| UniProt ID | SRS2_YEAST | |
|---|---|---|
| UniProt AC | P12954 | |
| Protein Name | ATP-dependent DNA helicase SRS2 | |
| Gene Name | SRS2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1174 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | ATP-dependent DNA helicase involved in DNA repair at least for UV-induced lesions. The polarity of the helicase activity was determined to be 3' to 5'.. | |
| Protein Sequence | MSSNNDLWLHLVSQLNTQQRAAALFDYTRGLQVIAGPGTGKTKVLTSRVAYLILHHHIHPRDIIVTTFTNKAANEMKERLQEMLRGAGVNISELLIGTFHSICLKILYRFGHLVDLQKDWRIIDEKEIDVILDDMIEKVPDQIRDYASSITRKVNLCMPSKNGDEWTIHPKLIKKQISKLKSNAILPEEYILDSNHDAALGYFYQIYQSELSKKNTLDFDDLLMYTFRLLTRVRVLSNIKHVLVDEFQDTNGIQLDLMFLFAKGNHHLSRGMTIVGDPDQSIYAFRNALAHNFLEMGRKCPIEYSTIILVENYRSSQKILNTSEILITQQNKGRQNRAPLRAQFDLDFPPVYMNFPAYFLEAPSLVRELLYLKALPNLFTFNDFAILVRQRRQIKRIESALIEHRIPYKIIRGHSFWDSKETRAMLNLLKLIFSPNDKHAILASLLYPARGLGPATGEKIKNALDTLATDVSCFQILKDISSKKIMLDIPTKGRSVIADFISMIENCQLLLQSTLLGGLSDLFDKLYELSGLKYEYLYKDGKKKNDQLEKSEPNLLNARHKNIELLKNYFLALLSKSESSDKEKNEAIKAATDEAEPIENKVITPKEYLRNFFNSLSLHSDAAEEEESESNKDAKIKREKNGFVTISTIHGAKGLEWPVVFIPGCEEGIIPCVFNDDKKDESEEDEEEDQENSKKDASPKKTRVLSVEDSIDEERRMFFVAQTRAKYLLYLSNTVTVEDVDRPRIASRFLTTDLIKAMSDSQKLFESTNSIKKLYRILNKKPPAEDDKLFSLDQLRKDYNQFIENRRERMIWQGIQMNDVYGIQLSRNKLLGSVSDFTSAADQLRLETQNSIFPQKKLIEKSRPSKINGNYAPKSRVKSPEKRYAPETTSFHSPTKKKVYAPQYVSTTNVPSRQEFHSSTGKNIPFLRREDRSITDISPRSSTRSLKGASPNKTSHMSDDLMRPSPTRKDKVTRNIHFATAGTFRIETQSNVDELHPPEYSNKSGQSLTSSEFSGFSSACSNSDQPTNLIEDINNELDLSDEELLNDISIERRRELLGSKKTKKIKPKTRNRKSKRGDKVKVEEVIDLKSEFEEDDSRNTTAAELLHNPDDTTVDNRPIISNAKFLADAAMKKTQKFSKKVKNEPASSQMDIFSQLSRAKKKSKLNNGEIIVID | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSSNNDLWL ------CCCCHHHHH | 53.75 | 30377154 | |
| 481 | Phosphorylation | FQILKDISSKKIMLD HHHHHHHCCCCEEEE | 46.36 | 28889911 | |
| 604 | Phosphorylation | PIENKVITPKEYLRN CCCCCCCCHHHHHHH | 31.15 | 15964827 | |
| 617 | Phosphorylation | RNFFNSLSLHSDAAE HHHHHHHCCCCHHHH | 24.69 | 27017623 | |
| 628 | Phosphorylation | DAAEEEESESNKDAK HHHHHHHHHCCCCCH | 49.99 | 27017623 | |
| 682 | Phosphorylation | NDDKKDESEEDEEED CCCCCCCCHHHHHHH | 57.32 | 28889911 | |
| 698 | Phosphorylation | ENSKKDASPKKTRVL HHHCCCCCCCCCEEE | 47.59 | 15964827 | |
| 833 | Phosphorylation | SRNKLLGSVSDFTSA CCCCCCCCHHHHCCH | 20.58 | 27214570 | |
| 835 | Phosphorylation | NKLLGSVSDFTSAAD CCCCCCHHHHCCHHH | 28.80 | 27214570 | |
| 839 | Phosphorylation | GSVSDFTSAADQLRL CCHHHHCCHHHHHHH | 22.81 | 27214570 | |
| 874 | Acetylation | INGNYAPKSRVKSPE CCCCCCCHHHCCCCC | 42.60 | 25381059 | |
| 879 | Phosphorylation | APKSRVKSPEKRYAP CCHHHCCCCCCCCCC | 35.12 | 15964827 | |
| 888 | Phosphorylation | EKRYAPETTSFHSPT CCCCCCCCCCCCCCC | 27.04 | 30377154 | |
| 889 | Phosphorylation | KRYAPETTSFHSPTK CCCCCCCCCCCCCCC | 27.94 | 30377154 | |
| 890 | Phosphorylation | RYAPETTSFHSPTKK CCCCCCCCCCCCCCC | 28.51 | 21440633 | |
| 893 | Phosphorylation | PETTSFHSPTKKKVY CCCCCCCCCCCCCEE | 32.05 | 15964827 | |
| 895 | Phosphorylation | TTSFHSPTKKKVYAP CCCCCCCCCCCEECC | 59.52 | 21440633 | |
| 904 | Phosphorylation | KKVYAPQYVSTTNVP CCEECCCEEECCCCC | 8.70 | 28889911 | |
| 906 | Phosphorylation | VYAPQYVSTTNVPSR EECCCEEECCCCCCH | 25.28 | 28889911 | |
| 907 | Phosphorylation | YAPQYVSTTNVPSRQ ECCCEEECCCCCCHH | 16.61 | 28889911 | |
| 933 | Phosphorylation | FLRREDRSITDISPR CCCCCCCCCCCCCCC | 42.01 | 22369663 | |
| 935 | Phosphorylation | RREDRSITDISPRSS CCCCCCCCCCCCCCC | 28.64 | 22369663 | |
| 938 | Phosphorylation | DRSITDISPRSSTRS CCCCCCCCCCCCCCC | 19.64 | 22369663 | |
| 950 | Phosphorylation | TRSLKGASPNKTSHM CCCCCCCCCCCCCCC | 37.36 | 15964827 | |
| 958 | Phosphorylation | PNKTSHMSDDLMRPS CCCCCCCCCCCCCCC | 23.66 | 21440633 | |
| 965 | Phosphorylation | SDDLMRPSPTRKDKV CCCCCCCCCCCCCCC | 28.65 | 21440633 | |
| 967 | Phosphorylation | DLMRPSPTRKDKVTR CCCCCCCCCCCCCCC | 55.47 | 24961812 | |
| 1090 | Phosphorylation | EEVIDLKSEFEEDDS EEEEEHHHHCCCCCC | 55.61 | 21551504 | |
| 1097 | Phosphorylation | SEFEEDDSRNTTAAE HHCCCCCCCCCCHHH | 39.49 | 21551504 | |
| 1163 | Phosphorylation | LSRAKKKSKLNNGEI HHHHHHHHCCCCCCE | 51.78 | 27017623 |
| 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 SRS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SRS2_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 SRS2_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-833 AND SER-933, ANDMASS SPECTROMETRY. | |
| "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-893, AND MASSSPECTROMETRY. | |
