UniProt ID | MRE11_YEAST | |
---|---|---|
UniProt AC | P32829 | |
Protein Name | Double-strand break repair protein MRE11 | |
Gene Name | MRE11 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 692 | |
Subcellular Localization | Nucleus. | |
Protein Description | Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing.. | |
Protein Sequence | MDYPDPDTIRILITTDNHVGYNENDPITGDDSWKTFHEVMMLAKNNNVDMVVQSGDLFHVNKPSKKSLYQVLKTLRLCCMGDKPCELELLSDPSQVFHYDEFTNVNYEDPNFNISIPVFGISGNHDDASGDSLLCPMDILHATGLINHFGKVIESDKIKVVPLLFQKGSTKLALYGLAAVRDERLFRTFKDGGVTFEVPTMREGEWFNLMCVHQNHTGHTNTAFLPEQFLPDFLDMVIWGHEHECIPNLVHNPIKNFDVLQPGSSVATSLCEAEAQPKYVFILDIKYGEAPKMTPIPLETIRTFKMKSISLQDVPHLRPHDKDATSKYLIEQVEEMIRDANEETKQKLADDGEGDMVAELPKPLIRLRVDYSAPSNTQSPIDYQVENPRRFSNRFVGRVANGNNVVQFYKKRSPVTRSKKSGINGTSISDRDVEKLFSESGGELEVQTLVNDLLNKMQLSLLPEVGLNEAVKKFVDKDEKTALKEFISHEISNEVGILSTNEEFLRTDDAEEMKALIKQVKRANSVRPTPPKENDETNFAFNGNGLDSFRSSNREVRTGSPDITQSHVDNESRITHISQAESSKPTSKPKRVRTATKKKIPAFSDSTVISDAENELGDNNDAQDDVDIDENDIIMVSTDEEDASYGLLNGRKTKTKTRPAASTKTASRRGKGRASRTPKTDILGSLLAKKRK | |
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 |
---|---|---|---|---|---|
294 | Phosphorylation | YGEAPKMTPIPLETI CCCCCCCCCCCHHHH | 24.96 | 28889911 | |
426 | Phosphorylation | KKSGINGTSISDRDV CCCCCCCCCCCHHHH | 20.56 | 30377154 | |
548 | Phosphorylation | FNGNGLDSFRSSNRE CCCCCHHHHHCCCCC | 27.83 | 30377154 | |
558 | Phosphorylation | SSNREVRTGSPDITQ CCCCCEECCCCCCCH | 47.38 | 22369663 | |
560 | Phosphorylation | NREVRTGSPDITQSH CCCEECCCCCCCHHH | 20.84 | 22369663 | |
564 | Phosphorylation | RTGSPDITQSHVDNE ECCCCCCCHHHCCCC | 31.25 | 29136822 | |
578 | Phosphorylation | ESRITHISQAESSKP CHHEEEHHHHHHCCC | 18.74 | 30377154 | |
637 | Phosphorylation | ENDIIMVSTDEEDAS CCCEEEEECCHHHHH | 16.86 | 27214570 | |
638 | Phosphorylation | NDIIMVSTDEEDASY CCEEEEECCHHHHHH | 35.70 | 27214570 | |
685 | Phosphorylation | PKTDILGSLLAKKRK CCHHHHHHHHHHHCC | 19.43 | 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 MRE11_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MRE11_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 MRE11_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-560, AND MASSSPECTROMETRY. | |
"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 THR-558 AND SER-560, ANDMASS SPECTROMETRY. |