SR protein: Difference between revisions
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[[File:Protein_SFRS9_PDB_1wg4.png|Protein SFRS9 PDB 1wg4|thumb]] | |||
[[File:SR_proteins_translocation_into_and_out_of_the_nucleus.png|SR proteins translocation into and out of the nucleus|thumb]] | |||
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'''SR proteins''' are a family of [[RNA-binding proteins]] that are essential for [[splicing]] of pre-mRNA in [[eukaryotic cells]]. They are characterized by the presence of one or two [[RNA recognition motif|RNA recognition motifs]] (RRMs) at the N-terminus and a C-terminal domain rich in [[serine]] and [[arginine]] residues, known as the RS domain. | '''SR proteins''' are a family of [[RNA-binding proteins]] that are essential for [[splicing]] of pre-mRNA in [[eukaryotic cells]]. They are characterized by the presence of one or two [[RNA recognition motif|RNA recognition motifs]] (RRMs) at the N-terminus and a C-terminal domain rich in [[serine]] and [[arginine]] residues, known as the RS domain. | ||
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* [[RNA-binding protein]] | * [[RNA-binding protein]] | ||
* [[SR protein kinase]] | * [[SR protein kinase]] | ||
== External links == | == External links == | ||
Latest revision as of 00:56, 28 February 2025
SR proteins are a family of RNA-binding proteins that are essential for splicing of pre-mRNA in eukaryotic cells. They are characterized by the presence of one or two RNA recognition motifs (RRMs) at the N-terminus and a C-terminal domain rich in serine and arginine residues, known as the RS domain.
Function[edit]
SR proteins play a crucial role in both constitutive splicing and alternative splicing of pre-mRNA. They are involved in the recognition of splice sites and the assembly of the spliceosome. SR proteins also participate in other aspects of RNA metabolism, including mRNA export, nonsense-mediated decay, and translation.
Structure[edit]
The structure of SR proteins typically includes:
- One or two RRMs that bind to specific RNA sequences.
- An RS domain that mediates protein-protein interactions and is subject to extensive phosphorylation.
Phosphorylation[edit]
Phosphorylation of the RS domain is critical for the function of SR proteins. It regulates their subcellular localization, interaction with other splicing factors, and activity in splicing. SR protein kinases (SRPKs) and Clk/Sty kinases are responsible for the phosphorylation of SR proteins.
Role in Disease[edit]
Dysregulation of SR proteins has been implicated in various diseases, including cancer, neurodegenerative disorders, and genetic diseases. Alterations in SR protein expression or function can lead to aberrant splicing and contribute to disease pathogenesis.
See also[edit]
External links[edit]
- [SR proteins at the Protein Data Bank]
- [SR proteins in the Human Protein Atlas]
