UniProt ID | MAF1_YEAST | |
---|---|---|
UniProt AC | P41910 | |
Protein Name | Repressor of RNA polymerase III transcription MAF1 | |
Gene Name | MAF1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 395 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.. | |
Protein Sequence | MKFIDELDIERVNQTLNFETNDCKIVGSCDIFTTKAVASDRKLYKTIDQHLDTILQENENYNATLQQQLAAPETNQSPCSSPFYSNRRDSNSFWEQKRRISFSEYNSNNNTNNSNGNSSNNNNYSGPNGSSPATFPKSAKLNDQNLKELVSNYDSGSMSSSSLDSSSKNDERIRRRSSSSISSFKSGKSSNNNYSSGTATNNVNKRRKSSINERPSNLSLGPFGPINEPSSRKIFAYLIAILNASYPDHDFSSVEPTDFVKTSLKTFISKFENTLYSLGRQPEEWVWEVINSHMTLSDCVLFQYSPSNSFLEDEPGYLWNLIGFLYNRKRKRVAYLYLICSRLNSSTGEVEDALAKKPQGKLIIDDGSNEYEGEYDFTYDENVIDDKSDQEESLQ | |
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 |
---|---|---|---|---|---|
90 | Phosphorylation | FYSNRRDSNSFWEQK CCCCCCCCCCHHHHH | 32.34 | 25533186 | |
92 | Phosphorylation | SNRRDSNSFWEQKRR CCCCCCCCHHHHHHC | 35.37 | 17330950 | |
101 | Phosphorylation | WEQKRRISFSEYNSN HHHHHCCCHHHHCCC | 22.40 | 21440633 | |
103 | Phosphorylation | QKRRISFSEYNSNNN HHHCCCHHHHCCCCC | 32.17 | 23749301 | |
105 | Phosphorylation | RRISFSEYNSNNNTN HCCCHHHHCCCCCCC | 23.77 | 21440633 | |
155 | Phosphorylation | ELVSNYDSGSMSSSS HHHHCCCCCCCCHHH | 23.54 | 25521595 | |
157 | Phosphorylation | VSNYDSGSMSSSSLD HHCCCCCCCCHHHCC | 21.31 | 24961812 | |
159 | Phosphorylation | NYDSGSMSSSSLDSS CCCCCCCCHHHCCCC | 28.85 | 20377248 | |
160 | Phosphorylation | YDSGSMSSSSLDSSS CCCCCCCHHHCCCCC | 18.46 | 21383183 | |
161 | Phosphorylation | DSGSMSSSSLDSSSK CCCCCCHHHCCCCCC | 27.84 | 21383183 | |
162 | Phosphorylation | SGSMSSSSLDSSSKN CCCCCHHHCCCCCCC | 37.84 | 20377248 | |
165 | Phosphorylation | MSSSSLDSSSKNDER CCHHHCCCCCCCHHH | 41.63 | 28889911 | |
166 | Phosphorylation | SSSSLDSSSKNDERI CHHHCCCCCCCHHHH | 45.02 | 24961812 | |
167 | Phosphorylation | SSSLDSSSKNDERIR HHHCCCCCCCHHHHH | 39.16 | 24961812 | |
177 | Phosphorylation | DERIRRRSSSSISSF HHHHHHHCCCCHHHH | 32.53 | 22369663 | |
178 | Phosphorylation | ERIRRRSSSSISSFK HHHHHHCCCCHHHHC | 26.71 | 22369663 | |
179 | Phosphorylation | RIRRRSSSSISSFKS HHHHHCCCCHHHHCC | 32.70 | 22369663 | |
180 | Phosphorylation | IRRRSSSSISSFKSG HHHHCCCCHHHHCCC | 28.56 | 22369663 | |
182 | Phosphorylation | RRSSSSISSFKSGKS HHCCCCHHHHCCCCC | 31.50 | 22369663 | |
183 | Phosphorylation | RSSSSISSFKSGKSS HCCCCHHHHCCCCCC | 34.72 | 27017623 | |
186 | Phosphorylation | SSISSFKSGKSSNNN CCHHHHCCCCCCCCC | 49.82 | 27717283 | |
189 | Phosphorylation | SSFKSGKSSNNNYSS HHHCCCCCCCCCCCC | 41.65 | 22369663 | |
190 | Phosphorylation | SFKSGKSSNNNYSSG HHCCCCCCCCCCCCC | 47.25 | 20377248 | |
194 | Phosphorylation | GKSSNNNYSSGTATN CCCCCCCCCCCCCCC | 13.31 | 22369663 | |
195 | Phosphorylation | KSSNNNYSSGTATNN CCCCCCCCCCCCCCC | 25.15 | 22369663 | |
196 | Phosphorylation | SSNNNYSSGTATNNV CCCCCCCCCCCCCCH | 29.78 | 22369663 | |
198 | Phosphorylation | NNNYSSGTATNNVNK CCCCCCCCCCCCHHH | 32.05 | 22369663 | |
200 | Phosphorylation | NYSSGTATNNVNKRR CCCCCCCCCCHHHHC | 27.45 | 22369663 | |
209 | Phosphorylation | NVNKRRKSSINERPS CHHHHCHHCCCCCCC | 34.34 | 22369663 | |
210 | Phosphorylation | VNKRRKSSINERPSN HHHHCHHCCCCCCCC | 32.25 | 22369663 | |
216 | Phosphorylation | SSINERPSNLSLGPF HCCCCCCCCCCCCCC | 57.53 | 17330950 | |
219 | Phosphorylation | NERPSNLSLGPFGPI CCCCCCCCCCCCCCC | 35.21 | 17330950 | |
345 | Phosphorylation | LICSRLNSSTGEVED HHHHHHCCCCCCHHH | 33.59 | 22369663 | |
346 | Phosphorylation | ICSRLNSSTGEVEDA HHHHHCCCCCCHHHH | 39.08 | 22369663 | |
347 | Phosphorylation | CSRLNSSTGEVEDAL HHHHCCCCCCHHHHH | 36.86 | 22369663 | |
388 | Phosphorylation | ENVIDDKSDQEESLQ CCCCCCCCHHHHHCC | 52.07 | 21383183 |
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 MAF1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MAF1_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 MAF1_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-90; SER-210 AND SER-346,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-177, 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-209 AND SER-210, ANDMASS SPECTROMETRY. |