Primary Information |
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| BoMiProt ID | Bomi83 |
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| Protein Name | Serine/arginine-rich splicing factor 2 |
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| Organism | Bos taurus |
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| Uniprot ID | Q3MHR5 |
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| Milk Fraction | MFGM |
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| Ref Sequence ID | NP_001029490.1 |
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| Aminoacid Length | 221 |
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| Molecular Weight | 25476 |
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| FASTA Sequence |
Download |
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| Gene Name | SRSF2 |
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| Gene ID | 508312 |
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| Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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| Protein Function | Plays an
important role in constitutive and alternative splicing
as well as during several steps of RNA metabolism; known to promote cross-intron and cross-exon interactions; interact with exonic splicing
enhancers and stimulate the splicing of adjacent
introns |
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| Biochemical Properties | Properties are characteristic
of intrinsically disordered (ID) proteins; RS domains are completely unstructured; prevalence of hydrophilic
and charged amino acids and lesser hydrophobic and
aromatic amino acids amongst the disordered regions; slightly enriched in tyrosin
residue- presence of partial hydrophobicity, aromatic side chain and a reactive
hydroxyl group might
participate in stacking interactions with the RNA bases; depletion of SR
proteins in the negatively charged D and E and their enrichment
in the positively charged K and R may be essential for
interaction with the negatively charged RNA |
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| PTMs | RS domains of SR proteins are extensively phosphorylated
by two families of kinases, the SR protein-specific
kinases (SRPKs) and Clk/Sty protein kinases; methylation and ubiquitination are also predicted to occur in disordered protein regions |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | (92-221) |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | Phosphorylation
is required for translocation of SR proteins from the
cytoplasm to the nucleus, and it is also known to regulate
the activity of SR proteins during early development |
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| Linking IDs | |
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| Bibliography | 1. Haynes, C., & Iakoucheva, L. M. (2006). Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Research, 34(1), 305–312. https://doi.org/10.1093/nar/gkj424 |
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