UniProt ID | T2FA_YEAST | |
---|---|---|
UniProt AC | P41895 | |
Protein Name | Transcription initiation factor IIF subunit alpha | |
Gene Name | TFG1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 735 | |
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.. | |
Protein Sequence | MSRRNPPGSRNGGGPTNASPFIKRDRMRRNFLRMRMGQNGSNSSSPGVPNGDNSRGSLVKKDDPEYAEEREKMLLQIGVEADAGRSNVKVKDEDPNEYNEFPLRAIPKEDLENMRTHLLKFQSKKKINPVTDFHLPVRLHRKDTRNLQFQLTRAEIVQRQKEISEYKKKAEQERSTPNSGGMNKSGTVSLNNTVKDGSQTPTVDSVTKDNTANGVNSSIPTVTGSSVPPASPTTVSAVESNGLSNGSTSAANGLDGNASTANLANGRPLVTKLEDAGPAEDPTKVGMVKYDGKEVTNEPEFEEGTMDPLADVAPDGGGRAKRGNLRRKTRQLKVLDENAKKLRFEEFYPWVMEDFDGYNTWVGSYEAGNSDSYVLLSVEDDGSFTMIPADKVYKFTARNKYATLTIDEAEKRMDKKSGEVPRWLMKHLDNIGTTTTRYDRTRRKLKAVADQQAMDEDDRDDNSEVELDYDEEFADDEEAPIIDGNEQENKESEQRIKKEMLQANAMGLRDEEAPSENEEDELFGEKKIDEDGERIKKALQKTELAALYSSDENEINPYLSESDIENKENESPVKKEEDSDTLSKSKRSSPKKQQKKATNAHVHKEPTLRVKSIKNCVIILKGDKKILKSFPEGEWNPQTTKAVDSSNNASNTVPSPIKQEEGLNSTVAEREETPAPTITEKDIIEAIGDGKVNIKEFGKFIRRKYPGAENKKLMFAIVKKLCRKVGNDHMELKKE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
19 | Phosphorylation | GGGPTNASPFIKRDR CCCCCCCCHHHCHHH | 23.55 | 21440633 | |
23 | Acetylation | TNASPFIKRDRMRRN CCCCHHHCHHHHHHH | 48.93 | 22865919 | |
41 | Phosphorylation | MRMGQNGSNSSSPGV HHCCCCCCCCCCCCC | 40.88 | 22369663 | |
43 | Phosphorylation | MGQNGSNSSSPGVPN CCCCCCCCCCCCCCC | 33.61 | 22369663 | |
44 | Phosphorylation | GQNGSNSSSPGVPNG CCCCCCCCCCCCCCC | 44.81 | 22369663 | |
45 | Phosphorylation | QNGSNSSSPGVPNGD CCCCCCCCCCCCCCC | 26.03 | 22369663 | |
54 | Phosphorylation | GVPNGDNSRGSLVKK CCCCCCCCCCCCCCC | 42.64 | 22369663 | |
57 | Phosphorylation | NGDNSRGSLVKKDDP CCCCCCCCCCCCCCH | 28.95 | 30377154 | |
61 | Acetylation | SRGSLVKKDDPEYAE CCCCCCCCCCHHHHH | 60.94 | 25381059 | |
120 | Acetylation | NMRTHLLKFQSKKKI HHHHHHHHHCCCCCC | 47.95 | 22865919 | |
126 | Ubiquitination | LKFQSKKKINPVTDF HHHCCCCCCCCCCCC | 51.99 | 17644757 | |
175 | Phosphorylation | KKAEQERSTPNSGGM HHHHHHCCCCCCCCC | 47.68 | 17287358 | |
176 | Phosphorylation | KAEQERSTPNSGGMN HHHHHCCCCCCCCCC | 32.48 | 17287358 | |
179 | Phosphorylation | QERSTPNSGGMNKSG HHCCCCCCCCCCCCC | 37.62 | 28889911 | |
185 | Phosphorylation | NSGGMNKSGTVSLNN CCCCCCCCCEEEECC | 34.39 | 23749301 | |
187 | Phosphorylation | GGMNKSGTVSLNNTV CCCCCCCEEEECCCC | 17.63 | 22369663 | |
189 | Phosphorylation | MNKSGTVSLNNTVKD CCCCCEEEECCCCCC | 25.80 | 22369663 | |
193 | Phosphorylation | GTVSLNNTVKDGSQT CEEEECCCCCCCCCC | 28.05 | 22369663 | |
195 | Acetylation | VSLNNTVKDGSQTPT EEECCCCCCCCCCCC | 55.09 | 24489116 | |
198 | Phosphorylation | NNTVKDGSQTPTVDS CCCCCCCCCCCCCCC | 40.80 | 22369663 | |
200 | Phosphorylation | TVKDGSQTPTVDSVT CCCCCCCCCCCCCCC | 23.71 | 22369663 | |
202 | Phosphorylation | KDGSQTPTVDSVTKD CCCCCCCCCCCCCCC | 40.09 | 24909858 | |
205 | Phosphorylation | SQTPTVDSVTKDNTA CCCCCCCCCCCCCCC | 27.61 | 22369663 | |
207 | Phosphorylation | TPTVDSVTKDNTANG CCCCCCCCCCCCCCC | 36.31 | 22369663 | |
271 | Phosphorylation | ANGRPLVTKLEDAGP CCCCCCEEEHHHCCC | 37.28 | 24909858 | |
272 | Acetylation | NGRPLVTKLEDAGPA CCCCCEEEHHHCCCC | 42.26 | 24489116 | |
284 | Acetylation | GPAEDPTKVGMVKYD CCCCCCCEEEEEEEC | 42.03 | 24489116 | |
289 | Acetylation | PTKVGMVKYDGKEVT CCEEEEEEECCEECC | 28.82 | 25381059 | |
296 | Phosphorylation | KYDGKEVTNEPEFEE EECCEECCCCCCCCC | 34.65 | 24961812 | |
340 | Ubiquitination | KVLDENAKKLRFEEF HHHHHHHHHCCHHHH | 65.01 | 23749301 | |
394 | Ubiquitination | IPADKVYKFTARNKY EECCCEEEEEECCCE | 38.95 | 23749301 | |
411 | Acetylation | LTIDEAEKRMDKKSG EEHHHHHHHHHHCCC | 61.13 | 24489116 | |
426 | Ubiquitination | EVPRWLMKHLDNIGT CHHHHHHHHHHHCCC | 38.55 | 17644757 | |
426 | Acetylation | EVPRWLMKHLDNIGT CHHHHHHHHHHHCCC | 38.55 | 24489116 | |
433 | Phosphorylation | KHLDNIGTTTTRYDR HHHHHCCCCCHHHHH | 19.71 | 19823750 | |
434 | Phosphorylation | HLDNIGTTTTRYDRT HHHHCCCCCHHHHHH | 22.43 | 19823750 | |
435 | Phosphorylation | LDNIGTTTTRYDRTR HHHCCCCCHHHHHHH | 14.76 | 19823750 | |
436 | Phosphorylation | DNIGTTTTRYDRTRR HHCCCCCHHHHHHHH | 25.74 | 19823750 | |
438 | Phosphorylation | IGTTTTRYDRTRRKL CCCCCHHHHHHHHHH | 14.00 | 19823750 | |
441 | Phosphorylation | TTTRYDRTRRKLKAV CCHHHHHHHHHHHHH | 31.74 | 19823750 | |
463 | Phosphorylation | EDDRDDNSEVELDYD CCCCCCCCCEECCCC | 50.44 | 28889911 | |
515 | Phosphorylation | LRDEEAPSENEEDEL CCCCCCCCCCCCCHH | 61.16 | 22369663 | |
542 | Phosphorylation | IKKALQKTELAALYS HHHHHHHHHHHHHHC | 24.22 | 21551504 | |
548 | Phosphorylation | KTELAALYSSDENEI HHHHHHHHCCCCCCC | 11.03 | 19795423 | |
549 | Phosphorylation | TELAALYSSDENEIN HHHHHHHCCCCCCCC | 31.96 | 19795423 | |
550 | Phosphorylation | ELAALYSSDENEINP HHHHHHCCCCCCCCC | 35.07 | 19795423 | |
558 | Phosphorylation | DENEINPYLSESDIE CCCCCCCCCCHHHHC | 20.55 | 19795423 | |
560 | Phosphorylation | NEINPYLSESDIENK CCCCCCCCHHHHCCC | 29.25 | 19795423 | |
562 | Phosphorylation | INPYLSESDIENKEN CCCCCCHHHHCCCCC | 40.28 | 19795423 | |
571 | Phosphorylation | IENKENESPVKKEED HCCCCCCCCCCHHHH | 46.72 | 22369663 | |
579 | Phosphorylation | PVKKEEDSDTLSKSK CCCHHHHHHCCCHHH | 35.46 | 25521595 | |
581 | Phosphorylation | KKEEDSDTLSKSKRS CHHHHHHCCCHHHCC | 36.56 | 19795423 | |
583 | Phosphorylation | EEDSDTLSKSKRSSP HHHHHCCCHHHCCCH | 36.65 | 22369663 | |
585 | Phosphorylation | DSDTLSKSKRSSPKK HHHCCCHHHCCCHHH | 29.90 | 24930733 | |
604 | Acetylation | ATNAHVHKEPTLRVK HHHCCCCCCCCCCCC | 65.39 | 22865919 | |
628 | Acetylation | KGDKKILKSFPEGEW CCCHHHHHHCCCCCC | 54.23 | 22865919 | |
645 | Phosphorylation | QTTKAVDSSNNASNT CCCCCCCCCCCCCCC | 28.50 | 28132839 | |
646 | Phosphorylation | TTKAVDSSNNASNTV CCCCCCCCCCCCCCC | 29.64 | 28132839 | |
650 | Phosphorylation | VDSSNNASNTVPSPI CCCCCCCCCCCCCCC | 34.85 | 22890988 | |
652 | Phosphorylation | SSNNASNTVPSPIKQ CCCCCCCCCCCCCCC | 31.16 | 22890988 | |
655 | Phosphorylation | NASNTVPSPIKQEEG CCCCCCCCCCCCCCC | 34.61 | 22369663 | |
665 | Phosphorylation | KQEEGLNSTVAEREE CCCCCCCCCCCCCCC | 29.33 | 20377248 | |
666 | Phosphorylation | QEEGLNSTVAEREET CCCCCCCCCCCCCCC | 23.74 | 22369663 | |
673 | Phosphorylation | TVAEREETPAPTITE CCCCCCCCCCCCCCH | 21.72 | 22369663 | |
677 | Phosphorylation | REETPAPTITEKDII CCCCCCCCCCHHHHH | 42.51 | 22369663 | |
679 | Phosphorylation | ETPAPTITEKDIIEA CCCCCCCCHHHHHHH | 39.19 | 22369663 | |
699 | Acetylation | VNIKEFGKFIRRKYP CCHHHHHHHHHHHCC | 42.83 | 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 T2FA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of T2FA_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 T2FA_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-198; THR-200; SER-515;SER-655 AND THR-673, 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-198; SER-515; SER-655AND THR-673, AND MASS SPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, 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 THR-200; SER-515 ANDSER-655, AND MASS SPECTROMETRY. |