| UniProt ID | PAT1_YEAST | |
|---|---|---|
| UniProt AC | P25644 | |
| Protein Name | DNA topoisomerase 2-associated protein PAT1 | |
| Gene Name | PAT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 796 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cytoplasm, P-body. | |
| Protein Description | Activator of decapping that functions as a general and active mechanism of translational repression and required for P-body formation. First decay factor recruited to mRNA, at a time when the mRNA is still associated with translation factors. Subsequently, PAT1 recruits the hepta-heterodimer LSM1-LSM7 complex to P-bodies. In association with the LSM1-LSM7 complex, stabilizes the 3' terminus of mRNAs. This association is also required for mosaic virus genomic RNA translation. Modulates the rates of mRNA-decapping that occur following deadenylation. Might be required for promoting the formation or the stabilization of the preinitiation translation complexes. Required for 40S ribosomal subunit joining to capped and/or polyadenylated mRNA. With other P-body components, enhances the formation of retrotransposition-competent Ty1 virus-like particles. Necessary for accurate chromosome transmission during cell division.. | |
| Protein Sequence | MSFFGLENSGNARDGPLDFEESYKGYGEHELEENDYLNDETFGDNVQVGTDFDFGNPHSSGSSGNAIGGNGVGATARSYVAATAEGISGPRTDGTAAAGPLDLKPMESLWSTAPPPAMAPSPQSTMAPAPAPQQMAPLQPILSMQDLERQQRQMQQQFMNFHAMGHPQGLPQGPPQQQFPMQPASGQPGPSQFAPPPPPPGVNVNMNQMPMGPVQVPVQASPSPIGMSNTPSPGPVVGATKMPLQSGRRSKRDLSPEEQRRLQIRHAKVEKILKYSGLMTPRDKDFITRYQLSQIVTEDPYNEDFYFQVYKIIQRGGITSESNKGLIARAYLEHSGHRLGGRYKRTDIALQRMQSQVEKAVTVAKERPSKLKDQQAAAGNSSQDNKQANTVLGKISSTLNSKNPRRQLQIPRQQPSDPDALKDVTDSLTNVDLASSGSSSTGSSAAAVASKQRRRSSYAFNNGNGATNLNKSGGKKFILELIETVYEEILDLEANLRNGQQTDSTAMWEALHIDDSSYDVNPFISMLSFDKGIKIMPRIFNFLDKQQKLKILQKIFNELSHLQIIILSSYKTTPKPTLTQLKKVDLFQMIILKIIVSFLSNNSNFIEIMGLLLQLIRNNNVSFLTTSKIGLNLITILISRAALIKQDSSRSNILSSPEISTWNEIYDKLFTSLESKIQLIFPPREYNDHIMRLQNDKFMDEAYIWQFLASLALSGKLNHQRIIIDEVRDEIFATINEAETLQKKEKELSVLPQRSQELDTELKSIIYNKEKLYQDLNLFLNVMGLVYRDGEISELK | |
| 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 | ------MSFFGLENS ------CCCCCCCCC | 29.32 | 22814378 | |
| 2 | Phosphorylation | ------MSFFGLENS ------CCCCCCCCC | 29.32 | 22369663 | |
| 9 | Phosphorylation | SFFGLENSGNARDGP CCCCCCCCCCCCCCC | 24.85 | 28889911 | |
| 60 | Phosphorylation | DFGNPHSSGSSGNAI CCCCCCCCCCCCCCC | 39.39 | 28889911 | |
| 63 | Phosphorylation | NPHSSGSSGNAIGGN CCCCCCCCCCCCCCC | 39.32 | 28889911 | |
| 78 | Phosphorylation | GVGATARSYVAATAE CCCHHHHHHHHHHCC | 22.84 | 22369663 | |
| 79 | Phosphorylation | VGATARSYVAATAEG CCHHHHHHHHHHCCC | 6.64 | 25752575 | |
| 232 | Phosphorylation | IGMSNTPSPGPVVGA CCCCCCCCCCCCCCC | 40.21 | 28889911 | |
| 255 | Phosphorylation | RRSKRDLSPEEQRRL CCCCCCCCHHHHHHH | 34.26 | 29136822 | |
| 320 | Phosphorylation | IQRGGITSESNKGLI HHCCCCCCCCCCCHH | 36.79 | 21551504 | |
| 324 | Ubiquitination | GITSESNKGLIARAY CCCCCCCCCHHHHHH | 65.46 | 23749301 | |
| 346 | Phosphorylation | LGGRYKRTDIALQRM CCCCHHHHHHHHHHH | 27.83 | 19823750 | |
| 355 | Phosphorylation | IALQRMQSQVEKAVT HHHHHHHHHHHHHHH | 27.18 | 20377248 | |
| 372 | Ubiquitination | KERPSKLKDQQAAAG HHCCHHHHHHHHHCC | 58.17 | 23749301 | |
| 381 | Phosphorylation | QQAAAGNSSQDNKQA HHHHCCCCCHHHHHH | 28.58 | 28889911 | |
| 382 | Phosphorylation | QAAAGNSSQDNKQAN HHHCCCCCHHHHHHH | 45.62 | 28889911 | |
| 386 | Ubiquitination | GNSSQDNKQANTVLG CCCCHHHHHHHHHHH | 60.11 | 23749301 | |
| 397 | Phosphorylation | TVLGKISSTLNSKNP HHHHHHHHHHCCCCH | 40.15 | 27017623 | |
| 416 | Phosphorylation | QIPRQQPSDPDALKD CCCCCCCCCHHHHHH | 58.39 | 28889911 | |
| 425 | Phosphorylation | PDALKDVTDSLTNVD HHHHHHHHHHHCCCE | 29.97 | 28889911 | |
| 427 | Phosphorylation | ALKDVTDSLTNVDLA HHHHHHHHHCCCEEC | 27.94 | 28889911 | |
| 435 | Phosphorylation | LTNVDLASSGSSSTG HCCCEECCCCCCCCC | 42.39 | 28889911 | |
| 436 | Phosphorylation | TNVDLASSGSSSTGS CCCEECCCCCCCCCH | 36.77 | 21551504 | |
| 438 | Phosphorylation | VDLASSGSSSTGSSA CEECCCCCCCCCHHH | 24.06 | 21551504 | |
| 439 | Phosphorylation | DLASSGSSSTGSSAA EECCCCCCCCCHHHH | 35.13 | 19779198 | |
| 450 | Phosphorylation | SSAAAVASKQRRRSS HHHHHHHHHCCCHHC | 23.79 | 28889911 | |
| 456 | Phosphorylation | ASKQRRRSSYAFNNG HHHCCCHHCCCCCCC | 26.37 | 22369663 | |
| 457 | Phosphorylation | SKQRRRSSYAFNNGN HHCCCHHCCCCCCCC | 20.76 | 22369663 | |
| 458 | Phosphorylation | KQRRRSSYAFNNGNG HCCCHHCCCCCCCCC | 19.23 | 22369663 | |
| 467 | Phosphorylation | FNNGNGATNLNKSGG CCCCCCCCCCCCCCC | 41.45 | 29136822 | |
| 472 | Phosphorylation | GATNLNKSGGKKFIL CCCCCCCCCCCHHHH | 52.27 | 21440633 | |
| 531 | Acetylation | ISMLSFDKGIKIMPR HHHHCCCCCCCHHHH | 61.60 | 25381059 | |
| 534 | Acetylation | LSFDKGIKIMPRIFN HCCCCCCCHHHHHHH | 41.44 | 25381059 | |
| 545 | Acetylation | RIFNFLDKQQKLKIL HHHHHCCHHHHHHHH | 57.69 | 24489116 | |
| 746 | Acetylation | ETLQKKEKELSVLPQ HHHHHHHHHHHCCCH | 73.21 | 24489116 | |
| 764 | Phosphorylation | ELDTELKSIIYNKEK HHHHHHHHHHHCHHH | 27.18 | 19823750 | |
| 767 | Phosphorylation | TELKSIIYNKEKLYQ HHHHHHHHCHHHHHH | 20.64 | 19823750 |
| 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 PAT1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PAT1_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 PAT1_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-60; SER-63; TYR-79;SER-232; SER-456; SER-457 AND TYR-458, AND MASS 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-456 AND SER-457, 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-456 AND SER-457, ANDMASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND TYR-458, ANDMASS SPECTROMETRY. | |
