| UniProt ID | DMA2_YEAST | |
|---|---|---|
| UniProt AC | P53924 | |
| Protein Name | E3 ubiquitin-protein ligase DMA2 | |
| Gene Name | DMA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 522 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | E3 ubiquitin-protein ligase which functions in cell cycle retarding in conjonction with the UBC4 and UBC13/MMS2 complex, 2 E2 ubiquitin conjugationg enzymes. Involved in nutritional control of the cell cycle. Required for proper spindle positioning, likely regulating septin ring deposition at the bud neck.. | |
| Protein Sequence | MYTPIPANTPAPTAPTSSMTSNSSSASNANTTSSSGINPRNRASGTPSNERARPASGISSFLNTFGIRQNSQTASSSAAPDQRLFGTTPSNSHMSVAMESIDTAPQQQEPRLHHPIQMPLSAQFHVHRNYQLPISISLTAPTTTDHQQSSAHNFEGNNVGNVQESLNQRQPNGTNNTTTSIISMAPAATTRNIVGGADGSTIVNNSQEMYKNLRHLIYAANQPNGTEILHLDLPATSAEESNNMFNVDEVTLKQRKDKHGLFSIRLTPFIDSSSTTNQGLFFEPIIRKAGPGSQLVIGRYTERVRDAISKIPEQYHPVVFKSKVVSRTHGCFKVDSQGNWYIKDVKSSSGTFLNHQRLSPASSLSKDTPLRDGDILQLGMDFRGGTEEIYRCVRMRIELNRSWKLKANSFNKEALQRLQNLQKLTTGIEEEDCSICLCKIKPCQAIFISPCAHSWHFRCVRRLVMLSYPQFVCPNCRSSCDLEASFESSDEEDESDVESEGDQLVDQLSVLMETSKDVDSHP | |
| 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 |
|---|---|---|---|---|---|
| 46 | Phosphorylation | PRNRASGTPSNERAR CCCCCCCCCCCCCCC | 22.50 | 28889911 | |
| 56 | Phosphorylation | NERARPASGISSFLN CCCCCCCCCHHHHHH | 39.06 | 30377154 | |
| 59 | Phosphorylation | ARPASGISSFLNTFG CCCCCCHHHHHHHHC | 20.68 | 30377154 | |
| 60 | Phosphorylation | RPASGISSFLNTFGI CCCCCHHHHHHHHCC | 31.65 | 30377154 | |
| 71 | Phosphorylation | TFGIRQNSQTASSSA HHCCCCCCCCCCCCC | 22.14 | 22369663 | |
| 73 | Phosphorylation | GIRQNSQTASSSAAP CCCCCCCCCCCCCCC | 28.47 | 22369663 | |
| 75 | Phosphorylation | RQNSQTASSSAAPDQ CCCCCCCCCCCCCCC | 28.36 | 22369663 | |
| 76 | Phosphorylation | QNSQTASSSAAPDQR CCCCCCCCCCCCCCC | 22.87 | 22369663 | |
| 77 | Phosphorylation | NSQTASSSAAPDQRL CCCCCCCCCCCCCCC | 26.42 | 22369663 | |
| 87 | Phosphorylation | PDQRLFGTTPSNSHM CCCCCCCCCCCCCCH | 28.35 | 23749301 | |
| 88 | Phosphorylation | DQRLFGTTPSNSHMS CCCCCCCCCCCCCHH | 25.71 | 25752575 | |
| 90 | Phosphorylation | RLFGTTPSNSHMSVA CCCCCCCCCCCHHEE | 49.20 | 27017623 | |
| 92 | Phosphorylation | FGTTPSNSHMSVAME CCCCCCCCCHHEEEE | 25.55 | 28889911 | |
| 95 | Phosphorylation | TPSNSHMSVAMESID CCCCCCHHEEEECCC | 10.99 | 28889911 | |
| 130 | Phosphorylation | QFHVHRNYQLPISIS EEEEECCCCCCEEEE | 16.04 | 29688323 | |
| 135 | Phosphorylation | RNYQLPISISLTAPT CCCCCCEEEEEECCC | 12.27 | 29688323 | |
| 137 | Phosphorylation | YQLPISISLTAPTTT CCCCEEEEEECCCCC | 16.93 | 29688323 | |
| 139 | Phosphorylation | LPISISLTAPTTTDH CCEEEEEECCCCCCC | 24.65 | 29688323 | |
| 142 | Phosphorylation | SISLTAPTTTDHQQS EEEEECCCCCCCCCH | 39.60 | 29688323 | |
| 143 | Phosphorylation | ISLTAPTTTDHQQSS EEEECCCCCCCCCHH | 29.21 | 29688323 | |
| 144 | Phosphorylation | SLTAPTTTDHQQSSA EEECCCCCCCCCHHC | 33.68 | 29688323 | |
| 149 | Phosphorylation | TTTDHQQSSAHNFEG CCCCCCCHHCCCCCC | 23.95 | 29688323 | |
| 150 | Phosphorylation | TTDHQQSSAHNFEGN CCCCCCHHCCCCCCC | 29.25 | 29688323 | |
| 165 | Phosphorylation | NVGNVQESLNQRQPN CCCCHHHHHHCCCCC | 18.61 | 29688323 | |
| 206 | Phosphorylation | GSTIVNNSQEMYKNL CCCCCCCCHHHHHHH | 23.47 | 25752575 | |
| 210 | Phosphorylation | VNNSQEMYKNLRHLI CCCCHHHHHHHHHHH | 8.93 | 27017623 | |
| 211 | Ubiquitination | NNSQEMYKNLRHLIY CCCHHHHHHHHHHHH | 48.47 | 18202552 | |
| 256 | Ubiquitination | EVTLKQRKDKHGLFS EEEEEECCCCCCCEE | 69.50 | 18202552 | |
| 258 | Ubiquitination | TLKQRKDKHGLFSIR EEEECCCCCCCEEEE | 42.48 | 18202552 | |
| 288 | Ubiquitination | FFEPIIRKAGPGSQL EEHHHHHHCCCCCEE | 47.49 | 23749301 | |
| 310 | Ubiquitination | RVRDAISKIPEQYHP HHHHHHHCCCHHHCC | 57.05 | 18202552 | |
| 333 | Ubiquitination | SRTHGCFKVDSQGNW EECCCEEEECCCCCE | 49.57 | 18202552 | |
| 343 | Ubiquitination | SQGNWYIKDVKSSSG CCCCEEEEEEECCCC | 40.55 | 18202552 | |
| 346 | Ubiquitination | NWYIKDVKSSSGTFL CEEEEEEECCCCCCC | 55.54 | 18202552 | |
| 362 | Phosphorylation | HQRLSPASSLSKDTP CCCCCCCHHCCCCCC | 34.88 | 27017623 | |
| 366 | Ubiquitination | SPASSLSKDTPLRDG CCCHHCCCCCCCCCC | 71.55 | 18202552 | |
| 406 | Ubiquitination | LNRSWKLKANSFNKE HCCCCEECCCCCCHH | 41.62 | 18202552 | |
| 409 | Phosphorylation | SWKLKANSFNKEALQ CCEECCCCCCHHHHH | 34.75 | 29136822 | |
| 412 | Ubiquitination | LKANSFNKEALQRLQ ECCCCCCHHHHHHHH | 42.21 | 23749301 | |
| 423 | Ubiquitination | QRLQNLQKLTTGIEE HHHHHHHHHHHCCCH | 51.47 | 18202552 |
| 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 DMA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 211 | K | ubiquitylation |
| 18202552 |
| 211 | K | ubiquitylation |
| 18202552 |
| 256 | K | ubiquitylation |
| 18202552 |
| 258 | K | ubiquitylation |
| 18202552 |
| 258 | K | ubiquitylation |
| 18202552 |
| 258 | K | ubiquitylation |
| 18202552 |
| 288 | K | ubiquitylation |
| 18202552 |
| 288 | K | ubiquitylation |
| 18202552 |
| 310 | K | ubiquitylation |
| 18202552 |
| 310 | K | ubiquitylation |
| 18202552 |
| 310 | K | ubiquitylation |
| 18202552 |
| 333 | K | ubiquitylation |
| 18202552 |
| 343 | K | ubiquitylation |
| 18202552 |
| 343 | K | ubiquitylation |
| 18202552 |
| 346 | K | ubiquitylation |
| 18202552 |
| 346 | K | ubiquitylation |
| 18202552 |
| 366 | K | ubiquitylation |
| 18202552 |
| 366 | K | ubiquitylation |
| 18202552 |
| 366 | K | ubiquitylation |
| 18202552 |
| 406 | K | ubiquitylation |
| 18202552 |
| 412 | K | ubiquitylation |
| 18202552 |
| 412 | K | ubiquitylation |
| 18202552 |
| 423 | K | ubiquitylation |
| 18202552 |
* 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 DMA2_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-92; SER-95 AND SER-206,AND MASS SPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 andUbc13/Mms2-dependent ubiquitination."; Loring G.L., Christensen K.C., Gerber S.A., Brenner C.; Cell Cycle 7:96-105(2008). Cited for: FUNCTION, MASS SPECTROMETRY, AND UBIQUITINATION AT LYS-211; LYS-256;LYS-258; LYS-288; LYS-310; LYS-333; LYS-343; LYS-346; LYS-366;LYS-406; LYS-412 AND LYS-423. | |