| UniProt ID | RFA1_YEAST | |
|---|---|---|
| UniProt AC | P22336 | |
| Protein Name | Replication factor A protein 1 | |
| Gene Name | RFA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 621 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism. Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.. | |
| Protein Sequence | MSSVQLSRGDFHSIFTNKQRYDNPTGGVYQVYNTRKSDGANSNRKNLIMISDGIYHMKALLRNQAASKFQSMELQRGDIIRVIIAEPAIVRERKKYVLLVDDFELVQSRADMVNQTSTFLDNYFSEHPNETLKDEDITDSGNVANQTNASNAGVPDMLHSNSNLNANERKFANENPNSQKTRPIFAIEQLSPYQNVWTIKARVSYKGEIKTWHNQRGDGKLFNVNFLDTSGEIRATAFNDFATKFNEILQEGKVYYVSKAKLQPAKPQFTNLTHPYELNLDRDTVIEECFDESNVPKTHFNFIKLDAIQNQEVNSNVDVLGIIQTINPHFELTSRAGKKFDRRDITIVDDSGFSISVGLWNQQALDFNLPEGSVAAIKGVRVTDFGGKSLSMGFSSTLIPNPEIPEAYALKGWYDSKGRNANFITLKQEPGMGGQSAASLTKFIAQRITIARAQAENLGRSEKGDFFSVKAAISFLKVDNFAYPACSNENCNKKVLEQPDGTWRCEKCDTNNARPNWRYILTISIIDETNQLWLTLFDDQAKQLLGVDANTLMSLKEEDPNEFTKITQSIQMNEYDFRIRAREDTYNDQSRIRYTVANLHSLNYRAEADYLADELSKALLA | |
| 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 | Acetylation | ------MSSVQLSRG ------CCCEECCCC | 38.94 | 22814378 | |
| 2 | Phosphorylation | ------MSSVQLSRG ------CCCEECCCC | 38.94 | 24961812 | |
| 3 | Phosphorylation | -----MSSVQLSRGD -----CCCEECCCCC | 16.75 | 24961812 | |
| 21 | Phosphorylation | IFTNKQRYDNPTGGV CCCCCCCCCCCCCCE | 19.99 | 28132839 | |
| 160 | Phosphorylation | GVPDMLHSNSNLNAN CCCCCCCCCCCCCHH | 37.68 | 27214570 | |
| 162 | Phosphorylation | PDMLHSNSNLNANER CCCCCCCCCCCHHHH | 45.79 | 27214570 | |
| 170 | Acetylation | NLNANERKFANENPN CCCHHHHHHCCCCCC | 42.52 | 25381059 | |
| 178 | Phosphorylation | FANENPNSQKTRPIF HCCCCCCCCCCCCEE | 34.02 | 22369663 | |
| 191 | Phosphorylation | IFAIEQLSPYQNVWT EEEEEECCCCCCEEE | 22.66 | 21440633 | |
| 220 | Acetylation | HNQRGDGKLFNVNFL EECCCCCCEEEEEEE | 55.43 | 24489116 | |
| 427 | Acetylation | NANFITLKQEPGMGG CCEEEEEECCCCCCC | 43.92 | 22865919 | |
| 442 | Acetylation | QSAASLTKFIAQRIT CCHHHHHHHHHHHHH | 39.81 | 24489116 | |
| 463 | Acetylation | ENLGRSEKGDFFSVK HHCCCCCCCCCCCHH | 66.09 | 22865919 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 178 | S | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 178 | S | Phosphorylation | Kinase | MEC1 | P38111 | GPS |
| 178 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | RSP5 | P39940 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RFA1_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 RFA1_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-160 AND SER-178, ANDMASS SPECTROMETRY. | |
| "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-178, AND MASSSPECTROMETRY. | |
