UniProt ID | TFC5_YEAST | |
---|---|---|
UniProt AC | P46678 | |
Protein Name | Transcription factor TFIIIB component B'' | |
Gene Name | BDP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 594 | |
Subcellular Localization | Nucleus. | |
Protein Description | General activator of RNA polymerase III transcription.. | |
Protein Sequence | MSSIVNKSGTRFAPKVRQRRAATGGTPTPKPRTPQLFIPESKEIEEDNSDNDKGVDENETAIVEKPSLVGERSLEGFTLTGTNGHDNEIGDEGPIDASTQNPKADVIEDNVTLKPAPLQTHRDQKVPRSSRLASLSKDNESRPSFKPSFLDSSSNSNGTARRLSTISNKLPKKIRLGSITENDMNLKTFKRHRVLGKPSSAKKPAGAHRISIVSKISPPTAMTDSLDRNEFSSETSTSREADENENYVISKVKDIPKKVRDGESAKYFIDEENFTMAELCKPNFPIGQISENFEKSKMAKKAKLEKRRHLRELRMRARQEFKPLHSLTKEEQEEEEEKRKEERDKLLNADIPESDRKAHTAIQLKLNPDGTMAIDEETMVVDRHKNASIENEYKEKVDENPFANLYNYGSYGRGSYTDPWTVEEMIKFYKALSMWGTDFNLISQLYPYRSRKQVKAKFVNEEKKRPILIELALRSKLPPNFDEYCCEIKKNIGTVADFNEKLIELQNEHKHHMKEIEEAKNTAKEEDQTAQRLNDANLNKKGSGGIMTNDLKVYRKTEVVLGTIDDLKRKKLKERNNDDNEDNEGSEEEPEIDQ | |
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 |
---|---|---|---|---|---|
23 | Phosphorylation | VRQRRAATGGTPTPK HHHHHHHCCCCCCCC | 34.85 | 30377154 | |
26 | Phosphorylation | RRAATGGTPTPKPRT HHHHCCCCCCCCCCC | 25.90 | 29136822 | |
28 | Phosphorylation | AATGGTPTPKPRTPQ HHCCCCCCCCCCCCC | 43.72 | 29136822 | |
33 | Phosphorylation | TPTPKPRTPQLFIPE CCCCCCCCCCCCCCC | 24.74 | 29136822 | |
41 | Phosphorylation | PQLFIPESKEIEEDN CCCCCCCCCCCCCCC | 30.18 | 29136822 | |
49 | Phosphorylation | KEIEEDNSDNDKGVD CCCCCCCCCCCCCCC | 50.54 | 22369663 | |
60 | Phosphorylation | KGVDENETAIVEKPS CCCCCCCCEEEECCC | 33.01 | 22369663 | |
67 | Phosphorylation | TAIVEKPSLVGERSL CEEEECCCCCCEECC | 46.91 | 22369663 | |
73 | Phosphorylation | PSLVGERSLEGFTLT CCCCCEECCCCEEEE | 26.86 | 23749301 | |
129 | Phosphorylation | RDQKVPRSSRLASLS CCCCCCCHHHHHHHC | 17.46 | 19823750 | |
130 | Phosphorylation | DQKVPRSSRLASLSK CCCCCCHHHHHHHCC | 32.37 | 19823750 | |
134 | Phosphorylation | PRSSRLASLSKDNES CCHHHHHHHCCCCCC | 37.45 | 24909858 | |
136 | Phosphorylation | SSRLASLSKDNESRP HHHHHHHCCCCCCCC | 35.15 | 24909858 | |
137 | Acetylation | SRLASLSKDNESRPS HHHHHHCCCCCCCCC | 70.62 | 25381059 | |
153 | Phosphorylation | KPSFLDSSSNSNGTA CHHHCCCCCCCCCCH | 32.95 | 21551504 | |
164 | Phosphorylation | NGTARRLSTISNKLP CCCHHHHHHHHHCCC | 23.14 | 25005228 | |
165 | Phosphorylation | GTARRLSTISNKLPK CCHHHHHHHHHCCCC | 32.77 | 21440633 | |
167 | Phosphorylation | ARRLSTISNKLPKKI HHHHHHHHHCCCCCE | 28.18 | 28889911 | |
169 | Acetylation | RLSTISNKLPKKIRL HHHHHHHCCCCCEEC | 60.42 | 24489116 | |
178 | Phosphorylation | PKKIRLGSITENDMN CCCEECCCCCCCCCC | 30.81 | 19823750 | |
180 | Phosphorylation | KIRLGSITENDMNLK CEECCCCCCCCCCHH | 30.36 | 22890988 | |
184 | Oxidation | GSITENDMNLKTFKR CCCCCCCCCHHHHHH | 10.76 | 15665377 | |
211 | Phosphorylation | PAGAHRISIVSKISP CCCCCEEEEEEECCC | 19.52 | 21440633 | |
214 | Phosphorylation | AHRISIVSKISPPTA CCEEEEEEECCCCCC | 23.70 | 27717283 | |
233 | Phosphorylation | LDRNEFSSETSTSRE CCCCCCCCCCCCCCC | 50.65 | 21551504 | |
235 | Phosphorylation | RNEFSSETSTSREAD CCCCCCCCCCCCCCC | 38.97 | 21551504 | |
236 | Phosphorylation | NEFSSETSTSREADE CCCCCCCCCCCCCCC | 21.97 | 30377154 | |
237 | Phosphorylation | EFSSETSTSREADEN CCCCCCCCCCCCCCC | 38.94 | 28889911 | |
238 | Phosphorylation | FSSETSTSREADENE CCCCCCCCCCCCCCC | 28.08 | 30377154 | |
247 | Phosphorylation | EADENENYVISKVKD CCCCCCCCEEEEEEC | 7.93 | 21551504 | |
250 | Phosphorylation | ENENYVISKVKDIPK CCCCCEEEEEECCCC | 22.73 | 21551504 | |
251 | Acetylation | NENYVISKVKDIPKK CCCCEEEEEECCCCC | 42.03 | 24489116 | |
388 | Phosphorylation | VDRHKNASIENEYKE EECCCCCCCCHHHHH | 39.57 | 30377154 | |
415 | Phosphorylation | YGSYGRGSYTDPWTV CCCCCCCCCCCCCCH | 24.41 | 30377154 | |
586 | Phosphorylation | DNEDNEGSEEEPEID CCCCCCCCCCCCCCC | 35.34 | 25521595 |
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 TFC5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TFC5_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 TFC5_YEAST !! |
Kegg Drug | ||||||
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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-49; SER-73 AND SER-178,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-49, AND MASSSPECTROMETRY. | |
"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-49, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND MASSSPECTROMETRY. |