UniProt ID | SUB1_YEAST | |
---|---|---|
UniProt AC | P54000 | |
Protein Name | RNA polymerase II transcriptional coactivator SUB1 | |
Gene Name | SUB1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 292 | |
Subcellular Localization | Nucleus . | |
Protein Description | Plays a role in the release of TFIIB from the transcription complex during transcription initiation. Binds to TFIIB and specifically inhibits the formation of the TBP-TFIIB-promoter complexes.. | |
Protein Sequence | MSYYNRYRNKRRSDNGGGNLSNSNNNNGGMPSGLSASDAIFDLGKNKRVTVRQFRNINLIDIREYYLDSSTGEMKPGKKGISLTEDLYDELLKHRLNIDEALRRLGSKRPKTKMVRLLSDDEYEDDNNNDSTNNDKDKNGKDKNSPKKRREDKSKASNESHDLEPRSKKKKPAPPTLLPHEENIQNAEREANATLIIPGQAGRKQQEERKQKEKEEAEEAKAKAVAEQEKEAKAKEKIAEPEPEPVPTLQAKKEDIVSNINESKDANSSDEEFAQSLEAEMNKAEDDISEEE | |
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 |
---|---|---|---|---|---|
32 | Phosphorylation | NNNGGMPSGLSASDA CCCCCCCCCCCHHHH | 43.40 | 30377154 | |
35 | Phosphorylation | GGMPSGLSASDAIFD CCCCCCCCHHHHHHH | 29.29 | 30377154 | |
93 | Acetylation | DLYDELLKHRLNIDE HHHHHHHHHCCCHHH | 39.03 | 24489116 | |
112 | Phosphorylation | LGSKRPKTKMVRLLS HCCCCCCCCEEEECC | 27.36 | 24961812 | |
119 | Phosphorylation | TKMVRLLSDDEYEDD CCEEEECCCCCCCCC | 47.83 | 22369663 | |
123 | Phosphorylation | RLLSDDEYEDDNNND EECCCCCCCCCCCCC | 31.49 | 22890988 | |
131 | Phosphorylation | EDDNNNDSTNNDKDK CCCCCCCCCCCHHCC | 34.85 | 22890988 | |
132 | Phosphorylation | DDNNNDSTNNDKDKN CCCCCCCCCCHHCCC | 40.69 | 22890988 | |
167 | Phosphorylation | SHDLEPRSKKKKPAP CCCCCCCCCCCCCCC | 60.59 | 27017623 | |
194 | Phosphorylation | AEREANATLIIPGQA HHHHHCCEEECCCHH | 20.49 | 29650682 | |
258 | Phosphorylation | AKKEDIVSNINESKD HCHHHHHHCCCCCCC | 32.12 | 21551504 | |
263 | Phosphorylation | IVSNINESKDANSSD HHHCCCCCCCCCCCH | 31.20 | 22369663 | |
268 | Phosphorylation | NESKDANSSDEEFAQ CCCCCCCCCHHHHHH | 40.67 | 22369663 | |
269 | Phosphorylation | ESKDANSSDEEFAQS CCCCCCCCHHHHHHH | 49.18 | 22369663 | |
276 | Phosphorylation | SDEEFAQSLEAEMNK CHHHHHHHHHHHHHH | 25.42 | 22890988 | |
289 | Phosphorylation | NKAEDDISEEE---- HHHHHCCCCCC---- | 46.05 | 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 SUB1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SUB1_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 SUB1_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-119 AND SER-289, ANDMASS 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-119, 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-119; SER-268 ANDSER-269, AND MASS SPECTROMETRY. |