| UniProt ID | ECM29_YEAST | |
|---|---|---|
| UniProt AC | P38737 | |
| Protein Name | Proteasome component ECM29 | |
| Gene Name | ECM29 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1868 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Stabilizes the proteasome holoenzyme, probably by tethering the 20S proteolytic core particle and the 19S regulatory particle. The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.. | |
| Protein Sequence | MSISSDEAKEKQLVEKAELRLAIADSPQKFETNLQTFLPPLLLKLASPHASVRTAVFSALKNLISRINTLPQVQLPVRALIVQAKEPNLAAQQDSTNVRLYSLLLASKGIDRLSLQDRQQLLPLVVSNISCLTGTVAARMFHILLKLILEWVAPQESSHEQEEFVQFLQLDNDGFSFLMRQFTRFFLLVPSKQVQVSQQPLSRGYTCPGLSLTDVAFFTYDAGVTFNKEQLNKFKKAIFQFVCRGMAATQTIEQSPRMIELMEFLCVVSTDSTNLSDDAAQFMKRFPMPYENEEFITFLQTLYIGNTANGRPPVKAILQEKILSILNRSHFATTKAECISLICSIGLHSSEYKLRSLTLSFIRHVAKLNYKNLNPASSSPSSTDFSTCIVSLIRNNLHAEGWPKLQLGPQTPAFNTAILQRQLQYETLGDILKRDFELVSDLSYIEFLFESLKNDLPQFRSSIQESLLSLVGHLSILPQQSKLKLKNLLRKNLSIDEQQREDNNDAVNSIMALKFVSIKFTNAAFPFHDPEARLFNIWGTVRTNRFDIIEESFKGLQPFWFRVNNASINTSATVKTSDLLGSHLSETEFPPFREFLQVLIDQLDSEAASITRKSLNNAVRFSKQCLISNAIYGKKTMVIQDEDWSVRIDKALELDDTVVSRVNEMVQGMNDDIFIRYLTLLSNEFTATNSKGEQIAIFPYQDPIFGSVLLTLLNFVSNNVLRRLEILVPDLYHLVIMKFQSLSDNDLAVCATIIGIISTAIADSTHVKRITKIAQSQTMAETYVASYVVPRLYLKDQTNHIESDSILNLLNILTTHLSHPGTNKDMILKLVCQVTKFGLLLQVSAQERKDFLKKVMDTIQDKLINDVTAIQTWSYLSLYSTDLENSSLFQEKLLETNVSKQNDFLFSVGESLSVVAGKWSSKYLIKQIDIPNFNVEIMQQKFPATNVTTILDEIFSGCDSTKPSLRKASCIWLLSYIQYLGHLPEVSSKCNDIHLRFMRFLADRDEFIQDSAARGLSLVYEIGGSDLKESMVKGLLKSFTESTAGSASTSATGISGSVSEETELFEPGVLNTGDGSISTYKDILNLASEVGDPALVYKFMSLAKSSALWSSRKGIAFGLGAIMSKSSLEELLLKDQQTAKKLIPKLYRYRFDPFQAVSRSMTDIWNTLIPESSLTISLYFNDILDELLCGMANKEWRVREASTSALLQLIQSQPQEKFSEKMLKIWTMAFRTMDDIKDSVREVGTKFTTVLAKILARSIDVEKGVNPTKSKEILDNILPFLWGPHGLNSDAEEVRNFALTTLIDLVKHSPGAIKPFTPKLIYDFITLFSSIEPQVINYLALNAANYNIDANVIDTQRKNGVTNSPLFQTIEKLINNSDDCMMEEIINVVIKASRKSVGLPSKVASSLVIIILVKRYSIEMKPYSGKLLKVCLTMFEDRNESVNIAFAISMGYLFKVSALDKCIKYSEKLITKYFEPTSTENNKKVVGTAIDSILNYAKSEFDNVASVFMPLIFIACNDEDKDLETLYNKIWTEASSSGAGTVKLYLPEILNVLCVNIKSNDFSIRKTCAKSVIQLCGGINDSIPYPQIVKLFDISREALSGRSWDGKEHIVAALVSLTEKFSQTVADNNDLQESINHVMYTEVSRKSMKYVKKILPLYARYINVNPQEETITFLIEKAKEMIRLLGSESDDSEGSIKQTSDESTIKRIKPNTEITQKSSKENIENEEYVINLLKVSVDICNNSKSRYPMNLLEFIIDEIAYLFHNDRIIHTWRTQLAASEIGISIVGRFSTISSADFIQNVGRLWDQTFPINCNKETIENVKLQMIKFGGLIIQKIPSLQNNIEENLRLLNSIDSTSRIELELKNIGL | |
| 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 | ------MSISSDEAK ------CCCCCHHHH | 42.34 | 22814378 | |
| 9 | Acetylation | SISSDEAKEKQLVEK CCCCHHHHHHHHHHH | 64.49 | 25381059 | |
| 29 | Ubiquitination | AIADSPQKFETNLQT HHCCCCHHHHHHHHH | 48.85 | 17644757 | |
| 44 | Ubiquitination | FLPPLLLKLASPHAS HHHHHHHHHHCCCHH | 41.81 | 17644757 | |
| 61 | Acetylation | TAVFSALKNLISRIN HHHHHHHHHHHHHHH | 49.80 | 24489116 | |
| 85 | Ubiquitination | RALIVQAKEPNLAAQ CEEEEECCCCCCCCC | 57.52 | 23749301 | |
| 108 | Ubiquitination | YSLLLASKGIDRLSL HHHHHHHCCCCCCCC | 55.04 | 17644757 | |
| 202 | Phosphorylation | QVSQQPLSRGYTCPG EECCCCCCCCCCCCC | 30.28 | 30377154 | |
| 377 | Phosphorylation | YKNLNPASSSPSSTD CCCCCCCCCCCCCCC | 32.38 | 30377154 | |
| 378 | Phosphorylation | KNLNPASSSPSSTDF CCCCCCCCCCCCCCH | 48.66 | 30377154 | |
| 386 | Phosphorylation | SPSSTDFSTCIVSLI CCCCCCHHHHHHHHH | 25.77 | 30377154 | |
| 404 | Ubiquitination | LHAEGWPKLQLGPQT CCCCCCCCCCCCCCC | 42.21 | 17644757 | |
| 425 | Phosphorylation | ILQRQLQYETLGDIL HHHHHHCHHCHHHHH | 21.34 | 28889911 | |
| 427 | Phosphorylation | QRQLQYETLGDILKR HHHHCHHCHHHHHHH | 30.98 | 28889911 | |
| 482 | Ubiquitination | SILPQQSKLKLKNLL HCCCCCCHHHHHHHH | 45.35 | 17644757 | |
| 519 | Ubiquitination | ALKFVSIKFTNAAFP HHHHHEEEEECCCCC | 38.33 | 17644757 | |
| 554 | Ubiquitination | DIIEESFKGLQPFWF HHHHHHCCCCCCEEE | 68.91 | 17644757 | |
| 575 | Ubiquitination | INTSATVKTSDLLGS CCCCCEEEHHHHCCC | 37.65 | 17644757 | |
| 614 | Phosphorylation | AASITRKSLNNAVRF HHHCHHHHHHHHHHH | 32.79 | 19823750 | |
| 622 | Phosphorylation | LNNAVRFSKQCLISN HHHHHHHHHHHHHCC | 15.97 | 19823750 | |
| 677 | Phosphorylation | NDDIFIRYLTLLSNE CHHHHHHHHHHHCCE | 10.14 | 28889911 | |
| 679 | Phosphorylation | DIFIRYLTLLSNEFT HHHHHHHHHHCCEEE | 19.40 | 28889911 | |
| 686 | Phosphorylation | TLLSNEFTATNSKGE HHHCCEEEECCCCCC | 26.79 | 28889911 | |
| 690 | Phosphorylation | NEFTATNSKGEQIAI CEEEECCCCCCEEEE | 37.37 | 28889911 | |
| 1049 | Phosphorylation | STAGSASTSATGISG CCCCCCCCCCCCCCC | 23.30 | 27017623 | |
| 1052 | Phosphorylation | GSASTSATGISGSVS CCCCCCCCCCCCCCC | 34.51 | 27017623 | |
| 1078 | Phosphorylation | NTGDGSISTYKDILN CCCCCCCHHHHHHHH | 27.64 | 27017623 | |
| 1079 | Phosphorylation | TGDGSISTYKDILNL CCCCCCHHHHHHHHH | 32.68 | 27017623 | |
| 1081 | Ubiquitination | DGSISTYKDILNLAS CCCCHHHHHHHHHHH | 38.08 | 17644757 | |
| 1098 | Ubiquitination | GDPALVYKFMSLAKS CCHHHHHHHHHHHHH | 27.41 | 17644757 | |
| 1125 | Ubiquitination | GLGAIMSKSSLEELL HHHHHHCCCHHHHHH | 27.04 | 17644757 | |
| 1134 | Acetylation | SLEELLLKDQQTAKK HHHHHHHCCHHHHHH | 54.16 | 24489116 | |
| 1134 | Ubiquitination | SLEELLLKDQQTAKK HHHHHHHCCHHHHHH | 54.16 | 17644757 | |
| 1140 | Ubiquitination | LKDQQTAKKLIPKLY HCCHHHHHHHHHHHH | 52.04 | 17644757 | |
| 1141 | Ubiquitination | KDQQTAKKLIPKLYR CCHHHHHHHHHHHHH | 49.54 | 17644757 | |
| 1217 | Ubiquitination | IQSQPQEKFSEKMLK HHCCCCHHHHHHHHH | 49.28 | 17644757 | |
| 1227 | Phosphorylation | EKMLKIWTMAFRTMD HHHHHHHHHHHHCHH | 11.33 | 30377154 | |
| 1232 | Phosphorylation | IWTMAFRTMDDIKDS HHHHHHHCHHHHHHH | 20.64 | 30377154 | |
| 1263 | Ubiquitination | ARSIDVEKGVNPTKS HHHCCHHCCCCCCCC | 68.92 | 23749301 | |
| 1396 | Phosphorylation | VIKASRKSVGLPSKV HHHHHHHCCCCCHHH | 21.95 | 21126336 | |
| 1483 | Ubiquitination | PTSTENNKKVVGTAI CCCCCCCCEEEHHHH | 59.53 | 17644757 | |
| 1484 | Ubiquitination | TSTENNKKVVGTAID CCCCCCCEEEHHHHH | 44.25 | 17644757 | |
| 1498 | Ubiquitination | DSILNYAKSEFDNVA HHHHHHHHHCCCHHH | 39.91 | 17644757 | |
| 1543 | Ubiquitination | SSGAGTVKLYLPEIL CCCCCEEEECHHHHH | 31.11 | 17644757 | |
| 1558 | Ubiquitination | NVLCVNIKSNDFSIR CEEEEECCCCCCCHH | 37.69 | 17644757 | |
| 1607 | Ubiquitination | SGRSWDGKEHIVAAL CCCCCCCHHHHHHHH | 43.58 | 17644757 | |
| 1620 | Ubiquitination | ALVSLTEKFSQTVAD HHHHHHHHHHHHHCC | 45.11 | 17644757 | |
| 1677 | Ubiquitination | TITFLIEKAKEMIRL HHHHHHHHHHHHHHH | 58.74 | 17644757 | |
| 1689 | Phosphorylation | IRLLGSESDDSEGSI HHHHCCCCCCCCCCE | 48.71 | 19779198 | |
| 1692 | Phosphorylation | LGSESDDSEGSIKQT HCCCCCCCCCCEEEC | 49.17 | 24909858 | |
| 1695 | Phosphorylation | ESDDSEGSIKQTSDE CCCCCCCCEEECCCH | 23.66 | 21440633 | |
| 1697 | Ubiquitination | DDSEGSIKQTSDEST CCCCCCEEECCCHHH | 49.58 | 23749301 | |
| 1703 | Phosphorylation | IKQTSDESTIKRIKP EEECCCHHHHHHCCC | 40.18 | 21440633 | |
| 1712 | Phosphorylation | IKRIKPNTEITQKSS HHHCCCCCCCCCCCC | 36.97 | 27017623 | |
| 1715 | Phosphorylation | IKPNTEITQKSSKEN CCCCCCCCCCCCHHH | 24.58 | 27017623 | |
| 1717 | Ubiquitination | PNTEITQKSSKENIE CCCCCCCCCCHHHCC | 48.31 | 17644757 | |
| 1720 | Ubiquitination | EITQKSSKENIENEE CCCCCCCHHHCCCHH | 62.97 | 17644757 | |
| 1734 | Ubiquitination | EYVINLLKVSVDICN HHHHHHHHHHHCCCC | 35.31 | 17644757 | |
| 1835 | Ubiquitination | FGGLIIQKIPSLQNN ECCCHHHCCHHHHCC | 46.29 | 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 ECM29_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ECM29_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 ECM29_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-1692 AND SER-1695, ANDMASS SPECTROMETRY. | |
