The tripartite motif family identifies cell compartments
Open accessAbstract
A functional genomic approach, based on systematic data gathering, was used to characterize a family of proteins containing a tripartite motif (TRIM). A total of 37 TRIM genes/proteins were studied, 21 of which were novel. The results demonstrate that TRIM proteins share a common function: by means of homo-multimerization they identify specific cell compartments.
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TRIM32 is a member of the tripartite-motif (TRIM) family of proteins.
“TRIM32is a member of the tripartite-motif (TRIM) family of proteins described elsewhere (Reymond et al. 2001).”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Reymond et al. 2001
TRIM32 is a member of the TRIM, or RING-B-box-coiled-coil, protein family.
“TRIM32 is a member of a growing family of TRIM, or RING-B-box-coiled-coil, proteins”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Reymond et al. 2001
TRIM32, previously known as HT2A, was originally discovered using a yeast two-hybrid assay with human immunodeficiency virus type 1 Tat as bait.
“It was originally discovered using a yeast two-hybrid assay with the human immunodeficiency virus type 1 Tat acting as bait (Fridell et al. 1995; Reymond et al. 2001).”
From Limb-Girdle Muscular Dystrophy Type 2H Associated with Mutation in TRIM32, a Putative E3-Ubiquitin–Ligase Gene (2002) · cites this paper as Reymond et al. 2001
The Bioinformatics section says the TRIM32 clone was received from R.A. Friedell, and the protein–protein interactions section describes this paper’s own two-hybrid methods. Neither passage says TRIM32 was formerly called HT2A or that it was originally discovered using HIV-1 Tat as bait. Searches for HT2A, Tat, and Fridell found no passage establishing that discovery account. (LLM, conf=0.73)
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- Authors
- Reymond, A., Meroni, G., Fantozzi, A., Merla, G., Cairo, S., Luzi, L., Riganelli, D., Zanaria, E., Messali, S., Cainarca, S., Guffanti, A., Minucci, S., Pelicci, P. G., & Ballabio, A.
- Affiliations
- University of Geneva (CH)
- Telethon Institute Of Genetics And Medicine (IT)
- University of Perugia (IT)
- European Institute of Oncology (IT)
- Vita-Salute San Raffaele University (IT)
- Corresponding author
- Pelicci, Pier Giuseppe
- Ballabio, Andrea
- ORCID
- Venue
- The EMBO Journal
- Published
- 2001-05-01
- Volume
- 20
- Issue
- 9
- Pages
- 2140-2151
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC125245
- OpenAlex
- W2116773729
- Cited by
- 1,366
- References
- 69
- Citations by year
- 2026: 27 · 2025: 32 · 2024: 57 · 2023: 54 · 2022: 63 · 2021: 84 · 2020: 52 · 2019: 67 · 2018: 41 · 2017: 59 · 2016: 51 · 2015: 50 · 2014: 56 · 2013: 66 · 2012: 70
- FWCI
- 8.73
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
- Institutional Research Information System University of Ferrara (University of Ferrara) (submittedVersion)
- Funders
- March of Dimes Foundation
- Associazione Italiana per la Ricerca sul Cancro
- Fondazione Italiana per la Ricerca sul Cancro
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- tripartite motif proteins, TRIM family, protein oligomerization, protein annotation, functional genomics
- MeSH terms
- Animals, Carrier Proteins, Cell Compartmentation, Cell Line, Chromosome Mapping, Cloning, Molecular, Embryo, Mammalian, Multigene Family, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Organ Specificity, Protein Binding, Proteins, Subcellular Fractions, Blotting, Northern, Databases, Factual, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, In Situ Hybridization, Protein Structure, Tertiary, Two-Hybrid System Techniques, Amino Acid Motifs, Ubiquitin-Protein Ligases, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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