| UniProt ID | RAD50_YEAST | |
|---|---|---|
| UniProt AC | P12753 | |
| Protein Name | DNA repair protein RAD50 | |
| Gene Name | RAD50 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1312 | |
| Subcellular Localization | ||
| Protein Description | Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site.. | |
| Protein Sequence | MSAIYKLSIQGIRSFDSNDRETIEFGKPLTLIVGMNGSGKTTIIECLKYATTGDLPPNSKGGVFIHDPKITGEKDIRAQVKLAFTSANGLNMIVTRNIQLLMKKTTTTFKTLEGQLVAINNSGDRSTLSTRSLELDAQVPLYLGVPKAILEYVIFCHQEDSLWPLSEPSNLKKKFDEIFQAMKFTKALDNLKSIKKDMSVDIKLLKQSVEHLKLDKDRSKAMKLNIHQLQTKIDQYNEEVSEIESQLNEITEKSDKLFKSNQDFQKILSKVENLKNTKLSISDQVKRLSNSIDILDLSKPDLQNLLANFSKVLMDKNNQLRDLETDISSLKDRQSSLQSLSNSLIRRQGELEAGKETYEKNRNHLSSLKEAFQHKFQGLSNIENSDMAQVNHEMSQFKAFISQDLTDTIDQFAKDIQLKETNLSDLIKSITVDSQNLEYNKKDRSKLIHDSEELAEKLKSFKSLSTQDSLNHELENLKTYKEKLQSWESENIIPKLNQKIEEKNNEMIILENQIEKFQDRIMKTNQQADLYAKLGLIKKSINTKLDELQKITEKLQNDSRIRQVFPLTQEFQRADLEMDFQKLFINMQKNIAINNKKMHELDRRYTNALYNLNTIEKDLQDNQKSKEKVIQLLSENLPEDCTIDEYNDVLEETELSYKTALENLKMHQTTLEFNRKALEIAERDSCCYLCSRKFENESFKSKLLQELKTKTDANFEKTLKDTVQNEKEYLHSLRLLEKHIITLNSINEKIDNSQKCLEKAKEETKTSKSKLDELEVDSTKLKDEKELAESEIRPLIEKFTYLEKELKDLENSSKTISEELSIYNTSEDGIQTVDELRDQQRKMNDSLRELRKTISDLQMEKDEKVRENSRMINLIKEKELTVSEIESSLTQKQNIDDSIRSKRENINDIDSRVKELEARIISLKNKKDEAQSVLDKVKNERDIQVRNKQKTVADINRLIDRFQTIYNEVVDFEAKGFDELQTTIKELELNKAQMLELKEQLDLKSNEVNEEKRKLADSNNEEKNLKQNLELIELKSQLQHIESEISRLDVQNAEAERDKYQEESLRLRTRFEKLSSENAGKLGEMKQLQNQIDSLTHQLRTDYKDIEKNYHKEWVELQTRSFVTDDIDVYSKALDSAIMKYHGLKMQDINRIIDELWKRTYSGTDIDTIKIRSDEVSSTVKGKSYNYRVVMYKQDVELDMRGRCSAGQKVLASIIIRLALSETFGANCGVIALDEPTTNLDEENIESLAKSLHNIINMRRHQKNFQLIVITHDEKFLGHMNAAAFTDHFFKVKRDDRQKSQIEWVDINRVTY | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MSAIYKLSIQGI ---CCCEEEEEECCC | 12.95 | 28132839 | |
| 105 | Phosphorylation | IQLLMKKTTTTFKTL HHHHHHCCCCEEEEE | 24.69 | 27017623 | |
| 106 | Phosphorylation | QLLMKKTTTTFKTLE HHHHHCCCCEEEEEC | 32.49 | 27017623 | |
| 107 | Phosphorylation | LLMKKTTTTFKTLEG HHHHCCCCEEEEECC | 35.15 | 27017623 | |
| 126 | Phosphorylation | INNSGDRSTLSTRSL ECCCCCCCEEECCCC | 38.14 | 27017623 | |
| 231 | Phosphorylation | LNIHQLQTKIDQYNE CCHHHHHHHHHHHHH | 38.26 | 28889911 | |
| 465 | Phosphorylation | LKSFKSLSTQDSLNH HHHHHCCCCHHHHHH | 30.98 | 30377154 | |
| 466 | Phosphorylation | KSFKSLSTQDSLNHE HHHHCCCCHHHHHHH | 41.51 | 28889911 | |
| 469 | Phosphorylation | KSLSTQDSLNHELEN HCCCCHHHHHHHHHH | 22.66 | 25752575 | |
| 524 | Phosphorylation | FQDRIMKTNQQADLY HHHHHHHHHHHHHHH | 22.37 | 23607784 | |
| 531 | Phosphorylation | TNQQADLYAKLGLIK HHHHHHHHHHHCHHH | 11.39 | 23607784 | |
| 568 | Phosphorylation | IRQVFPLTQEFQRAD HHHHCHHCHHHHHHC | 26.70 | 25752575 | |
| 869 | Phosphorylation | DEKVRENSRMINLIK HHHHHHHHHHHHHHH | 20.62 | 27017623 | |
| 1018 | Phosphorylation | EKRKLADSNNEEKNL HHHHHHCCCCHHHHH | 35.63 | 24961812 | |
| 1059 | Acetylation | NAEAERDKYQEESLR CHHHHHHHHHHHHHH | 55.87 | 24489116 | |
| 1121 | Phosphorylation | WVELQTRSFVTDDID HHHHHHCCCCCCCHH | 27.70 | 30377154 | |
| 1131 | Phosphorylation | TDDIDVYSKALDSAI CCCHHHHHHHHHHHH | 15.99 | 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 RAD50_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD50_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 RAD50_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-466; SER-469 ANDTHR-568, AND MASS SPECTROMETRY. | |
