| UniProt ID | PTA1_YEAST | |
|---|---|---|
| UniProt AC | Q01329 | |
| Protein Name | Pre-tRNA-processing protein PTA1 | |
| Gene Name | PTA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 785 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential in pre-tRNA processing. Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent transcript 3'-end formation.. | |
| Protein Sequence | MSSAEMEQLLQAKTLAMHNNPTEMLPKVLETTASMYHNGNLSKLKLPLAKFFTQLVLDVVSMDSPIANTERPFIAAQYLPLLLAMAQSTADVLVYKNIVLIMCASYPLVLDLVAKTSNQEMFDQLCMLKKFVLSHWRTAYPLRATVDDETDVEQWLAQIDQNIGVKLATIKFISEVVLSQTKSPSGNEINSSTIPDNHPVLNKPALESEAKRLLDMLLNYLIEEQYMVSSVFIGIINSLSFVIKRRPQTTIRILSGLLRFNVDAKFPLEGKSDLNYKLSKRFVERAYKNFVQFGLKNQIITKSLSSGSGSSIYSKLTKISQTLHVIGEETKSKGILNFDPSKGNSKKTLSRQDKLKYISLWKRQLSALLSTLGVSTKTPTPVSAPATGSSTENMLDQLKILQKYTLNKASHQGNTFFNNSPKPISNTYSSVYSLMNSSNSNQDVTQLPNDILIKLSTEAILQMDSTKLITGLSIVASRYTDLMNTYINSVPSSSSSKRKSDDDDDGNDNEEVGNDGPTANSKKIKMETEPLAEEPEEPEDDDRMQKMLQEEESAQEISGDANKSTSAIKEIAPPFEPDSLTQDEKLKYLSKLTKKLFELSGRQDTTRAKSSSSSSILLDDDDSSSWLHVLIRLVTRGIEAQEASDLIREELLGFFIQDFEQRVSLIIEWLNEEWFFQTSLHQDPSNYKKWSLRVLESLGPFLENKHRRFFIRLMSELPSLQSDHLEALKPICLDPARSSLGFQTLKFLIMFRPPVQDTVRDLLHQLKQEDEGLHKQCDSLLDRLK | |
| 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 |
|---|---|---|---|---|---|
| 13 | Acetylation | MEQLLQAKTLAMHNN HHHHHHHHHHHHCCC | 30.98 | 25381059 | |
| 27 | Acetylation | NPTEMLPKVLETTAS CHHHHHHHHHHHHHH | 56.33 | 25381059 | |
| 303 | Phosphorylation | KNQIITKSLSSGSGS CCCEEEEECCCCCCH | 25.49 | 27017623 | |
| 308 | Phosphorylation | TKSLSSGSGSSIYSK EEECCCCCCHHHHHH | 37.13 | 27017623 | |
| 311 | Phosphorylation | LSSGSGSSIYSKLTK CCCCCCHHHHHHHHH | 29.13 | 27017623 | |
| 315 | Acetylation | SGSSIYSKLTKISQT CCHHHHHHHHHHHHH | 43.11 | 24489116 | |
| 318 | Acetylation | SIYSKLTKISQTLHV HHHHHHHHHHHHEEC | 51.28 | 24489116 | |
| 320 | Phosphorylation | YSKLTKISQTLHVIG HHHHHHHHHHEECCC | 20.76 | 28889911 | |
| 322 | Phosphorylation | KLTKISQTLHVIGEE HHHHHHHHEECCCCC | 16.43 | 28889911 | |
| 330 | Phosphorylation | LHVIGEETKSKGILN EECCCCCCCCCCCCC | 35.99 | 28889911 | |
| 342 | Acetylation | ILNFDPSKGNSKKTL CCCCCCCCCCCCCCC | 68.45 | 24489116 | |
| 378 | Phosphorylation | TLGVSTKTPTPVSAP HHCCCCCCCCCCCCC | 32.27 | 27214570 | |
| 380 | Phosphorylation | GVSTKTPTPVSAPAT CCCCCCCCCCCCCCC | 41.37 | 27214570 | |
| 383 | Phosphorylation | TKTPTPVSAPATGSS CCCCCCCCCCCCCCC | 29.73 | 30377154 | |
| 403 | Acetylation | DQLKILQKYTLNKAS HHHHHHHHHCCCCCC | 36.44 | 24489116 | |
| 420 | Phosphorylation | GNTFFNNSPKPISNT CCCCCCCCCCCCCCC | 35.09 | 28889911 | |
| 427 | Phosphorylation | SPKPISNTYSSVYSL CCCCCCCCHHHHHHH | 20.28 | 27017623 | |
| 430 | Phosphorylation | PISNTYSSVYSLMNS CCCCCHHHHHHHHHC | 18.05 | 27017623 | |
| 432 | Phosphorylation | SNTYSSVYSLMNSSN CCCHHHHHHHHHCCC | 9.68 | 27017623 | |
| 433 | Phosphorylation | NTYSSVYSLMNSSNS CCHHHHHHHHHCCCC | 20.98 | 27017623 | |
| 438 | Phosphorylation | VYSLMNSSNSNQDVT HHHHHHCCCCCCCHH | 38.99 | 27017623 | |
| 440 | Phosphorylation | SLMNSSNSNQDVTQL HHHHCCCCCCCHHHC | 37.50 | 27017623 | |
| 477 | Phosphorylation | TGLSIVASRYTDLMN HHHHHHHHHHHHHHH | 18.22 | 27017623 | |
| 479 | Phosphorylation | LSIVASRYTDLMNTY HHHHHHHHHHHHHHH | 11.34 | 30377154 | |
| 489 | Phosphorylation | LMNTYINSVPSSSSS HHHHHHHCCCCCCCC | 26.33 | 30377154 | |
| 493 | Phosphorylation | YINSVPSSSSSKRKS HHHCCCCCCCCCCCC | 28.33 | 23749301 | |
| 494 | Phosphorylation | INSVPSSSSSKRKSD HHCCCCCCCCCCCCC | 42.86 | 23749301 | |
| 495 | Phosphorylation | NSVPSSSSSKRKSDD HCCCCCCCCCCCCCC | 41.65 | 23749301 | |
| 496 | Phosphorylation | SVPSSSSSKRKSDDD CCCCCCCCCCCCCCC | 38.13 | 23749301 | |
| 500 | Phosphorylation | SSSSKRKSDDDDDGN CCCCCCCCCCCCCCC | 50.75 | 25533186 | |
| 525 | Acetylation | TANSKKIKMETEPLA CCCCCCCCEECCCCC | 39.29 | 24489116 | |
| 528 | Phosphorylation | SKKIKMETEPLAEEP CCCCCEECCCCCCCC | 39.13 | 29688323 | |
| 553 | Phosphorylation | KMLQEEESAQEISGD HHHHHHHHHHHHCCC | 38.23 | 28889911 | |
| 558 | Phosphorylation | EESAQEISGDANKST HHHHHHHCCCCCCCH | 29.84 | 28889911 | |
| 566 | Phosphorylation | GDANKSTSAIKEIAP CCCCCCHHHHHHHCC | 34.78 | 25752575 | |
| 569 | Acetylation | NKSTSAIKEIAPPFE CCCHHHHHHHCCCCC | 42.66 | 24489116 | |
| 579 | Phosphorylation | APPFEPDSLTQDEKL CCCCCCCCCCHHHHH | 43.99 | 25704821 | |
| 588 | Phosphorylation | TQDEKLKYLSKLTKK CHHHHHHHHHHHHHH | 27.01 | 28889911 | |
| 590 | Phosphorylation | DEKLKYLSKLTKKLF HHHHHHHHHHHHHHH | 23.64 | 28889911 | |
| 593 | Phosphorylation | LKYLSKLTKKLFELS HHHHHHHHHHHHHHH | 29.84 | 28889911 | |
| 697 | Phosphorylation | WSLRVLESLGPFLEN HHHHHHHHHHHHHCH | 34.17 | 27017623 | |
| 779 | Phosphorylation | GLHKQCDSLLDRLK- HHHHHHHHHHHHHC- | 38.16 | 30377154 |
| 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 PTA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTA1_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 PTA1_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 THR-378 AND THR-380, ANDMASS SPECTROMETRY. | |
