Affinage

SRP14

Signal recognition particle 14 kDa protein · UniProt P37108

Length
136 aa
Mass
14.6 kDa
Annotated
2026-06-10
63 papers in source corpus 29 papers cited in narrative 29 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SRP14 is the defining protein component of the signal recognition particle (SRP) Alu domain, the module that couples nascent-chain elongation to membrane targeting. It functions as an obligate heterodimer with SRP9: neither protein alone binds SRP RNA specifically, and the heterodimer is required both for stable RNA association and for restoring elongation arrest activity to SRP depleted of SRP9/14 (PMID:2153922). Crystallography shows SRP9 and SRP14 adopt a shared alpha-beta-beta-beta-alpha fold that assembles into a pseudo-2-fold symmetric saddle presenting a positively charged concave surface that docks onto the conserved U-turn core of the Alu RNA 5' domain, after which the 3' domain folds back to form the compact Alu RNP (PMID:9233785, PMID:11089964, PMID:11350037, PMID:40345827). Functionally, the C-terminal tail of SRP14 mediates ribosomal contacts required for elongation arrest — its truncation abolishes arrest while leaving signal recognition, targeting, and ribosome binding intact (PMID:9115358) — and a basic platform formed by the KRDKK pentapeptide of SRP14 together with lysines of SRP9 contacts the ribosome at the subunit interface to delay elongation (PMID:14705936, PMID:20348448). This elongation arrest is physiologically important: it keeps nascent chains translocation-competent when SRP receptor is rate-limiting, so arrest-deficient SRP14 produces secretion defects and reduced growth that are rescued by lowering translation rate or raising receptor levels (PMID:18455985). The arrest function is conserved to yeast, where Srp14p acts as a homodimer on scR1 RNA and its C-terminal truncation impairs translocation and growth in vivo (PMID:10573124, PMID:10921896). Beyond its core SRP role, SRP9/SRP14 exists in large cytoplasmic excess over SRP and binds Alu and neural BC200 RNAs in vivo (PMID:7542942, PMID:9605471), localizes to the nucleus where it transcriptionally promotes 7SL and BC200 RNA expression (PMID:37156570), and participates in the PERK-driven unfolded protein response, where PERK-mediated loss of SRP14 attenuates translocation as a protective ER-stress mechanism dependent on its elongation-arrest activity (PMID:38943644).

Mechanistic history

Synthesis pass · year-by-year structured walk · 27 steps
  1. 1990 High

    Established that SRP14 does not act alone but requires SRP9 to form a functional RNA-binding unit, defining the molecular basis of the Alu domain.

    Evidence In vitro reconstitution with recombinant proteins and elongation arrest assays in cell-free translation

    PMID:2153922

    Open questions at the time
    • Did not resolve the structural basis of heterodimerization
    • Did not map which residues contact RNA
  2. 1994 High

    Showed the heterodimer fold, not the native chain termini, is what matters, since single-chain fusions in either permutation reconstitute RNA binding and function.

    Evidence Single-chain SRP9-SRP14 fusion proteins tested in RNA-binding and cell-free arrest/translocation assays

    PMID:7518078

    Open questions at the time
    • Did not define the minimal RNA element recognized
    • Did not localize ribosome-contacting regions
  3. 1995 High

    Revealed that SRP9/14 is far more abundant than SRP and binds Alu RNAs as a distinct 8.5S particle in vivo, implying functions beyond the canonical SRP.

    Evidence Immunoprecipitation, subcellular fractionation and quantitative immunoblotting in primate cells

    PMID:7542942

    Open questions at the time
    • Function of the excess cytoplasmic pool not determined
    • Significance of Alu RNA complexes left open
  4. 1995 Medium

    Linked an anthropoid GCA-repeat expansion to extended alanine-rich SRP14 isoforms with elevated protein levels and Alu RNA-binding activity, an evolutionary specialization.

    Evidence Gene cloning, sequencing, in vitro binding assays and comparative genomics

    PMID:7534378

    Open questions at the time
    • Functional consequence of the C-terminal extension for SRP not directly tested
    • Mechanism linking extension to higher protein levels unknown
  5. 1997 High

    Provided the atomic structure of the heterodimer, showing a saddle-shaped pseudo-symmetric dimer with a basic concave RNA-binding surface.

    Evidence 2.5 A X-ray crystal structure of mouse SRP9/14

    PMID:9233785

    Open questions at the time
    • Structure was protein-only, without bound RNA
    • Ribosome contacts not visualized
  6. 1997 High

    Separated SRP14's roles by mutation: the C-terminus is dispensable for assembly and targeting but specifically required for ribosome contacts that produce elongation arrest, and it influences Alu RNA conformation.

    Evidence C-terminal truncation (SRP14-20C) reconstitution, RNA chemical probing, cell-free arrest/translocation assays

    PMID:9115358

    Open questions at the time
    • Exact ribosomal partners of the C-terminus not identified
    • Structural detail of the RNA conformational change unresolved
  7. 1997 High

    Mapped residue-level determinants of RNA binding and dimerization, distinguishing the contributions of SRP9 and SRP14 to the complex.

    Evidence Site-directed mutagenesis with in vitro dimerization and RNA-binding assays

    PMID:9214658

    Open questions at the time
    • Did not connect these residues to elongation arrest output
    • Did not test mutants in cellular context
  8. 1997 High

    Defined an 86-nt minimal autonomous Alu RNA folding unit (SA86) sufficient for SRP9/14 recognition, delimiting the binding determinant.

    Evidence Ribozyme-generated RNA variants and quantitative equilibrium competition binding assays

    PMID:9409618

    Open questions at the time
    • Structure of the bound minimal RNA not resolved at this stage
    • Functional readout of arrest not tested with minimal RNA
  9. 1997 Medium

    Showed binding affinity for diverse Alu-like RNAs (including BC200) scales inversely with evolutionary distance from 7SL, indicating broad but ranked recognition.

    Evidence Quantitative competition binding with recombinant human and mouse SRP9/14 across RNA species

    PMID:9016560

    Open questions at the time
    • Higher human affinity not explained by the C-terminal extension
    • In vivo consequence of differential affinity not established
  10. 1998 Medium

    Demonstrated SRP9/14 is a bona fide component of the neural BC200 RNP in primate brain, extending its biology to a non-SRP context in vivo.

    Evidence Immunoprecipitation of BC200 RNA with anti-SRP9 antibodies from brain tissue

    PMID:9605471

    Open questions at the time
    • Functional role within the BC200 RNP not determined
    • Single immunoprecipitation without reciprocal validation
  11. 1999 High

    Established conservation and divergence of the Alu domain in yeast, where Srp14p binds scR1 RNA as a homodimer using conserved RNA motifs and basic residues.

    Evidence Immunoprecipitation, RNA footprinting and mutagenesis in S. cerevisiae

    PMID:10573124

    Open questions at the time
    • Why yeast uses a homodimer versus heterodimer not explained
    • Did not test elongation arrest in this study
  12. 2000 High

    Visualized SRP9/14 bound to Alu RNA, showing tight binding to the U-turn core of the 5' domain and weaker docking of the 3' domain, yielding a model of the assembled Alu domain.

    Evidence Two X-ray crystal structures of SRP9/14-Alu RNA complexes with biochemical validation

    PMID:11089964

    Open questions at the time
    • Conformation in the context of the ribosome not captured
    • Dynamics of 3' domain docking inferred, not directly observed
  13. 2000 High

    Showed elongation arrest is a physiologically essential, conserved SRP function by tying Srp14p C-terminal truncation to translocation defects and growth phenotypes in vivo.

    Evidence Yeast SRP purification, in vitro arrest assays, in vivo growth and translocation assays with deltaC29 mutant

    PMID:10921896

    Open questions at the time
    • Molecular detail of ribosome interaction in yeast not mapped
    • Did not establish the mammalian in vivo requirement
  14. 2001 High

    Defined the ordered assembly pathway: heterodimerization precedes 5' domain binding, which creates the site for a 180-degree fold-back of the 3' domain into the compact Alu RNP.

    Evidence Gel shift, filter binding, small-angle X-ray scattering and analytical ultracentrifugation

    PMID:11350037

    Open questions at the time
    • Trigger for the large conformational change not defined
    • Kinetics of assembly in cells unknown
  15. 2004 High

    Placed the Alu domain physically at the ribosomal subunit interface, with SRP14 contacting both subunits upon signal sequence recognition, explaining how arrest is effected.

    Evidence Protein-protein cross-linking in functional SRP-ribosome complexes with immunoprecipitation

    PMID:14705936

    Open questions at the time
    • Identity of all contacted ribosomal proteins not fully resolved
    • Static rather than dynamic view of the interaction
  16. 2010 High

    Identified the basic platform—SRP14 KRDKK plus SRP9 lysines clustered on one heterodimer face—as the elongation-arrest interface with ribosomal RNA.

    Evidence Site-directed mutagenesis with cell-free and mammalian cell complementation arrest assays

    PMID:20348448

    Open questions at the time
    • Direct structural contact with rRNA phosphate backbone inferred, not visualized
    • Whether these residues also contact ribosomal proteins unresolved
  17. 2008 High

    Demonstrated the physiological purpose of elongation arrest in mammals: it keeps nascent chains translocation-competent when SRP receptor is limiting, with arrest-deficient SRP14 causing secretion and growth defects rescuable by tuning translation or receptor levels.

    Evidence siRNA depletion and mutant complementation in mammalian cells with secretion, growth, and SR-overexpression rescue

    PMID:18455985

    Open questions at the time
    • Quantitative thresholds of SR limitation not defined
    • Did not address SRP14 roles outside targeting
  18. 2008 Medium

    Linked SRP14 (via 7SL RNA) to competition with APOBEC3 proteins for HIV virion packaging, an unexpected virology connection.

    Evidence siRNA knockdown of SRP14, HIV virion infectivity assays and 7SL RT-PCR

    PMID:18597676

    Open questions at the time
    • 7SL shown not essential for APOBEC3 packaging
    • Direct SRP14 involvement versus 7SL effect not separated
  19. 2009 Medium

    Provided a structural ortholog (S. pombe SRP14 homodimer) supporting conservation of U-turn-centered RNA contacts across fungi.

    Evidence X-ray crystallography of SpSRP14 with structural comparison to human complex

    PMID:19390147

    Open questions at the time
    • Functional inference by structural comparison only
    • No bound RNA in the structure
  20. 2013 Medium

    Showed SRP14 is rate-limiting for translocation in industrial cells, since its overexpression rescued processing and secretion of an arrest-prone antibody.

    Evidence Overexpression in CHO cells with secretion and fractionation assays

    PMID:23380542

    Open questions at the time
    • Mechanistic specificity to SRP14 versus co-overexpressed factors not isolated
    • Single cell-engineering context
  21. 2021 Medium

    Identified a non-canonical SRP14 role in HIV biology through direct binding to the tat mRNA TIM-TAM element, controlling tat translation and latency.

    Evidence AP-MS, RNA footprinting, knockdown, reporter assays and overexpression in primary CD4+ T cells

    PMID:34194479

    Open questions at the time
    • Relationship to canonical SRP function unclear
    • Single lab without independent confirmation
  22. 2022 Medium

    Extended SRP14 to another viral system, showing interaction with PRRSV Nsp2 to promote genome synthesis under miR-10a/IRF8 regulation.

    Evidence Co-immunoprecipitation, knockdown, replication assays and miR-10a reporter assays

    PMID:35293774

    Open questions at the time
    • Direct versus indirect SRP14-Nsp2 interaction not fully characterized
    • Mechanism of genome synthesis support unresolved
  23. 2023 Medium

    Revealed a nuclear, transcription-regulatory function: SRP9/SRP14 promotes 7SL and BC200 transcription, indicating feedback control over its own RNA partners.

    Evidence Knockdown with transcription-rate and stability measurements, immunofluorescence and subcellular fractionation

    PMID:37156570

    Open questions at the time
    • Mechanism of transcriptional stimulation unknown
    • Nuclear import pathway not defined
  24. 2024 High

    Placed SRP14 in the unfolded protein response, where PERK-driven loss of SRP14 attenuates translocation as a protective mechanism dependent on its arrest activity.

    Evidence Multi-omics, knockdown and wild-type/arrest-mutant overexpression with cathepsin D translocation and viability assays

    PMID:38943644

    Open questions at the time
    • Mechanism of PERK-driven SRP14 reduction not fully defined
    • Breadth of substrates affected during stress unknown
  25. 2024 Medium

    Classified the C-terminal P124A change as a functionally neutral natural variant, refining interpretation of SRP14 sequence variation.

    Evidence Mutagenesis with ectopic expression and growth, morphology and RNA-stability assays across cell lines

    PMID:38273782

    Open questions at the time
    • Did not test elongation arrest directly
    • Other C-terminal variants not surveyed
  26. 2025 Medium

    Pinpointed the pseudoknot U-turn structure as the structural requirement for SRP9/SRP14 binding to Alu RNAs, including BC200.

    Evidence Mutagenesis, immunoprecipitation, expression analysis, SAXS and computational structure prediction

    PMID:40345827

    Open questions at the time
    • Affinity contributions of individual U-turn residues not quantified
    • Functional consequence for SRP arrest not tested
  27. 2025 Low

    Suggested the Alu domain targets SRP RNAs to lysosomes for autophagy-dependent degradation, implicating SRP14 in RNA turnover.

    Evidence Lysosomal RNA profiling, autophagy mutant analysis and domain-swap experiments (preprint)

    PMID:40964324

    Open questions at the time
    • Preprint, not peer-reviewed
    • SRP14-specific contribution not separated from SRP9
    • Physiological role of this degradation pathway unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How SRP14's canonical SRP/translocation function mechanistically relates to its nuclear transcriptional regulation, non-SRP RNP partnerships, and the diverse viral interactions remains unresolved.
  • No unified model linking cytoplasmic SRP, nuclear, and viral functions
  • Nuclear import and transcriptional mechanism undefined
  • Direct structural basis of viral RNA/protein interactions uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 6 GO:0045182 translation regulator activity 4 GO:0060089 molecular transducer activity 4 GO:0140110 transcription regulator activity 1
Localization
GO:0005829 cytosol 2 GO:0005634 nucleus 1 GO:0005840 ribosome 1
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-9609507 Protein localization 2 R-HSA-8953854 Metabolism of RNA 1 R-HSA-8953897 Cellular responses to stimuli 1
Partners
HPIPPRRSV NSP2SRP9
Complex memberships
BC200 RNPSRP9/SRP14 heterodimer (Alu domain)signal recognition particle (SRP)

Evidence

Reading pass · 29 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 SRP9 and SRP14 form a heterodimer that is required for stable binding to SRP RNA; neither protein alone binds specifically to SRP RNA. The heterodimer is also required to restore elongation arrest activity to SRP depleted of SRP9/14. In vitro reconstitution with recombinant proteins, RNA-protein binding assay, elongation arrest assay in cell-free translation system Molecular and cellular biology High 2153922
1994 Single-chain fusion proteins encoding SRP14 and SRP9 sequences in either permutation bind SRP RNA as monomers folded into a heterodimer-like structure and restore elongation arrest and translocation activity to SRP(-9/14), demonstrating that the N- and C-termini of both proteins are dispensable for folding, RNA binding, and biological function. In vitro reconstitution, RNA-binding assay, cell-free elongation arrest and translocation assays Nucleic acids research High 7518078
1995 SRP9/14 heterodimer is present at more than 20-fold excess over SRP in primate cells, with the majority cytoplasmic and not bound to small RNAs; a significant fraction of small cytoplasmic Alu RNA is complexed with SRP9/14 in an 8.5S particle in vivo. Immunoprecipitation, subcellular fractionation, sucrose gradient sedimentation, quantitative immunoblotting Molecular biology of the cell High 7542942
1995 In early anthropoids, the SRP14 gene acquired a GCA trinucleotide repeat in its 3'-coding region producing SRP14 isoforms with extended alanine-rich C-terminal tails; this C-terminal extension is associated with increased SRP14 polypeptide levels and Alu RNA-binding activity. Gene cloning, sequencing, in vitro binding assays, comparative genomics Molecular and cellular biology Medium 7534378
1996 Monomeric scAlu RNA and nascent dimeric Alu RNAs are assembled into SRP9/14-containing RNPs in vivo after adenovirus infection, while SRP levels remain unchanged, demonstrating that induced Alu transcripts are specifically recruited to SRP9/14. Immunoprecipitation with anti-SRP9 antisera, Northern blotting Nucleic acids research Medium 8932367
1997 Crystal structure of the mouse SRP9/14 heterodimer resolved at 2.5 Å reveals that SRP9 and SRP14 share an alpha-beta-beta-beta-alpha fold (Alu binding module), form a pseudo 2-fold symmetric saddle-like heterodimer with a curved six-stranded amphipathic beta-sheet, and present a positively charged concave surface for RNA binding. X-ray crystallography at 2.5 Å resolution The EMBO journal High 9233785
1997 C-terminal truncation of SRP14 (SRP14-20C) forms a stable complex with SRP9 and SRP RNA but completely abolishes elongation arrest activity; the truncated particle retains signal recognition, targeting, and ribosome binding, indicating that the C-terminus of SRP14 is specifically required for interactions with the ribosome that effect elongation arrest. The truncation also induces tertiary structure changes in the Alu RNA, revealing a critical role of the RNA conformation in elongation arrest. In vitro reconstitution, cell-free translation/translocation assay, chemical probing of RNA structure, elongation arrest assay Nucleic acids research High 9115358
1997 Mutational analysis identified that in SRP9, acidic residues in the N-terminal alpha-helix and adjacent loop are critical for RNA binding, while in SRP14, a flexible internal loop region is critical for RNA binding; dimerization requirements differ substantially between SRP9 and SRP14. SRP RNA can rescue certain dimerization-defective SRP14 variants into stable complexes. In vitro dimerization and RNA-binding assays, site-directed mutagenesis RNA (New York, N.Y.) High 9214658
1997 An 86-nucleotide minimal Alu RNA folding domain (SA86) was defined that specifically binds SRPphi14-9 (single-chain SRP14-SRP9 fusion); this minimal domain consists of two stem-loops connected by a conserved bulge and part of the central adaptor stem, and it functions as an autonomous folding unit for SRP9/14 recognition. Ribozyme-mediated in vitro RNA production, quantitative equilibrium competition binding assay RNA (New York, N.Y.) High 9409618
1997 Human SRP9/14 binds with higher affinity than mouse SRP9/14 to all Alu-like RNAs tested including BC200 RNA; the relative dissociation constants are inversely proportional to evolutionary distance between the Alu RNA species and 7SL RNA. The additional C-terminal domain of anthropoid SRP14 does not explain this higher affinity. Quantitative binding assays (equilibrium competition), comparison of recombinant human and mouse SRP9/14 Nucleic acids research Medium 9016560
1998 The SRP9 protein (and by inference the SRP9/14 heterodimer) is an integral part of the neural BC200 RNP in primate brain in vivo, as demonstrated by immunoprecipitation of BC200 RNA with anti-SRP9 antibodies. Immunoprecipitation from brain tissue with anti-SRP9 antibodies Neuroscience letters Medium 9605471
1999 In S. cerevisiae, the Alu domain homolog consists of Srp14p bound as a homodimer (not a heterodimer with SRP9) to the 5' sequences of scR1 RNA; the minimal binding site is 99 nt. The conserved UGUAAU motif and certain basic amino acid residues conserved between mammalian SRP14 and yeast Srp14p are essential for RNA binding in both organisms. Immunoprecipitation, RNA footprinting, site-directed mutagenesis, in vitro binding assays RNA (New York, N.Y.) High 10573124
2000 Two crystal structures of the SRP9/14 heterodimer bound to the Alu RNA 5' domain, and to a construct containing both 5' and 3' domains, revealed that SRP9/14 binds strongly to the conserved core of the 5' domain which forms a U-turn, and that the 3' domain docks more weakly. A model of the complete Alu domain consistent with biochemical data was proposed. X-ray crystallography (two structures), biochemical validation Nature High 11089964
2000 Yeast SRP has elongation arrest activity; C-terminal truncation of Srp14p (deltaC29) eliminates elongation arrest, substantially reduces translocation efficiency, and causes constitutive defects in coupling protein translation and translocation and temperature-sensitive growth in vivo. This demonstrates that elongation arrest is a physiologically important and conserved function of eukaryotic SRP. Yeast SRP purification, in vitro elongation arrest assay, in vivo growth and translocation assays, genetic analysis The EMBO journal High 10921896
2001 The SRP Alu domain assembles hierarchically: SRP9 and SRP14 first heterodimerize, then bind the Alu RNA 5' domain, creating the binding site for the 3' domain; Alu RNA then undergoes a large conformational change where the flexibly linked 3' domain folds back 180° onto the 5' domain complex to form the final compact Alu RNP. Biochemical assembly assays (gel shift, filter binding), small-angle X-ray scattering, analytical ultracentrifugation RNA (New York, N.Y.) High 11350037
2004 Protein cross-linking in functional complexes demonstrates that SRP14 is in close physical proximity to several ribosomal proteins; cross-linking occurs even without a signal sequence, but upon signal sequence recognition, SRP14 cross-links to proteins from both the large and small ribosomal subunits, indicating that the Alu domain occupies a defined position at the ribosomal subunit interface during elongation arrest. Protein-protein cross-linking in functional SRP-ribosome complexes, immunoprecipitation Biochemistry High 14705936
2008 SRP14 depletion in mammalian cells causes inefficient targeting of preproteins due to rate-limiting SRP receptor (SR) concentrations; complementation with elongation-arrest-deficient SRP14 mutants results in defects in secretion, depletion of endogenous membrane proteins, and reduced cell growth. These defects are rescued by reducing protein synthesis rate or increasing SR expression, demonstrating that the elongation arrest function of SRP14 keeps nascent chains translocation-competent during SR-limited targeting. siRNA depletion in mammalian cells, complementation with mutant SRP14 variants, secretion assays, cell growth assays, SR overexpression rescue Cell High 18455985
2008 APOBEC3G and APOBEC3F are recruited into HIV virions when SRP14 (or SRP19) is depleted by RNA interference, indicating that 7SL RNA (which requires SRP14 for its assembly into SRP) competes with APOBEC3 proteins for virion packaging but is not an essential mediator of APOBEC3F/3G packaging. siRNA knockdown of SRP14, HIV virion infectivity assay, RT-PCR for 7SL RNA Retrovirology Medium 18597676
2010 Mutational analysis identified two patches of basic amino acid residues essential for SRP elongation arrest activity: a basic pentapeptide KRDKK in SRP14 and three lysines in the solvent-accessible alpha2 helix of SRP9; the internal loop of SRP14 is dispensable. All essential residues cluster on one face of the heterodimer, suggesting they form a positively charged platform for interactions with ribosomal RNA phosphate backbone. Site-directed mutagenesis, cell-free translation/translocation assay, mammalian cell complementation assay RNA (New York, N.Y.) High 20348448
2009 Crystal structure of S. pombe SRP14 (SpSRP14) reveals it crystallizes as a homodimer; comparison with human SRP9/14-Alu RNA complex suggests that many protein-RNA contacts centered on the conserved U-turn motif are likely conserved in fission yeast. X-ray crystallography (RIP and SAD phasing), structural comparison Acta crystallographica. Section D, Biological crystallography Medium 19390147
2013 Overexpression of human SRP14 (along with other secretory pathway components) in CHO cells restored proper processing and secretion of a difficult-to-express immunoglobulin that was subject to translational arrest, improper light chain cleavage, and insoluble aggregation, demonstrating that SRP14 is rate-limiting for protein translocation efficiency. Overexpression in CHO cells, secretion assays, protein fractionation, Western blotting Metabolic engineering Medium 23380542
2021 SRP14 binds directly to TIM-TAM, a conserved RNA sequence-structure in HIV tat mRNA that functions as a Tat IRES modulator; knockdown of SRP14 negatively affects tat mRNA processing and translation as well as Tat-mediated transactivation, increasing latent infection. Overexpression of SRP14 in resting CD4+ T cells from ART patients reversed HIV-1 latency and induced virus production. Affinity purification-mass spectrometry, RNA footprinting, siRNA knockdown, luciferase reporter assay, dual-color HIV reporter virus infection, overexpression in primary T cells Frontiers in genetics Medium 34194479
2021 SRP14 interacts with HPIP (under hypoxic conditions) and stimulates MMP9 synthesis, contributing to cell migration/invasion and EMT in breast cancer cells. Co-immunoprecipitation, siRNA knockdown, MMP9 expression assays, migration/invasion assays Cancer letters Low 34767928
2022 SRP14 promotes PRRSV genome synthesis by interacting with viral nonstructural protein Nsp2; knockdown of SRP14 inhibits PRRSV replication, and this pathway is regulated upstream by IRF8 (which suppresses miR-10a) and miR-10a (which targets SRP14 mRNA for translational repression). Co-immunoprecipitation (SRP14-Nsp2 interaction), siRNA knockdown, viral replication assays, luciferase reporter assay for miR-10a targeting Journal of virology Medium 35293774
2023 SRP9/SRP14 localizes to the nucleus and transcriptionally regulates 7SL RNA and BC200 RNA expression; knockdown of SRP9/SRP14 reduces 7SL and BC200 steady-state levels by reducing their transcription rate rather than altering RNA decay. Nuclear localization of SRP9/SRP14 was confirmed by immunofluorescence and subcellular fractionation. siRNA knockdown, RNA transcription rate measurements, RNA stability assays, immunofluorescence, subcellular fractionation RNA (New York, N.Y.) Medium 37156570
2024 During ER stress, PERK-mediated eIF2α phosphorylation causes a reduction in SRP14 protein levels (independent of ATF4/ATF3 transcription factors); this SRP14 reduction correlates with decreased translocation of cathepsin D. Enforced expression of elongation-arrest-capable SRP14 prevents reduced translocation in stressed cells, whereas an elongation-arrest-deficient mutant does not. Overexpression of SRP14 augments UPR and aggravates ER-stress-induced cell death, indicating that the PERK-SRP14 axis mediates translocational attenuation as a protective UPR mechanism. Multi-omics analysis, siRNA knockdown, overexpression of wild-type and mutant SRP14, cathepsin D translocation assay, cell viability assays Cell reports High 38943644
2024 The P124A mutation in the alanine-rich C-terminal domain of SRP14 causes faster migration on SDS-PAGE but does not affect SRP RNA stability, cell morphology, or cell growth, demonstrating it is a functionally neutral natural variant. Mutagenesis, SDS-PAGE, ectopic expression in multiple cell lines, functional assays (cell growth, morphology, SRP RNA stability) Acta biochimica et biophysica Sinica Medium 38273782
2025 The Alu domain of SRP RNAs (mediated by SRP9 and SRP14 protein interactions) is sufficient to target SRP RNAs to lysosomes for degradation in an autophagy-dependent manner. Lysosomal RNA profiling, autophagy mutant analysis, domain-swap experiments bioRxivpreprint Low 40964324
2025 Mutation of a critical guanosine in the U-turn motif of the BC200 Alu pseudoknot domain significantly reduces BC200 expression. A short human Alu RNA (EB120) lacking the canonical U-turn nucleotide triad also lacks association with SRP9/SRP14 in a cellular context, demonstrating that the pseudoknot U-turn structure is required for SRP9/SRP14 binding to Alu RNAs. Site-directed mutagenesis, immunoprecipitation, cell line and tissue expression analysis, small-angle X-ray scattering, computational structure prediction RNA (New York, N.Y.) Medium 40345827

Source papers

Stage 0 corpus · 63 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2023 The genetic basis of endometriosis and comorbidity with other pain and inflammatory conditions. Nature genetics 199 36914876
2000 Structure and assembly of the Alu domain of the mammalian signal recognition particle. Nature 152 11089964
2013 CHO cell engineering to prevent polypeptide aggregation and improve therapeutic protein secretion. Metabolic engineering 115 23380542
2008 SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sites. Cell 112 18455985
1994 Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. The EMBO journal 104 7925282
2000 Elongation arrest is a physiologically important function of signal recognition particle. The EMBO journal 98 10921896
2003 SRPDB: Signal Recognition Particle Database. Nucleic acids research 95 12520023
2006 The tmRDB and SRPDB resources. Nucleic acids research 88 16381838
1990 Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Molecular and cellular biology 74 2153922
2008 Characterization of APOBEC3G binding to 7SL RNA. Retrovirology 66 18597676
2015 Genetic ablation of ataxin-2 increases several global translation factors in their transcript abundance but decreases translation rate. Neurogenetics 59 25721894
1995 The SRP9/14 subunit of the signal recognition particle (SRP) is present in more than 20-fold excess over SRP in primate cells and exists primarily free but also in complex with small cytoplasmic Alu RNAs. Molecular biology of the cell 54 7542942
2014 Plasmodium falciparum signal recognition particle components and anti-parasitic effect of ivermectin in blocking nucleo-cytoplasmic shuttling of SRP. Cell death & disease 49 24434517
2008 Genomic selection of reference genes for real-time PCR in human myocardium. BMC medical genomics 49 19114010
1996 Monomeric scAlu and nascent dimeric Alu RNAs induced by adenovirus are assembled into SRP9/14-containing RNPs in HeLa cells. Nucleic acids research 49 8932367
2001 SRPDB (Signal Recognition Particle Database). Nucleic acids research 47 11125080
1997 The SRP9/14 subunit of the human signal recognition particle binds to a variety of Alu-like RNAs and with higher affinity than its mouse homolog. Nucleic acids research 46 9016560
1997 The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14. The EMBO journal 46 9233785
2004 Identification and comparative analysis of components from the signal recognition particle in protozoa and fungi. BMC genomics 41 14720308
1997 A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle. Nucleic acids research 40 9115358
2010 Residues in SRP9/14 essential for elongation arrest activity of the signal recognition particle define a positively charged functional domain on one side of the protein. RNA (New York, N.Y.) 39 20348448
1998 Heterodimer SRP9/14 is an integral part of the neural BC200 RNP in primate brain. Neuroscience letters 37 9605471
2001 Hierarchical assembly of the Alu domain of the mammalian signal recognition particle. RNA (New York, N.Y.) 35 11350037
1998 The Signal Recognition Particle Database (SRPDB). Nucleic acids research 35 9399828
2019 Analysis of Promoter-Associated Chromatin Interactions Reveals Biologically Relevant Candidate Target Genes at Endometrial Cancer Risk Loci. Cancers 34 31561579
1997 Identification of a minimal Alu RNA folding domain that specifically binds SRP9/14. RNA (New York, N.Y.) 30 9409618
2017 Cellular microRNA miR-10a-5p inhibits replication of porcine reproductive and respiratory syndrome virus by targeting the host factor signal recognition particle 14. The Journal of general virology 26 28086075
2004 Signal recognition particle Alu domain occupies a defined site at the ribosomal subunit interface upon signal sequence recognition. Biochemistry 26 14705936
1989 Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition particle by cross-hybridization of differently primed polymerase chain reactions. Proceedings of the National Academy of Sciences of the United States of America 26 2557625
1995 A trinucleotide repeat-associated increase in the level of Alu RNA-binding protein occurred during the same period as the major Alu amplification that accompanied anthropoid evolution. Molecular and cellular biology 25 7534378
2022 Host Cells Actively Resist Porcine Reproductive and Respiratory Syndrome Virus Infection via the IRF8-MicroRNA-10a-SRP14 Regulatory Pathway. Journal of virology 24 35293774
1999 The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure. RNA (New York, N.Y.) 24 10573124
2007 Unraveling the components of protein translocation pathway in human malaria parasite Plasmodium falciparum. Archives of biochemistry and biophysics 23 17919451
1994 The heterodimeric subunit SRP9/14 of the signal recognition particle functions as permuted single polypeptide chain. Nucleic acids research 23 7518078
2021 Noncanonical Functions and Cellular Dynamics of the Mammalian Signal Recognition Particle Components. Frontiers in molecular biosciences 21 34113652
1996 The Signal Recognition Particle Database (SRPDB). Nucleic acids research 17 8594607
2007 A new mechanism of 6-((2-(dimethylamino)ethyl)amino)-3-hydroxy-7H-indeno(2,1-c)quinolin-7-one dihydrochloride (TAS-103) action discovered by target screening with drug-immobilized affinity beads. Molecular pharmacology 16 18089836
2021 A reciprocal feedback loop between HIF-1α and HPIP controls phenotypic plasticity in breast cancer cells. Cancer letters 15 34767928
2021 The RNA-Binding Proteins SRP14 and HMGB3 Control HIV-1 Tat mRNA Processing and Translation During HIV-1 Latency. Frontiers in genetics 12 34194479
2011 Establishing reference genes for use in real-time quantitative PCR analysis of early equine embryos. Reproduction, fertility, and development 12 21211469
1997 The Signal Recognition Particle Database (SRPDB). Nucleic acids research 12 9016514
2009 Structure of SRP14 from the Schizosaccharomyces pombe signal recognition particle. Acta crystallographica. Section D, Biological crystallography 9 19390147
1997 Mutational analysis of the protein subunits of the signal recognition particle Alu-domain. RNA (New York, N.Y.) 9 9214658
1996 The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames. Yeast (Chichester, England) 9 8923743
2024 Characterised intron retention profiles in muscle tissue of idiopathic inflammatory myopathy subtypes. Annals of the rheumatic diseases 7 38302260
2024 The role of SRP9/SRP14 in regulating Alu RNA. RNA biology 6 39563162
2019 Selection of reference genes for quantitative studies in acute myeloid leukaemia. The Malaysian journal of pathology 6 31901916
1994 The signal recognition particle database (SRPDB). Nucleic acids research 6 7524020
2025 Deciphering Immunometabolic Landscape in Rheumatoid Arthritis: Integrative Multiomics, Explainable Machine Learning and Experimental Validation. Journal of inflammation research 5 39835297
2024 Translocational attenuation mediated by the PERK-SRP14 axis is a protective mechanism of unfolded protein response. Cell reports 5 38943644
2023 Nuclear SRP9/SRP14 heterodimer transcriptionally regulates 7SL and BC200 RNA expression. RNA (New York, N.Y.) 5 37156570
2003 Advances in the structure and functions of signal recognition particle in protein targeting. Journal of biological regulators and homeostatic agents 4 15065758
2024 The P124A mutation of SRP14 alters its migration on SDS-PAGE without impacting its function. Acta biochimica et biophysica Sinica 3 38273782
2025 Lysosomal RNA profiling reveals targeting of specific types of RNAs for degradation. bioRxiv : the preprint server for biology 2 40964324
2024 Higher expression of TSR2 aggravating hypertension via the PPAR signaling pathway. Aging 2 38814181
2025 Discovery of myeloid zinc finger (MZF) 1 nuclear bodies. Biochemical and biophysical research communications 1 39954358
2025 Integrated transcriptomic and single-cell RNA sequencing identifies lysosomal ion channel genes as potential biomarkers for Alzheimer's disease. Frontiers in genetics 1 41132791
2024 Exploring potential causal genetic variants and genes for endometrial cancer: Open Targets Genetics, Mendelian randomization, and multi-tissue transcriptome-wide association analysis. Translational cancer research 1 39697733
2023 Genome-wide analysis of circRNA regulation during spleen development of Chinese indigenous breed Meishan pigs. BMC genomics 1 37612620
2026 Investigation of gene stability in equine luteal tissue during mid-diestrus phase and early pregnancy - Research Article. BMC veterinary research 0 41507934
2025 Alu RNA pseudoknot alterations influence SRP9/SRP14 association. RNA (New York, N.Y.) 0 40345827
2025 Endometriosis: From Genes to Global Burden. International journal of molecular sciences 0 41516028
2024 Expression of signal recognition particle 14 in hepatocellular carcinoma and its relationship with disease progression and patient survival. Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences 0 39183055

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