| UniProt ID | IWS1_YEAST | |
|---|---|---|
| UniProt AC | Q06505 | |
| Protein Name | Transcription factor SPN1 | |
| Gene Name | SPN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 410 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.. | |
| Protein Sequence | MSTADQEQPKVVEATPEDGTASSQKSTINAENENTKQNQSMEPQETSKGTSNDTKDPDNGEKNEEAAIDENSNVEAAERKRKHISTDFSDDDLEKEEHNDQSLQPTVENRASKDRDSSATPSSRQELEEKLDRILKKPKVRRTRRDEDDLEQYLDEKILRLKDEMNIAAQLDIDTLNKRIETGDTSLIAMQKVKLLPKVVSVLSKANLADTILDNNLLQSVRIWLEPLPDGSLPSFEIQKSLFAALNDLPVKTEHLKESGLGRVVIFYTKSKRVEAQLARLAEKLIAEWTRPIIGASDNYRDKRIMQLEFDSEKLRKKSVMDSAKNRKKKSKSGEDPTSRGSSVQTLYEQAAARRNRAAAPAQTTTDYKYAPVSNLSAVPTNARAVGVGSTLNNSEMYKRLTSRLNKKHK | |
| 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 | ------MSTADQEQP ------CCCCCCCCC | 32.10 | 30377154 | |
| 3 | Phosphorylation | -----MSTADQEQPK -----CCCCCCCCCC | 32.71 | 27717283 | |
| 15 | Phosphorylation | QPKVVEATPEDGTAS CCCEEEECCCCCCCC | 17.44 | 22369663 | |
| 20 | Phosphorylation | EATPEDGTASSQKST EECCCCCCCCCCCCC | 35.37 | 22369663 | |
| 22 | Phosphorylation | TPEDGTASSQKSTIN CCCCCCCCCCCCCCC | 32.89 | 22369663 | |
| 23 | Phosphorylation | PEDGTASSQKSTINA CCCCCCCCCCCCCCC | 38.88 | 22369663 | |
| 25 | Acetylation | DGTASSQKSTINAEN CCCCCCCCCCCCCCC | 52.06 | 24489116 | |
| 25 | Ubiquitination | DGTASSQKSTINAEN CCCCCCCCCCCCCCC | 52.06 | 23749301 | |
| 26 | Phosphorylation | GTASSQKSTINAENE CCCCCCCCCCCCCCC | 27.21 | 25521595 | |
| 27 | Phosphorylation | TASSQKSTINAENEN CCCCCCCCCCCCCCC | 25.86 | 25521595 | |
| 35 | Phosphorylation | INAENENTKQNQSME CCCCCCCCCCCCCCC | 28.03 | 22369663 | |
| 36 | Ubiquitination | NAENENTKQNQSMEP CCCCCCCCCCCCCCC | 59.85 | 23749301 | |
| 40 | Phosphorylation | ENTKQNQSMEPQETS CCCCCCCCCCCCCCC | 32.44 | 21551504 | |
| 46 | Phosphorylation | QSMEPQETSKGTSND CCCCCCCCCCCCCCC | 30.41 | 27717283 | |
| 50 | Phosphorylation | PQETSKGTSNDTKDP CCCCCCCCCCCCCCC | 28.26 | 27017623 | |
| 51 | Phosphorylation | QETSKGTSNDTKDPD CCCCCCCCCCCCCCC | 41.18 | 27017623 | |
| 54 | Phosphorylation | SKGTSNDTKDPDNGE CCCCCCCCCCCCCCC | 41.41 | 27017623 | |
| 72 | Phosphorylation | EAAIDENSNVEAAER HHHHCCCCCHHHHHH | 39.96 | 22369663 | |
| 85 | Phosphorylation | ERKRKHISTDFSDDD HHHHHHHCCCCCCCH | 22.95 | 22369663 | |
| 86 | Phosphorylation | RKRKHISTDFSDDDL HHHHHHCCCCCCCHH | 40.22 | 22369663 | |
| 89 | Phosphorylation | KHISTDFSDDDLEKE HHHCCCCCCCHHHHH | 42.83 | 22369663 | |
| 102 | Phosphorylation | KEEHNDQSLQPTVEN HHHHCCCCCHHHHHH | 31.66 | 22890988 | |
| 106 | Phosphorylation | NDQSLQPTVENRASK CCCCCHHHHHHHHCC | 27.73 | 22890988 | |
| 117 | Phosphorylation | RASKDRDSSATPSSR HHCCCCCCCCCHHHH | 23.83 | 22369663 | |
| 118 | Phosphorylation | ASKDRDSSATPSSRQ HCCCCCCCCCHHHHH | 40.21 | 25521595 | |
| 120 | Phosphorylation | KDRDSSATPSSRQEL CCCCCCCCHHHHHHH | 26.17 | 22369663 | |
| 122 | Phosphorylation | RDSSATPSSRQELEE CCCCCCHHHHHHHHH | 33.52 | 22369663 | |
| 123 | Phosphorylation | DSSATPSSRQELEEK CCCCCHHHHHHHHHH | 38.90 | 22369663 | |
| 130 | Acetylation | SRQELEEKLDRILKK HHHHHHHHHHHHHCC | 46.44 | 25381059 | |
| 157 | Acetylation | LEQYLDEKILRLKDE HHHHHHHHHHHHHHH | 46.86 | 24489116 | |
| 201 | Phosphorylation | KLLPKVVSVLSKANL CHHHHHHHHHHHCCC | 21.96 | 27214570 | |
| 241 | Phosphorylation | PSFEIQKSLFAALND CHHHHHHHHHHHHCC | 16.61 | 19795423 | |
| 252 | Acetylation | ALNDLPVKTEHLKES HHCCCCCCHHHHHHC | 46.38 | 24489116 | |
| 257 | Acetylation | PVKTEHLKESGLGRV CCCHHHHHHCCCCCE | 52.31 | 24489116 | |
| 284 | Acetylation | QLARLAEKLIAEWTR HHHHHHHHHHHHHHC | 39.32 | 24489116 | |
| 297 | Phosphorylation | TRPIIGASDNYRDKR HCCCCCCCCCCCCCC | 22.60 | 30377154 | |
| 314 | Acetylation | QLEFDSEKLRKKSVM CCCCCHHHHHHHHHH | 58.50 | 24489116 | |
| 319 | Phosphorylation | SEKLRKKSVMDSAKN HHHHHHHHHHHHHHH | 26.21 | 30377154 | |
| 325 | Acetylation | KSVMDSAKNRKKKSK HHHHHHHHHHHHCCC | 62.33 | 25381059 | |
| 339 | Phosphorylation | KSGEDPTSRGSSVQT CCCCCCCCCCHHHHH | 39.78 | 28889911 | |
| 342 | Phosphorylation | EDPTSRGSSVQTLYE CCCCCCCHHHHHHHH | 26.65 | 28889911 | |
| 343 | Phosphorylation | DPTSRGSSVQTLYEQ CCCCCCHHHHHHHHH | 22.52 | 28889911 | |
| 346 | Phosphorylation | SRGSSVQTLYEQAAA CCCHHHHHHHHHHHH | 29.20 | 28889911 | |
| 369 | Acetylation | AQTTTDYKYAPVSNL CCCCCCCCCCCCCCC | 37.43 | 24489116 | |
| 369 | Ubiquitination | AQTTTDYKYAPVSNL CCCCCCCCCCCCCCC | 37.43 | 23749301 | |
| 390 | Phosphorylation | ARAVGVGSTLNNSEM CCCCCCCCCCCCHHH | 27.58 | 21440633 | |
| 399 | Acetylation | LNNSEMYKRLTSRLN CCCHHHHHHHHHHHH | 39.35 | 24489116 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IWS1_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 IWS1_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 THR-15; SER-22; SER-23;SER-26; SER-40 AND SER-89, 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-23; SER-89 AND SER-118,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-89, 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-23 AND SER-89, AND MASSSPECTROMETRY. | |
| "RNA polymerase II elongation factors of Saccharomyces cerevisiae: atargeted proteomics approach."; Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G.,Emili A., Shilatifard A., Buratowski S., Greenblatt J.F.; Mol. Cell. Biol. 22:6979-6992(2002). Cited for: INTERACTION WITH SPT6, AND PHOSPHORYLATION AT SER-89. | |
