| UniProt ID | PRP43_YEAST | |
|---|---|---|
| UniProt AC | P53131 | |
| Protein Name | Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43 | |
| Gene Name | PRP43 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 767 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.. | |
| Protein Sequence | MGSKRRFSSEHPDPVETSIPEQAAEIAEELSKQHPLPSEEPLVHHDAGEFKGLQRHHTSAEEAQKLEDGKINPFTGREFTPKYVDILKIRRELPVHAQRDEFLKLYQNNQIMVFVGETGSGKTTQIPQFVLFDEMPHLENTQVACTQPRRVAAMSVAQRVAEEMDVKLGEEVGYSIRFENKTSNKTILKYMTDGMLLREAMEDHDLSRYSCIILDEAHERTLATDILMGLLKQVVKRRPDLKIIIMSATLDAEKFQRYFNDAPLLAVPGRTYPVELYYTPEFQRDYLDSAIRTVLQIHATEEAGDILLFLTGEDEIEDAVRKISLEGDQLVREEGCGPLSVYPLYGSLPPHQQQRIFEPAPESHNGRPGRKVVISTNIAETSLTIDGIVYVVDPGFSKQKVYNPRIRVESLLVSPISKASAQQRAGRAGRTRPGKCFRLYTEEAFQKELIEQSYPEILRSNLSSTVLELKKLGIDDLVHFDFMDPPAPETMMRALEELNYLACLDDEGNLTPLGRLASQFPLDPMLAVMLIGSFEFQCSQEILTIVAMLSVPNVFIRPTKDKKRADDAKNIFAHPDGDHITLLNVYHAFKSDEAYEYGIHKWCRDHYLNYRSLSAADNIRSQLERLMNRYNLELNTTDYESPKYFDNIRKALASGFFMQVAKKRSGAKGYITVKDNQDVLIHPSTVLGHDAEWVIYNEFVLTSKNYIRTVTSVRPEWLIEIAPAYYDLSNFQKGDVKLSLERIKEKVDRLNELKQGKNKKKSKHSKK | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MGSKRRFSSEHPDPV CCCCCCCCCCCCCCC | 32.76 | 22369663 | |
| 9 | Phosphorylation | GSKRRFSSEHPDPVE CCCCCCCCCCCCCCC | 36.89 | 22369663 | |
| 17 | Phosphorylation | EHPDPVETSIPEQAA CCCCCCCCCCHHHHH | 31.99 | 22890988 | |
| 18 | Phosphorylation | HPDPVETSIPEQAAE CCCCCCCCCHHHHHH | 23.73 | 25521595 | |
| 31 | Phosphorylation | AEIAEELSKQHPLPS HHHHHHHHHHCCCCC | 33.28 | 22890988 | |
| 38 | Phosphorylation | SKQHPLPSEEPLVHH HHHCCCCCCCCCCCC | 63.37 | 21440633 | |
| 82 | Acetylation | TGREFTPKYVDILKI CCCCCCHHHHHHHHH | 55.65 | 24489116 | |
| 88 | Acetylation | PKYVDILKIRRELPV HHHHHHHHHHCCCCC | 34.20 | 24489116 | |
| 183 | Phosphorylation | IRFENKTSNKTILKY EEECCCCCCCCHHHH | 37.63 | 27017623 | |
| 192 | Phosphorylation | KTILKYMTDGMLLRE CCHHHHHHCCHHHHH | 26.72 | 27017623 | |
| 247 | Phosphorylation | DLKIIIMSATLDAEK CCEEEEEECCCCHHH | 14.00 | 21126336 | |
| 249 | Phosphorylation | KIIIMSATLDAEKFQ EEEEEECCCCHHHHH | 20.19 | 21126336 | |
| 324 | Phosphorylation | EDAVRKISLEGDQLV HHHHHHHCCCHHHHH | 24.33 | 28889911 | |
| 414 | Phosphorylation | RVESLLVSPISKASA EEEEEEECCCCHHHH | 19.24 | 25521595 | |
| 417 | Phosphorylation | SLLVSPISKASAQQR EEEECCCCHHHHHHH | 26.08 | 24961812 | |
| 460 | Phosphorylation | SYPEILRSNLSSTVL HHHHHHHCCCCHHHH | 38.38 | 21126336 | |
| 614 | Phosphorylation | YLNYRSLSAADNIRS CCCHHHCHHHHHHHH | 23.74 | 28889911 | |
| 643 | Acetylation | TTDYESPKYFDNIRK CCCCCCCHHHHHHHH | 68.76 | 24489116 | |
| 654 | Phosphorylation | NIRKALASGFFMQVA HHHHHHHHCHHHHHH | 36.66 | 27017623 | |
| 662 | Methylation | GFFMQVAKKRSGAKG CHHHHHHHHCCCCCC | 50.27 | 20137074 | |
| 670 | Phosphorylation | KRSGAKGYITVKDNQ HCCCCCCEEEEECCC | 7.85 | 21440633 | |
| 672 | Phosphorylation | SGAKGYITVKDNQDV CCCCCEEEEECCCCE | 17.02 | 21440633 |
| 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 PRP43_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRP43_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 PRP43_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-9, AND MASSSPECTROMETRY. | |
| "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 SER-8; SER-9 AND SER-18, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASSSPECTROMETRY. | |
