| UniProt ID | DEF1_YEAST | |
|---|---|---|
| UniProt AC | P35732 | |
| Protein Name | RNA polymerase II degradation factor 1 | |
| Gene Name | DEF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 738 | |
| Subcellular Localization | Nucleus . Chromosome, telomere . | |
| Protein Description | RNA polymerase II degradation factor recruits the ubiquitination machinery to the RNA polymerase II for polyubiquitination, removal and degradation, when RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation.. | |
| Protein Sequence | MSTQFRKSNHNSHSSKKLNPALKSKIDTLTELFPDWTSDDLIDIVQEYDDLETIIDKITSGAVTRWDEVKKPAKKEKYEKKEQQHSYVPQQHLPNPEDDITYKSSNNSNSFTSTKHNSSNNYTQARNKKKVQTPRAHTTGKHVNLDKGKHVPSKPVSNTTSWAAAVSVDTKHDVPQDSNDNNNEELEAQGQQAQEKNQEKEQEEQQQQEGHNNKEEHKQIEQPSLSSKKTTSRTSASQPKKMSWAAIATPKPKAVKKTESPLENVAELKKEISDIKKDDQKSEASEEKVNEQETSAQEQEEETAEPSEENEDRVPEVDGEEVQEEAEKKEQVKEEEQTAEELEQEQDNVAAPEEEVTVVEEKVEISAVISEPPEDQANTVPQPQQQSQQPQQPQQPQQPQQPQQPQQQQQPQQPQQPQQQLQQQQQQQQQPVQAQAQAQEEQLSQNYYTQQQQQQYAQQQHQLQQQYLSQQQQYAQQQQQHPQPQSQQPQSQQSPQSQKQGNNVAAQQYYMYQNQFPGYSYPGMFDSQGYAYGQQYQQLAQNNAQTSGNANQYNFQQGYGQAGANTAAANLTSAAAAAAASPATAHAQPQQQQPYGGSFMPYYAHFYQQSFPYGQPQYGVAGQYPYQLPKNNYNYYQTQNGQEQQSPNQGVAQHSEDSQQKQSQQQQQQQPQGQPQPEVQMQNGQPVNPQQQMQFQQYYQFQQQQQQAAAAAAAAAQQGVPYGYNGYDYNSKNSRGFY | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MSTQFRKSNHNSHSS CCCCCCCCCCCCCCH | 38.78 | 28889911 | |
| 103 | Acetylation | PEDDITYKSSNNSNS CCCCCEEECCCCCCC | 38.46 | 24489116 | |
| 104 | Phosphorylation | EDDITYKSSNNSNSF CCCCEEECCCCCCCC | 28.08 | 22369663 | |
| 105 | Phosphorylation | DDITYKSSNNSNSFT CCCEEECCCCCCCCC | 35.56 | 22369663 | |
| 108 | Phosphorylation | TYKSSNNSNSFTSTK EEECCCCCCCCCCCC | 37.79 | 22369663 | |
| 110 | Phosphorylation | KSSNNSNSFTSTKHN ECCCCCCCCCCCCCC | 29.71 | 22369663 | |
| 112 | Phosphorylation | SNNSNSFTSTKHNSS CCCCCCCCCCCCCCC | 34.99 | 22369663 | |
| 113 | Phosphorylation | NNSNSFTSTKHNSSN CCCCCCCCCCCCCCC | 33.19 | 22369663 | |
| 114 | Phosphorylation | NSNSFTSTKHNSSNN CCCCCCCCCCCCCCC | 33.01 | 22369663 | |
| 115 | Ubiquitination | SNSFTSTKHNSSNNY CCCCCCCCCCCCCCC | 40.32 | 23749301 | |
| 118 | Phosphorylation | FTSTKHNSSNNYTQA CCCCCCCCCCCCCCC | 33.88 | 28889911 | |
| 119 | Phosphorylation | TSTKHNSSNNYTQAR CCCCCCCCCCCCCCC | 34.12 | 28889911 | |
| 133 | Phosphorylation | RNKKKVQTPRAHTTG CCCCCCCCCCCCCCC | 20.10 | 27717283 | |
| 141 | Acetylation | PRAHTTGKHVNLDKG CCCCCCCCCCCCCCC | 42.14 | 23572591 | |
| 147 | Ubiquitination | GKHVNLDKGKHVPSK CCCCCCCCCCCCCCC | 73.38 | 23749301 | |
| 147 | Acetylation | GKHVNLDKGKHVPSK CCCCCCCCCCCCCCC | 73.38 | 24489116 | |
| 149 | Ubiquitination | HVNLDKGKHVPSKPV CCCCCCCCCCCCCCC | 47.36 | 22817900 | |
| 178 | Phosphorylation | KHDVPQDSNDNNNEE CCCCCCCCCCCCHHH | 40.61 | 19795423 | |
| 196 | Ubiquitination | QGQQAQEKNQEKEQE HHHHHHHHHHHHHHH | 52.42 | 22106047 | |
| 224 | Phosphorylation | HKQIEQPSLSSKKTT HHHCCCCCCCCCCCC | 40.35 | 19823750 | |
| 226 | Phosphorylation | QIEQPSLSSKKTTSR HCCCCCCCCCCCCCC | 44.44 | 24909858 | |
| 227 | Phosphorylation | IEQPSLSSKKTTSRT CCCCCCCCCCCCCCC | 43.39 | 19823750 | |
| 234 | Phosphorylation | SKKTTSRTSASQPKK CCCCCCCCCCCCCCC | 28.54 | 24909858 | |
| 235 | Phosphorylation | KKTTSRTSASQPKKM CCCCCCCCCCCCCCC | 25.47 | 24909858 | |
| 243 | Phosphorylation | ASQPKKMSWAAIATP CCCCCCCCEEEECCC | 23.57 | 21440633 | |
| 249 | Phosphorylation | MSWAAIATPKPKAVK CCEEEECCCCCCCCC | 26.23 | 21440633 | |
| 258 | Phosphorylation | KPKAVKKTESPLENV CCCCCCCCCCCCHHH | 35.66 | 22369663 | |
| 260 | Phosphorylation | KAVKKTESPLENVAE CCCCCCCCCCHHHHH | 39.76 | 22369663 | |
| 269 | Acetylation | LENVAELKKEISDIK CHHHHHHHHHHHHHC | 39.61 | 24489116 | |
| 273 | Phosphorylation | AELKKEISDIKKDDQ HHHHHHHHHHCHHHH | 34.08 | 19823750 | |
| 282 | Phosphorylation | IKKDDQKSEASEEKV HCHHHHCCHHHHHHH | 32.53 | 23749301 | |
| 285 | Phosphorylation | DDQKSEASEEKVNEQ HHHCCHHHHHHHHHH | 42.09 | 23749301 | |
| 294 | Phosphorylation | EKVNEQETSAQEQEE HHHHHHHHHHHHHHH | 29.11 | 19823750 | |
| 295 | Phosphorylation | KVNEQETSAQEQEEE HHHHHHHHHHHHHHH | 27.48 | 21440633 | |
| 303 | Phosphorylation | AQEQEEETAEPSEEN HHHHHHHHCCCCCCC | 39.33 | 19823750 | |
| 307 | Phosphorylation | EEETAEPSEENEDRV HHHHCCCCCCCCCCC | 49.39 | 19823750 | |
| 338 | Phosphorylation | QVKEEEQTAEELEQE HHHHHHHHHHHHHHH | 39.04 | 22369663 | |
| 357 | Phosphorylation | AAPEEEVTVVEEKVE CCCHHHEEEEEEEEE | 23.32 | 22369663 | |
| 494 | Phosphorylation | QQPQSQQSPQSQKQG CCCCHHCCCCHHHHC | 19.78 | 28889911 | |
| 497 | Phosphorylation | QSQQSPQSQKQGNNV CHHCCCCHHHHCCCH | 42.61 | 28889911 | |
| 633 | Phosphorylation | YQLPKNNYNYYQTQN CCCCCCCCCCEECCC | 17.59 | 22890988 | |
| 635 | Phosphorylation | LPKNNYNYYQTQNGQ CCCCCCCCEECCCCC | 6.13 | 22890988 | |
| 636 | Phosphorylation | PKNNYNYYQTQNGQE CCCCCCCEECCCCCC | 11.05 | 22890988 | |
| 638 | Phosphorylation | NNYNYYQTQNGQEQQ CCCCCEECCCCCCCC | 14.10 | 22890988 | |
| 646 | Phosphorylation | QNGQEQQSPNQGVAQ CCCCCCCCCCCCCCC | 26.05 | 22369663 | |
| 655 | Phosphorylation | NQGVAQHSEDSQQKQ CCCCCCCCHHHHHHH | 30.90 | 22890988 | |
| 658 | Phosphorylation | VAQHSEDSQQKQSQQ CCCCCHHHHHHHHHH | 30.38 | 22890988 |
| 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 DEF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DEF1_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 DEF1_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-108; SER-110; SER-118;SER-260; THR-338; SER-494; SER-497 AND SER-646, 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-260; SER-273 ANDSER-646, AND MASS SPECTROMETRY. | |
| "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 SER-260 AND SER-273, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-646, ANDMASS SPECTROMETRY. | |
