UniProt ID | T2FB_YEAST | |
---|---|---|
UniProt AC | P41896 | |
Protein Name | Transcription initiation factor IIF subunit beta | |
Gene Name | TFG2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 400 | |
Subcellular Localization | Nucleus. | |
Protein Description | TFIIF is a general transcription initiation factor that binds to RNA polymerase II. Its functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. TFG2 shows ATP-dependent DNA-helicase activity (By similarity).. | |
Protein Sequence | MSSGSAGAPALSNNSTNSVAKEKSGNISGDEYLSQEEEVFDGNDIENNETKVYEESLDLDLERSNRQVWLVRLPMFLAEKWRDRNNLHGQELGKIRINKDGSKITLLLNENDNDSIPHEYDLELTKKVVENEYVFTEQNLKKYQQRKKELEADPEKQRQAYLKKQEREEELKKKQQQQKRRNNRKKFNHRVMTDRDGRDRYIPYVKTIPKKTAIVGTVCHECQVMPSMNDPNYHKIVEQRRNIVKLNNKERITTLDETVGVTMSHTGMSMRSDNSNFLKVGREKAKSNIKSIRMPKKEILDYLFKLFDEYDYWSLKGLKERTRQPEAHLKECLDKVATLVKKGPYAFKYTLRPEYKKLKEEERKATLGELADEQTGSAGDNAQGDAEADLEDEIEMEDVV | |
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 | ------MSSGSAGAP ------CCCCCCCCC | 43.32 | 28152593 | |
5 | Phosphorylation | ---MSSGSAGAPALS ---CCCCCCCCCCCC | 26.02 | 30377154 | |
12 | Phosphorylation | SAGAPALSNNSTNSV CCCCCCCCCCCCCCC | 35.75 | 30377154 | |
15 | Phosphorylation | APALSNNSTNSVAKE CCCCCCCCCCCCCCH | 32.96 | 30377154 | |
16 | Phosphorylation | PALSNNSTNSVAKEK CCCCCCCCCCCCCHH | 33.37 | 30377154 | |
18 | Phosphorylation | LSNNSTNSVAKEKSG CCCCCCCCCCCHHCC | 24.44 | 30377154 | |
24 | Phosphorylation | NSVAKEKSGNISGDE CCCCCHHCCCCCCCH | 37.86 | 22369663 | |
28 | Phosphorylation | KEKSGNISGDEYLSQ CHHCCCCCCCHHHCC | 44.16 | 22369663 | |
32 | Phosphorylation | GNISGDEYLSQEEEV CCCCCCHHHCCCEEC | 19.18 | 22369663 | |
34 | Phosphorylation | ISGDEYLSQEEEVFD CCCCHHHCCCEECCC | 34.34 | 22369663 | |
56 | Phosphorylation | ETKVYEESLDLDLER CCCEEEHHHCCCHHH | 18.42 | 28889911 | |
80 | Acetylation | LPMFLAEKWRDRNNL HHHHHHHHHHHCCCC | 41.75 | 24489116 | |
80 | Ubiquitination | LPMFLAEKWRDRNNL HHHHHHHHHHHCCCC | 41.75 | 23749301 | |
141 | Acetylation | VFTEQNLKKYQQRKK CCCHHHHHHHHHHHH | 57.91 | 24489116 | |
245 | Acetylation | EQRRNIVKLNNKERI HHHHHHHHCCCCCCE | 41.52 | 25381059 | |
253 | Phosphorylation | LNNKERITTLDETVG CCCCCCEEECHHHCC | 27.77 | 28889911 | |
254 | Phosphorylation | NNKERITTLDETVGV CCCCCEEECHHHCCC | 29.82 | 30377154 | |
264 | Phosphorylation | ETVGVTMSHTGMSMR HHCCCEECCCCCCCC | 14.45 | 28889911 | |
266 | Phosphorylation | VGVTMSHTGMSMRSD CCCEECCCCCCCCCC | 27.54 | 28889911 | |
269 | Phosphorylation | TMSHTGMSMRSDNSN EECCCCCCCCCCCCC | 16.64 | 28889911 | |
272 | Phosphorylation | HTGMSMRSDNSNFLK CCCCCCCCCCCCCCH | 32.28 | 28889911 | |
275 | Phosphorylation | MSMRSDNSNFLKVGR CCCCCCCCCCCHHCH | 33.67 | 30377154 | |
279 | Acetylation | SDNSNFLKVGREKAK CCCCCCCHHCHHHHH | 38.21 | 25381059 | |
316 | Acetylation | EYDYWSLKGLKERTR HHCHHHHHCHHHHHC | 57.59 | 24489116 | |
335 | Acetylation | HLKECLDKVATLVKK HHHHHHHHHHHHHHH | 22.33 | 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 T2FB_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of T2FB_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 T2FB_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-28; SER-34 AND SER-56,AND MASS SPECTROMETRY. |