| UniProt ID | RAD52_YEAST | |
|---|---|---|
| UniProt AC | P06778 | |
| Protein Name | DNA repair and recombination protein RAD52 | |
| Gene Name | RAD52 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 471 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.. | |
| Protein Sequence | MNEIMDMDEKKPVFGNHSEDIQTKLDKKLGPEYISKRVGFGTSRIAYIEGWRVINLANQIFGYNGWSTEVKSVVIDFLDERQGKFSIGCTAIVRVTLTSGTYREDIGYGTVENERRKPAAFERAKKSAVTDALKRSLRGFGNALGNCLYDKDFLAKIDKVKFDPPDFDENNLFRPTDEISESSRTNTLHENQEQQQYPNKRRQLTKVTNTNPDSTKNLVKIENTVSRGTPMMAAPAEANSKNSSNKDTDLKSLDASKQDQDDLLDDSLMFSDDFQDDDLINMGNTNSNVLTTEKDPVVAKQSPTASSNPEAEQITFVTAKAATSVQNERYIGEESIFDPKYQAQSIRHTVDQTTSKHIPASVLKDKTMTTARDSVYEKFAPKGKQLSMKNNDKELGPHMLEGAGNQVPRETTPIKTNATAFPPAAAPRFAPPSKVVHPNGNGAVPAVPQQRSTRREVGRPKINPLHARKPT | |
| 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 |
|---|---|---|---|---|---|
| 10 | Sumoylation | EIMDMDEKKPVFGNH CCCCCCCCCCCCCCC | 59.10 | - | |
| 11 | Sumoylation | IMDMDEKKPVFGNHS CCCCCCCCCCCCCCC | 44.35 | - | |
| 126 | Sumoylation | AAFERAKKSAVTDAL HHHHHHHHHHHHHHH | 42.54 | - | |
| 180 | Phosphorylation | FRPTDEISESSRTNT CCCCHHHCCCHHCCC | 29.40 | 27214570 | |
| 182 | Phosphorylation | PTDEISESSRTNTLH CCHHHCCCHHCCCCC | 20.52 | 27214570 | |
| 200 | Sumoylation | EQQQYPNKRRQLTKV HHHHCCCHHHHCEEC | 44.44 | - | |
| 214 | Phosphorylation | VTNTNPDSTKNLVKI CCCCCCHHHCCEEEE | 42.40 | 27214570 | |
| 216 | Acetylation | NTNPDSTKNLVKIEN CCCCHHHCCEEEEEC | 52.84 | 25381059 | |
| 220 | Acetylation | DSTKNLVKIENTVSR HHHCCEEEEECCCCC | 47.68 | 25381059 | |
| 220 | Sumoylation | DSTKNLVKIENTVSR HHHCCEEEEECCCCC | 47.68 | - | |
| 226 | Phosphorylation | VKIENTVSRGTPMMA EEEECCCCCCCCCEE | 23.97 | 23749301 | |
| 229 | Phosphorylation | ENTVSRGTPMMAAPA ECCCCCCCCCEECCH | 13.60 | 28889911 | |
| 252 | Phosphorylation | NKDTDLKSLDASKQD CCCCCHHHCCCHHCC | 38.49 | 27017623 | |
| 302 | Phosphorylation | DPVVAKQSPTASSNP CCEECCCCCCCCCCC | 24.42 | 22369663 | |
| 304 | Phosphorylation | VVAKQSPTASSNPEA EECCCCCCCCCCCCH | 44.40 | 25521595 | |
| 306 | Phosphorylation | AKQSPTASSNPEAEQ CCCCCCCCCCCCHHH | 32.88 | 22369663 | |
| 307 | Phosphorylation | KQSPTASSNPEAEQI CCCCCCCCCCCHHHE | 54.67 | 22369663 | |
| 324 | Phosphorylation | VTAKAATSVQNERYI EEECCCCCCCCCCCC | 19.58 | 30377154 | |
| 335 | Phosphorylation | ERYIGEESIFDPKYQ CCCCCCCCCCCHHHH | 25.01 | 27017623 | |
| 340 | Acetylation | EESIFDPKYQAQSIR CCCCCCHHHHHHHHH | 52.41 | 24489116 | |
| 349 | Phosphorylation | QAQSIRHTVDQTTSK HHHHHHHCCCCCCCC | 18.87 | 19779198 | |
| 354 | Phosphorylation | RHTVDQTTSKHIPAS HHCCCCCCCCCCCHH | 30.09 | 19779198 | |
| 356 | Acetylation | TVDQTTSKHIPASVL CCCCCCCCCCCHHHH | 43.38 | 25381059 | |
| 361 | Phosphorylation | TSKHIPASVLKDKTM CCCCCCHHHHCCCCC | 23.72 | 19779198 | |
| 374 | Phosphorylation | TMTTARDSVYEKFAP CCCCHHHHHHHHHCC | 22.50 | 30377154 | |
| 378 | Acetylation | ARDSVYEKFAPKGKQ HHHHHHHHHCCCCCC | 29.19 | 24489116 | |
| 393 | Acetylation | LSMKNNDKELGPHML CCCCCCCCCCCHHHH | 57.89 | 24489116 | |
| 411 | Phosphorylation | GNQVPRETTPIKTNA CCCCCCCCCCCCCCC | 38.87 | 20377248 | |
| 412 | Phosphorylation | NQVPRETTPIKTNAT CCCCCCCCCCCCCCC | 20.47 | 20377248 | |
| 416 | Phosphorylation | RETTPIKTNATAFPP CCCCCCCCCCCCCCC | 30.70 | 29136822 | |
| 419 | Phosphorylation | TPIKTNATAFPPAAA CCCCCCCCCCCCCCC | 30.79 | 29136822 |
| 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 RAD52_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD52_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 RAD52_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-302; THR-304; SER-306AND SER-307, AND MASS SPECTROMETRY. | |
