UniProt ID | RLP7_YEAST | |
---|---|---|
UniProt AC | P40693 | |
Protein Name | Ribosome biogenesis protein RLP7 | |
Gene Name | RLP7 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 322 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs.. | |
Protein Sequence | MSSTQDSKAQTLNSNPEILLRKRRNADRTRIERQELAKKKREEQIKKKRSNKNKFVRAESIVAKTLATSREKERIKRVSILEDKKAKNETQHIASGKDFILKITEKANGAEENSVDLEETEEEEDDGLIREKTTYDGKPALLFIVRVRGPLAVNIPNKAFKILSLLRLVETNTGVFVKLTKNVYPLLKVIAPYVVIGKPSLSSIRSLIQKRGRIIYKGENEAEPHEIVLNDNNIVEEQLGDHGIICVEDIIHEIATMGESFSVCNFFLQPFKLNREVSGFGSLNRLRKIKQREAESRTRQFSNAATAPVIEVDIDSLLAKLN | |
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 | Acetylation | ------MSSTQDSKA ------CCCCCCHHC | 41.93 | 22814378 | |
11 | Phosphorylation | TQDSKAQTLNSNPEI CCCHHCHHCCCCHHH | 32.54 | 28889911 | |
14 | Phosphorylation | SKAQTLNSNPEILLR HHCHHCCCCHHHHHH | 57.80 | 25752575 | |
60 | Phosphorylation | NKFVRAESIVAKTLA CHHCHHHHHHHHHHC | 22.75 | 25521595 | |
64 | Acetylation | RAESIVAKTLATSRE HHHHHHHHHHCCHHH | 32.93 | 24489116 | |
79 | Phosphorylation | KERIKRVSILEDKKA HHHHHHHHHHCCHHH | 26.03 | 21440633 | |
97 | Acetylation | TQHIASGKDFILKIT CCHHHCCCCEEEHHH | 47.15 | 24489116 | |
114 | Phosphorylation | ANGAEENSVDLEETE HCCCCCCCCCHHHCC | 21.93 | 29136822 | |
120 | Phosphorylation | NSVDLEETEEEEDDG CCCCHHHCCCHHCCC | 39.04 | 22369663 | |
138 | Acetylation | EKTTYDGKPALLFIV ECEEECCCEEEEEEE | 24.99 | 24489116 | |
158 | Acetylation | LAVNIPNKAFKILSL EEECCCCHHHHHHHH | 50.25 | 24489116 | |
161 | Acetylation | NIPNKAFKILSLLRL CCCCHHHHHHHHHHH | 47.82 | 24489116 | |
198 | Acetylation | APYVVIGKPSLSSIR CCEEEECCCCHHHHH | 21.95 | 24489116 | |
278 | Phosphorylation | FKLNREVSGFGSLNR CCCCCCCCCCCHHHH | 24.53 | 20190278 | |
282 | Phosphorylation | REVSGFGSLNRLRKI CCCCCCCHHHHHHHH | 21.88 | 30377154 |
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 RLP7_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RLP7_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 RLP7_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-14; THR-120 AND SER-278,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-278, 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 THR-120, AND MASSSPECTROMETRY. |