Evidence map›Paper›PMID 35863866›Full record

ArticleRNA (New York, N.Y.)2022

Expansion and functional analysis of the SR-related protein family across the domains of life.

Sean M Cascarina, Eric D Ross

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 20 citations in OpenAlex.

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  15. Interplays betweenInternational journal of molecular sciences · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Sean M CascarinaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523, USA.ORCID 0000-0002-3054-2332
Eric D RossDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523, USA.ORCID 0000-0002-6473-9977
Colorado State University · US

Funding

Functional and Pathological Assembly of Prion-like DomainsR35GM130352 · NIGMS · COLORADO STATE UNIVERSITY · PI Eric D Ross · 2019 to 2026
$3.1M
NIGMS NIH HHS R35 GM130352
6 · The paper itself

Abstract

Serine/arginine-rich (SR) proteins comprise a family of proteins that is predominantly found in eukaryotes and plays a prominent role in RNA splicing. A characteristic feature of SR proteins is the presence of an S/R-rich low-complexity domain (RS domain), often in conjunction with spatially distinct RNA recognition motifs (RRMs). To date, 52 human proteins have been classified as SR or SR-related proteins. Here, using an unbiased series of composition criteria together with enrichment for known RNA binding activity, we identified >100 putative SR-related proteins in the human proteome. This method recovers known SR and SR-related proteins with high sensitivity (∼94%), yet identifies a number of additional proteins with many of the hallmark features of true SR-related proteins. Newly identified SR-related proteins display slightly different amino acid compositions yet similar levels of post-translational modification, suggesting that these new SR-related candidates are regulated in vivo and functionally important. Furthermore, candidate SR-related proteins with known RNA-binding activity (but not currently recognized as SR-related proteins) are nevertheless strongly associated with a variety of functions related to mRNA splicing and nuclear speckles. Finally, we applied our SR search method to all available reference proteomes, and provide maps of RS domains and Pfam annotations for all putative SR-related proteins as a resource. Together, these results expand the set of SR-related proteins in humans, and identify the most common functions associated with SR-related proteins across all domains of life.

Indexed as

ProteomeRNA-Binding ProteinsAnimalsArginineHumansNuclear ProteinsRNARNA, MessengerRNA PrecursorsRNA SplicingSerineSerine-Arginine Splicing FactorsArginineNuclear ProteinsProteomeRNARNA-Binding ProteinsRNA, MessengerRNA PrecursorsSerineSerine-Arginine Splicing Factorslow-complexity domainRNA-binding proteinRNA metabolismsplicingSR protein

Identifiers

PMID35863866
PMCPMC9479744
OpenAlexW4286203348

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.