| UniProt ID | MFT1_YEAST | |
|---|---|---|
| UniProt AC | P33441 | |
| Protein Name | THO complex subunit MFT1 | |
| Gene Name | MFT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 392 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.. | |
| Protein Sequence | MPLSQKQIDQVRTKVHYSEVDTPFNKYLDILGKVTKLTGSIINGTLSNDDSKIEKLTEQNISQLKESAHLRFLDLQSSIDTKKVADENWETCQQETLAKLENLKDKLPDIKSIHSKLLLRIGKLQGLYDSVQVINREVEGLSEGRTSLVVTRAEWEKELGTDLVKFLIEKNYLKLVDPGLKKDSSEERYRIYDDFSKGPKELESINASMKSDIENVRQEVSSYKEKWLRDAEIFGKITSIFKEELLKRDGLLNEAEGDNIDEDYESDEDEERKERFKRQRSMVEVNTIENVDEKEESDHEYDDQEDEENEEEDDMEVDVEDIKEDNEVDGESSQQEDNSRQGNNEETDKETGVIEEPDAVNDAEEADSDHSSRKLGGTTSDFSASSSVEEVK | |
| 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 |
|---|---|---|---|---|---|
| 38 | Phosphorylation | LGKVTKLTGSIINGT HHHHHHHCCCHHCCC | 30.36 | 27017623 | |
| 45 | Phosphorylation | TGSIINGTLSNDDSK CCCHHCCCCCCCHHH | 23.64 | 30377154 | |
| 47 | Phosphorylation | SIINGTLSNDDSKIE CHHCCCCCCCHHHHH | 37.74 | 28889911 | |
| 65 | Ubiquitination | EQNISQLKESAHLRF HHCHHHHHHHHHHHH | 41.82 | 24961812 | |
| 104 | Acetylation | LAKLENLKDKLPDIK HHHHHCHHHHCCCHH | 65.48 | 24489116 | |
| 115 | Phosphorylation | PDIKSIHSKLLLRIG CCHHHHHHHHHHHHH | 24.27 | 28889911 | |
| 123 | Acetylation | KLLLRIGKLQGLYDS HHHHHHHCHHCHHHH | 34.95 | 24489116 | |
| 184 | Phosphorylation | DPGLKKDSSEERYRI CCCCCCCCCHHHHHH | 48.83 | 21551504 | |
| 185 | Phosphorylation | PGLKKDSSEERYRIY CCCCCCCCHHHHHHH | 54.32 | 21551504 | |
| 192 | Phosphorylation | SEERYRIYDDFSKGP CHHHHHHHCCCCCCH | 10.64 | 21551504 | |
| 264 | Phosphorylation | GDNIDEDYESDEDEE CCCCCCCCCCCCHHH | 18.45 | 25521595 | |
| 266 | Phosphorylation | NIDEDYESDEDEERK CCCCCCCCCCHHHHH | 39.82 | 22369663 | |
| 281 | Phosphorylation | ERFKRQRSMVEVNTI HHHHHHHHCEEEHHC | 20.88 | 24909858 | |
| 332 | Phosphorylation | DNEVDGESSQQEDNS HCCCCCCCCCCCCCC | 38.69 | 28132839 | |
| 333 | Phosphorylation | NEVDGESSQQEDNSR CCCCCCCCCCCCCCC | 31.42 | 28889911 | |
| 339 | Phosphorylation | SSQQEDNSRQGNNEE CCCCCCCCCCCCCHH | 38.00 | 28889911 | |
| 347 | Phosphorylation | RQGNNEETDKETGVI CCCCCHHHHHHCCCC | 46.31 | 28889911 | |
| 351 | Phosphorylation | NEETDKETGVIEEPD CHHHHHHCCCCCCCC | 42.35 | 19779198 | |
| 368 | Phosphorylation | NDAEEADSDHSSRKL CCHHHCCCCCCCCCC | 44.25 | 19823750 | |
| 371 | Phosphorylation | EEADSDHSSRKLGGT HHCCCCCCCCCCCCC | 36.51 | 29136822 | |
| 372 | Phosphorylation | EADSDHSSRKLGGTT HCCCCCCCCCCCCCC | 29.98 | 29136822 | |
| 378 | Phosphorylation | SSRKLGGTTSDFSAS CCCCCCCCCCCCCCC | 22.71 | 19795423 | |
| 379 | Phosphorylation | SRKLGGTTSDFSASS CCCCCCCCCCCCCCC | 29.58 | 19795423 | |
| 380 | Phosphorylation | RKLGGTTSDFSASSS CCCCCCCCCCCCCCC | 36.17 | 19795423 | |
| 383 | Phosphorylation | GGTTSDFSASSSVEE CCCCCCCCCCCCCCC | 32.03 | 19795423 | |
| 385 | Phosphorylation | TTSDFSASSSVEEVK CCCCCCCCCCCCCCC | 23.19 | 19795423 | |
| 386 | Phosphorylation | TSDFSASSSVEEVK- CCCCCCCCCCCCCC- | 37.81 | 19795423 | |
| 387 | Phosphorylation | SDFSASSSVEEVK-- CCCCCCCCCCCCC-- | 30.93 | 19795423 |
| 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 MFT1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MFT1_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 MFT1_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-47; SER-115 AND SER-266,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-266 AND SER-368, 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-266, AND MASSSPECTROMETRY. | |
