UniProt ID | STB1_YEAST | |
---|---|---|
UniProt AC | P42845 | |
Protein Name | Protein STB1 | |
Gene Name | STB1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 420 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Involved in the regulation and timing of MBF-dependent transcription in late G1 of the cell cycle.. | |
Protein Sequence | MSQPQMSPEKEQELASKILHRAELAQMTRQLKLGLSNVPSTKRKQDSTTKKRSGEDAEDVDEDHKTLLEAISPAKKPLHDDTNKMTVISPVKFVEKPNTPPSSRQRKAEDRSQQIKPRKEDTPSTPRASATPIILPHASSHYQRPHDKNFMTPKRNNNNSSNHSNNNNNIKKKAAGSKDAPQDSDNTAGADLLMYLATSPYNKSSHHGTPMAVRMPTTPRSYHYASQLSLNGNTASTSNDAVRFSHIKPSASSPQSTFKSNLLPNFPDESLMDSPSLYLSNNNGSVQATLSPQQRRKPTTNTLHPPSNVPTTPSRELNGTNFNLLRTPNFNMGDYLHNLFSPSPRVPAQQGASNTSASIPSVPAMVPGSSSNTSAIATAAISSHTTNNFLDMNANGIPLIVGPGTDRIGEGESIDDKLTD | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSQPQMSPE ------CCCCCCCHH | 51.04 | 24909858 | |
2 | Acetylation | ------MSQPQMSPE ------CCCCCCCHH | 51.04 | 15665377 | |
7 | Phosphorylation | -MSQPQMSPEKEQEL -CCCCCCCHHHHHHH | 25.35 | 22369663 | |
16 | Phosphorylation | EKEQELASKILHRAE HHHHHHHHHHHHHHH | 32.62 | 22369663 | |
66 | Phosphorylation | DVDEDHKTLLEAISP HCCHHHHHHHHHHCC | 32.91 | 22890988 | |
72 | Phosphorylation | KTLLEAISPAKKPLH HHHHHHHCCCCCCCC | 26.34 | 22369663 | |
82 | Phosphorylation | KKPLHDDTNKMTVIS CCCCCCCCCCCEEEE | 42.68 | 21440633 | |
86 | Phosphorylation | HDDTNKMTVISPVKF CCCCCCCEEEECEEE | 19.12 | 19684113 | |
89 | Phosphorylation | TNKMTVISPVKFVEK CCCCEEEECEEEECC | 21.21 | 22369663 | |
99 | Phosphorylation | KFVEKPNTPPSSRQR EEECCCCCCCCHHHH | 45.14 | 22369663 | |
102 | Phosphorylation | EKPNTPPSSRQRKAE CCCCCCCCHHHHHHH | 39.08 | 22369663 | |
103 | Phosphorylation | KPNTPPSSRQRKAED CCCCCCCHHHHHHHH | 37.90 | 22369663 | |
122 | Phosphorylation | IKPRKEDTPSTPRAS CCCCCCCCCCCCCCC | 21.89 | 23749301 | |
124 | Phosphorylation | PRKEDTPSTPRASAT CCCCCCCCCCCCCCC | 53.81 | 24909858 | |
125 | Phosphorylation | RKEDTPSTPRASATP CCCCCCCCCCCCCCC | 20.28 | 28889911 | |
129 | Phosphorylation | TPSTPRASATPIILP CCCCCCCCCCCEECC | 33.67 | 28132839 | |
131 | Phosphorylation | STPRASATPIILPHA CCCCCCCCCEECCCC | 16.72 | 28132839 | |
139 | Phosphorylation | PIILPHASSHYQRPH CEECCCCHHCCCCCC | 18.02 | 24961812 | |
140 | Phosphorylation | IILPHASSHYQRPHD EECCCCHHCCCCCCC | 27.31 | 24961812 | |
142 | Phosphorylation | LPHASSHYQRPHDKN CCCCHHCCCCCCCCC | 14.25 | 24961812 | |
152 | Phosphorylation | PHDKNFMTPKRNNNN CCCCCCCCCCCCCCC | 22.86 | 21440633 | |
164 | Phosphorylation | NNNSSNHSNNNNNIK CCCCCCCCCCCHHHH | 45.57 | 19684113 | |
198 | Phosphorylation | DLLMYLATSPYNKSS HHHHHHHCCCCCCCC | 27.86 | 28132839 | |
199 | Phosphorylation | LLMYLATSPYNKSSH HHHHHHCCCCCCCCC | 21.56 | 28132839 | |
204 | Phosphorylation | ATSPYNKSSHHGTPM HCCCCCCCCCCCCCE | 31.13 | 28889911 | |
205 | Phosphorylation | TSPYNKSSHHGTPMA CCCCCCCCCCCCCEE | 22.55 | 28889911 | |
209 | Phosphorylation | NKSSHHGTPMAVRMP CCCCCCCCCEEEECC | 12.92 | 28889911 | |
217 | Phosphorylation | PMAVRMPTTPRSYHY CEEEECCCCCCCEEE | 39.84 | 24909858 | |
218 | Phosphorylation | MAVRMPTTPRSYHYA EEEECCCCCCCEEEE | 15.72 | 27017623 | |
221 | Phosphorylation | RMPTTPRSYHYASQL ECCCCCCCEEEEEEE | 19.91 | 27017623 | |
224 | Phosphorylation | TTPRSYHYASQLSLN CCCCCEEEEEEEEEC | 10.34 | 27017623 | |
226 | Phosphorylation | PRSYHYASQLSLNGN CCCEEEEEEEEECCC | 25.20 | 23749301 | |
229 | Phosphorylation | YHYASQLSLNGNTAS EEEEEEEEECCCCCC | 16.50 | 23749301 | |
245 | Phosphorylation | SNDAVRFSHIKPSAS CCCCEEECCCCCCCC | 17.46 | 29650682 | |
250 | Phosphorylation | RFSHIKPSASSPQST EECCCCCCCCCCCHH | 35.46 | 28889911 | |
252 | Phosphorylation | SHIKPSASSPQSTFK CCCCCCCCCCCHHHH | 47.06 | 19684113 | |
253 | Phosphorylation | HIKPSASSPQSTFKS CCCCCCCCCCHHHHC | 27.03 | 25533186 | |
256 | Phosphorylation | PSASSPQSTFKSNLL CCCCCCCHHHHCCCC | 38.91 | 19684113 | |
257 | Phosphorylation | SASSPQSTFKSNLLP CCCCCCHHHHCCCCC | 29.81 | 28889911 | |
307 | Phosphorylation | TNTLHPPSNVPTTPS CCCCCCCCCCCCCCC | 55.71 | 28132839 | |
311 | Phosphorylation | HPPSNVPTTPSRELN CCCCCCCCCCCCCCC | 47.24 | 28132839 | |
312 | Phosphorylation | PPSNVPTTPSRELNG CCCCCCCCCCCCCCC | 17.13 | 28132839 | |
314 | Phosphorylation | SNVPTTPSRELNGTN CCCCCCCCCCCCCCC | 35.97 | 28132839 | |
327 | Phosphorylation | TNFNLLRTPNFNMGD CCCCCCCCCCCCHHH | 23.66 | 28132839 | |
335 | Phosphorylation | PNFNMGDYLHNLFSP CCCCHHHHHHHHCCC | 12.25 | 28132839 | |
341 | Phosphorylation | DYLHNLFSPSPRVPA HHHHHHCCCCCCCCC | 27.86 | 28132839 | |
343 | Phosphorylation | LHNLFSPSPRVPAQQ HHHHCCCCCCCCCCC | 24.92 | 29650682 | |
413 | Phosphorylation | DRIGEGESIDDKLTD CCCCCCCCCCCCCCC | 42.02 | 23749301 | |
419 | Phosphorylation | ESIDDKLTD------ CCCCCCCCC------ | 45.46 | 22369663 |
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 STB1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STB1_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 STB1_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-72; SER-89; THR-99;SER-102; SER-253 AND THR-419, 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 THR-99 AND SER-102, 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 THR-99 AND SER-102, AND MASSSPECTROMETRY. |