| UniProt ID | KRE29_YEAST | |
|---|---|---|
| UniProt AC | P40026 | |
| Protein Name | DNA repair protein KRE29 | |
| Gene Name | KRE29 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 464 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.. | |
| Protein Sequence | MGSVNSSPNEEFETVPDSQISGFDSPLIPTSVGSYFRDDDDDEKVHPNFISDPENDSLNSDEEFSSLENSDLNLSGAKAESGDDFDPILKRTIISKRKAPSNNEDEEIVKTPRKLVNYVPLKIFNLGDSFDDTITTTVAKLQDLKKEILDSPRSNKSIVITSNTVAKSELQKSIKFSGSIPEIYLDVVTKETISDKYKDWHFISKNCHYEQLMDLEMKDTAYSFLFGSSRSQGKVPEFVHLKCPSITNLLVLFGVNQEKCNSLKINYEKKENSRYDNLCTIFPVNKMLKFLMYFYSDDDNDDVREFFLKAFICLILDRKVFNAMESDHRLCFKVLELFNEAHFINSYFEIVDKNDFFLHYRLLQIFPHLQSALLRRRFSEKQGRTETIQQNIIKEFNEFFDCKNYKNLLYFILTMYGSKFIPFGPKCQVTEYFKDCILDISNETTNDVEISILKGILNLFSKIR | |
| 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 |
|---|---|---|---|---|---|
| 81 | Phosphorylation | LSGAKAESGDDFDPI CCCCCCCCCCCCHHH | 53.00 | 25521595 | |
| 101 | Phosphorylation | ISKRKAPSNNEDEEI HHCCCCCCCCCCHHH | 58.09 | 19795423 | |
| 111 | Phosphorylation | EDEEIVKTPRKLVNY CCHHHHCCHHHHHHC | 19.89 | 23749301 | |
| 129 | Phosphorylation | KIFNLGDSFDDTITT EEEECCCCCCHHHHH | 28.86 | 27017623 | |
| 151 | Phosphorylation | LKKEILDSPRSNKSI HHHHHHCCCCCCCCE | 20.83 | 28889911 | |
| 154 | Phosphorylation | EILDSPRSNKSIVIT HHHCCCCCCCCEEEE | 52.58 | 21551504 | |
| 175 | Ubiquitination | SELQKSIKFSGSIPE HHHHHHCCCCCCCCE | 40.34 | 23749301 | |
| 184 | Phosphorylation | SGSIPEIYLDVVTKE CCCCCEEEEEEECCH | 8.66 | 23749301 | |
| 220 | Phosphorylation | MDLEMKDTAYSFLFG CCHHCHHHHHHHHHC | 23.21 | 28889911 | |
| 222 | Phosphorylation | LEMKDTAYSFLFGSS HHCHHHHHHHHHCCC | 11.31 | 28889911 | |
| 229 | Phosphorylation | YSFLFGSSRSQGKVP HHHHHCCCCCCCCCC | 36.01 | 28889911 |
| 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 KRE29_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KRE29_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 KRE29_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-81 AND SER-101, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASSSPECTROMETRY. | |
