| UniProt ID | RUP1_YEAST | |
|---|---|---|
| UniProt AC | Q12242 | |
| Protein Name | UBA domain-containing protein RUP1 | |
| Gene Name | RUP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 671 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Modulates the activity of the RSP5 HECT ubiquitin-protein ligase through its mediation of the interaction between RSP5 and the deubiquitinase UBP2. Involved in regulation of cell wall homeostasis.. | |
| Protein Sequence | MMDNQAVKSLLEMGIPHEVAVDALQRTGGNLEAAVNFIFSNELPEQAEMGEENDGSQPRISENKIVAGTKPCDVPNNGDQDIDMPDVSGVDVDYDDDEDITDERSGSNSTSGCRVTAQNYDRYSISETSIPPPSYSIVQHNEFKSNVGDPTVVLPLPLNSLIESYFGLFALLTAVYFPHVFLKPDFKDLNYRADWFKGSSFTEPKYRLAYCEAEDGSTTSEIVLASGPNEGLQPHLLWQLQKLISVVNTRKCERAFVSAKVFTSSLEPQLRSKLADSEHLYEVLPAFIKSLAVDLEMCPGIRDRETRSLFISSALHTPNKNEPPMETFLSLFHFLPEEYDSNLYKMFNVLLYPEEEEEEEDVIRGGEQEEARYVEPENTLKEVAPVLTILFNELETNTESVSLPNGVDIPLEFYPQLYTKQCKDQLIRHIISKRKQARTRSRCLLQEINELKSYQGKNISTILESTLAYLQTIPDDANNEAAKQIASLKDTLNSARAAKMEEYKDLASKLHGEWNLSHPETHIINTAKQLGLIENPYILTMAALSPYSYFIRSRNGAWSWIQSNTLGTEFKVKKCSSPSVVQEAIKHGTKYASETPLMFIYCEEGKIPTEEVVAEALKSNSGCLKFAEDDQNSLKTLRSQFFDGMGDPEQATNNINNGNDNDNDDDIDSDN | |
| 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 |
|---|---|---|---|---|---|
| 56 | Phosphorylation | MGEENDGSQPRISEN CCCCCCCCCCCCCCC | 39.62 | 28889911 | |
| 101 | Phosphorylation | YDDDEDITDERSGSN CCCCCCCCCCCCCCC | 44.10 | 28889911 | |
| 107 | Phosphorylation | ITDERSGSNSTSGCR CCCCCCCCCCCCCCE | 28.93 | 28889911 | |
| 109 | Phosphorylation | DERSGSNSTSGCRVT CCCCCCCCCCCCEEE | 26.16 | 27214570 | |
| 110 | Phosphorylation | ERSGSNSTSGCRVTA CCCCCCCCCCCEEEE | 33.13 | 27214570 | |
| 111 | Phosphorylation | RSGSNSTSGCRVTAQ CCCCCCCCCCEEEEC | 35.40 | 25752575 | |
| 116 | Phosphorylation | STSGCRVTAQNYDRY CCCCCEEEECCCCCC | 11.81 | 22369663 | |
| 120 | Phosphorylation | CRVTAQNYDRYSISE CEEEECCCCCCCCCC | 6.96 | 22369663 | |
| 123 | Phosphorylation | TAQNYDRYSISETSI EECCCCCCCCCCCCC | 13.88 | 22369663 | |
| 124 | Phosphorylation | AQNYDRYSISETSIP ECCCCCCCCCCCCCC | 22.11 | 22369663 | |
| 126 | Phosphorylation | NYDRYSISETSIPPP CCCCCCCCCCCCCCC | 28.96 | 22369663 | |
| 128 | Phosphorylation | DRYSISETSIPPPSY CCCCCCCCCCCCCCC | 25.76 | 22369663 | |
| 129 | Phosphorylation | RYSISETSIPPPSYS CCCCCCCCCCCCCCC | 29.10 | 22369663 | |
| 134 | Phosphorylation | ETSIPPPSYSIVQHN CCCCCCCCCCEEECC | 36.97 | 22369663 | |
| 135 | Phosphorylation | TSIPPPSYSIVQHNE CCCCCCCCCEEECCC | 14.27 | 22369663 | |
| 136 | Phosphorylation | SIPPPSYSIVQHNEF CCCCCCCCEEECCCC | 22.18 | 22369663 | |
| 210 | Phosphorylation | EPKYRLAYCEAEDGS CCCEEEEEEECCCCC | 8.73 | 29688323 | |
| 217 | Phosphorylation | YCEAEDGSTTSEIVL EEECCCCCCEEEEEE | 40.61 | 29688323 | |
| 218 | Phosphorylation | CEAEDGSTTSEIVLA EECCCCCCEEEEEEE | 39.61 | 29688323 | |
| 219 | Phosphorylation | EAEDGSTTSEIVLAS ECCCCCCEEEEEEEC | 26.51 | 29688323 | |
| 220 | Phosphorylation | AEDGSTTSEIVLASG CCCCCCEEEEEEECC | 25.97 | 29688323 | |
| 226 | Phosphorylation | TSEIVLASGPNEGLQ EEEEEEECCCCCCCC | 51.09 | 29688323 | |
| 273 | Acetylation | LEPQLRSKLADSEHL CCHHHHHHHCCCHHH | 41.06 | 24489116 | |
| 273 | Ubiquitination | LEPQLRSKLADSEHL CCHHHHHHHCCCHHH | 41.06 | 23749301 | |
| 489 | Ubiquitination | AKQIASLKDTLNSAR HHHHHHHHHHHHHHH | 46.28 | 19722269 | |
| 499 | Ubiquitination | LNSARAAKMEEYKDL HHHHHHHHHHHHHHH | 45.95 | 19722269 | |
| 576 | Phosphorylation | EFKVKKCSSPSVVQE EEEEEECCCHHHHHH | 54.91 | 27017623 | |
| 579 | Phosphorylation | VKKCSSPSVVQEAIK EEECCCHHHHHHHHH | 36.55 | 27017623 | |
| 633 | Phosphorylation | FAEDDQNSLKTLRSQ CCCCCHHHHHHHHHH | 26.13 | 22369663 | |
| 635 | Ubiquitination | EDDQNSLKTLRSQFF CCCHHHHHHHHHHHC | 45.38 | 23749301 | |
| 639 | Phosphorylation | NSLKTLRSQFFDGMG HHHHHHHHHHCCCCC | 34.16 | 22369663 | |
| 652 | Phosphorylation | MGDPEQATNNINNGN CCCHHHHHCCCCCCC | 28.61 | 22369663 | |
| 669 | Phosphorylation | DNDDDIDSDN----- CCCCCCCCCC----- | 39.11 | 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 RUP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RUP1_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 RUP1_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-56; SER-126 AND SER-129,AND MASS SPECTROMETRY. | |