retained as a valid interaction record (partner RBMX). Reason: Valid interaction evidence but the generic 'protein binding' term conveys no specific molecular function; kept as-is per convention. |
| GO:0005515 protein binding | IPI PMID:16713569 A protein-protein interaction network for human inherited at... | ACCEPT | Summary: Interaction with ATXN1 from an inherited-ataxia interaction network screen. Uninformative generic term; retained as an interaction record. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | ACCEPT | Summary: High-throughput interaction (partner HNRNPK). Uninformative generic term; retained as an interaction record. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | ACCEPT | Summary: Interaction detected in the human spliceosome protein-interaction map (partner HNRNPK). Uninformative generic term; also note this is the source of the spliceosome-association (over-annotated) terms above. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | ACCEPT | Summary: Multiple interactions from a proteome-scale binary interactome map (partners include SNRPA, RBMX, RBMY, HNRNPK, KHDRBS2, LNX1). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m... | ACCEPT | Summary: High-throughput interaction (partner HNRNPK). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | ACCEPT | Summary: High-throughput interaction (partners SNRPA, KHDRBS2). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:32234784 Nonclassical nuclear localization signals mediate nuclear im... | ACCEPT | Summary: Interaction with the nuclear import receptors Transportin-1 (TNPO1) and Transportin-3 (TNPO3). Although recorded as generic 'protein binding', this interaction is functionally meaningful: TNPO1 recognizes the RG/RGG region and TNPO3 the RSY motif to mediate CIRBP nuclear import. Reason: Valid and functionally important interaction; the generic term itself is non-specific but correct. Supporting Evidence: PMID:32234784 both TNPO1 and Transportin-3 (TNPO3) recognize two nonclassical NLSs within the cold-inducible RNA-binding protein (CIRBP) |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | ACCEPT | Summary: High-throughput binary interactome interactions (partners HNRNPK, SRSF3). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | ACCEPT | Summary: Interaction from a neurodegenerative-disease interactome map (partner ATXN1). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | ACCEPT | Summary: High-throughput interaction (partner TNPO3) from a cell-specific interactome remodeling study. Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | ACCEPT | Summary: Endogenous-tagging (OpenCell) interaction (partner TNPO3). Uninformative generic term; retained. Reason: Valid interaction evidence; 'protein binding' is non-specific. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Direct immunofluorescence (Human Protein Atlas) annotation of nucleoplasmic localization, consistent with the steady-state nuclear localization of CIRBP. Reason: Well-supported localization; CIRBP is predominantly nucleoplasmic when unstressed. Supporting Evidence: PMID:9151692 CIRP was localized in the nucleoplasm of BALB/3T3 mouse fibroblasts |
| GO:0005634 nucleus | HDA PMID:16791210 Dynamic proteomics in individual human cells uncovers widesp... | ACCEPT | Summary: High-throughput proteomic (dynamic proteomics) annotation of nuclear localization. Consistent with the established predominantly nuclear localization of CIRBP. Reason: Nuclear localization is well established. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: CIRBP identified as an RNA-binding protein in an unbiased mRNA-interactome capture atlas (UV crosslinking + oligo(dT)) in HeLa cells. Strong, direct high-throughput support for RNA binding. Reason: Robust experimental evidence that CIRBP binds mRNA in cells. Supporting Evidence: PMID:22658674 We identify 860 proteins that qualify as RBPs by biochemical and statistical criteria |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: CIRBP identified in a second, independent mRNA-bound proteome study (HEK293, photoreactive nucleotide crosslinking). Corroborates RNA binding. Reason: Independent high-throughput evidence for RNA binding. Supporting Evidence: PMID:22681889 nearly one-third were not previously annotated as RNA binding |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of nuclear localization from an ortholog. Consistent with direct evidence (IDA/HDA) for nuclear localization of CIRBP. Reason: Nuclear localization is independently supported by experimental evidence. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of cytoplasmic localization. Consistent with stress-induced nucleus-to-cytoplasm translocation documented by IDA. Reason: Cytoplasmic localization is independently supported by experimental evidence. |
| GO:0009411 response to UV | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct evidence that CIRBP (A18 hnRNP) is induced by UV, translocates to the cytoplasm, and stabilizes UV/stress-responsive transcripts; cells with reduced CIRBP are more sensitive to UV. Strong support for a role in the UV response. Reason: Experimentally demonstrated participation in the genotoxic/UV stress response. Supporting Evidence: PMID:11574538 is induced and translocated from the nuclei to the cytoplasm after exposure to UV radiation |
| GO:0010494 cytoplasmic stress granule | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of stress granule localization. CIRBP is recruited into cytoplasmic stress granules upon various stresses (methylation of its RGG motif is a prerequisite), so this localization is well supported by the broader literature. Reason: Stress granule localization of CIRBP is documented; the ISS term is consistent with direct studies of SG recruitment. Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md Methylation of arginine residues within the RGG motif is essential for CIRBP recruitment to stress granules |
| GO:0030371 translation repressor activity | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of translation repressor activity. The C-terminal RGG domain mediates translational repression, and CIRBP acts as a translational repressor when recruited into stress granules. This is context-dependent: CIRBP can also enhance translation of specific stabilized targets via eIF4G1. Reason: Translational repression is a documented activity of CIRBP, complementing its positive regulation of translation of stabilized transcripts. Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md under severe stress, CIRBP is recruited to stress granules |
| GO:0034063 stress granule assembly | ISS GO_REF:0000024 | ACCEPT | Summary: Sequence-similarity transfer of a role in stress granule assembly. UniProt notes that CIRBP promotes assembly of stress granules when overexpressed, and its RGG-dependent phase separation underlies SG recruitment. Reason: Consistent with CIRBP's documented role in promoting/participating in stress granule formation. Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md Methylation of arginine residues within the RGG motif is essential for CIRBP recruitment to stress granules |
| GO:0070181 small ribosomal subunit rRNA binding | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | UNDECIDED | Summary: IDA annotation of small ribosomal subunit rRNA binding citing PMID:11574538. The cached abstract of this paper describes CIRBP binding to mRNA 3'-UTRs (RPA2, TXN), not to ribosomal RNA; the full text is not available in the cache, so the specific evidence for rRNA binding cannot be verified here. CIRBP does associate with ribosomes (PMID:16513844), but ribosome association is not equivalent to small-subunit rRNA binding. Reason: The supporting evidence for rRNA (as opposed to mRNA) binding cannot be confirmed from the available (abstract-only) text, and the abstract foregrounds mRNA 3'-UTR binding. Per curation guidance, an experimental annotation should not be removed on incomplete evidence; full text is required to confirm or correct this term. Supporting Evidence: PMID:11574538 A18 hnRNP binds specifically to the 3'-untranslated region of RPA2 transcript independently of its poly(A) tail |
| GO:0003730 mRNA 3'-UTR binding | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct demonstration that CIRBP (A18 hnRNP) binds specifically to the 3'-UTR of the RPA2 transcript. This is the most specific and informative molecular-function annotation for CIRBP and represents a core function. Reason: Sequence-specific 3'-UTR binding is the experimentally defined molecular activity through which CIRBP regulates target mRNA stability and translation. Supporting Evidence: PMID:11574538 A18 hnRNP binds specifically to the 3'-untranslated region of RPA2 transcript independently of its poly(A) tail |
| GO:0003730 mRNA 3'-UTR binding | IDA PMID:16513844 Post-transcriptional regulation of thioredoxin by the stress... | ACCEPT | Summary: Independent direct evidence that the CIRBP RRM and RGG domains both bind the thioredoxin (TXN) 3'-UTR. Corroborates the core 3'-UTR-binding molecular function. Reason: Second experimental demonstration of sequence-specific 3'-UTR binding (TXN), reinforcing this as a core function. Supporting Evidence: PMID:16513844 the heterogenous ribonucleoprotein A18 (hnRNP A18) RNA Binding Domain (RBD) and the arginine, glycine (RGG) rich domain can bind TRX 3'-untranslated region (3'-UTR) independently |
| GO:0005515 protein binding | IPI PMID:16513844 Post-transcriptional regulation of thioredoxin by the stress... | ACCEPT | Summary: Interaction with EIF4G1 (eukaryotic translation initiation factor 4 gamma 1). Recorded as generic 'protein binding', but mechanistically important: CIRBP interacts with eIF4G to promote translation of its target transcripts and associates with ribosomes. Reason: Valid and functionally significant interaction; the generic term is correct but uninformative. Supporting Evidence: PMID:16513844 hnRNP A18 increases TRX translation and interacts with the eukaryotic Initiation Factor 4G (eIF4G) |
| GO:0005634 nucleus | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct evidence of nuclear localization of CIRBP, which translocates to the cytoplasm after UV exposure. Consistent with all other localization evidence. Reason: Experimentally documented nuclear localization (steady state). Supporting Evidence: PMID:11574538 is induced and translocated from the nuclei to the cytoplasm after exposure to UV radiation |
| GO:0005737 cytoplasm | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct evidence of cytoplasmic localization of CIRBP following UV-induced translocation, where it stabilizes target transcripts and enhances their translation. Reason: Experimentally documented stress-induced cytoplasmic localization. Supporting Evidence: PMID:11574538 is induced and translocated from the nuclei to the cytoplasm after exposure to UV radiation |
| GO:0045727 positive regulation of translation | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct evidence that overexpression of CIRBP increases the stability of target mRNAs and consequently enhances their translation in a dose-dependent manner. A core post- transcriptional regulatory function for its stabilized targets. Reason: Experimentally demonstrated enhancement of translation of stabilized target mRNAs. Supporting Evidence: PMID:11574538 Overexpression of A18 hnRNP increases the mRNAs stability and consequently enhances translation in a dose-dependent manner |
| GO:0048255 mRNA stabilization | IDA PMID:11574538 The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a... | ACCEPT | Summary: Direct evidence that CIRBP increases the stability of bound target mRNAs (e.g. RPA2, TXN), a core function executed through 3'-UTR binding. Reason: Experimentally demonstrated mRNA-stabilizing activity; this is a central, defining function of CIRBP. Supporting Evidence: PMID:11574538 Overexpression of A18 hnRNP increases the mRNAs stability and consequently enhances translation in a dose-dependent manner |
| GO:0009409 response to cold | TAS PMID:9151692 A glycine-rich RNA-binding protein mediating cold-inducible ... | ACCEPT | Summary: Traceable author statement from the founding study, which showed that CIRP is induced on cooling (37 to 32 C) and mediates cold-induced suppression of cell growth. Defines the hallmark cold-stress role of CIRBP. Reason: The cold-stress response is the original and defining function of CIRBP, supported by direct experiments in the cited paper. Supporting Evidence: PMID:9151692 CIRP plays an essential role in cold-induced growth suppression of mouse fibroblasts |
| GO:0005576 extracellular region | TAS file:human/CIRBP/CIRBP-deep-research-falcon.md | NEW | Summary: Not present in current GOA. Extensively documented in the literature: under severe stress (hemorrhagic shock, sepsis, ischemia-reperfusion) CIRBP is released from cells into the extracellular space as extracellular CIRP (eCIRP) via unconventional secretion. This is a moonlighting/released location distinct from its intracellular RNA-binding role. Reason: The extracellular localization of CIRBP (eCIRP) is a well-established, heavily studied aspect of its biology that is missing from the current annotation set; adding it captures the location where its DAMP function occurs. Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md is released into the extracellular space as extracellular CIRP |
| GO:0050729 positive regulation of inflammatory response | TAS file:human/CIRBP/CIRBP-deep-research-falcon.md | NEW | Summary: Not present in current GOA. As a released damage-associated molecular pattern (eCIRP), CIRBP promotes inflammation by engaging receptors including TLR4/MD2, TREM-1 and IL-6R, driving pro-inflammatory cytokine production and inflammatory cell death. This is a moonlighting function of the extracellular protein rather than its evolved intracellular RNA-binding activity. Reason: The pro-inflammatory DAMP activity of eCIRP is one of the most studied aspects of CIRBP biology and is absent from the existing annotations; it should be captured (as a non-core, extracellular function). Supporting Evidence: file:human/CIRBP/CIRBP-deep-research-falcon.md When released extracellularly as eCIRP, it functions as a potent DAMP, engaging TLR4, TREM-1, and IL-6R to drive inflammation |
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Download this section (compressed HTML)Q: Does CIRBP genuinely bind small ribosomal subunit rRNA (GO:0070181), or does the existing IDA annotation reflect its documented association with ribosomes/mRNPs rather than direct rRNA binding?
Suggested experts: Carrier F, Yang R
Q: Should the extracellular DAMP activity of CIRBP (eCIRP) be formally captured in GO as a moonlighting function distinct from its intracellular RNA-binding role, and what is the most appropriate term set (e.g. extracellular space, positive regulation of inflammatory response, Toll-like receptor binding)?
Suggested experts: Aziz M, Wang P
Experiment: Perform transcriptome-wide CLIP-seq (e.g. iCLIP/eCLIP) for endogenous CIRBP under basal and cold/UV stress, integrated with RNA stability (e.g. SLAM-seq) and ribosome profiling, to define direct binding sites (3'-UTR enrichment), stabilized targets, and translational effects; test for any splicing changes to evaluate the spliceosome-associated annotations.
Hypothesis: CIRBP's core in vivo molecular function is sequence-specific 3'-UTR binding that stabilizes a defined regulon of stress/survival transcripts, rather than a general role in splicing.
Type: CLIP-seq with RNA stability and ribosome profiling
Experiment: Use in vitro binding assays (EMSA/filter binding, SPR) with purified CIRBP against defined mRNA 3'-UTR fragments versus 18S rRNA, plus CLIP recovery of rRNA versus mRNA, to determine whether direct small-subunit rRNA binding occurs.
Hypothesis: The GO:0070181 small ribosomal subunit rRNA binding annotation overstates a ribosome association; CIRBP does not directly contact 18S rRNA.
Type: in vitro RNA-binding specificity assay
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