| UniProt ID | T2EB_YEAST | |
|---|---|---|
| UniProt AC | P36145 | |
| Protein Name | Transcription initiation factor IIE subunit beta | |
| Gene Name | TFA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 328 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase (By similarity).. | |
| Protein Sequence | MSKNRDPLLANLNAFKSKVKSAPVIAPAKVGQKKTNDTVITIDGNTRKRTASERAQENTLNSAKNPVLVDIKKEAGSNSSNAISLDDDDDDEDFGSSPSKKVRPGSIAAAALQANQTDISKSHDSSKLLWATEYIQKKGKPVLVNELLDYLSMKKDDKVIELLKKLDRIEFDPKKGTFKYLSTYDVHSPSELLKLLRSQVTFKGISCKDLKDGWPQCDETINQLEEDSKILVLRTKKDKTPRYVWYNSGGNLKCIDEEFVKMWENVQLPQFAELPRKLQDLGLKPASVDPATIKRQTKRVEVKKKRQRKGKITNTHMTGILKDYSHRV | |
| 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 |
|---|---|---|---|---|---|
| 3 | Acetylation | -----MSKNRDPLLA -----CCCCCCHHHH | 55.49 | 24489116 | |
| 16 | Acetylation | LANLNAFKSKVKSAP HHHHHHHHHHHCCCC | 47.13 | 25381059 | |
| 21 | Phosphorylation | AFKSKVKSAPVIAPA HHHHHHCCCCEECCC | 40.57 | 21440633 | |
| 50 | Phosphorylation | DGNTRKRTASERAQE CCCCCCCCHHHHHHH | 37.26 | 22369663 | |
| 52 | Phosphorylation | NTRKRTASERAQENT CCCCCCHHHHHHHHH | 27.31 | 22369663 | |
| 59 | Phosphorylation | SERAQENTLNSAKNP HHHHHHHHHHCCCCC | 26.94 | 22369663 | |
| 62 | Phosphorylation | AQENTLNSAKNPVLV HHHHHHHCCCCCEEE | 43.67 | 22369663 | |
| 64 | Acetylation | ENTLNSAKNPVLVDI HHHHHCCCCCEEEEE | 62.70 | 25381059 | |
| 84 | Phosphorylation | SNSSNAISLDDDDDD CCCCCCEECCCCCCC | 24.28 | 23749301 | |
| 96 | Phosphorylation | DDDEDFGSSPSKKVR CCCCCCCCCCCCCCC | 38.78 | 22369663 | |
| 97 | Phosphorylation | DDEDFGSSPSKKVRP CCCCCCCCCCCCCCC | 33.31 | 22369663 | |
| 99 | Phosphorylation | EDFGSSPSKKVRPGS CCCCCCCCCCCCCCH | 47.24 | 22369663 | |
| 106 | Phosphorylation | SKKVRPGSIAAAALQ CCCCCCCHHHHHHHH | 16.25 | 21551504 | |
| 117 | Phosphorylation | AALQANQTDISKSHD HHHHCCCCCHHHCCC | 34.80 | 29136822 | |
| 120 | Phosphorylation | QANQTDISKSHDSSK HCCCCCHHHCCCHHH | 30.80 | 29136822 | |
| 121 | Acetylation | ANQTDISKSHDSSKL CCCCCHHHCCCHHHH | 52.74 | 24489116 | |
| 122 | Phosphorylation | NQTDISKSHDSSKLL CCCCHHHCCCHHHHH | 26.24 | 29136822 | |
| 125 | Phosphorylation | DISKSHDSSKLLWAT CHHHCCCHHHHHHHH | 24.77 | 29136822 | |
| 126 | Phosphorylation | ISKSHDSSKLLWATE HHHCCCHHHHHHHHH | 33.12 | 29136822 | |
| 132 | Phosphorylation | SSKLLWATEYIQKKG HHHHHHHHHHHHHCC | 20.10 | 19795423 | |
| 134 | Phosphorylation | KLLWATEYIQKKGKP HHHHHHHHHHHCCCC | 12.33 | 19795423 | |
| 155 | Acetylation | LDYLSMKKDDKVIEL HHHHCCCCCHHHHHH | 63.62 | 24489116 | |
| 158 | Acetylation | LSMKKDDKVIELLKK HCCCCCHHHHHHHHH | 56.07 | 24489116 | |
| 174 | Acetylation | DRIEFDPKKGTFKYL CCCCCCCCCCCEEEC | 66.72 | 24489116 | |
| 188 | Phosphorylation | LSTYDVHSPSELLKL CEECCCCCHHHHHHH | 29.94 | 21440633 | |
| 194 | Acetylation | HSPSELLKLLRSQVT CCHHHHHHHHHCCCC | 59.09 | 24489116 | |
| 322 | Acetylation | THMTGILKDYSHRV- HHHHHHHCCCCCCC- | 53.34 | 25381059 | |
| 324 | Phosphorylation | MTGILKDYSHRV--- HHHHHCCCCCCC--- | 12.56 | 28132839 |
| 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 T2EB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of T2EB_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 T2EB_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-106, AND MASSSPECTROMETRY. | |
| "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-96, AND MASSSPECTROMETRY. | |
| "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-52, AND MASSSPECTROMETRY. | |
