InterPro : IPR004123

Name  mRNA splicing factor, thioredoxin-like U5 snRNP Short Name  mRNA_splic_U5
Type  Family Description  Thioredoxins [, , , ]are small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulphide, accompanied by the transfer of 2 electrons and 2 protons. The net result is the covalent interconversion of a disulphide and a dithiol. Compared to human thioredoxin, human U5 snRNP-specific protein U5-15kDa contains 37 additional residues that may cause structural changes which most likely form putative binding sites for other spliceosomal proteins or RNA. Although U5-15kDa apparently lacks protein disulphide isomerase activity, it isstrictly required for pre-mRNA splicing [].
 Feedback

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Holmgren A Thioredoxin and glutaredoxin systems. 1989 J Biol Chem 264 13963-6
Holmgren A Thioredoxin. 1985 Annu Rev Biochem 54 237-71
Holmgren A Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. 1995 Structure 3 239-43
Martin JL Thioredoxin--a fold for all reasons. 1995 Structure 3 245-50
Reuter K Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. 1999 J Mol Biol 294 515-25



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)