| UniProt ID | RPB1_YEAST | |
|---|---|---|
| UniProt AC | P04050 | |
| Protein Name | DNA-directed RNA polymerase II subunit RPB1 | |
| Gene Name | RPO21 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1733 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. During a transcription cycle, Pol II, general transcription factors and the Mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Pol II is composed of mobile elements that move relative to each other. The core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center. The clamp element (portions of RPB1, RPB2 and RPB3) is connected to the core through a set of flexible switches and moves to open and close the cleft. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. In elongating Pol II, the lid loop (RPB1) appears to act as a wedge to drive apart the DNA and RNA strands at the upstream end of the transcription bubble and guide the RNA strand toward the RNA exit groove located near the base of the largely unstructured CTD domain of RPB1. The rudder loop (RPB1) interacts with single-stranded DNA after separation from the RNA strand, likely preventing reassociation with the exiting RNA. The cleft is surrounded by jaws: an upper jaw formed by portions of RBP1, RPB2 and RPB9, and a lower jaw, formed by RPB5 and portions of RBP1. The jaws are thought to grab the incoming DNA template, mainly by RPB5 direct contacts to DNA.. | |
| Protein Sequence | MVGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMDETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFGHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELMRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLVSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVLSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLNTFHFAGVASKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLLDEEAEQSFDQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRCRVVRPKSLDAETEAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTGAFDVMIDEESLVKYMPEQKITEIEDGQDGGVTPYSNESGLVNADLDVKDELMFSPLVDSGSNDAMAGGFTAYGGADYGEATSPFGAYGEAPTSPGFGVSSPGFSPTSPTYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPNYSPTSPSYSPTSPGYSPGSPAYSPKQDEQKHNENENSR | |
| 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 |
|---|---|---|---|---|---|
| 13 | Phosphorylation | YSSAPLRTVKEVQFG CCCCCCCCCEEEECC | 43.54 | 30377154 | |
| 15 | Ubiquitination | SAPLRTVKEVQFGLF CCCCCCCEEEECCCC | 52.10 | 17644757 | |
| 23 | Phosphorylation | EVQFGLFSPEEVRAI EEECCCCCHHHHHEE | 36.12 | 30377154 | |
| 129 | Ubiquitination | MRQALAIKDSKKRFA HHHHHHHHCHHHHHH | 50.79 | 17644757 | |
| 132 | Ubiquitination | ALAIKDSKKRFAAIW HHHHHCHHHHHHHHH | 59.09 | 17644757 | |
| 133 | Ubiquitination | LAIKDSKKRFAAIWT HHHHCHHHHHHHHHH | 57.61 | 17644757 | |
| 143 | Ubiquitination | AAIWTLCKTKMVCET HHHHHHHCCCEEECC | 55.05 | 23749301 | |
| 145 | Ubiquitination | IWTLCKTKMVCETDV HHHHHCCCEEECCCC | 18.16 | 23749301 | |
| 186 | Ubiquitination | LKLVGSWKKDRATGD EEEEEEECCCCCCCC | 46.63 | 23749301 | |
| 187 | Ubiquitination | KLVGSWKKDRATGDA EEEEEECCCCCCCCC | 46.30 | 22817900 | |
| 191 | Phosphorylation | SWKKDRATGDADEPE EECCCCCCCCCCCCC | 36.17 | 23749301 | |
| 212 | Ubiquitination | EEILNIFKHISVKDF HHHHHHHHHCCHHHC | 35.91 | 15699485 | |
| 343 | Ubiquitination | IRGNLMGKRVDFSAR CCCCCCCCCCCCCCC | 34.97 | 17644757 | |
| 368 | Acetylation | LDQVGVPKSIAKTLT CHHCCCCHHHHHHCC | 52.68 | 24489116 | |
| 368 | Ubiquitination | LDQVGVPKSIAKTLT CHHCCCCHHHHHHCC | 52.68 | 23749301 | |
| 372 | Ubiquitination | GVPKSIAKTLTYPEV CCCHHHHHHCCCCCC | 42.26 | 23749301 | |
| 373 | Phosphorylation | VPKSIAKTLTYPEVV CCHHHHHHCCCCCCC | 18.47 | 30377154 | |
| 403 | Acetylation | PNEHPGAKYVIRDSG CCCCCCCCEEECCCC | 46.06 | 25381059 | |
| 449 | Phosphorylation | VLFNRQPSLHKMSMM CCCCCCCHHHHHHHH | 34.46 | 21440633 | |
| 595 | Phosphorylation | LQRFDEGTTLLSPKD EEEECCCCEEECCCC | 16.54 | 28889911 | |
| 596 | Phosphorylation | QRFDEGTTLLSPKDN EEECCCCEEECCCCC | 36.24 | 28889911 | |
| 599 | Phosphorylation | DEGTTLLSPKDNGML CCCCEEECCCCCCEE | 32.77 | 28889911 | |
| 620 | Ubiquitination | IFGVVEKKTVGSSNG EEEEEEEEEECCCCC | 34.63 | 17644757 | |
| 621 | Phosphorylation | FGVVEKKTVGSSNGG EEEEEEEEECCCCCC | 40.96 | 22369663 | |
| 624 | Phosphorylation | VEKKTVGSSNGGLIH EEEEEECCCCCCEEE | 19.12 | 22369663 | |
| 625 | Phosphorylation | EKKTVGSSNGGLIHV EEEEECCCCCCEEEE | 33.30 | 22369663 | |
| 634 | Phosphorylation | GGLIHVVTREKGPQV CCEEEEEECCCCHHH | 31.83 | 22369663 | |
| 687 | Ubiquitination | TETIAEAKKKVLDVT HHHHHHHHHHHHHHC | 44.63 | 23749301 | |
| 688 | Ubiquitination | ETIAEAKKKVLDVTK HHHHHHHHHHHHHCH | 55.98 | 15699485 | |
| 689 | Ubiquitination | TIAEAKKKVLDVTKE HHHHHHHHHHHHCHH | 47.53 | 23749301 | |
| 695 | Acetylation | KKVLDVTKEAQANLL HHHHHHCHHHHHHHH | 51.40 | 24489116 | |
| 695 | Ubiquitination | KKVLDVTKEAQANLL HHHHHHCHHHHHHHH | 51.40 | 23749301 | |
| 705 | Ubiquitination | QANLLTAKHGMTLRE HHHHHHHHCCCCHHH | 35.14 | 23749301 | |
| 738 | Acetylation | RLAEVNLKDLNNVKQ CEEECCHHHHCCHHH | 55.77 | 24489116 | |
| 738 | Succinylation | RLAEVNLKDLNNVKQ CEEECCHHHHCCHHH | 55.77 | 23954790 | |
| 738 | Ubiquitination | RLAEVNLKDLNNVKQ CEEECCHHHHCCHHH | 55.77 | 23749301 | |
| 744 | Ubiquitination | LKDLNNVKQMVMAGS HHHHCCHHHHHHCCC | 34.50 | 23749301 | |
| 754 | Phosphorylation | VMAGSKGSFINIAQM HHCCCCCCCEEHHHH | 27.04 | 30377154 | |
| 789 | Acetylation | RTLPHFSKDDYSPES CCCCCCCCCCCCCCC | 54.39 | 24489116 | |
| 789 | Ubiquitination | RTLPHFSKDDYSPES CCCCCCCCCCCCCCC | 54.39 | 23749301 | |
| 793 | Phosphorylation | HFSKDDYSPESKGFV CCCCCCCCCCCCCCC | 29.23 | 28889911 | |
| 797 | Ubiquitination | DDYSPESKGFVENSY CCCCCCCCCCCCCCH | 55.49 | 23749301 | |
| 830 | Ubiquitination | GLIDTAVKTAETGYI CHHHHHHHHCHHHHH | 39.28 | 23749301 | |
| 831 | Phosphorylation | LIDTAVKTAETGYIQ HHHHHHHHCHHHHHH | 24.11 | 22369663 | |
| 834 | Phosphorylation | TAVKTAETGYIQRRL HHHHHCHHHHHHHHH | 32.59 | 22369663 | |
| 836 | Phosphorylation | VKTAETGYIQRRLVK HHHCHHHHHHHHHHH | 10.99 | 22369663 | |
| 843 | Ubiquitination | YIQRRLVKALEDIMV HHHHHHHHHHHHHHH | 52.42 | 23749301 | |
| 859 | Phosphorylation | YDNTTRNSLGNVIQF CCCCCCCCHHCHHHH | 34.07 | 30377154 | |
| 895 | Acetylation | GSDAAFEKRYRVDLL CCHHHHHHHHCEECC | 48.56 | 24489116 | |
| 895 | Ubiquitination | GSDAAFEKRYRVDLL CCHHHHHHHHCEECC | 48.56 | 23749301 | |
| 924 | Ubiquitination | SEILGDLKLQVLLDE HHHHHHHHHHHHCCH | 41.43 | 17644757 | |
| 933 | Phosphorylation | QVLLDEEYKQLVKDR HHHCCHHHHHHHHCC | 11.29 | 28889911 | |
| 934 | Acetylation | VLLDEEYKQLVKDRK HHCCHHHHHHHHCCH | 40.20 | 24489116 | |
| 977 | Ubiquitination | TFHIDHTKPSDLTIK HCCCCCCCCCCCCHH | 38.82 | 17644757 | |
| 984 | Acetylation | KPSDLTIKDIVLGVK CCCCCCHHHHEECCH | 35.85 | 24489116 | |
| 984 | Ubiquitination | KPSDLTIKDIVLGVK CCCCCCHHHHEECCH | 35.85 | 17644757 | |
| 991 | Ubiquitination | KDIVLGVKDLQENLL HHHEECCHHHHHCEE | 51.42 | 17644757 | |
| 1003 | 2-Hydroxyisobutyrylation | NLLVLRGKNEIIQNA CEEEECCHHHHHHHH | 45.00 | - | |
| 1003 | Ubiquitination | NLLVLRGKNEIIQNA CEEEECCHHHHHHHH | 45.00 | 23749301 | |
| 1039 | Ubiquitination | LQEYRLTKQAFDWVL HHHHHHHHHHHHHHH | 44.19 | 23749301 | |
| 1093 | Ubiquitination | FAGVASKKVTSGVPR HCCCCCCCCCCCCCC | 48.53 | 23749301 | |
| 1095 | Phosphorylation | GVASKKVTSGVPRLK CCCCCCCCCCCCCHH | 28.74 | 27214570 | |
| 1096 | Phosphorylation | VASKKVTSGVPRLKE CCCCCCCCCCCCHHH | 40.56 | 27214570 | |
| 1102 | Acetylation | TSGVPRLKEILNVAK CCCCCCHHHHHHHHH | 43.94 | 24489116 | |
| 1102 | Ubiquitination | TSGVPRLKEILNVAK CCCCCCHHHHHHHHH | 43.94 | 23749301 | |
| 1112 | Ubiquitination | LNVAKNMKTPSLTVY HHHHHHCCCCCEEEE | 67.68 | 17644757 | |
| 1132 | Acetylation | AADQEQAKLIRSAIE CCCHHHHHHHHHHHH | 44.11 | 24489116 | |
| 1132 | Ubiquitination | AADQEQAKLIRSAIE CCCHHHHHHHHHHHH | 44.11 | 24961812 | |
| 1205 | Acetylation | DRAAMNDKDLTMGQV HHHHHCCCCCCHHHH | 50.02 | 24489116 | |
| 1205 | Ubiquitination | DRAAMNDKDLTMGQV HHHHHCCCCCCHHHH | 50.02 | 23749301 | |
| 1246 | Acetylation | RCRVVRPKSLDAETE EEEEECCCCCCCCCH | 53.76 | 24489116 | |
| 1246 | Ubiquitination | RCRVVRPKSLDAETE EEEEECCCCCCCCCH | 53.76 | 23749301 | |
| 1261 | Acetylation | AEEDHMLKKIENTML HHHHHHHHHHHHHHH | 44.10 | 24489116 | |
| 1261 | Ubiquitination | AEEDHMLKKIENTML HHHHHHHHHHHHHHH | 44.10 | 22817900 | |
| 1262 | Ubiquitination | EEDHMLKKIENTMLE HHHHHHHHHHHHHHH | 51.82 | 24961812 | |
| 1286 | Ubiquitination | IERVVMMKYDRKVPS EEEEEEEECCCCCCC | 26.38 | 23749301 | |
| 1290 | Ubiquitination | VMMKYDRKVPSPTGE EEEECCCCCCCCCCC | 56.45 | 22817900 | |
| 1293 | Phosphorylation | KYDRKVPSPTGEYVK ECCCCCCCCCCCCCC | 37.77 | 22369663 | |
| 1295 | Phosphorylation | DRKVPSPTGEYVKEP CCCCCCCCCCCCCCC | 47.16 | 22369663 | |
| 1298 | Phosphorylation | VPSPTGEYVKEPEWV CCCCCCCCCCCCCEE | 20.40 | 22369663 | |
| 1350 | Ubiquitination | AGRAALYKEVYNVIA HHHHHHHHHHHHHHH | 41.37 | 23749301 | |
| 1394 | Phosphorylation | HGFNRSNTGALMRCS CCCCCCCCCCCEECC | 25.69 | 30377154 | |
| 1460 | Phosphorylation | YMPEQKITEIEDGQD HCCCCCEEEEECCCC | 37.64 | 22369663 | |
| 1471 | Phosphorylation | DGQDGGVTPYSNESG CCCCCCCCCCCCCCC | 21.56 | 22369663 | |
| 1473 | Phosphorylation | QDGGVTPYSNESGLV CCCCCCCCCCCCCCC | 18.11 | 22369663 | |
| 1474 | Phosphorylation | DGGVTPYSNESGLVN CCCCCCCCCCCCCCC | 35.01 | 29734811 | |
| 1477 | Phosphorylation | VTPYSNESGLVNADL CCCCCCCCCCCCCCC | 41.50 | 22369663 | |
| 1487 | Sumoylation | VNADLDVKDELMFSP CCCCCCCCCHHCCCC | 45.19 | - | |
| 1543 | Phosphorylation | GVSSPGFSPTSPTYS CCCCCCCCCCCCCCC | 32.93 | 11018013 | |
| 1546 | Phosphorylation | SPGFSPTSPTYSPTS CCCCCCCCCCCCCCC | 20.73 | 11018013 | |
| 1550 | Phosphorylation | SPTSPTYSPTSPAYS CCCCCCCCCCCCCCC | 24.95 | 11018013 | |
| 1553 | Phosphorylation | SPTYSPTSPAYSPTS CCCCCCCCCCCCCCC | 15.77 | 11018013 | |
| 1557 | Phosphorylation | SPTSPAYSPTSPSYS CCCCCCCCCCCCCCC | 24.65 | 11018013 | |
| 1560 | Phosphorylation | SPAYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1562 | Phosphorylation | AYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1564 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1567 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1569 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1571 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1574 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1576 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1578 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1581 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1583 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1585 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1588 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1590 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1592 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1595 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1597 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1599 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1602 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1604 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1606 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1609 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1611 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1613 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1616 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1618 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1620 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1623 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1625 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1627 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1630 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1632 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1634 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1637 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1639 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1641 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1644 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1646 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1648 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1651 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1653 | Phosphorylation | SYSPTSPSYSPTSPA CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1655 | Phosphorylation | SPTSPSYSPTSPAYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1658 | Phosphorylation | SPSYSPTSPAYSPTS CCCCCCCCCCCCCCC | 15.77 | 11018013 | |
| 1662 | Phosphorylation | SPTSPAYSPTSPSYS CCCCCCCCCCCCCCC | 24.65 | 11018013 | |
| 1665 | Phosphorylation | SPAYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1667 | Phosphorylation | AYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1669 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1672 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1674 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1676 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1679 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1681 | Phosphorylation | SYSPTSPSYSPTSPS CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1683 | Phosphorylation | SPTSPSYSPTSPSYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1686 | Phosphorylation | SPSYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1688 | Phosphorylation | SYSPTSPSYSPTSPN CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1690 | Phosphorylation | SPTSPSYSPTSPNYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1693 | Phosphorylation | SPSYSPTSPNYSPTS CCCCCCCCCCCCCCC | 17.96 | 11018013 | |
| 1697 | Phosphorylation | SPTSPNYSPTSPSYS CCCCCCCCCCCCCCC | 28.48 | 11018013 | |
| 1700 | Phosphorylation | SPNYSPTSPSYSPTS CCCCCCCCCCCCCCC | 18.42 | 11018013 | |
| 1702 | Phosphorylation | NYSPTSPSYSPTSPG CCCCCCCCCCCCCCC | 37.70 | 28889911 | |
| 1704 | Phosphorylation | SPTSPSYSPTSPGYS CCCCCCCCCCCCCCC | 26.49 | 11018013 | |
| 1707 | Phosphorylation | SPSYSPTSPGYSPGS CCCCCCCCCCCCCCC | 21.51 | 11018013 | |
| 1711 | Phosphorylation | SPTSPGYSPGSPAYS CCCCCCCCCCCCCCC | 28.79 | 11018013 | |
| 1714 | Phosphorylation | SPGYSPGSPAYSPKQ CCCCCCCCCCCCCCH | 15.11 | 11018013 | |
| 1718 | Phosphorylation | SPGSPAYSPKQDEQK CCCCCCCCCCHHHHH | 27.94 | 11018013 |
* 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 RPB1_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 THR-1471 AND TYR-1473, ANDMASS 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 THR-621, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-695, AND MASSSPECTROMETRY. | |
