| UniProt ID | NSE4_YEAST | |
|---|---|---|
| UniProt AC | P43124 | |
| Protein Name | Non-structural maintenance of chromosome element 4 | |
| Gene Name | NSE4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 402 | |
| Subcellular Localization | Nucleus . | |
| 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 | MSSTVISRKRRNSTVTEPDSSGETRKQKKSRSDEKSSSSKDGDPQLEFKVLQGYRDLESEMHKGRAQVTRTGDIGVAMDNLNAVDSLFNKVIGIKNNGLFAHDARAMVSISELAQISVRNLKFDDSRSMVNLENIVNSLKRYMLKEHFKLNNIAENRNDLTLAADEQSAADQQEESDGDIDRTPDDNHTDKATSSFKATSMRHSYLQQFSHYNEFSQFNWFRIGALYNTISKNAPITDHLMGPLSIEKKPRVLTQRRRNNDQVGEKITAEKITQHSLNSTQQETTPEQVKKCFKKLSKKLGPEGSINLFKFIIDPNSFSRSIENLFYTSFLIKEGKLLMEHDEEGLPTIKIKQSISHTDSRSKEIERQRRRAAHQNHIIFQMDMPTWRKLIKKYNITSPFLD | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | ISRKRRNSTVTEPDS CCCCCCCCCCCCCCC | 23.57 | 22369663 | |
| 14 | Phosphorylation | SRKRRNSTVTEPDSS CCCCCCCCCCCCCCC | 34.69 | 22369663 | |
| 16 | Phosphorylation | KRRNSTVTEPDSSGE CCCCCCCCCCCCCCC | 41.72 | 22369663 | |
| 20 | Phosphorylation | STVTEPDSSGETRKQ CCCCCCCCCCCHHHH | 51.46 | 22369663 | |
| 21 | Phosphorylation | TVTEPDSSGETRKQK CCCCCCCCCCHHHHH | 48.29 | 22369663 | |
| 24 | Phosphorylation | EPDSSGETRKQKKSR CCCCCCCHHHHHCCC | 46.85 | 22369663 | |
| 109 | Phosphorylation | HDARAMVSISELAQI HHHHHHHCHHHHHHH | 13.81 | 30377154 | |
| 117 | Phosphorylation | ISELAQISVRNLKFD HHHHHHHHHCCCCCC | 11.71 | 30377154 | |
| 176 | Phosphorylation | AADQQEESDGDIDRT HHHHHHHCCCCCCCC | 46.25 | 28152593 | |
| 183 | Phosphorylation | SDGDIDRTPDDNHTD CCCCCCCCCCCCCCC | 27.59 | 21440633 | |
| 189 | Phosphorylation | RTPDDNHTDKATSSF CCCCCCCCCHHHHCC | 45.51 | 19779198 | |
| 279 | Phosphorylation | ITQHSLNSTQQETTP HHHHHCCCCCCCCCH | 32.65 | 28889911 | |
| 280 | Phosphorylation | TQHSLNSTQQETTPE HHHHCCCCCCCCCHH | 32.95 | 28889911 | |
| 284 | Phosphorylation | LNSTQQETTPEQVKK CCCCCCCCCHHHHHH | 43.23 | 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 NSE4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NSE4_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 NSE4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-13 AND THR-14, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY. | |
| "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-14, AND MASSSPECTROMETRY. | |
