Rs domain - OmicsDI

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Instrument Platform

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See manuscript (1)
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UNIPROT ID/AC

Q08999 (1)
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CHEBI ID

CHEBI:16704 (6)
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CHEBI:15996 (1)
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CHEBI:16905 (1)
CHEBI:17665 (1)
CHEBI:16761 (1)
CHEBI:16908 (1)
CHEBI:15846 (1)
CHEBI:18021 (1)
CHEBI:15946 (1)

Metabolite Name

Choline (5)
Creatine (5)
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DCMP (3)
D-Erythrose 4-phosphate (3)
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First Public Date

2022 (5)
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Modelling Approach

Ordinary differential equation model (8)
Constraint-based model (2)

Lab affiliation

Brazilian Biosciences National Laboratory (LNBio), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, Sao Paulo, Brazil, Zip Code 13083-970 (1)
CEITEC—Central European Institute of Technology, Masaryk University, Brno, Czech Republic National Centre for Biomolecular Research, Faculty of Science, Masaryk University, Brno, Czech Republic (1)
Cell Signalling and Immunology, School of Life Sciences, University of Dundee, Dundee (1)
Central European Institute of Technology, Masaryk University, Brno, Czech Republic National Centre for Biomolecular research, Masaryk University, Brno, Czech Republic (1)
Charles Perkins Centre, School of Medical Sciences, The University of Sydney, Sydney, NSW, Australia. (1)
Children's Medical Research Institute, Westmead, NSW (1)
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Colson lab, Dept. of Cellular & Molecular Medicine, University of Arizona, Tucson, AZ, USA (1)
Complex Carbohydrate Research Center (1)
Complex Carbohydrate Research Center, Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, USA. (1)
Complex Carbohydrate Reserach Center Department of Biochemistry and Molecular Biology University of Georgia Athens, GA 30621 USA (1)
Department of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, The University of Georgia, U.S.A. (1)
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA ( lab head ) (1)
Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Boston, MA 02215, USA, Department of Medicine, Harvard Medical School, Boston, MA 02115, USA (1)
Department of Chemistry and Biochemistry, The University of Texas at Dallas (1)
Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden (1)
Department of Laboratory Medicine and Helen Diller Family Comprehensive Cancer Center, University of California San Francisco, United States of America (1)
Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. Pok Man Leung, pok.leung@monash.edu, Department of Microbiology, Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia Ralf B. Schittenhelm, ralf.schittenhelm@monash.edu, Monash Proteomics and Metabolomics Facility and Department of Biochemistry, Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia (1)
Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY (1)
Division of Cell and Developmental Biology, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD15EH, Scotland, UK. (1)
Drug Discovery Biology Theme Monash Institute of Pharmaceutical Sciences Monash University 399 Royal Parade (Mail address: 381 Royal Parade) Parkville VIC 3052 Australia (1)
Emory University School of Medicine Departments of Biochemistry and Neurology (1)
Faculty of Medical Sciences, Institute for Cell and Molecular Biosciences, Newcastle upon Tyne, UK (1)
Genome Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany; Genome Center, Department of Genetics, Stanford University School of Medicine, CA, USA. (1)
INSERM, laboratory: INSERM UMR1204, Structure-Activité des Biomolécules Normales et Pathologiques, Université d'Evry/Paris-Saclay France (1)
MRC Laboratory of Molecular Biology (1)
MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, UK. (1)
McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA (1)
McKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University, Baltimore, Maryland 21205 USA (1)
Medical Research Council (MRC) Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K. (1)

IsPrivate

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Model Flag

Non Kinetic (3)

Classification

fungi (1)

Study type

Transcription profiling by array (317)
RNA-seq of coding RNA (116)
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Release Date

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Phosphorylation of CPSF6 RS-like domain

Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor CPSF6, regulates alternative polyadenylation (APA). CPSF6 has a RS-like domain which plays role in protein -protein interactions. This interaction might have role in alternative polyadenylation s...

ORGANISM(S): Homo sapiens (Human)

2019-04-01 | PXD012713 | Pride

U2AF2 controls alternative splicing in speckles proximal regions in an RS domain-dependent manner

Splicing factor U2AF2 is known to play a pivotal role for 3' splice site recognition at an early step of spliceosome assembly. Here using proximity labeling and biochemical confirmations, we extend the repertoire of putative functional partners of U2AF2 mainly for splicing, chromatin modification, t...

ORGANISM(S): Homo sapiens (Human)

2026-03-09 | PXD065448 | Pride

U2af2/ rs domain/ alternative splicing/ nuclear sepckles/ phosphorylation

Deletion of the RS domain in RBM20 leads to dilated cardiomyopathy

PRJNA877291 | ENA

Deletion of the RS domain in RBM20 leads to dilated cardiomyopathy

Human patients carrying genetic mutations in RBM20 develop a clinically aggressive dilated cardiomyopathy (DCM) characterized by early onset heart failure, high mortality, and sudden death, which is recapitulated in animal models. RBM20 has two primary domains, an RNA recognition motif (RRM) that bi...

ORGANISM(S): Mus musculus

2023-01-02 | GSE212799 | GEO

Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing.

Not available

S-EPMC108778 | biostudies-literature

Epigenetic Repogramming by an Environmental Carcinogen Through Chromatin Domain Disruption

Histone modifications associated with gene silencing typically mark large contiguous regions of the genome forming repressive chromatin domain structures. Since the repressive domains exist in close proximity to active regions, maintenance of domain structure is critically important. This study show...

ORGANISM(S): Homo sapiens

2014-09-24 | E-GEOD-56053 | biostudies-arrayexpress

U2AF2 controls alternative splicing in speckles proximal regions in an RS domain-dependent manner.

PRJNA1280687 | ENA

SRPK1 and Akt Protein Kinases Phosphorylate the RS Domain of Lamin B Receptor with Distinct Specificity: A Combined Biochemical and In Silico Approach.

Not available

S-EPMC4841541 | biostudies-literature

Distinctive features of Drosophila alternative splicing factor RS domain: implication for specific phosphorylation, shuttling, and splicing activation.

Not available

S-EPMC99587 | biostudies-literature

Epigenetic Repogramming by an Environmental Carcinogen Through Chromatin Domain Disruption [RNA-Seq]

Alterations in chromatin modifications, including DNA methylation and histone modification patterns, have been characterized under exposure of several environmental pollutants, including nickel. As with other carcinogenic metals, the mutagenic potential of nickel compounds is low and is not well cor...

ORGANISM(S): Homo sapiens

2014-09-26 | E-GEOD-56052 | biostudies-arrayexpress

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