| UniProt ID | XRN1_YEAST | |
|---|---|---|
| UniProt AC | P22147 | |
| Protein Name | 5'-3' exoribonuclease 1 | |
| Gene Name | XRN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1528 | |
| Subcellular Localization | Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. | |
| Protein Description | Multifunctional protein that exhibits several independent functions at different levels of the cellular processes. 5'-3' exonuclease component of the nonsense-mediated mRNA decay (NMD) which is a highly conserved mRNA degradation pathway, an RNA surveillance system whose role is to identify and rid cells of mRNA with premature termination codons and thus prevents accumulation of potentially harmful truncated proteins. The NMD pathway has a second role regulating the decay of wild-type mRNAs, and especially mRNAs that are important for telomere functions. Participate in CTH2-mediated and VTS1-mediated mRNA turnover. Involved in the degradation of several hypomodified mature tRNA species and participates in the 5'-processing or the degradation of the snoRNA precursors and rRNA processing. Involved in defense against virus and suppresses viral RNA recombination by rapidly removing the 5'-truncated RNAs, the substrates of recombination, and thus reducing the chance for recombination to occur in the parental strain. Required for the assembly of the virus-like particles of the Ty3 retrotransposon and contributes to the efficient generation of narnavirus 20S RNA by playing a major role in the elimination of the non-viral upstream sequences from the primary transcripts. Degrades single-stranded DNA (ss-DNA) and can renature complementary ss-DNA as well as catalyzes the formation of heteroduplex DNA from circular ss-DNA and homologous linear ds-DNA in vitro. Acts as a microtubule-associated protein which interacts with cytoplasmic microtubules through beta-tubulin and promotes in vitro assembly of tubulin into microtubules. Associates with microtubule functions such as chromosome transmission, nuclear migration, and SPB duplication. Has also a role in G1 to S transition and is involved in nuclear fusion during karyogamy. Required for the expression of ROK1 at the post-transcriptional level and for the alpha-factor induction of the karyogamy genes KAR3 and KAR4. Plays a role in filamentous growth.. | |
| Protein Sequence | MGIPKFFRYISERWPMILQLIEGTQIPEFDNLYLDMNSILHNCTHGNDDDVTKRLTEEEVFAKICTYIDHLFQTIKPKKIFYMAIDGVAPRAKMNQQRARRFRTAMDAEKALKKAIENGDEIPKGEPFDSNSITPGTEFMAKLTKNLQYFIHDKISNDSKWREVQIIFSGHEVPGEGEHKIMNFIRHLKSQKDFNQNTRHCIYGLDADLIMLGLSTHGPHFALLREEVTFGRRNSEKKSLEHQNFYLLHLSLLREYMELEFKEIADEMQFEYNFERILDDFILVMFVIGNDFLPNLPDLHLNKGAFPVLLQTFKEALLHTDGYINEHGKINLKRLGVWLNYLSQFELLNFEKDDIDVEWFNKQLENISLEGERKRQRVGKKLLVKQQKKLIGSIKPWLMEQLQEKLSPDLPDEEIPTLELPKDLDMKDHLEFLKEFAFDLGLFITHSKSKGSYSLKMDLDSINPDETEEEFQNRVNSIRKTIKKYQNAIIVEDKEELETEKTIYNERFERWKHEYYHDKLKFTTDSEEKVRDLAKDYVEGLQWVLYYYYRGCPSWSWYYPHHYAPRISDLAKGLDQDIEFDLSKPFTPFQQLMAVLPERSKNLIPPAFRPLMYDEQSPIHDFYPAEVQLDKNGKTADWEAVVLISFVDEKRLIEAMQPYLRKLSPEEKTRNQFGKDLIYSFNPQVDNLYKSPLGGIFSDIEHNHCVEKEYITIPLDSSEIRYGLLPNAKLGAEMLAGFPTLLSLPFTSSLEYNETMVFQQPSKQQSMVLQITDIYKTNNVTLEDFSKRHLNKVIYTRWPYLRESKLVSLTDGKTIYEYQESNDKKKFGFITKPAETQDKKLFNSLKNSMLRMYAKQKAVKIGPMEAIATVFPVTGLVRDSDGGYIKTFSPTPDYYPLQLVVESVVNEDERYKERGPIPIEEEFPLNSKVIFLGDYAYGGETTIDGYSSDRRLKITVEKKFLDSEPTIGKERLQMDHQAVKYYPSYIVSKNMHLHPLFLSKITSKFMITDATGKHINVGIPVKFEARHQKVLGYARRNPRGWEYSNLTLNLLKEYRQTFPDFFFRLSKVGNDIPVLEDLFPDTSTKDAMNLLDGIKQWLKYVSSKFIAVSLESDSLTKTSIAAVEDHIMKYAANIEGHERKQLAKVPREAVLNPRSSFALLRSQKFDLGDRVVYIQDSGKVPIFSKGTVVGYTTLSSSLSIQVLFDHEIVAGNNFGGRLRTNRGLGLDASFLLNITNRQFIYHSKASKKALEKKKQSNNRNNNTKTAHKTPSKQQSEEKLRKERAHDLLNFIKKDTNEKNSESVDNKSMGSQKDSKPAKKVLLKRPAQKSSENVQVDLANFEKAPLDNPTVAGSIFNAVANQYSDGIGSNLNIPTPPHPMNVVGGPIPGANDVADVGLPYNIPPGFMTHPNGLHPLHPHQMPYPNMNGMSIPPPAPHGFGQPISFPPPPPMTNVSDQGSRIVVNEKESQDLKKFINGKQHSNGSTIGGETKNSRKGEIKPSSGTNSTECQSPKSQSNAADRDNKKDEST | |
| 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 |
|---|---|---|---|---|---|
| 124 | Ubiquitination | ENGDEIPKGEPFDSN HCCCCCCCCCCCCCC | 79.96 | 23749301 | |
| 124 | Acetylation | ENGDEIPKGEPFDSN HCCCCCCCCCCCCCC | 79.96 | 24489116 | |
| 149 | Phosphorylation | KLTKNLQYFIHDKIS HHHHHHHHHHCCCCC | 13.99 | 28132839 | |
| 154 | Acetylation | LQYFIHDKISNDSKW HHHHHCCCCCCCCCC | 33.59 | 24489116 | |
| 189 | Ubiquitination | MNFIRHLKSQKDFNQ HHHHHHHHHCCCCCC | 44.72 | 22817900 | |
| 192 | Ubiquitination | IRHLKSQKDFNQNTR HHHHHHCCCCCCCHH | 71.96 | 23749301 | |
| 395 | Acetylation | KKLIGSIKPWLMEQL HHHHHHHHHHHHHHH | 31.66 | 24489116 | |
| 450 | Acetylation | FITHSKSKGSYSLKM EEEECCCCCCEEEEE | 56.46 | 24489116 | |
| 454 | Phosphorylation | SKSKGSYSLKMDLDS CCCCCCEEEEEEHHH | 24.18 | 17563356 | |
| 456 | Ubiquitination | SKGSYSLKMDLDSIN CCCCEEEEEEHHHCC | 25.16 | 17644757 | |
| 494 | Acetylation | NAIIVEDKEELETEK CEEEECCHHHHHCCC | 39.31 | 24489116 | |
| 529 | 2-Hydroxyisobutyrylation | FTTDSEEKVRDLAKD CCCCCHHHHHHHHHH | 38.22 | - | |
| 600 | Phosphorylation | MAVLPERSKNLIPPA HHHCCHHHCCCCCCC | 25.00 | 21440633 | |
| 690 | Ubiquitination | PQVDNLYKSPLGGIF HHHHHHHCCCCCCCC | 49.08 | 17644757 | |
| 698 | Phosphorylation | SPLGGIFSDIEHNHC CCCCCCCCCCCCCCC | 35.44 | 21440633 | |
| 708 | Ubiquitination | EHNHCVEKEYITIPL CCCCCEECEEEEEEC | 35.11 | 17644757 | |
| 787 | Acetylation | VTLEDFSKRHLNKVI CCHHHHHHHHHHHHH | 43.78 | 24489116 | |
| 813 | Acetylation | LVSLTDGKTIYEYQE EEECCCCCEEEEEHH | 34.26 | 24489116 | |
| 831 | Phosphorylation | KKKFGFITKPAETQD CEEEEEECCCHHHCC | 28.81 | 22369663 | |
| 836 | Phosphorylation | FITKPAETQDKKLFN EECCCHHHCCHHHHH | 44.14 | 22369663 | |
| 839 | Acetylation | KPAETQDKKLFNSLK CCHHHCCHHHHHHHH | 41.37 | 24489116 | |
| 887 | Phosphorylation | SDGGYIKTFSPTPDY CCCCEEEEECCCCCC | 21.56 | 22369663 | |
| 889 | Phosphorylation | GGYIKTFSPTPDYYP CCEEEEECCCCCCCC | 32.85 | 22369663 | |
| 891 | Phosphorylation | YIKTFSPTPDYYPLQ EEEEECCCCCCCCCC | 27.82 | 22369663 | |
| 894 | Phosphorylation | TFSPTPDYYPLQLVV EECCCCCCCCCCEEE | 14.26 | 22369663 | |
| 895 | Phosphorylation | FSPTPDYYPLQLVVE ECCCCCCCCCCEEEE | 12.59 | 22369663 | |
| 903 | Phosphorylation | PLQLVVESVVNEDER CCCEEEEECCCCCHH | 21.54 | 22369663 | |
| 980 | Acetylation | QMDHQAVKYYPSYIV HCCHHHHHHCCHHHH | 41.92 | 24489116 | |
| 989 | Acetylation | YPSYIVSKNMHLHPL CCHHHHCCCCCCCHH | 47.60 | 24489116 | |
| 1004 | Acetylation | FLSKITSKFMITDAT HHHHHCCCEEEECCC | 30.24 | 24489116 | |
| 1022 | Acetylation | INVGIPVKFEARHQK EEEECEEEEEEHHHH | 31.94 | 24489116 | |
| 1067 | Ubiquitination | DFFFRLSKVGNDIPV HHHHHHHHCCCCCCC | 59.77 | 17644757 | |
| 1082 | Phosphorylation | LEDLFPDTSTKDAMN HHHHCCCCCCHHHHH | 38.24 | 26447709 | |
| 1083 | Phosphorylation | EDLFPDTSTKDAMNL HHHCCCCCCHHHHHH | 40.62 | 26447709 | |
| 1084 | Phosphorylation | DLFPDTSTKDAMNLL HHCCCCCCHHHHHHH | 34.73 | 26447709 | |
| 1085 | Ubiquitination | LFPDTSTKDAMNLLD HCCCCCCHHHHHHHH | 43.17 | 17644757 | |
| 1099 | Acetylation | DGIKQWLKYVSSKFI HHHHHHHHHHHHCEE | 40.42 | 24489116 | |
| 1156 | Phosphorylation | AVLNPRSSFALLRSQ HHCCCHHHHHHHHHC | 18.80 | 21440633 | |
| 1177 | Phosphorylation | RVVYIQDSGKVPIFS EEEEEECCCCEEEEC | 24.92 | 27017623 | |
| 1272 | Acetylation | TAHKTPSKQQSEEKL CCCCCCCHHHHHHHH | 54.26 | 23572591 | |
| 1292 | Acetylation | HDLLNFIKKDTNEKN HHHHHHHHHCCCCCC | 40.22 | 24489116 | |
| 1298 | Ubiquitination | IKKDTNEKNSESVDN HHHCCCCCCCCCCCC | 68.77 | 23749301 | |
| 1300 | Phosphorylation | KDTNEKNSESVDNKS HCCCCCCCCCCCCCC | 42.17 | 19795423 | |
| 1302 | Phosphorylation | TNEKNSESVDNKSMG CCCCCCCCCCCCCCC | 34.29 | 29136822 | |
| 1307 | Phosphorylation | SESVDNKSMGSQKDS CCCCCCCCCCCCCCC | 34.33 | 23749301 | |
| 1310 | Phosphorylation | VDNKSMGSQKDSKPA CCCCCCCCCCCCCCH | 25.97 | 29136822 | |
| 1329 | Phosphorylation | LKRPAQKSSENVQVD HCCCCCCCCCCCEEE | 30.70 | 22369663 | |
| 1330 | Phosphorylation | KRPAQKSSENVQVDL CCCCCCCCCCCEEEC | 39.98 | 25521595 | |
| 1467 | Phosphorylation | IVVNEKESQDLKKFI EEECCCCCCCHHHHH | 39.81 | 30377154 | |
| 1480 | Phosphorylation | FINGKQHSNGSTIGG HHCCEECCCCCCCCC | 40.15 | 22369663 | |
| 1483 | Phosphorylation | GKQHSNGSTIGGETK CEECCCCCCCCCCCC | 22.54 | 22369663 | |
| 1484 | Phosphorylation | KQHSNGSTIGGETKN EECCCCCCCCCCCCC | 25.66 | 22369663 | |
| 1489 | Phosphorylation | GSTIGGETKNSRKGE CCCCCCCCCCCCCCC | 38.51 | 22369663 | |
| 1492 | Phosphorylation | IGGETKNSRKGEIKP CCCCCCCCCCCCCCC | 36.60 | 27017623 | |
| 1494 | Ubiquitination | GETKNSRKGEIKPSS CCCCCCCCCCCCCCC | 61.79 | 23749301 | |
| 1498 | Ubiquitination | NSRKGEIKPSSGTNS CCCCCCCCCCCCCCC | 34.25 | 23749301 | |
| 1500 | Phosphorylation | RKGEIKPSSGTNSTE CCCCCCCCCCCCCCC | 36.08 | 22369663 | |
| 1501 | Phosphorylation | KGEIKPSSGTNSTEC CCCCCCCCCCCCCCC | 59.15 | 22890988 | |
| 1503 | Phosphorylation | EIKPSSGTNSTECQS CCCCCCCCCCCCCCC | 28.13 | 22890988 | |
| 1505 | Phosphorylation | KPSSGTNSTECQSPK CCCCCCCCCCCCCCH | 25.97 | 22369663 | |
| 1506 | Phosphorylation | PSSGTNSTECQSPKS CCCCCCCCCCCCCHH | 42.73 | 22369663 | |
| 1510 | Phosphorylation | TNSTECQSPKSQSNA CCCCCCCCCHHHCCC | 46.05 | 22369663 | |
| 1512 | Ubiquitination | STECQSPKSQSNAAD CCCCCCCHHHCCCCC | 67.39 | 17644757 | |
| 1513 | Phosphorylation | TECQSPKSQSNAADR CCCCCCHHHCCCCCC | 42.07 | 20377248 | |
| 1515 | Phosphorylation | CQSPKSQSNAADRDN CCCCHHHCCCCCCCC | 35.21 | 21551504 | |
| 1523 | Ubiquitination | NAADRDNKKDEST-- CCCCCCCCCCCCC-- | 66.93 | 17644757 | |
| 1524 | Ubiquitination | AADRDNKKDEST--- CCCCCCCCCCCC--- | 73.34 | 17644757 |
| 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 XRN1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of XRN1_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 XRN1_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-1329; SER-1330 ANDSER-1510, 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-454; SER-1505 ANDSER-1510, AND MASS 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-1329 AND SER-1510, ANDMASS SPECTROMETRY. | |
| "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-1329, AND MASSSPECTROMETRY. | |
