UniProt ID | RRP8_YEAST | |
---|---|---|
UniProt AC | P38961 | |
Protein Name | 25S rRNA (adenine(645)-N(1))-methyltransferase | |
Gene Name | RRP8 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 392 | |
Subcellular Localization | Nucleus, nucleolus . Chromosome, telomere . | |
Protein Description | S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the N(1) position of adenine 645 in 25S rRNA. Required both for ribosomal 40S and 60S subunits biogenesis. Required for efficient pre-rRNA cleavage at site A2. Also involved in telomere length regulation and maintenance.. | |
Protein Sequence | MALFNVEGWSIKTKTVAFDNKTNKSSKDKKKNNRKNGKLTREQKLKEETEAELKEQVEDIPSEGSVAKDIPKKNQEKSDQNETSKKRKHDEEAPLMQVKENIEKPTKKQLTPLQQKMMAKLTGSRFRWINEQLYTISSDEALKLIKEQPQLFDEYHDGFRSQVQAWPENPVDVFVDQIRYRCMKPVNAPGGLPGLKDSKEIVIADMGCGEAQLALEINNFFKNYNKKAKKYLKRRHKVHSFDLKKANERITVADIRNVPLPDESCTIVVFCLALMGTNFLDFIKEAYRILAPRGELWIAEIKSRFSDGKGNEFVDALKLMGFFHKKTFDENKMFTRFEFFKPPAEIIEERRQKLERRQKFIEVETEKEELEKKRRKIAEGKWLLKPCIYKRR | |
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 |
---|---|---|---|---|---|
12 | Acetylation | NVEGWSIKTKTVAFD EEECEEEEEEEEEEE | 38.15 | 25381059 | |
21 | Acetylation | KTVAFDNKTNKSSKD EEEEEECCCCCCHHH | 56.15 | 25381059 | |
62 | Phosphorylation | EQVEDIPSEGSVAKD HHHHCCCCCCCCCCC | 55.73 | 25521595 | |
65 | Phosphorylation | EDIPSEGSVAKDIPK HCCCCCCCCCCCCCC | 18.17 | 20377248 | |
68 | Acetylation | PSEGSVAKDIPKKNQ CCCCCCCCCCCCCCH | 54.77 | 24489116 | |
84 | Phosphorylation | KSDQNETSKKRKHDE HCCCCHHHHHHHCCC | 29.96 | 27017623 | |
107 | Acetylation | ENIEKPTKKQLTPLQ HHHCCCCHHHCCHHH | 47.23 | 25381059 | |
196 | Succinylation | PGGLPGLKDSKEIVI CCCCCCCCCCCEEEE | 66.91 | 23954790 | |
359 | Acetylation | QKLERRQKFIEVETE HHHHHHHHHHHHHHH | 46.64 | 22865919 | |
372 | Acetylation | TEKEELEKKRRKIAE HHHHHHHHHHHHHHC | 65.29 | 24489116 | |
381 | Acetylation | RRKIAEGKWLLKPCI HHHHHCCCCCCCCCC | 26.61 | 22865919 | |
385 | Acetylation | AEGKWLLKPCIYKRR HCCCCCCCCCCCCCC | 35.36 | 24489116 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of RRP8_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRP8_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 RRP8_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-62, AND MASSSPECTROMETRY. |