| UniProt ID | LEO1_YEAST | |
|---|---|---|
| UniProt AC | P38439 | |
| Protein Name | RNA polymerase-associated protein LEO1 | |
| Gene Name | LEO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 464 | |
| Subcellular Localization | Nucleus, nucleoplasm . | |
| Protein Description | The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2.. | |
| Protein Sequence | MSSESPQDQPQKEQISNNVGVTTNSTSNEETSRSQDDNVKEVNGNDDTKEEEQEEDAELDDLFGDDNDDDDDDDVKKSETEKSDSDSDEDDEGENINHRSRHRESLGLDDDEAEEQAMYTRKFYGEDANNFSDQDETTHTFKEENVELVRHIIPSKANVNETASHNEIFYARIPNFLTIDPIPFDPPSFEAKVNERASNSASREDQLDDRLIDENTVRWRYSRDKDQHVFKESNTQIVQWSDGTYSLKVGEECTDILVNDTSNTFLTVSHDQQELIQCYEGGEIKKTLMFIPTSTNSKIHQKLSKAVIRRNQRQSKGPGTYIVSMDPEVEKKELERKQSQILRDRRRRQLKEKEKQESPDAAFETGFRKQNSPTTYGASRRNEYEEDDFLVDDDEEEEAAFDDEEDDNEEEEEEEDADEENASRLRNLKREGAAMYREEEEEEKDRSETKRRRVAVIEDDEDED | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSSESPQDQ ------CCCCCCCCC | 42.69 | 22369663 | |
| 3 | Phosphorylation | -----MSSESPQDQP -----CCCCCCCCCC | 40.57 | 22369663 | |
| 5 | Phosphorylation | ---MSSESPQDQPQK ---CCCCCCCCCCCH | 29.79 | 22369663 | |
| 16 | Phosphorylation | QPQKEQISNNVGVTT CCCHHHHHCCCCCCC | 23.26 | 22369663 | |
| 22 | Phosphorylation | ISNNVGVTTNSTSNE HHCCCCCCCCCCCCC | 17.84 | 22369663 | |
| 23 | Phosphorylation | SNNVGVTTNSTSNEE HCCCCCCCCCCCCCC | 25.43 | 22369663 | |
| 25 | Phosphorylation | NVGVTTNSTSNEETS CCCCCCCCCCCCCCC | 30.99 | 22369663 | |
| 26 | Phosphorylation | VGVTTNSTSNEETSR CCCCCCCCCCCCCCC | 37.33 | 22369663 | |
| 27 | Phosphorylation | GVTTNSTSNEETSRS CCCCCCCCCCCCCCC | 41.90 | 22369663 | |
| 31 | Phosphorylation | NSTSNEETSRSQDDN CCCCCCCCCCCCCCC | 24.22 | 20377248 | |
| 32 | Phosphorylation | STSNEETSRSQDDNV CCCCCCCCCCCCCCC | 32.96 | 20377248 | |
| 34 | Phosphorylation | SNEETSRSQDDNVKE CCCCCCCCCCCCCEE | 37.42 | 20377248 | |
| 48 | Phosphorylation | EVNGNDDTKEEEQEE ECCCCCCCHHHHHHH | 43.13 | 28889911 | |
| 78 | Phosphorylation | DDDDVKKSETEKSDS CCCHHHHHHHHCCCC | 43.99 | 28889911 | |
| 83 | Phosphorylation | KKSETEKSDSDSDED HHHHHHCCCCCCCCC | 35.79 | 19795423 | |
| 85 | Phosphorylation | SETEKSDSDSDEDDE HHHHCCCCCCCCCCC | 46.21 | 19795423 | |
| 87 | Phosphorylation | TEKSDSDSDEDDEGE HHCCCCCCCCCCCCC | 47.02 | 19795423 | |
| 105 | Phosphorylation | HRSRHRESLGLDDDE HHHHHHHHHCCCCHH | 27.91 | 22369663 | |
| 119 | Phosphorylation | EAEEQAMYTRKFYGE HHHHHHHHHHHHHCC | 13.35 | 22369663 | |
| 120 | Phosphorylation | AEEQAMYTRKFYGED HHHHHHHHHHHHCCC | 17.82 | 22369663 | |
| 124 | Phosphorylation | AMYTRKFYGEDANNF HHHHHHHHCCCCCCC | 23.73 | 22890988 | |
| 132 | Phosphorylation | GEDANNFSDQDETTH CCCCCCCCCCCCCCC | 36.16 | 22369663 | |
| 137 | Phosphorylation | NFSDQDETTHTFKEE CCCCCCCCCCCCHHH | 31.97 | 22890988 | |
| 138 | Phosphorylation | FSDQDETTHTFKEEN CCCCCCCCCCCHHHH | 19.51 | 22890988 | |
| 140 | Phosphorylation | DQDETTHTFKEENVE CCCCCCCCCHHHHHH | 34.02 | 22890988 | |
| 188 | Phosphorylation | PIPFDPPSFEAKVNE CCCCCCCCHHHHHHH | 40.90 | 28889911 | |
| 200 | Phosphorylation | VNERASNSASREDQL HHHHHCCCCCCHHHH | 25.73 | 23749301 | |
| 287 | Phosphorylation | EGGEIKKTLMFIPTS ECCCEEEEEEECCCC | 20.60 | 19823750 | |
| 293 | Phosphorylation | KTLMFIPTSTNSKIH EEEEECCCCCCHHHH | 43.28 | 19823750 | |
| 294 | Phosphorylation | TLMFIPTSTNSKIHQ EEEECCCCCCHHHHH | 21.90 | 19823750 | |
| 295 | Phosphorylation | LMFIPTSTNSKIHQK EEECCCCCCHHHHHH | 46.09 | 19823750 | |
| 297 | Phosphorylation | FIPTSTNSKIHQKLS ECCCCCCHHHHHHHH | 32.83 | 19823750 | |
| 298 | Acetylation | IPTSTNSKIHQKLSK CCCCCCHHHHHHHHH | 46.40 | 24489116 | |
| 302 | Acetylation | TNSKIHQKLSKAVIR CCHHHHHHHHHHHHH | 40.33 | 25381059 | |
| 331 | Acetylation | SMDPEVEKKELERKQ ECCHHHHHHHHHHHH | 57.64 | 24489116 | |
| 339 | Phosphorylation | KELERKQSQILRDRR HHHHHHHHHHHHHHH | 23.40 | 20190278 | |
| 358 | Phosphorylation | KEKEKQESPDAAFET HHHHHHHCCCHHHHH | 26.11 | 22369663 | |
| 365 | Phosphorylation | SPDAAFETGFRKQNS CCCHHHHHCCCCCCC | 34.86 | 22369663 | |
| 372 | Phosphorylation | TGFRKQNSPTTYGAS HCCCCCCCCCCCCCC | 22.56 | 22369663 | |
| 374 | Phosphorylation | FRKQNSPTTYGASRR CCCCCCCCCCCCCCC | 32.25 | 22369663 | |
| 375 | Phosphorylation | RKQNSPTTYGASRRN CCCCCCCCCCCCCCC | 24.28 | 22890988 | |
| 376 | Phosphorylation | KQNSPTTYGASRRNE CCCCCCCCCCCCCCC | 17.11 | 22890988 | |
| 379 | Phosphorylation | SPTTYGASRRNEYEE CCCCCCCCCCCCCCC | 27.66 | 22890988 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 34 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LEO1_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 LEO1_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-105; SER-132; SER-188;SER-358; SER-372; THR-374 AND THR-375, 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-34; SER-339; SER-358;SER-372 AND THR-374, AND MASS 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-105; SER-132 ANDSER-358, AND MASS SPECTROMETRY. | |
