| UniProt ID | RPN1_YEAST | |
|---|---|---|
| UniProt AC | P38764 | |
| Protein Name | 26S proteasome regulatory subunit RPN1 | |
| Gene Name | RPN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 993 | |
| Subcellular Localization | ||
| Protein Description | Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.. | |
| Protein Sequence | MVDESDKKQQTIDEQSQISPEKQTPNKKDKKKEEEEQLSEEDAKLKTDLELLVERLKEDDSSLYEASLNALKESIKNSTSSMTAVPKPLKFLRPTYPDLCSIYDKWTDPNLKSSLADVLSILAMTYSENGKHDSLRYRLLSDVSDFEGWGHEYIRHLALEIGEVYNDQVEKDAEDETSSDGSKSDGSAATSGFEFSKEDTLRLCLDIVPYFLKHNGEEDAVDLLLEIESIDKLPQFVDENTFQRVCQYMVACVPLLPPPEDVAFLKTAYSIYLSQNELTDAIALAVRLGEEDMIRSVFDATSDPVMHKQLAYILAAQKTSFEYEGVQDIIGNGKLSEHFLYLAKELNLTGPKVPEDIYKSHLDNSKSVFSSAGLDSAQQNLASSFVNGFLNLGYCNDKLIVDNDNWVYKTKGDGMTSAVASIGSIYQWNLDGLQQLDKYLYVDEPEVKAGALLGIGISASGVHDGEVEPALLLLQDYVTNPDTKISSAAILGLGIAFAGSKNDEVLGLLLPIAASTDLPIETAAMASLALAHVFVGTCNGDITTSIMDNFLERTAIELKTDWVRFLALALGILYMGQGEQVDDVLETISAIEHPMTSAIEVLVGSCAYTGTGDVLLIQDLLHRLTPKNVKGEEDADEEETAEGQTNSISDFLGEQVNEPTKNEEAEIEVDEMEVDAEGEEVEVKAEITEKKNGESLEGEEIKSEEKKGKSSDKDATTDGKNDDEEEEKEAGIVDELAYAVLGIALIALGEDIGKEMSLRHFGHLMHYGNEHIRRMVPLAMGIVSVSDPQMKVFDTLTRFSHDADLEVSMNSIFAMGLCGAGTNNARLAQLLRQLASYYSREQDALFITRLAQGLLHLGKGTMTMDVFNDAHVLNKVTLASILTTAVGLVSPSFMLKHHQLFYMLNAGIRPKFILALNDEGEPIKVNVRVGQAVETVGQAGRPKKITGWITQSTPVLLNHGERAELETDEYISYTSHIEGVVILKKNPDYREEE | |
| 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 |
|---|---|---|---|---|---|
| 7 | Ubiquitination | -MVDESDKKQQTIDE -CCCHHHHHCCCHHH | 62.86 | 17644757 | |
| 8 | Ubiquitination | MVDESDKKQQTIDEQ CCCHHHHHCCCHHHH | 53.26 | 17644757 | |
| 11 | Phosphorylation | ESDKKQQTIDEQSQI HHHHHCCCHHHHHCC | 28.09 | 22890988 | |
| 16 | Phosphorylation | QQTIDEQSQISPEKQ CCCHHHHHCCCCCCC | 27.68 | 22369663 | |
| 19 | Phosphorylation | IDEQSQISPEKQTPN HHHHHCCCCCCCCCC | 21.26 | 22369663 | |
| 22 | Ubiquitination | QSQISPEKQTPNKKD HHCCCCCCCCCCHHH | 63.96 | 23749301 | |
| 24 | Phosphorylation | QISPEKQTPNKKDKK CCCCCCCCCCHHHHH | 39.64 | 22369663 | |
| 27 | Ubiquitination | PEKQTPNKKDKKKEE CCCCCCCHHHHHHHH | 64.65 | 17644757 | |
| 28 | Ubiquitination | EKQTPNKKDKKKEEE CCCCCCHHHHHHHHH | 79.86 | 17644757 | |
| 30 | Ubiquitination | QTPNKKDKKKEEEEQ CCCCHHHHHHHHHHH | 74.71 | 17644757 | |
| 31 | Ubiquitination | TPNKKDKKKEEEEQL CCCHHHHHHHHHHHH | 75.46 | 17644757 | |
| 32 | Ubiquitination | PNKKDKKKEEEEQLS CCHHHHHHHHHHHHC | 75.89 | 17644757 | |
| 39 | Phosphorylation | KEEEEQLSEEDAKLK HHHHHHHCHHHHHHH | 38.34 | 28889911 | |
| 44 | Ubiquitination | QLSEEDAKLKTDLEL HHCHHHHHHHHHHHH | 63.94 | 17644757 | |
| 46 | Ubiquitination | SEEDAKLKTDLELLV CHHHHHHHHHHHHHH | 39.01 | 17644757 | |
| 57 | Ubiquitination | ELLVERLKEDDSSLY HHHHHHHHCCCCHHH | 66.38 | 17644757 | |
| 61 | Phosphorylation | ERLKEDDSSLYEASL HHHHCCCCHHHHHHH | 34.27 | 19779198 | |
| 72 | Ubiquitination | EASLNALKESIKNST HHHHHHHHHHHHCCC | 47.18 | 17644757 | |
| 74 | Phosphorylation | SLNALKESIKNSTSS HHHHHHHHHHCCCCC | 36.96 | 19823750 | |
| 76 | Ubiquitination | NALKESIKNSTSSMT HHHHHHHHCCCCCCC | 54.87 | 17644757 | |
| 78 | Phosphorylation | LKESIKNSTSSMTAV HHHHHHCCCCCCCCC | 25.35 | 19823750 | |
| 79 | Phosphorylation | KESIKNSTSSMTAVP HHHHHCCCCCCCCCC | 33.93 | 19823750 | |
| 80 | Phosphorylation | ESIKNSTSSMTAVPK HHHHCCCCCCCCCCC | 20.24 | 19823750 | |
| 81 | Phosphorylation | SIKNSTSSMTAVPKP HHHCCCCCCCCCCCC | 21.90 | 19823750 | |
| 83 | Phosphorylation | KNSTSSMTAVPKPLK HCCCCCCCCCCCCCH | 26.84 | 19823750 | |
| 87 | Ubiquitination | SSMTAVPKPLKFLRP CCCCCCCCCCHHHCC | 57.28 | 17644757 | |
| 90 | Ubiquitination | TAVPKPLKFLRPTYP CCCCCCCHHHCCCCH | 51.37 | 17644757 | |
| 105 | Ubiquitination | DLCSIYDKWTDPNLK HHHHHHHCCCCCCHH | 34.71 | 17644757 | |
| 112 | Ubiquitination | KWTDPNLKSSLADVL CCCCCCHHHHHHHHH | 44.64 | 17644757 | |
| 131 | Ubiquitination | MTYSENGKHDSLRYR HHCCCCCCCCCHHHH | 56.68 | 17644757 | |
| 165 | Phosphorylation | ALEIGEVYNDQVEKD HHHHHHHHCHHHHHC | 14.55 | 29688323 | |
| 177 | Phosphorylation | EKDAEDETSSDGSKS HHCCCCCCCCCCCCC | 45.94 | 25521595 | |
| 178 | Phosphorylation | KDAEDETSSDGSKSD HCCCCCCCCCCCCCC | 25.12 | 25521595 | |
| 179 | Phosphorylation | DAEDETSSDGSKSDG CCCCCCCCCCCCCCC | 54.10 | 20486117 | |
| 182 | Phosphorylation | DETSSDGSKSDGSAA CCCCCCCCCCCCCCC | 33.70 | 22369663 | |
| 183 | Ubiquitination | ETSSDGSKSDGSAAT CCCCCCCCCCCCCCC | 59.08 | 17644757 | |
| 184 | Phosphorylation | TSSDGSKSDGSAATS CCCCCCCCCCCCCCC | 49.23 | 22369663 | |
| 187 | Phosphorylation | DGSKSDGSAATSGFE CCCCCCCCCCCCCCC | 21.52 | 22369663 | |
| 190 | Phosphorylation | KSDGSAATSGFEFSK CCCCCCCCCCCCCCH | 29.15 | 20486117 | |
| 191 | Phosphorylation | SDGSAATSGFEFSKE CCCCCCCCCCCCCHH | 36.44 | 22369663 | |
| 196 | Phosphorylation | ATSGFEFSKEDTLRL CCCCCCCCHHHHHHH | 28.12 | 22369663 | |
| 197 | Acetylation | TSGFEFSKEDTLRLC CCCCCCCHHHHHHHH | 66.00 | 24489116 | |
| 197 | Ubiquitination | TSGFEFSKEDTLRLC CCCCCCCHHHHHHHH | 66.00 | 23749301 | |
| 213 | Ubiquitination | DIVPYFLKHNGEEDA HHHHHHHHCCCCCCH | 25.73 | 17644757 | |
| 232 | Ubiquitination | LEIESIDKLPQFVDE HHHHHHHCCCCCCCC | 61.47 | 17644757 | |
| 266 | Ubiquitination | PEDVAFLKTAYSIYL HHHHHHHHHHHHHHC | 25.34 | 17644757 | |
| 308 | Ubiquitination | TSDPVMHKQLAYILA CCCHHHHHHHHHHHH | 28.98 | 24961812 | |
| 318 | Ubiquitination | AYILAAQKTSFEYEG HHHHHHHHCCCEECC | 41.22 | 17644757 | |
| 334 | Ubiquitination | QDIIGNGKLSEHFLY HHHCCCCCHHHHHHH | 53.49 | 17644757 | |
| 344 | Ubiquitination | EHFLYLAKELNLTGP HHHHHHHHHCCCCCC | 61.20 | 23749301 | |
| 349 | Phosphorylation | LAKELNLTGPKVPED HHHHCCCCCCCCCHH | 50.82 | 28889911 | |
| 352 | Ubiquitination | ELNLTGPKVPEDIYK HCCCCCCCCCHHHHH | 72.30 | 23749301 | |
| 352 | Acetylation | ELNLTGPKVPEDIYK HCCCCCCCCCHHHHH | 72.30 | 24489116 | |
| 359 | Acetylation | KVPEDIYKSHLDNSK CCCHHHHHHHCCCCC | 31.56 | 24489116 | |
| 359 | Ubiquitination | KVPEDIYKSHLDNSK CCCHHHHHHHCCCCC | 31.56 | 17644757 | |
| 366 | Ubiquitination | KSHLDNSKSVFSSAG HHHCCCCCHHHHHCC | 57.82 | 17644757 | |
| 398 | Ubiquitination | NLGYCNDKLIVDNDN CCCCCCCEEEEECCC | 26.56 | 17644757 | |
| 409 | Acetylation | DNDNWVYKTKGDGMT ECCCEEEEECCCCCC | 33.86 | 24489116 | |
| 409 | Ubiquitination | DNDNWVYKTKGDGMT ECCCEEEEECCCCCC | 33.86 | 23749301 | |
| 411 | Ubiquitination | DNWVYKTKGDGMTSA CCEEEEECCCCCCHH | 51.34 | 17644757 | |
| 438 | Ubiquitination | DGLQQLDKYLYVDEP HHHHHHHHEEECCCH | 45.83 | 17644757 | |
| 448 | Ubiquitination | YVDEPEVKAGALLGI ECCCHHHCCCCEEEE | 39.17 | 17644757 | |
| 484 | Ubiquitination | YVTNPDTKISSAAIL HCCCCCCCCCHHHHH | 48.23 | 17644757 | |
| 640 | Phosphorylation | EDADEEETAEGQTNS CCCCHHHHCCCCCCC | 33.03 | 20486117 | |
| 645 | Phosphorylation | EETAEGQTNSISDFL HHHCCCCCCCHHHHH | 41.62 | 20377248 | |
| 647 | Phosphorylation | TAEGQTNSISDFLGE HCCCCCCCHHHHHHH | 27.19 | 25521595 | |
| 649 | Phosphorylation | EGQTNSISDFLGEQV CCCCCCHHHHHHHCC | 23.33 | 22369663 | |
| 690 | Ubiquitination | VKAEITEKKNGESLE EEEEEEECCCCCCCC | 42.78 | 17644757 | |
| 691 | Ubiquitination | KAEITEKKNGESLEG EEEEEECCCCCCCCC | 65.04 | 17644757 | |
| 695 | Phosphorylation | TEKKNGESLEGEEIK EECCCCCCCCCHHCC | 32.87 | 28889911 | |
| 702 | Ubiquitination | SLEGEEIKSEEKKGK CCCCHHCCCCCCCCC | 55.91 | 17644757 | |
| 706 | Ubiquitination | EEIKSEEKKGKSSDK HHCCCCCCCCCCCCC | 63.88 | 17644757 | |
| 707 | Ubiquitination | EIKSEEKKGKSSDKD HCCCCCCCCCCCCCC | 74.89 | 17644757 | |
| 716 | Phosphorylation | KSSDKDATTDGKNDD CCCCCCCCCCCCCCC | 35.24 | 21551504 | |
| 717 | Phosphorylation | SSDKDATTDGKNDDE CCCCCCCCCCCCCCH | 44.46 | 28889911 | |
| 791 | Acetylation | SVSDPQMKVFDTLTR ECCCHHHHHHHHHHC | 34.21 | 25381059 | |
| 791 | Ubiquitination | SVSDPQMKVFDTLTR ECCCHHHHHHHHHHC | 34.21 | 17644757 | |
| 877 | Phosphorylation | AHVLNKVTLASILTT HHHHCHHHHHHHHHH | 20.44 | 19823750 | |
| 880 | Phosphorylation | LNKVTLASILTTAVG HCHHHHHHHHHHHHH | 22.65 | 19823750 | |
| 883 | Phosphorylation | VTLASILTTAVGLVS HHHHHHHHHHHHCCC | 15.84 | 19823750 | |
| 884 | Phosphorylation | TLASILTTAVGLVSP HHHHHHHHHHHCCCH | 18.85 | 19823750 | |
| 890 | Phosphorylation | TTAVGLVSPSFMLKH HHHHHCCCHHHHHHH | 21.62 | 19823750 | |
| 892 | Phosphorylation | AVGLVSPSFMLKHHQ HHHCCCHHHHHHHHH | 18.78 | 19823750 | |
| 911 | Ubiquitination | LNAGIRPKFILALND HCCCCCCEEEEEECC | 34.88 | 17644757 | |
| 924 | Ubiquitination | NDEGEPIKVNVRVGQ CCCCCCEEEEEECCC | 38.17 | 17644757 | |
| 943 | Ubiquitination | VGQAGRPKKITGWIT EHHCCCCCCCCEEEC | 56.28 | 17644757 | |
| 944 | Ubiquitination | GQAGRPKKITGWITQ HHCCCCCCCCEEECC | 48.46 | 17644757 |
| 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 RPN1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN1_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 RPN1_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-16; SER-19; SER-187 ANDSER-695, 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-19 AND THR-24, 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 THR-24, AND MASSSPECTROMETRY. | |
