Affinage

ZMAT5

Zinc finger matrin-type protein 5 · UniProt Q9UDW3

Length
170 aa
Mass
20.0 kDa
Annotated
2026-06-11
4 papers in source corpus 1 papers cited in narrative 1 extracted findings
Cross-family judge faithfulness: 2/2 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ZMAT5 (SNRNP20) is a subunit of the human U11 snRNP particle of the minor spliceosome, where it contributes to recognition of U12-type 5' splice sites (PMID:39809272). Within the 13-subunit U11 snRNP, cryo-EM structures in apo and substrate-bound states position ZMAT5 near the 5' end of U11 snRNA, where it cooperates with SNRNP48 to stabilize binding of the incoming U12-type 5' splice site through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3 (PMID:39809272). Beyond this structural role in 5' splice site recognition, no further mechanistic detail has been characterized in the available corpus.

Mechanistic history

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

    Whether and how ZMAT5 participates in minor spliceosome function was resolved by placing it structurally within the U11 snRNP and assigning it a role in 5' splice site recognition.

    Evidence Cryo-EM reconstruction of the human U11 snRNP in apo and substrate-bound states, resolving subunit architecture and the 5'SS recognition mechanism

    PMID:39809272

    Open questions at the time
    • Functional consequences of ZMAT5 loss on U12-dependent intron splicing not tested
    • Contribution of ZMAT5 versus SNRNP48 to 5'SS stabilization not separated experimentally
    • No data on ZMAT5 outside the U11 snRNP context

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 1
Pathway
R-HSA-8953854 Metabolism of RNA 1
Partners
SNRNP48
Complex memberships
U11 snRNP (minor spliceosome)

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2025 ZMAT5 is a subunit of the 13-subunit human U11 snRNP complex of the minor spliceosome. Cryo-EM structures in apo and substrate-bound forms show that ZMAT5 is positioned near the 5' end of U11 snRNA, where it cooperates with SNRNP48 to stabilize binding of the incoming U12-type 5' splice site (5'SS). Recognition of the 5'SS is achieved through base-pairing to the 5' end of U11 snRNA and non-canonical base-triple interactions with U11 snRNA stem-loop 3. Cryo-EM reconstruction of the human U11 snRNP complex in apo and substrate-bound states, revealing subunit architecture and 5' splice site recognition mechanism Molecular cell High 39809272

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2020 Genome-Wide Association Analysis Reveals Key Genes Responsible for Egg Production of Lion Head Goose. Frontiers in genetics 23 32047514
2023 Identification of candidate genomic regions for egg yolk moisture content based on a genome-wide association study. BMC genomics 8 36918797
2025 Structural basis of 5' splice site recognition by the minor spliceosome. Molecular cell 7 39809272
2012 Search for chromosome rearrangements: new approaches toward discovery of novel translocations in head and neck squamous cell carcinoma. Head & neck 2 22807096

Missed literature

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