| UniProt ID | RTF1_YEAST | |
|---|---|---|
| UniProt AC | P53064 | |
| Protein Name | RNA polymerase-associated protein RTF1 | |
| Gene Name | RTF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 558 | |
| 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. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of SPT15, the TATA box-binding protein, and the relative activities of different TATA elements.. | |
| Protein Sequence | MSDLDEDLLALAGADESEEEDQVLTTTSAKRAKNNDQSLSKKRRIEVGSVEDDDEEDDYNPYSVGNADYGSEEEEEANPFPLEGKYKDESDREHLESLPEMERETLLFERSQIMQKYQERKLFRARGRDMKEQQQRAKNDEDSRKTRASTRSTHATGHSDIKASKLSQLKKQRARKNRHYSDNEDEDDEEDYREEDYKDDEGSEYGDDEEYNPFDRRDTYDKREEVEWAEEEDEQDREPEISDFNKLRIGRSFVAKFCFYPGFEDAVKGCYGRVNVGTDKRTGKTSYRMVRIERVFLQKPYNMGKFYTNQYFGVTQGKDRKVFQMNYFSDGLFAEDEYQRYLRALDNSQMIKPSLHSLSNKTKEVMDFVNTPLTDKTTDEVVRHRMQFNKKLSGTNAVLEKTVLREKLQYAKETNNEKDIAKYSAQLRNFEKRMSVYEKHHENDQSDIKKLGELTSKNRKLNMSNIRNAEHVKKEDSNNFDSKSDPFSRLKTRTKVYYQEIQKEENAKAKEIAQQEKLQEDKDAKDKREKELLVAQFRRLGGLERMVGELDIKFDLKF | |
| 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 | ------MSDLDEDLL ------CCCHHHHHH | 47.05 | 22369663 | |
| 17 | Phosphorylation | ALAGADESEEEDQVL HHCCCCCCHHHHCCC | 51.35 | 22369663 | |
| 25 | Phosphorylation | EEEDQVLTTTSAKRA HHHHCCCHHHHHHHH | 29.22 | 22369663 | |
| 26 | Phosphorylation | EEDQVLTTTSAKRAK HHHCCCHHHHHHHHH | 18.00 | 22369663 | |
| 27 | Phosphorylation | EDQVLTTTSAKRAKN HHCCCHHHHHHHHHC | 22.81 | 22369663 | |
| 28 | Phosphorylation | DQVLTTTSAKRAKNN HCCCHHHHHHHHHCC | 29.69 | 22369663 | |
| 41 | Acetylation | NNDQSLSKKRRIEVG CCCCCCHHCCCEECC | 56.44 | 25381059 | |
| 49 | Phosphorylation | KRRIEVGSVEDDDEE CCCEECCCCCCCCCC | 27.75 | 21440633 | |
| 59 | Phosphorylation | DDDEEDDYNPYSVGN CCCCCCCCCCCCCCC | 30.29 | 19823750 | |
| 62 | Phosphorylation | EEDDYNPYSVGNADY CCCCCCCCCCCCCCC | 16.61 | 19823750 | |
| 63 | Phosphorylation | EDDYNPYSVGNADYG CCCCCCCCCCCCCCC | 25.46 | 21440633 | |
| 69 | Phosphorylation | YSVGNADYGSEEEEE CCCCCCCCCCCCHHC | 21.82 | 19823750 | |
| 71 | Phosphorylation | VGNADYGSEEEEEAN CCCCCCCCCCHHCCC | 35.29 | 19823750 | |
| 86 | Phosphorylation | PFPLEGKYKDESDRE CCCCCCCCCCHHHHH | 34.23 | 29136822 | |
| 87 | Ubiquitination | FPLEGKYKDESDREH CCCCCCCCCHHHHHH | 59.51 | 24961812 | |
| 90 | Phosphorylation | EGKYKDESDREHLES CCCCCCHHHHHHHHH | 52.69 | 29136822 | |
| 97 | Phosphorylation | SDREHLESLPEMERE HHHHHHHHCHHHHHH | 56.43 | 23607784 | |
| 116 | Ubiquitination | ERSQIMQKYQERKLF HHHHHHHHHHHHHHH | 31.36 | 24961812 | |
| 116 | Acetylation | ERSQIMQKYQERKLF HHHHHHHHHHHHHHH | 31.36 | 22865919 | |
| 153 | Phosphorylation | TRASTRSTHATGHSD HHHHHHHHHHCCCHH | 16.55 | 27017623 | |
| 159 | Phosphorylation | STHATGHSDIKASKL HHHHCCCHHHCHHHH | 42.23 | 27017623 | |
| 162 | Acetylation | ATGHSDIKASKLSQL HCCCHHHCHHHHHHH | 52.15 | 25381059 | |
| 165 | Acetylation | HSDIKASKLSQLKKQ CHHHCHHHHHHHHHH | 57.95 | 24489116 | |
| 167 | Phosphorylation | DIKASKLSQLKKQRA HHCHHHHHHHHHHHH | 36.88 | 30377154 | |
| 180 | Phosphorylation | RARKNRHYSDNEDED HHHHCCCCCCCCCCC | 17.93 | 29734811 | |
| 181 | Phosphorylation | ARKNRHYSDNEDEDD HHHCCCCCCCCCCCC | 28.03 | 17287358 | |
| 203 | Phosphorylation | DYKDDEGSEYGDDEE HCCCCCCCCCCCCCC | 26.12 | 22369663 | |
| 205 | Phosphorylation | KDDEGSEYGDDEEYN CCCCCCCCCCCCCCC | 27.79 | 22369663 | |
| 252 | Phosphorylation | NKLRIGRSFVAKFCF HHHHCCHHHHHHHCC | 20.89 | 21440633 | |
| 280 | Acetylation | RVNVGTDKRTGKTSY EECCCCCCCCCCCEE | 52.26 | 24489116 | |
| 299 | Acetylation | IERVFLQKPYNMGKF EEEEEECCCCCCCCC | 52.17 | 24489116 | |
| 318 | Ubiquitination | YFGVTQGKDRKVFQM CCCEECCCCCCEEEE | 44.54 | 24961812 | |
| 393 | Phosphorylation | MQFNKKLSGTNAVLE HHHCHHHCCCCHHHH | 53.07 | 22369663 | |
| 395 | Phosphorylation | FNKKLSGTNAVLEKT HCHHHCCCCHHHHHH | 19.34 | 22369663 | |
| 401 | Acetylation | GTNAVLEKTVLREKL CCCHHHHHHHHHHHH | 39.51 | 24489116 | |
| 412 | Acetylation | REKLQYAKETNNEKD HHHHHHHHHHCCHHH | 61.20 | 22865919 | |
| 422 | Acetylation | NNEKDIAKYSAQLRN CCHHHHHHHHHHHHH | 39.82 | 24489116 | |
| 435 | Phosphorylation | RNFEKRMSVYEKHHE HHHHHHHHHHHHHCC | 26.11 | 24930733 | |
| 456 | Phosphorylation | KKLGELTSKNRKLNM HHHHHHHHHCCCCCH | 40.32 | 30377154 | |
| 464 | Phosphorylation | KNRKLNMSNIRNAEH HCCCCCHHHCCCHHH | 28.21 | 28889911 | |
| 477 | Phosphorylation | EHVKKEDSNNFDSKS HHHCHHHCCCCCCCC | 34.46 | 28889911 | |
| 483 | Acetylation | DSNNFDSKSDPFSRL HCCCCCCCCCHHHHH | 61.80 | 24489116 | |
| 484 | Phosphorylation | SNNFDSKSDPFSRLK CCCCCCCCCHHHHHH | 55.24 | 21440633 | |
| 488 | Phosphorylation | DSKSDPFSRLKTRTK CCCCCHHHHHHHHHH | 41.93 | 30377154 | |
| 503 | Acetylation | VYYQEIQKEENAKAK HHHHHHHHHHHHHHH | 73.06 | 24489116 |
| 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 RTF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RTF1_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 RTF1_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-17; TYR-69; SER-71 ANDSER-477, AND MASS SPECTROMETRY. | |
