Search by BoMiProt ID - Bomi2756


Primary Information

BoMiProt ID Bomi2756
Protein Name Serine/arginine-rich splicing factor 7
Organism Bos taurus
Uniprot IDQ3T106
Milk FractionMFGM
Ref Sequence ID NP_001029449.1
Aminoacid Length 235
Molecular Weight 26941
FASTA Sequence Download
Gene Name SRSF7
Gene ID 507066
Protein Existence Status Reveiwed:Experimental evidence at transcript level

Secondary Information

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
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
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
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
Linking IDs Bomi83
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
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions (123-235)
DisProt Annotation
TM Helix Prediction No TM helices