Affinage

SNRNP48

U11/U12 small nuclear ribonucleoprotein 48 kDa protein · UniProt Q6IEG0

Length
339 aa
Mass
40.0 kDa
Annotated
2026-06-10
2 papers in source corpus 1 papers cited in narrative 2 extracted findings
Cross-family judge faithfulness: 3/3 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SNRNP48 is a protein component of the human U11 snRNP of the minor spliceosome, where it participates in recognition of U12-type 5' splice sites (PMID:39809272). Within the 13-subunit U11 particle, SNRNP48 is positioned near the 5' end of the U11 snRNA and stabilizes binding of the incoming 5' splice site, with PDCD7 bridging SNRNP48 to SNRNP25 across distal ends of the particle (PMID:39809272). SNRNP48 acts together with ZMAT5 to stabilize engagement of the U12-type 5' splice site, contributing directly to splice-site recognition by the minor spliceosome (PMID:39809272). Beyond its structural role in the U11 snRNP defined by cryo-EM, no further mechanistic detail has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2025 High

    The architecture of the human U11 snRNP and the spatial position of SNRNP48 within it were unknown; resolving the complex established where SNRNP48 sits and how it connects to other subunits.

    Evidence Cryo-EM reconstruction of the 13-subunit human U11 snRNP in apo and substrate-bound forms

    PMID:39809272

    Open questions at the time
    • Functional consequence of SNRNP48 loss on minor-spliceosome activity not tested
    • Whether the PDCD7-bridged arrangement is dynamic during the splicing cycle is unresolved
  2. 2025 High

    How the minor spliceosome stabilizes the U12-type 5' splice site was unclear; structural analysis showed SNRNP48 and ZMAT5 cooperate to secure this contact.

    Evidence Cryo-EM structural analysis of the substrate-bound U11 snRNP

    PMID:39809272

    Open questions at the time
    • Quantitative contribution of SNRNP48 versus ZMAT5 to splice-site affinity not separated
    • No mutational dissection of the residues mediating 5'SS stabilization

Open questions

Synthesis pass · forward-looking unresolved questions
  • Whether SNRNP48 has roles beyond the U11 snRNP, and the phenotypic effect of its disruption, remain undefined.
  • No loss-of-function or depletion studies in the corpus
  • No disease association documented
  • No biochemical activity assigned beyond structural participation

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 2 GO:0003723 RNA binding 1
Pathway
R-HSA-8953854 Metabolism of RNA 2
Complex memberships
U11 snRNPminor spliceosome

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2025 Cryo-EM reconstruction of the 13-subunit human U11 snRNP complex revealed that SNRNP48 is positioned near the 5' end of U11 snRNA, where it stabilizes binding of the incoming 5' splice site (5'SS). PDCD7 bridges SNRNP25 and SNRNP48, which are located at distal ends of the particle. Cryo-EM structural reconstruction of the human U11 snRNP in apo and substrate-bound forms Molecular cell High 39809272
2025 SNRNP48 and ZMAT5 cooperate to stabilize binding of the incoming U12-type 5' splice site to the U11 snRNP, contributing to 5'SS recognition by the minor spliceosome. Cryo-EM structural analysis of substrate-bound U11 snRNP complex Molecular cell High 39809272

Source papers

Stage 0 corpus · 2 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2021 Integrative proteomic and lipidomic analysis of Kaili Sour Soup-mediated attenuation of high-fat diet-induced nonalcoholic fatty liver disease in a rat model. Nutrition & metabolism 17 33691721
2025 Structural basis of 5' splice site recognition by the minor spliceosome. Molecular cell 7 39809272

Missed literature

Know a paper Affinage missed for SNRNP48? Flag it for the maintainers and the community.

No submissions yet.