UniProt ID | XRS2_YEAST | |
---|---|---|
UniProt AC | P33301 | |
Protein Name | DNA repair protein XRS2 | |
Gene Name | XRS2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 854 | |
Subcellular Localization | ||
Protein Description | During meiosis is involved in homologous recombination and during vegetative growth it is necessary for DNA repair. It probably regulates the 5'-3' exonuclease degradation of double strand breaks either at the initiation stage or a later stage.. | |
Protein Sequence | MWVVRYQNTLEDGSISFISCCLQAFKTYSIGRSSKNPLIIKNDKSISRQHITFKWEINNSSDLKHSSLCLVNKGKLTSLNKKFMKVGETFTINASDVLKSTIIELGTTPIRIEFEWINEVWNIPPHLTQFRTMLSEYGISTEISINDIPANLMISDYPKSEDNSIRELYALVSTIPMKKSRFLMELCNTLLPTSKTNLKFDEMWNDMISNPEYNVFDFDPNILLSKFMRLNNIRVLTTIKSEPRLSSLLRTFNINLFAFDNIDSLYKYVDSLEASTEYLILTTTDKKENGKILCTIKTMLTSIIDGTLSAVINMKGASSRTLDNGKFDQISEGMSTILKTSRAPEVEASPVVSKKRKLNRRRVLPLDSLDFFAGGLSTKTLSENRSLTDAKRLNCGAESKTVISSPNIAEADEKHAPFLQNALKPTEDIGKKSGHSSPGAIIVSSPNLGTVNTSEDSLDKSLQSHKLPQPSLPEVAGIGSQTISSNSADYETAAVNSMDDAEVTKNFRVNHHQNIEQPSKNIRKLSNYSREISSPLQENCKSPVKELSIKEKSGTPHAFVEAIQETKNREVKRVKSTIVELKDEELSEEAINQLKNLAIVEPSNNLLRKSFDSEGNKTSRTTEKWENSLMEPEWHKRKNFKTFVKVRPKSKAHKEEGKNNTQSSDFIRNAAFLITRNYVPLKKYSKKDTTTKWGTEENEDMFALTEMERFGSNTFMSDNINSNTIQKRSQALNRFTNEDSSNEGEEDSFSFSRCSGTAASVQPLKNKIFITDEDDLGDIDDKSDRLNHRENNRNLFVVKEMNLRPNLSEECSKQSRHSRSATSRSRGSFGASNNGDGDDDDDDGPKFTFKRRKG | |
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 |
---|---|---|---|---|---|
44 | Acetylation | PLIIKNDKSISRQHI CEEEECCCCCCCCCE | 60.11 | 25381059 | |
268 | Phosphorylation | NIDSLYKYVDSLEAS CHHHHHHHHHHHHHC | 8.91 | 30377154 | |
271 | Phosphorylation | SLYKYVDSLEASTEY HHHHHHHHHHHCCCE | 20.33 | 30377154 | |
278 | Phosphorylation | SLEASTEYLILTTTD HHHHCCCEEEEEECC | 10.11 | 30377154 | |
349 | Phosphorylation | RAPEVEASPVVSKKR CCCCCCCCCCCCCCC | 12.53 | 25533186 | |
353 | Phosphorylation | VEASPVVSKKRKLNR CCCCCCCCCCCCCCC | 32.47 | 30377154 | |
386 | Phosphorylation | KTLSENRSLTDAKRL CCHHCCCCCCHHHHC | 47.40 | 28889911 | |
388 | Phosphorylation | LSENRSLTDAKRLNC HHCCCCCCHHHHCCC | 34.85 | 28889911 | |
401 | Phosphorylation | NCGAESKTVISSPNI CCCCCCCEEECCCCH | 32.14 | 21126336 | |
404 | Phosphorylation | AESKTVISSPNIAEA CCCCEEECCCCHHHH | 35.09 | 21551504 | |
405 | Phosphorylation | ESKTVISSPNIAEAD CCCEEECCCCHHHHH | 15.73 | 25752575 | |
433 | Phosphorylation | TEDIGKKSGHSSPGA HHHCCCCCCCCCCCE | 45.27 | 20377248 | |
436 | Phosphorylation | IGKKSGHSSPGAIIV CCCCCCCCCCCEEEE | 41.58 | 28889911 | |
437 | Phosphorylation | GKKSGHSSPGAIIVS CCCCCCCCCCEEEEE | 22.98 | 20377248 | |
444 | Phosphorylation | SPGAIIVSSPNLGTV CCCEEEEECCCCCCC | 29.66 | 28889911 | |
445 | Phosphorylation | PGAIIVSSPNLGTVN CCEEEEECCCCCCCC | 13.60 | 25752575 | |
450 | Phosphorylation | VSSPNLGTVNTSEDS EECCCCCCCCCCHHH | 17.47 | 19779198 | |
453 | Phosphorylation | PNLGTVNTSEDSLDK CCCCCCCCCHHHHHH | 29.20 | 28889911 | |
457 | Phosphorylation | TVNTSEDSLDKSLQS CCCCCHHHHHHHHHH | 34.12 | 28889911 | |
526 | Phosphorylation | SKNIRKLSNYSREIS CHHHHHHHHHHHHCC | 36.44 | 19823750 | |
528 | Phosphorylation | NIRKLSNYSREISSP HHHHHHHHHHHCCCH | 13.01 | 19823750 | |
529 | Phosphorylation | IRKLSNYSREISSPL HHHHHHHHHHCCCHH | 27.90 | 19823750 | |
533 | Phosphorylation | SNYSREISSPLQENC HHHHHHCCCHHHHHC | 22.58 | 20377248 | |
534 | Phosphorylation | NYSREISSPLQENCK HHHHHCCCHHHHHCC | 34.98 | 19823750 | |
542 | Phosphorylation | PLQENCKSPVKELSI HHHHHCCCCCCCCCC | 36.81 | 28152593 | |
553 | Phosphorylation | ELSIKEKSGTPHAFV CCCCCCCCCCCHHHH | 49.33 | 28889911 | |
555 | Phosphorylation | SIKEKSGTPHAFVEA CCCCCCCCCHHHHHH | 20.99 | 28889911 | |
576 | Phosphorylation | REVKRVKSTIVELKD HHHHHHHEEEEECCC | 22.10 | 28889911 | |
587 | Phosphorylation | ELKDEELSEEAINQL ECCCHHHCHHHHHHH | 36.35 | 28889911 | |
610 | Phosphorylation | SNNLLRKSFDSEGNK CCCHHHHHCCCCCCC | 28.05 | 28889911 | |
661 | Phosphorylation | KEEGKNNTQSSDFIR HHCCCCCCCCHHHHH | 38.94 | 22369663 | |
663 | Phosphorylation | EGKNNTQSSDFIRNA CCCCCCCCHHHHHHH | 29.81 | 22369663 | |
664 | Phosphorylation | GKNNTQSSDFIRNAA CCCCCCCHHHHHHHH | 27.07 | 22369663 | |
675 | Phosphorylation | RNAAFLITRNYVPLK HHHHHHHHCCCCCCC | 18.27 | 27017623 | |
712 | Phosphorylation | TEMERFGSNTFMSDN ECHHHHCCCCCCCCC | 29.95 | 23749301 | |
714 | Phosphorylation | MERFGSNTFMSDNIN HHHHCCCCCCCCCCC | 23.55 | 30377154 | |
717 | Phosphorylation | FGSNTFMSDNINSNT HCCCCCCCCCCCCHH | 24.26 | 30377154 | |
722 | Phosphorylation | FMSDNINSNTIQKRS CCCCCCCCHHHHHHH | 31.39 | 30377154 | |
736 | Phosphorylation | SQALNRFTNEDSSNE HHHHHHHCCCCCCCC | 34.17 | 27017623 | |
740 | Phosphorylation | NRFTNEDSSNEGEED HHHCCCCCCCCCCCC | 28.96 | 21440633 | |
741 | Phosphorylation | RFTNEDSSNEGEEDS HHCCCCCCCCCCCCC | 51.74 | 27017623 | |
755 | Phosphorylation | SFSFSRCSGTAASVQ CCEEECCCCCCCCCC | 37.76 | 30377154 | |
818 | Phosphorylation | CSKQSRHSRSATSRS HHHHHHCCCCCCCCC | 27.16 | 21551504 | |
825 | Phosphorylation | SRSATSRSRGSFGAS CCCCCCCCCCCCCCC | 40.54 | 17563356 | |
828 | Phosphorylation | ATSRSRGSFGASNNG CCCCCCCCCCCCCCC | 21.28 | 23749301 | |
832 | Phosphorylation | SRGSFGASNNGDGDD CCCCCCCCCCCCCCC | 31.07 | 21551504 | |
848 | Phosphorylation | DDDGPKFTFKRRKG- CCCCCCCCEEECCC- | 34.08 | 27017623 |
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 XRS2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of XRS2_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 XRS2_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-349; SER-445; SER-533AND SER-534, 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-825, AND MASSSPECTROMETRY. |