UniProt ID | RRP14_YEAST | |
---|---|---|
UniProt AC | P36080 | |
Protein Name | Ribosomal RNA-processing protein 14 | |
Gene Name | RRP14 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 434 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in ribosome biogenesis and cell polarity. Required for the synthesis of both 40S and 60S ribosomal subunits and may also play some direct role in correct positioning of the mitotic spindle during mitosis.. | |
Protein Sequence | MSNSLEERLRANSSAFDGLLALIPAKYYYDEKSQEQWKAKKKTKEQSKNDKLKKLDPEQRDDETSSTLEVMKKKEKDAKPVVLPGEKFKHMKMQKQKEATSKVEGDSDLNVEVNDPMIIAPDEDEEEEEDIKVIFDDEGNEIPLESKKDTTEPDRSVEKKSITEEEKLQRKKNLEALRSKLQAKISDMKSKRKAPGSREAILAQRKRKEELKKRKRLESEQEQDQDEIASDSDMEDIDSDLENNSKKRFKKGKKDSEINADGVMFQNIIFDDGARATSDLQRLRKAGRTKGPAKNDVKSHLKLLEAKKNKMEAKDELEQIKQKEKEKWQKAMLQAEGIKIRDDEKLLRKAIKRKEAQKRKSAIEWSERKRVVEDTISERQKRREENLRIRKDNKGKKRNKQEKMKRKYVGSAVPKKRAGFEGRLKTGKKKGGPK | |
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 | ------MSNSLEERL ------CCCCHHHHH | 34.82 | 22814378 | |
4 | Phosphorylation | ----MSNSLEERLRA ----CCCCHHHHHHH | 29.83 | 30377154 | |
13 | Phosphorylation | EERLRANSSAFDGLL HHHHHHCCHHHHHHH | 23.27 | 28889911 | |
14 | Phosphorylation | ERLRANSSAFDGLLA HHHHHCCHHHHHHHH | 32.53 | 30377154 | |
54 | Acetylation | SKNDKLKKLDPEQRD HHCHHHHCCCHHHCC | 69.43 | 22865919 | |
64 | Phosphorylation | PEQRDDETSSTLEVM HHHCCCCCCHHHHHH | 34.66 | 30377154 | |
65 | Phosphorylation | EQRDDETSSTLEVMK HHCCCCCCHHHHHHH | 21.19 | 30377154 | |
66 | Phosphorylation | QRDDETSSTLEVMKK HCCCCCCHHHHHHHH | 44.42 | 30377154 | |
87 | Acetylation | PVVLPGEKFKHMKMQ CCCCCCHHHHHHHHH | 66.67 | 24489116 | |
100 | Phosphorylation | MQKQKEATSKVEGDS HHHHHHHHHCCCCCC | 30.12 | 24961812 | |
101 | Phosphorylation | QKQKEATSKVEGDSD HHHHHHHHCCCCCCC | 41.57 | 24961812 | |
107 | Phosphorylation | TSKVEGDSDLNVEVN HHCCCCCCCCCCEEC | 55.65 | 22369663 | |
156 | Phosphorylation | DTTEPDRSVEKKSIT CCCCCCCCCCCCCCC | 41.84 | 27717283 | |
184 | Acetylation | LRSKLQAKISDMKSK HHHHHHHHHHHHHHH | 29.77 | 25381059 | |
219 | Phosphorylation | KKRKRLESEQEQDQD HHHHHHHHHHHHCHH | 49.53 | 19823750 | |
230 | Phosphorylation | QDQDEIASDSDMEDI HCHHHHHCCCCHHHH | 43.22 | 22369663 | |
232 | Phosphorylation | QDEIASDSDMEDIDS HHHHHCCCCHHHHHH | 36.04 | 22369663 | |
239 | Phosphorylation | SDMEDIDSDLENNSK CCHHHHHHHHHHHHH | 44.42 | 22369663 | |
245 | Phosphorylation | DSDLENNSKKRFKKG HHHHHHHHHHHHHCC | 51.65 | 19823750 | |
277 | Phosphorylation | FDDGARATSDLQRLR ECCCCCCCHHHHHHH | 19.74 | 28889911 | |
278 | Phosphorylation | DDGARATSDLQRLRK CCCCCCCHHHHHHHH | 35.03 | 28889911 | |
407 | Acetylation | KQEKMKRKYVGSAVP HHHHHHHHHCCCCCC | 38.48 | 25381059 | |
411 | Phosphorylation | MKRKYVGSAVPKKRA HHHHHCCCCCCCCCC | 18.95 | 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 RRP14_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RRP14_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 RRP14_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-239, AND MASSSPECTROMETRY. |