UniProt ID | PRP19_YEAST | |
---|---|---|
UniProt AC | P32523 | |
Protein Name | Pre-mRNA-processing factor 19 {ECO:0000305} | |
Gene Name | PRP19 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 503 | |
Subcellular Localization | Nucleus . | |
Protein Description | Probable ubiquitin-protein ligase involved in pre-mRNA splicing. Acts as a central component of the NTC complex (or PRP19-associated complex) that associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. It is also probably involved in DNA repair.. | |
Protein Sequence | MLCAISGKVPRRPVLSPKSRTIFEKSLLEQYVKDTGNDPITNEPLSIEEIVEIVPSAQQASLTESTNSATLKANYSIPNLLTSLQNEWDAIMLENFKLRSTLDSLTKKLSTVMYERDAAKLVAAQLLMEKNEDSKDLPKSSQQAVAITREEFLQGLLQSSRDFVARGKLKAPKWPILKNLELLQAQNYSRNIKTFPYKELNKSMYYDKWVCMCRCEDGALHFTQLKDSKTITTITTPNPRTGGEHPAIISRGPCNRLLLLYPGNQITILDSKTNKVLREIEVDSANEIIYMYGHNEVNTEYFIWADNRGTIGFQSYEDDSQYIVHSAKSDVEYSSGVLHKDSLLLALYSPDGILDVYNLSSPDQASSRFPVDEEAKIKEVKFADNGYWMVVECDQTVVCFDLRKDVGTLAYPTYTIPEFKTGTVTYDIDDSGKNMIAYSNESNSLTIYKFDKKTKNWTKDEESALCLQSDTADFTDMDVVCGDGGIAAILKTNDSFNIVALTP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
19 | Phosphorylation | RPVLSPKSRTIFEKS CCCCCCCCCCHHHHH | 37.73 | 21440633 | |
21 | Phosphorylation | VLSPKSRTIFEKSLL CCCCCCCCHHHHHHH | 36.79 | 21440633 | |
31 | Phosphorylation | EKSLLEQYVKDTGND HHHHHHHHHHHHCCC | 10.49 | 21440633 | |
110 | Phosphorylation | DSLTKKLSTVMYERD HHHHHHHHHHHHHHH | 28.03 | 19779198 | |
140 | Phosphorylation | DSKDLPKSSQQAVAI CCCCCCHHHHHHHHH | 31.29 | 22369663 | |
141 | Phosphorylation | SKDLPKSSQQAVAIT CCCCCHHHHHHHHHC | 32.22 | 22369663 | |
148 | Phosphorylation | SQQAVAITREEFLQG HHHHHHHCHHHHHHH | 23.45 | 22369663 | |
159 | Phosphorylation | FLQGLLQSSRDFVAR HHHHHHHHCCHHHHC | 27.58 | 22369663 | |
160 | Phosphorylation | LQGLLQSSRDFVARG HHHHHHHCCHHHHCC | 23.94 | 22369663 | |
173 | Acetylation | RGKLKAPKWPILKNL CCCCCCCCCHHHHCH | 71.15 | 24489116 | |
329 | Phosphorylation | YIVHSAKSDVEYSSG EEEEECCCCCEECCC | 46.75 | 30377154 | |
333 | Phosphorylation | SAKSDVEYSSGVLHK ECCCCCEECCCCCCC | 14.16 | 30377154 | |
334 | Phosphorylation | AKSDVEYSSGVLHKD CCCCCEECCCCCCCC | 13.70 | 30377154 | |
335 | Phosphorylation | KSDVEYSSGVLHKDS CCCCEECCCCCCCCE | 31.83 | 30377154 | |
348 | Phosphorylation | DSLLLALYSPDGILD CEEEEEEECCCCEEE | 16.73 | 30377154 | |
349 | Phosphorylation | SLLLALYSPDGILDV EEEEEEECCCCEEEE | 19.84 | 30377154 | |
404 | Acetylation | VVCFDLRKDVGTLAY EEEEEECCCCEECCC | 65.15 | 24489116 | |
433 | Acetylation | YDIDDSGKNMIAYSN EEECCCCCEEEEEEC | 47.50 | 24489116 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
141 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PRP19_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 PRP19_YEAST !! |
Kegg Drug | ||||||
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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-140 AND SER-141, ANDMASS SPECTROMETRY. | |
"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-141, AND MASSSPECTROMETRY. |