| UniProt ID | PRP2_YEAST | |
|---|---|---|
| UniProt AC | P20095 | |
| Protein Name | Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein PRP2 | |
| Gene Name | PRP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 876 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Involved in pre-mRNA splicing. Is required together with ATP and at least one other factor, for the first cleavage-ligation reaction. Functions as a molecular motor in the activation of the precatalytic spliceosome for the first transesterification reaction of pre-mRNA splicing by hydrolyzing ATP to cause the activation of the spliceosome without the occurrence of splicing. Capable of hydrolyzing nucleoside triphosphates in the presence of single-stranded RNAs such as poly(U).. | |
| Protein Sequence | MSSITSETGKRRVKRTYEVTRQNDNAVRIEPSSLGEEEDKEAKDKNSALQLKRSRYDPNKVFSNTNQGPEKNNLKGEQLGSQKKSSKYDEKITSNNELTTKKGLLGDSENETKYASSNSKFNVEVTHKIKNAKEIDKINRQRMWEEQQLRNAMAGQSDHPDDITLEGSDKYDYVFDTDAMIDYTNEEDDLLPEEKLQYEARLAQALETEEKRILTIQEARKLLPVHQYKDELLQEIKKNQVLIIMGETGSGKTTQLPQYLVEDGFTDQGKLQIAITQPRRVAATSVAARVADEMNVVLGKEVGYQIRFEDKTTPNKTVLKYMTDGMLLREFLTDSKLSKYSCIMIDEAHERTLATDILIGLLKDILPQRPTLKLLISSATMNAKKFSEFFDNCPIFNVPGRRYPVDIHYTLQPEANYIHAAITTIFQIHTTQSLPGDILVFLTGQEEIERTKTKLEEIMSKLGSRTKQMIITPIYANLPQEQQLKIFQPTPENCRKVVLATNIAETSLTIDGIRYVIDPGFVKENSYVPSTGMTQLLTVPCSRASVDQRAGRAGRVGPGKCFRIFTKWSYLHELELMPKPEITRTNLSNTVLLLLSLGVTDLIKFPLMDKPSIPTLRKSLENLYILGALNSKGTITRLGKMMCEFPCEPEFAKVLYTAATHEQCQGVLEECLTIVSMLHETPSLFIGQKRDAAASVLSEVESDHILYLEIFNQWRNSKFSRSWCQDHKIQFKTMLRVRNIRNQLFRCSEKVGLVEKNDQARMKIGNIAGYINARITRCFISGFPMNIVQLGPTGYQTMGRSSGGLNVSVHPTSILFVNHKEKAQRPSKYVLYQQLMLTSKEFIRDCLVIPKEEWLIDMVPQIFKDLIDDKTNRGRR | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSITSETG ------CCCCCCHHH | 30.37 | 22814378 | |
| 47 | Phosphorylation | KEAKDKNSALQLKRS HHHCCCCHHHHHHHH | 35.78 | 21126336 | |
| 94 | Phosphorylation | KYDEKITSNNELTTK CCCCCCCCCCCEECC | 40.92 | 30377154 | |
| 101 | Acetylation | SNNELTTKKGLLGDS CCCCEECCCCCCCCC | 39.34 | 25381059 | |
| 120 | Acetylation | KYASSNSKFNVEVTH HCCCCCCCCEEEEEE | 45.25 | 25381059 | |
| 284 | Phosphorylation | QPRRVAATSVAARVA CCCHHHHHHHHHHHH | 17.62 | 17563356 | |
| 619 | Phosphorylation | SIPTLRKSLENLYIL CCHHHHHHHHHHHHH | 34.19 | 28889911 | |
| 624 | Phosphorylation | RKSLENLYILGALNS HHHHHHHHHHHHHCC | 12.99 | 28889911 | |
| 631 | Phosphorylation | YILGALNSKGTITRL HHHHHHCCCCCCCHH | 33.06 | 28889911 |
| 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 PRP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRP2_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 PRP2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-284, AND MASSSPECTROMETRY. | |
