UniProt ID | RRP9_YEAST | |
---|---|---|
UniProt AC | Q06506 | |
Protein Name | Ribosomal RNA-processing protein 9 | |
Gene Name | RRP9 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 573 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in nucleolar processing of pre-18S ribosomal RNA. Required for efficient pre-rRNA cleavage at sites A0, A1 and A2, and biosynthesis of 18S rRNA.. | |
Protein Sequence | MSDVTQQKKRKRSKGEVNPSKPTVDEEITDPSSNEDEQLEVSDEEDALESEEEFEGENPADKRRRLAKQYLENLKSEANDILTDNRNAEEKDLNNLKERTIDEYNNFDAGDLDKDIIASRLKEDVAEQQGRVFRYFGDKLLISEAKQSFTRVGENNLTCISCFQPVLNKYTFEESSNGDKNKGRLFAYTVSKDLQLTKYDITDFSKRPKKLKYAKGGAKYIPTSKHEYENTTEGHYDEILTVAASPDGKYVVTGGRDRKLIVWSTESLSPVKVIPTKDRRGEVLSLAFRKNSDQLYASCADFKIRTYSINQFSQLEILYGHHDIVEDISALAMERCVTVGARDRTAMLWKIPDETRLTFRGGDEPQKLLRRWMKENAKEGEDGEVKYPDESEAPLFFCEGSIDVVSMVDDFHFITGSDNGNICLWSLAKKKPIFTERIAHGILPEPSFNDISGETDEELRKRQLQGKKLLQPFWITSLYAIPYSNVFISGSWSGSLKVWKISDNLRSFELLGELSGAKGVVTKIQVVESGKHGKEKFRILASIAKEHRLGRWIANVSGARNGIYSAVIDQTGF | |
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 | ------MSDVTQQKK ------CCHHHHHHH | 40.56 | 22814378 | |
2 | Phosphorylation | ------MSDVTQQKK ------CCHHHHHHH | 40.56 | 27717283 | |
29 | Phosphorylation | PTVDEEITDPSSNED CCCCCCCCCCCCCCC | 45.17 | 19795423 | |
50 | Phosphorylation | DEEDALESEEEFEGE CHHHHHHCHHHHCCC | 51.67 | 28889911 | |
68 | Acetylation | DKRRRLAKQYLENLK HHHHHHHHHHHHHHH | 44.03 | 25381059 | |
70 | Phosphorylation | RRRLAKQYLENLKSE HHHHHHHHHHHHHHH | 18.44 | 19779198 | |
76 | Phosphorylation | QYLENLKSEANDILT HHHHHHHHHHHHHHC | 45.14 | 21440633 | |
100 | Phosphorylation | LNNLKERTIDEYNNF HHHHHHHCHHHHCCC | 33.59 | 20377248 | |
104 | Phosphorylation | KERTIDEYNNFDAGD HHHCHHHHCCCCHHH | 16.20 | 21440633 | |
114 | Acetylation | FDAGDLDKDIIASRL CCHHHCCHHHHHHHH | 59.11 | 24489116 | |
175 | Phosphorylation | NKYTFEESSNGDKNK HCCCCEECCCCCCCC | 23.16 | 27717283 | |
176 | Phosphorylation | KYTFEESSNGDKNKG CCCCEECCCCCCCCC | 48.38 | 23749301 | |
198 | Ubiquitination | SKDLQLTKYDITDFS CCCCCCCCCCCCCCC | 49.90 | 24961812 | |
269 | Phosphorylation | VWSTESLSPVKVIPT EEECCCCCCCEEEEC | 36.61 | 28152593 | |
290 | Ubiquitination | VLSLAFRKNSDQLYA EEEEEEECCCCHHHH | 55.11 | 23749301 |
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 RRP9_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRP9_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 RRP9_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-50, AND MASSSPECTROMETRY. |