| UniProt ID | DOA10_YEAST | |
|---|---|---|
| UniProt AC | P40318 | |
| Protein Name | ERAD-associated E3 ubiquitin-protein ligase DOA10 | |
| Gene Name | SSM4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1319 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . Nucleus inner membrane Multi-pass membrane protein . |
|
| Protein Description | E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8.. | |
| Protein Sequence | MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNIDISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMMLDGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPRLSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLRHVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQNEFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAVVFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNGYTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPILAGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKILHDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESSSYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVRDVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPDFRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCLSKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSKLNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDVDSDVN -------CCCCCCCC | 47.20 | 22814378 | |
| 5 | Phosphorylation | ---MDVDSDVNVSRL ---CCCCCCCCHHHH | 43.22 | 24909858 | |
| 10 | Phosphorylation | VDSDVNVSRLRDELH CCCCCCHHHHHHHHH | 22.01 | 24961812 | |
| 18 | Ubiquitination | RLRDELHKVANEETD HHHHHHHHHHCCCCC | 56.52 | 17644757 | |
| 26 | Phosphorylation | VANEETDTATFNDDA HHCCCCCCCCCCCCC | 34.71 | 21440633 | |
| 28 | Phosphorylation | NEETDTATFNDDAPS CCCCCCCCCCCCCCC | 25.68 | 20377248 | |
| 57 | Ubiquitination | NPLFHPCKCRGSIKY CCCCCCCCCCCCHHH | 31.27 | 17644757 | |
| 63 | Ubiquitination | CKCRGSIKYMHESCL CCCCCCHHHCCHHHH | 37.91 | 17644757 | |
| 76 | Phosphorylation | CLLEWVASKNIDISK HHHHHHHHCCCCCCC | 19.33 | 25704821 | |
| 77 | Ubiquitination | LLEWVASKNIDISKP HHHHHHHCCCCCCCC | 48.46 | 17644757 | |
| 83 | Ubiquitination | SKNIDISKPGADVKC HCCCCCCCCCCCCCC | 48.05 | 23749301 | |
| 89 | Ubiquitination | SKPGADVKCDICHYP CCCCCCCCCCCCCCE | 27.08 | 17644757 | |
| 100 | Ubiquitination | CHYPIQFKTIYAENM CCCEEEEEEEECCCC | 20.03 | 17644757 | |
| 172 | Ubiquitination | PYPGDFLKSLIYGYD CCCCHHHHHHHHCCC | 43.12 | 17644757 | |
| 264 | Phosphorylation | MDDRMVEYLAREMRA CCHHHHHHHHHHHHH | 8.34 | 28132839 | |
| 339 | Phosphorylation | EEHENNDSDNSLPSG HHHCCCCCCCCCCCC | 40.59 | 28889911 | |
| 342 | Phosphorylation | ENNDSDNSLPSGDDS CCCCCCCCCCCCCCC | 46.80 | 28889911 | |
| 345 | Phosphorylation | DSDNSLPSGDDSSRI CCCCCCCCCCCCCCC | 61.21 | 28889911 | |
| 349 | Phosphorylation | SLPSGDDSSRILPGS CCCCCCCCCCCCCCC | 26.68 | 19779198 | |
| 356 | Phosphorylation | SSRILPGSSSDNEED CCCCCCCCCCCCHHH | 25.40 | 19795423 | |
| 357 | Phosphorylation | SRILPGSSSDNEEDE CCCCCCCCCCCHHHH | 47.85 | 19795423 | |
| 358 | Phosphorylation | RILPGSSSDNEEDEE CCCCCCCCCCHHHHH | 46.26 | 19795423 | |
| 692 | Phosphorylation | YMYWFAKYIGMIRKN HHHHHHHHHHHHHHC | 10.16 | 21126336 | |
| 768 | Phosphorylation | MLKSNLLSVPEAYKP HHHCCCCCCCHHHCC | 38.50 | 28889911 | |
| 799 | Phosphorylation | FTKRILESSSYVKPL HHHHHHHCCCCHHHH | 22.57 | 30377154 | |
| 800 | Phosphorylation | TKRILESSSYVKPLL HHHHHHCCCCHHHHH | 19.13 | 30377154 | |
| 831 | Ubiquitination | LSSFILGKDTPTERG HHHHHCCCCCCCCCC | 55.79 | 24961812 | |
| 848 | Acetylation | VYRNLFYKYIAAKNA EHHHHHHHHHHHHCC | 23.89 | 24489116 | |
| 853 | Ubiquitination | FYKYIAAKNAEWSNQ HHHHHHHHCCCCCCH | 47.90 | 17644757 | |
| 865 | Ubiquitination | SNQELFTKPKTLEQA CCHHHCCCCCHHHHH | 36.86 | 17644757 | |
| 867 | Ubiquitination | QELFTKPKTLEQAEE HHHCCCCCHHHHHHH | 68.26 | 17644757 | |
| 897 | Phosphorylation | GVLMRVPSSDIVSRN CEEEECCCHHHCCCC | 37.47 | 23749301 | |
| 915 | Ubiquitination | TMFVPVTKDDKLLKP EEEEEECCCCCCCCC | 65.25 | 17644757 | |
| 921 | Acetylation | TKDDKLLKPLDLERI CCCCCCCCCCCHHHH | 54.71 | 24489116 |
| 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 DOA10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DOA10_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 DOA10_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-897, AND MASSSPECTROMETRY. | |
