Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation

19 Apr 2005

Abstract excerpt

The U5 snRNP plays an essential role in both U2- and U12-dependent splicing. Here, we have characterized a 52-kDa protein associated with the human U5 snRNP, designated U5-52K. Protein sequencing revealed that U5-52K is identical to the CD2BP2, which interacts with the cytoplasmic portion of the human T-cell surface protein CD2. Consistent with it associating with an snRNP, immunofluorescence studies demonstrated...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to RNA modifications and cancer
Share to RNA Research and Splicing
Share to Viral Infections and Immunology Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15840814
DOI: 10.1261/rna.2300805

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formationPMID 15840814Read ↗

The network of protein–protein interactions within the human U4/U6.U5 tri-snRNPSemantic proximity Read ↗

Functional interaction of a novel 15.5kD [U4/U6.U5] tri-snRNP protein with the 5' stem-loop of U4 snRNA.Semantic proximity Read ↗

Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones.Semantic proximity Read ↗

An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.Semantic proximity Read ↗

Identification of a 35S U4/U6.U5 tri-small nuclear ribonucleoprotein (tri-snRNP) complex intermediate in spliceosome assembly.Semantic proximity Read ↗

Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae.Semantic proximity Read ↗

A spliceosome intermediate with loosely associated tri-snRNP accumulates in the absence of Prp28 ATPase activity.Semantic proximity Read ↗

p110, a novel human U6 snRNP protein and U4/U6 snRNP recycling factorSemantic proximity Read ↗

Structural basis for dual roles of Aar2p in U5 snRNP assembly.Semantic proximity Read ↗

A comprehensive biochemical and genetic analysis of the yeast U1 snRNP reveals five novel proteins.Semantic proximity Read ↗

Biochemical characterization and crystal structure of a Dim1 family associated protein: Dim2.Semantic proximity Read ↗

Mechanism for Aar2p function as a U5 snRNP assembly factor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.