DIM1Mitosis protein DIM1 |
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| SMART accession number: | SM01410
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| Description: |
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| Interpro abstract (IPR004123): |
This entry represents fission yeast Dim1 and its homologues, including Dib1 from budding yeasts, YLS8 from plants and TXNL4 from animals. Dim1 was originally identified as a mitosis protein [ (PUBMED:9182666) ]. Later, it was found to interact with spliceosome component Prp6, which is involved in pre-mRNA splicing [ (PUBMED:11054566) ]. Dim1 may act at the level of mRNA, which impacts the functioning of the APC/C, a critical complex in controlling mitotic progression [ (PUBMED:15755920) ]. It's worth noting that although the Dim proteins exhibit a thioredoxin-like fold, they lack the disulfide bond required for the thioredoxin redox activity [ (PUBMED:17558560) ].
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| GO process: | mRNA splicing, via spliceosome (GO:0000398) |
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| GO component: | U4/U6 x U5 tri-snRNP complex (GO:0046540) |
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| Family alignment: |
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There are 0 DIM1 domains in 0 proteins in SMART's nrdb database.
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Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R
- Identification, characterization and crystal structure analysis of the humanspliceosomal U5 snRNP-specific 15 kD protein.
- J Mol Biol. 1999; 294: 515-25
- Display abstract
The U5 small ribonucleoprotein particle (snRNP) contains various proteinsinvolved in catalytic activities mediating conformational rearrangements of thespliceosome. We have isolated and characterized the evolutionarily highlyconserved human U5 snRNP-specific protein U5-15kD. The crystal structure ofU5-15kD determined at 1.4 A resolution revealed a thioredoxin-like fold andrepresents the first structure of a U5 snRNP-specific protein known so far. With respect to human thioredoxin the U5-15kD protein contains 37 additional residues causing structural changes which most likely form putative binding sites forother spliceosomal proteins or RNA. Moreover, a novel intramolecular disulfidebond replaces the canonical one found in the thioredoxin family. Even thoughU5-15kD appears to lack protein disulfide isomerase activity, it is strictlyrequired for pre-mRNA splicing in vivo as we demonstrate by genetic depletion of its ortholog in Saccharomyces cerevisiae. Our data suggest that the previouslyreported involvement of its Schizosaccharomyces pombe ortholog Dim1p in cellcycle regulation is a consequence of its essential role in pre-mRNA splicing.
Structure (3D structures containing this domain)3D Structures of DIM1 domains in PDB
| PDB code | Main view | Title | | 1pqn |  | dominant negative human hDim1 (hDim1 1-128) |
| 1qgv |  | HUMAN SPLICEOSOMAL PROTEIN U5-15KD |
| 1syx |  | The crystal structure of a binary U5 snRNP complex |
| 1xbs |  | Crystal structure of human dim2: a dim1-like protein |
| 2av4 |  | Crystal structure of Plasmodium yoelii thioredoxin-like protein 4A (DIM1) |
| 3gix |  | Crystal structure of human splicing factor dim2 |
| 3jcm |  | 3JCM |
| 3jcr |  | 3JCR |
| 4bwq |  | Crystal structure of U5-15kD in a complex with PQBP1 |
| 4bws |  | Crystal structure of the heterotrimer of PQBP1, U5-15kD and U5-52kD. |
| 4cdo |  | Crystal structure of PQBP1 bound to spliceosomal U5-15kD |
| 4in0 |  | Crystal Structure of human splicing factor dim2/TXNL4B |
| 5gan |  | 5GAN |
| 5gap |  | 5GAP |
Links (links to other resources describing this domain)
