| UniProt ID | DOA1_YEAST | |
|---|---|---|
| UniProt AC | P36037 | |
| Protein Name | Protein DOA1 | |
| Gene Name | DOA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 715 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Participates in the regulation of the ubiquitin conjugation pathway involving CDC48 by hindering multiubiquitination of substrates at the CDC48 chaperone. May act by preventing the interaction between CDC48 and the E4 enzyme UFD2, leading to prevent multiubiquitination of substrates and subsequent degradation. Essential for maintaining cellular ubiquitin levels.. | |
| Protein Sequence | MGYQLSATLKGHDQDVRDVVAVDDSKVASVSRDGTVRLWSKDDQWLGTVVYTGQGFLNSVCYDSEKELLLFGGKDTMINGVPLFATSGEDPLYTLIGHQGNVCSLSFQDGVVISGSWDKTAKVWKEGSLVYNLQAHNASVWDAKVVSFSENKFLTASADKTIKLWQNDKVIKTFSGIHNDVVRHLAVVDDGHFISCSNDGLIKLVDMHTGDVLRTYEGHESFVYCIKLLPNGDIVSCGEDRTVRIWSKENGSLKQVITLPAISIWSVDCMSNGDIIVGSSDNLVRIFSQEKSRWASEDEINELSTQVEKSTISSKTIEFDESKLSPYEILQSPGRKEGQIVVVKSPQGTIEAHQFSNSSWKKVGDVVGAGATGNDKKIEFEGKTYDYVFDVDIEDGKPPLKLPINVSDNPYTAADNFLARYELPMSYRDQVVQFILKNTNGISLDQPNDNASSSAVSPSKTSVMKVLPVKQYLIMENYNPDTIFNGIVKINSNEKTFDDEILAQIGGALHDIDESWELLLSFANTIRSNWEIKTPAYDIVRLIVKKLPYSSDIKDYIEEGLGNKNITLTMLTVRILVNCFNNENWGVKLLESNQVYKSIFETIDTEFSQASAKQSQNLAIAVSTLIFNYSALVTKGNSDLELLPIVADAINTKYGPLEEYQECEEAAYRLTVAYGNLATVEPTLRQFANSVTWLANIKRSYGNVPRFKDIFDDLS | |
| 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 |
|---|---|---|---|---|---|
| 26 | Ubiquitination | VVAVDDSKVASVSRD EEEECCCCEEEECCC | 49.14 | 24961812 | |
| 152 | Ubiquitination | VVSFSENKFLTASAD EEEECCCEEECCCCC | 37.39 | 17644757 | |
| 160 | Acetylation | FLTASADKTIKLWQN EECCCCCCCEEHHCC | 52.44 | 24489116 | |
| 160 | Ubiquitination | FLTASADKTIKLWQN EECCCCCCCEEHHCC | 52.44 | 17644757 | |
| 172 | Ubiquitination | WQNDKVIKTFSGIHN HCCCCEEHCCCCCCH | 46.64 | 17644757 | |
| 325 | Phosphorylation | EFDESKLSPYEILQS EECHHHCCHHHHHCC | 29.22 | 22369663 | |
| 327 | Phosphorylation | DESKLSPYEILQSPG CHHHCCHHHHHCCCC | 16.54 | 22369663 | |
| 332 | Phosphorylation | SPYEILQSPGRKEGQ CHHHHHCCCCCCCCE | 26.35 | 22369663 | |
| 344 | Ubiquitination | EGQIVVVKSPQGTIE CCEEEEEECCCCCEE | 44.82 | 17644757 | |
| 345 | Phosphorylation | GQIVVVKSPQGTIEA CEEEEEECCCCCEEE | 15.73 | 27017623 | |
| 356 | Phosphorylation | TIEAHQFSNSSWKKV CEEEEEECCCCCEEE | 29.27 | 27017623 | |
| 358 | Phosphorylation | EAHQFSNSSWKKVGD EEEEECCCCCEEEEE | 36.06 | 27017623 | |
| 361 | Ubiquitination | QFSNSSWKKVGDVVG EECCCCCEEEEEEEC | 39.26 | 17644757 | |
| 362 | Ubiquitination | FSNSSWKKVGDVVGA ECCCCCEEEEEEECC | 45.23 | 17644757 | |
| 376 | Ubiquitination | AGATGNDKKIEFEGK CCCCCCCCEEEEECE | 60.70 | 17644757 | |
| 377 | Ubiquitination | GATGNDKKIEFEGKT CCCCCCCEEEEECEE | 50.78 | 17644757 | |
| 439 | Phosphorylation | VQFILKNTNGISLDQ HHHHHHCCCCCCCCC | 32.98 | 28889911 | |
| 443 | Phosphorylation | LKNTNGISLDQPNDN HHCCCCCCCCCCCCC | 27.56 | 22369663 | |
| 452 | Phosphorylation | DQPNDNASSSAVSPS CCCCCCCCCCCCCCC | 30.95 | 22369663 | |
| 453 | Phosphorylation | QPNDNASSSAVSPSK CCCCCCCCCCCCCCC | 21.65 | 22369663 | |
| 454 | Phosphorylation | PNDNASSSAVSPSKT CCCCCCCCCCCCCCC | 30.14 | 22369663 | |
| 457 | Phosphorylation | NASSSAVSPSKTSVM CCCCCCCCCCCCCCE | 24.15 | 22369663 | |
| 459 | Phosphorylation | SSSAVSPSKTSVMKV CCCCCCCCCCCCEEE | 40.85 | 22369663 | |
| 460 | Ubiquitination | SSAVSPSKTSVMKVL CCCCCCCCCCCEEEE | 48.48 | 23749301 | |
| 461 | Phosphorylation | SAVSPSKTSVMKVLP CCCCCCCCCCEEEEE | 30.78 | 26447709 | |
| 462 | Phosphorylation | AVSPSKTSVMKVLPV CCCCCCCCCEEEEEC | 24.77 | 28889911 | |
| 465 | Ubiquitination | PSKTSVMKVLPVKQY CCCCCCEEEEECCEE | 38.16 | 23749301 | |
| 472 | Phosphorylation | KVLPVKQYLIMENYN EEEECCEEEEECCCC | 7.77 | 28132839 | |
| 478 | Phosphorylation | QYLIMENYNPDTIFN EEEEECCCCCCCEEE | 18.11 | 28132839 | |
| 567 | Phosphorylation | GLGNKNITLTMLTVR CCCCCCEEEEEEEEH | 26.10 | 27017623 |
| 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 DOA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DOA1_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 DOA1_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-332; SER-454; SER-457AND SER-459, 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-332 AND SER-457, ANDMASS SPECTROMETRY. | |
