| UniProt ID | RAD18_YEAST | |
|---|---|---|
| UniProt AC | P10862 | |
| Protein Name | Postreplication repair E3 ubiquitin-protein ligase RAD18 | |
| Gene Name | RAD18 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 487 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. The UBC2-RAD18 complex cooperates with RAD5 and the UBC13-MMS2 dimer to attach mono-ubiquitin chains on 'Lys-164' of POL30, which is necessary for PRR. The UBC2-RAD18 complex is also involved in prevention of spontaneous mutations caused by 7,8-dihydro-8-oxoguanine.. | |
| Protein Sequence | MDHQITTASDFTTTSIPSLYQLDTLLRCHICKDFLKVPVLTPCGHTFCSLCIRTHLNNQPNCPLCLFEFRESLLRSEFLVSEIIQSYTSLRSSLLDALRIPKPTPVPENEEVPGPENSSWIELISESESDSVNAADDDLQIVATSERKLAKRSMTDILPLSSKPSKRNFAMFRSERIKKKSKPNEQMAQCPICQQFYPLKALEKTHLDECLTLQSLGKKPKISTTFPTESNPHNKSSSRFKVRTPEVDKSSCGETSHVDKYLNSMMSAEHQRLPKINFTSMTQSQIKQKLSSLGLSTNGTRQNMIKRYNHYEMLWNSNFCDSLEPVDEAELKRQLLSWDVSHNKTPQNSSNKGGISKLMIMKSNGKSSSYRKLLENFKNDKFNRKGWMVMFRKDFARLIREAKMKIKTGSSDSSGSVGHSNDGDGVEKVQSDQGTEDQQMEKDQDTVINEDRVAGERNLPNEDSTDADLSRELMDLNEYSKDPPGNN | |
| 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 |
|---|---|---|---|---|---|
| 153 | Phosphorylation | ERKLAKRSMTDILPL HHHHHHCCCCCCCCC | 25.90 | 22369663 | |
| 155 | Phosphorylation | KLAKRSMTDILPLSS HHHHCCCCCCCCCCC | 22.57 | 22369663 | |
| 161 | Phosphorylation | MTDILPLSSKPSKRN CCCCCCCCCCCCCCC | 34.08 | 28889911 | |
| 162 | Phosphorylation | TDILPLSSKPSKRNF CCCCCCCCCCCCCCC | 57.16 | 27017623 | |
| 165 | Phosphorylation | LPLSSKPSKRNFAMF CCCCCCCCCCCCHHH | 48.24 | 28889911 | |
| 174 | Phosphorylation | RNFAMFRSERIKKKS CCCHHHHHHHHHHCC | 21.69 | 17287358 | |
| 181 | Phosphorylation | SERIKKKSKPNEQMA HHHHHHCCCCCHHHH | 63.32 | 17287358 | |
| 200 | Ubiquitination | CQQFYPLKALEKTHL HHHHCCHHHHHHCCH | 46.55 | 23749301 | |
| 204 | Ubiquitination | YPLKALEKTHLDECL CCHHHHHHCCHHHHH | 41.94 | 23749301 | |
| 223 | Phosphorylation | LGKKPKISTTFPTES CCCCCCCCCCCCCCC | 27.76 | 29734811 | |
| 224 | Phosphorylation | GKKPKISTTFPTESN CCCCCCCCCCCCCCC | 35.61 | 29734811 | |
| 244 | Phosphorylation | SSRFKVRTPEVDKSS CCCCEECCCCCCHHH | 27.13 | 29136822 | |
| 249 | Acetylation | VRTPEVDKSSCGETS ECCCCCCHHHCCCHH | 49.82 | 25381059 | |
| 282 | Phosphorylation | KINFTSMTQSQIKQK CCCCCCCCHHHHHHH | 25.49 | 30377154 | |
| 284 | Phosphorylation | NFTSMTQSQIKQKLS CCCCCCHHHHHHHHH | 25.38 | 25752575 | |
| 356 | Phosphorylation | SSNKGGISKLMIMKS CCCCCCCCEEEEECC | 24.02 | 21440633 | |
| 414 | Phosphorylation | KTGSSDSSGSVGHSN CCCCCCCCCCCCCCC | 39.83 | 30377154 | |
| 416 | Phosphorylation | GSSDSSGSVGHSNDG CCCCCCCCCCCCCCC | 27.20 | 21440633 | |
| 420 | Phosphorylation | SSGSVGHSNDGDGVE CCCCCCCCCCCCCCE | 30.59 | 28889911 | |
| 431 | Phosphorylation | DGVEKVQSDQGTEDQ CCCEEECCCCCCCHH | 34.58 | 22369663 | |
| 435 | Phosphorylation | KVQSDQGTEDQQMEK EECCCCCCCHHHHHH | 30.65 | 25521595 | |
| 446 | Phosphorylation | QMEKDQDTVINEDRV HHHHHHCCCCCCHHH | 20.04 | 23749301 | |
| 464 | Phosphorylation | RNLPNEDSTDADLSR CCCCCCCCCCHHHHH | 23.23 | 23749301 | |
| 465 | Phosphorylation | NLPNEDSTDADLSRE CCCCCCCCCHHHHHH | 47.75 | 25752575 | |
| 470 | Phosphorylation | DSTDADLSRELMDLN CCCCHHHHHHHHCHH | 25.02 | 23749301 |
| 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 RAD18_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAD18_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 RAD18_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-153; THR-155; THR-244;SER-284 AND SER-464, AND MASS 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 THR-155; SER-174 ANDSER-181, AND MASS SPECTROMETRY. | |
