| UniProt ID | DXO_YEAST | |
|---|---|---|
| UniProt AC | P53063 | |
| Protein Name | Decapping nuclease RAI1 | |
| Gene Name | RAI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 387 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping and pyrophosphohydrolase activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates. Stimulates exoribonuclease activity of RAT1, allowing it to degrade RNAs with stable secondary structure more effectively. Required for the processing of nuclear mRNA and rRNA precursors. May promote termination of transcription by RNA polymerase II.. | |
| Protein Sequence | MGVSANLFVKQRGSTTALKQPKEIGFYSRTKDEEYLISDDTNLNYYYLPDAELDRKLDLSSGFQKFKDYYKDFEDRCSLRGLLETIESSERHKGKKINADIITFRGIARKLISCAFDSPSFNTVDLRIVSFNGQLFIKEVPEAVNAAKASSATEAGRNINQDLNVFTGYKFETLATLSNPLQYTPREVIEKRTKRIVSHGDEYISVVRTGVGNCKLILGAEVDCIFDFKENGRDNLKHYAELKCTQQVANISDTHKFERKLFRTWLQCFLVGIPRIIYGFKDDHYVLKTVEEFSTEEVPVLLKNNNPQVGSACLEAIKWYGLLTEWLLKMIPRDEDPHSQIRAFKLVFENNHLRLSEIEESDEEYSGLIDGEHILSNGFKEWRKSLK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MGVSANLFVKQ ----CCCCCEEEEEE | 30377154 | ||
| 41 | Phosphorylation | EYLISDDTNLNYYYL CEEECCCCCCCEEEC | 28889911 | ||
| 45 | Phosphorylation | SDDTNLNYYYLPDAE CCCCCCCEEECCHHH | 28889911 | ||
| 46 | Phosphorylation | DDTNLNYYYLPDAEL CCCCCCEEECCHHHH | 28889911 | ||
| 47 | Phosphorylation | DTNLNYYYLPDAELD CCCCCEEECCHHHHC | 28889911 | ||
| 65 | Acetylation | DLSSGFQKFKDYYKD CCCCCHHHHHHHHHC | 24489116 | ||
| 67 | Acetylation | SSGFQKFKDYYKDFE CCCHHHHHHHHHCHH | 24489116 | ||
| 71 | Acetylation | QKFKDYYKDFEDRCS HHHHHHHHCHHHHHH | 24489116 | ||
| 198 | Phosphorylation | KRTKRIVSHGDEYIS HHHHHHHHCCCCEEE | 25752575 | ||
| 256 | Acetylation | ANISDTHKFERKLFR CCCCCCHHHHHHHHH | 24489116 | ||
| 281 | Acetylation | PRIIYGFKDDHYVLK CHHHHEECCCCEEEE | 24489116 | ||
| 356 | Phosphorylation | ENNHLRLSEIEESDE ECCEEEHHHCCCCCC | 22369663 | ||
| 361 | Phosphorylation | RLSEIEESDEEYSGL EHHHCCCCCCHHCCC | 22369663 | ||
| 365 | Phosphorylation | IEESDEEYSGLIDGE CCCCCCHHCCCCCHH | 22369663 | ||
| 366 | Phosphorylation | EESDEEYSGLIDGEH CCCCCHHCCCCCHHH | 22369663 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of DXO_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DXO_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DXO_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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