| UniProt ID | RFA2_YEAST | |
|---|---|---|
| UniProt AC | P26754 | |
| Protein Name | Replication factor A protein 2 | |
| Gene Name | RFA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 273 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | 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 | MATYQPYNEYSSVTGGGFENSESRPGSGESETNTRVNTLTPVTIKQILESKQDIQDGPFVSHNQELHHVCFVGVVRNITDHTANIFLTIEDGTGQIEVRKWSEDANDLAAGNDDSSGKGYGSQVAQQFEIGGYVKVFGALKEFGGKKNIQYAVIKPIDSFNEVLTHHLEVIKCHSIASGMMKQPLESASNNNGQSLFVKDDNDTSSGSSPLQRILEFCKKQCEGKDANSFAVPIPLISQSLNLDETTVRNCCTTLTDQGFIYPTFDDNNFFAL | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MATYQPYNEY -----CCCCCCCCCC | 22.76 | 27017623 | |
| 4 | Phosphorylation | ----MATYQPYNEYS ----CCCCCCCCCCC | 9.65 | 30377154 | |
| 7 | Phosphorylation | -MATYQPYNEYSSVT -CCCCCCCCCCCCCC | 12.71 | 27017623 | |
| 10 | Phosphorylation | TYQPYNEYSSVTGGG CCCCCCCCCCCCCCC | 11.56 | 27017623 | |
| 11 | Phosphorylation | YQPYNEYSSVTGGGF CCCCCCCCCCCCCCC | 16.50 | 30377154 | |
| 21 | Phosphorylation | TGGGFENSESRPGSG CCCCCCCCCCCCCCC | 29.74 | 27017623 | |
| 23 | Phosphorylation | GGFENSESRPGSGES CCCCCCCCCCCCCCC | 43.53 | 27017623 | |
| 27 | Phosphorylation | NSESRPGSGESETNT CCCCCCCCCCCCCCC | 41.91 | 17137646 | |
| 30 | Phosphorylation | SRPGSGESETNTRVN CCCCCCCCCCCCCCC | 53.93 | 27214570 | |
| 32 | Phosphorylation | PGSGESETNTRVNTL CCCCCCCCCCCCCCC | 51.69 | 30377154 | |
| 38 | Phosphorylation | ETNTRVNTLTPVTIK CCCCCCCCCCCCCHH | 29.20 | 27214570 | |
| 40 | Phosphorylation | NTRVNTLTPVTIKQI CCCCCCCCCCCHHHH | 17.42 | 27214570 | |
| 45 | Acetylation | TLTPVTIKQILESKQ CCCCCCHHHHHHHCC | 23.17 | 24489116 | |
| 100 | Ubiquitination | TGQIEVRKWSEDAND CCEEEEEEECCCCCH | 61.31 | 23749301 | |
| 102 | Phosphorylation | QIEVRKWSEDANDLA EEEEEEECCCCCHHC | 28.74 | 19823750 | |
| 115 | Phosphorylation | LAAGNDDSSGKGYGS HCCCCCCCCCCCCCH | 43.80 | 25521595 | |
| 116 | Phosphorylation | AAGNDDSSGKGYGSQ CCCCCCCCCCCCCHH | 52.06 | 22369663 | |
| 120 | Phosphorylation | DDSSGKGYGSQVAQQ CCCCCCCCCHHHHHH | 19.65 | 25521595 | |
| 122 | Phosphorylation | SSGKGYGSQVAQQFE CCCCCCCHHHHHHEE | 17.01 | 22369663 | |
| 141 | Acetylation | VKVFGALKEFGGKKN EEEEEEHHHHCCCCC | 50.92 | 24489116 | |
| 187 | Phosphorylation | MMKQPLESASNNNGQ CCCCCCHHHCCCCCC | 44.68 | 27214570 | |
| 189 | Phosphorylation | KQPLESASNNNGQSL CCCCHHHCCCCCCCE | 49.74 | 17563356 | |
| 204 | Phosphorylation | FVKDDNDTSSGSSPL EEECCCCCCCCCCHH | 30.92 | 23749301 | |
| 205 | Phosphorylation | VKDDNDTSSGSSPLQ EECCCCCCCCCCHHH | 35.25 | 30377154 | |
| 206 | Phosphorylation | KDDNDTSSGSSPLQR ECCCCCCCCCCHHHH | 44.80 | 22369663 | |
| 208 | Phosphorylation | DNDTSSGSSPLQRIL CCCCCCCCCHHHHHH | 30.63 | 22369663 | |
| 209 | Phosphorylation | NDTSSGSSPLQRILE CCCCCCCCHHHHHHH | 32.91 | 22369663 |
| 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 RFA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RFA2_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 RFA2_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-27; TYR-120; SER-122 ANDSER-189, AND MASS 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-189, 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-122, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY. | |
