| UniProt ID | RFC1_YEAST | |
|---|---|---|
| UniProt AC | P38630 | |
| Protein Name | Replication factor C subunit 1 | |
| Gene Name | RFC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 861 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the ATP-dependent clamp loader RFC complex for the POL30/PCNA homotrimer DNA clamp. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA. Replication factor C (RFC or activator 1) complex acts during elongation of primed DNA templates by DNA polymerase delta and epsilon. RFC has an essential but redundant activity in sister chromatid cohesion establishment.. | |
| Protein Sequence | MVNISDFFGKNKKSVRSSTSRPTRQVGSSKPEVIDLDTESDQESTNKTPKKMPVSNVIDVSETPEGEKKLPLPAKRKASSPTVKPASSKKTKPSSKSSDSASNITAQDVLDKIPSLDLSNVHVKENAKFDFKSANSNADPDEIVSEIGSFPEGKPNCLLGLTIVFTGVLPTLERGASEALAKRYGARVTKSISSKTSVVVLGDEAGPKKLEKIKQLKIKAIDEEGFKQLIAGMPAEGGDGEAAEKARRKLEEQHNIATKEAELLVKKEEERSKKLAATRVSGGHLERDNVVREEDKLWTVKYAPTNLQQVCGNKGSVMKLKNWLANWENSKKNSFKHAGKDGSGVFRAAMLYGPPGIGKTTAAHLVAQELGYDILEQNASDVRSKTLLNAGVKNALDNMSVVGYFKHNEEAQNLNGKHFVIIMDEVDGMSGGDRGGVGQLAQFCRKTSTPLILICNERNLPKMRPFDRVCLDIQFRRPDANSIKSRLMTIAIREKFKLDPNVIDRLIQTTRGDIRQVINLLSTISTTTKTINHENINEISKAWEKNIALKPFDIAHKMLDGQIYSDIGSRNFTLNDKIALYFDDFDFTPLMIQENYLSTRPSVLKPGQSHLEAVAEAANCISLGDIVEKKIRSSEQLWSLLPLHAVLSSVYPASKVAGHMAGRINFTAWLGQNSKSAKYYRLLQEIHYHTRLGTSTDKIGLRLDYLPTFRKRLLDPFLKQGADAISSVIEVMDDYYLTKEDWDSIMEFFVGPDVTTAIIKKIPATVKSGFTRKYNSMTHPVAIYRTGSTIGGGGVGTSTSTPDFEDVVDADDNPVPADDEETQDSSTDLKKDKLIKQKAKPTKRKTATSKPGGSKKRKTKA | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MVNISDFFGKNK ---CCCHHHHCCCCC | 24.14 | 30377154 | |
| 14 | Phosphorylation | FFGKNKKSVRSSTSR HCCCCCCCCCCCCCC | 25.11 | 19823750 | |
| 17 | Phosphorylation | KNKKSVRSSTSRPTR CCCCCCCCCCCCCCC | 35.49 | 19823750 | |
| 18 | Phosphorylation | NKKSVRSSTSRPTRQ CCCCCCCCCCCCCCC | 21.60 | 19823750 | |
| 19 | Phosphorylation | KKSVRSSTSRPTRQV CCCCCCCCCCCCCCC | 29.96 | 21551504 | |
| 20 | Phosphorylation | KSVRSSTSRPTRQVG CCCCCCCCCCCCCCC | 37.90 | 19823750 | |
| 23 | Phosphorylation | RSSTSRPTRQVGSSK CCCCCCCCCCCCCCC | 32.40 | 19823750 | |
| 28 | Phosphorylation | RPTRQVGSSKPEVID CCCCCCCCCCCEEEE | 36.01 | 22369663 | |
| 29 | Phosphorylation | PTRQVGSSKPEVIDL CCCCCCCCCCEEEEC | 46.42 | 20377248 | |
| 38 | Phosphorylation | PEVIDLDTESDQEST CEEEECCCCCCHHHC | 44.69 | 22369663 | |
| 40 | Phosphorylation | VIDLDTESDQESTNK EEECCCCCCHHHCCC | 46.84 | 22369663 | |
| 44 | Phosphorylation | DTESDQESTNKTPKK CCCCCHHHCCCCCCC | 31.48 | 22369663 | |
| 45 | Phosphorylation | TESDQESTNKTPKKM CCCCHHHCCCCCCCC | 39.73 | 22369663 | |
| 48 | Phosphorylation | DQESTNKTPKKMPVS CHHHCCCCCCCCCCC | 42.27 | 29136822 | |
| 50 | Ubiquitination | ESTNKTPKKMPVSNV HHCCCCCCCCCCCCE | 67.92 | 15699485 | |
| 51 | Ubiquitination | STNKTPKKMPVSNVI HCCCCCCCCCCCCEE | 50.03 | 15699485 | |
| 55 | Phosphorylation | TPKKMPVSNVIDVSE CCCCCCCCCEEECCC | 21.36 | 26447709 | |
| 61 | Phosphorylation | VSNVIDVSETPEGEK CCCEEECCCCCCCCC | 31.82 | 28152593 | |
| 63 | Phosphorylation | NVIDVSETPEGEKKL CEEECCCCCCCCCCC | 21.09 | 25521595 | |
| 68 | Ubiquitination | SETPEGEKKLPLPAK CCCCCCCCCCCCCCC | 71.16 | 15699485 | |
| 68 | Acetylation | SETPEGEKKLPLPAK CCCCCCCCCCCCCCC | 71.16 | 24489116 | |
| 69 | Ubiquitination | ETPEGEKKLPLPAKR CCCCCCCCCCCCCCC | 51.54 | 15699485 | |
| 79 | Phosphorylation | LPAKRKASSPTVKPA CCCCCCCCCCCCCCC | 39.63 | 19823750 | |
| 80 | Phosphorylation | PAKRKASSPTVKPAS CCCCCCCCCCCCCCC | 29.47 | 19823750 | |
| 82 | Phosphorylation | KRKASSPTVKPASSK CCCCCCCCCCCCCCC | 43.01 | 29136822 | |
| 87 | Phosphorylation | SPTVKPASSKKTKPS CCCCCCCCCCCCCCC | 51.74 | 29136822 | |
| 88 | Phosphorylation | PTVKPASSKKTKPSS CCCCCCCCCCCCCCC | 40.03 | 29136822 | |
| 96 | Ubiquitination | KKTKPSSKSSDSASN CCCCCCCCCCCCCCC | 59.31 | 17644757 | |
| 98 | Phosphorylation | TKPSSKSSDSASNIT CCCCCCCCCCCCCCC | 39.04 | 28889911 | |
| 100 | Phosphorylation | PSSKSSDSASNITAQ CCCCCCCCCCCCCHH | 35.23 | 19779198 | |
| 112 | Ubiquitination | TAQDVLDKIPSLDLS CHHHHHHHCCCCCCC | 52.97 | 17644757 | |
| 115 | Phosphorylation | DVLDKIPSLDLSNVH HHHHHCCCCCCCCCC | 37.68 | 21440633 | |
| 124 | Ubiquitination | DLSNVHVKENAKFDF CCCCCCCCCCCEECC | 30.30 | 17644757 | |
| 128 | Acetylation | VHVKENAKFDFKSAN CCCCCCCEECCCCCC | 57.98 | 22865919 | |
| 296 | Acetylation | NVVREEDKLWTVKYA CCCCCCHHEEEEEEC | 49.56 | 24489116 | |
| 529 | Ubiquitination | STISTTTKTINHENI HHHCCCCCCCCCCCH | 45.36 | 17644757 | |
| 541 | Ubiquitination | ENINEISKAWEKNIA CCHHHHHHHHHHCCC | 64.28 | 17644757 | |
| 541 | Acetylation | ENINEISKAWEKNIA CCHHHHHHHHHHCCC | 64.28 | 24489116 | |
| 550 | Acetylation | WEKNIALKPFDIAHK HHHCCCCCHHHHHHH | 34.32 | 24489116 | |
| 655 | Ubiquitination | SSVYPASKVAGHMAG HHHCCHHHHHHHHHC | 37.90 | 23749301 | |
| 667 | Phosphorylation | MAGRINFTAWLGQNS HHCCEEEEEECCCCC | 16.67 | 28889911 | |
| 674 | Phosphorylation | TAWLGQNSKSAKYYR EEECCCCCHHHHHHH | 21.79 | 28889911 | |
| 675 | Ubiquitination | AWLGQNSKSAKYYRL EECCCCCHHHHHHHH | 63.08 | 22817900 | |
| 678 | Ubiquitination | GQNSKSAKYYRLLQE CCCCHHHHHHHHHHH | 50.32 | 22817900 | |
| 694 | Phosphorylation | HYHTRLGTSTDKIGL HHHHCCCCCCCCCCC | 32.80 | 27017623 | |
| 695 | Phosphorylation | YHTRLGTSTDKIGLR HHHCCCCCCCCCCCC | 32.58 | 27017623 | |
| 696 | Phosphorylation | HTRLGTSTDKIGLRL HHCCCCCCCCCCCCC | 40.94 | 27017623 | |
| 698 | Ubiquitination | RLGTSTDKIGLRLDY CCCCCCCCCCCCCCC | 38.47 | 23749301 | |
| 708 | Phosphorylation | LRLDYLPTFRKRLLD CCCCCHHHHHHHHHH | 33.21 | 27017623 | |
| 773 | Acetylation | VKSGFTRKYNSMTHP CCCCCCCCCCCCCCC | 45.81 | 25381059 | |
| 786 | Phosphorylation | HPVAIYRTGSTIGGG CCEEEEECCCCCCCC | 20.65 | 30377154 | |
| 822 | Phosphorylation | VPADDEETQDSSTDL CCCCCCCCCCCCCHH | 35.31 | 19779198 | |
| 825 | Phosphorylation | DDEETQDSSTDLKKD CCCCCCCCCCHHHHH | 25.89 | 27214570 | |
| 826 | Phosphorylation | DEETQDSSTDLKKDK CCCCCCCCCHHHHHH | 33.94 | 19779198 | |
| 827 | Phosphorylation | EETQDSSTDLKKDKL CCCCCCCCHHHHHHH | 49.67 | 21440633 | |
| 838 | Acetylation | KDKLIKQKAKPTKRK HHHHHHHHCCCCCCC | 54.07 | 25381059 | |
| 840 | Acetylation | KLIKQKAKPTKRKTA HHHHHHCCCCCCCCC | 61.32 | 25381059 |
| 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 RFC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RFC1_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 RFC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 THR-38; SER-40; THR-63 ANDSER-80, 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 THR-38; SER-40; SER-79 ANDSER-80, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38 AND SER-40, AND MASSSPECTROMETRY. | |
