UniProt ID | RIA1_YEAST | |
---|---|---|
UniProt AC | P53893 | |
Protein Name | Ribosome assembly protein 1 | |
Gene Name | RIA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1110 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | GTPase involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with SDO1, may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating TIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Inhibits GTPase activity of ribosome-bound EF-2.. | |
Protein Sequence | MPRVESETYKRLQNDPSCIRNICIVAHVDHGKTSLSDSLLASNGIISQRLAGKIRFLDARPDEQLRGITMESSAISLYFRVLRKQEGSDEPLVSEHLVNLIDSPGHIDFSSEVSAASRLCDGAVVLVDVVEGVCSQTVTVLRQCWTEKLKPILVLNKIDRLITELQLTPQEAYIHLSKVIEQVNSVIGSFFANERQLDDLFWREQLEKNENAEYIEKDDSGIYFNPTDNNVIFASAIDGWGFNIGQLAKFYEQKLGAKRENLQKVLWGDFYMDPKTKKIINNKGLKGRSLKPLFTSLILENIWKIYQNIITSRDSEMVEKIAKTLNIKLLARDLRSKDDKQLLRTIMGQWLPVSTAVLLTVIEKLPSPLESQTDRLNTILVSESDTAAMDPRLLKAMKTCDKEGPVSAYVSKMLSIPREELPVESKRIASSDELMERSRKAREEALNAAKHAGMVENMAMMDLNDNSKNTSDLYKRAKDTVMTPEVGEQTKPKPSRNNDVFCVVSEPSSALDLEFEYEGEDDSDSQDNFGLDFVPTDIDPNDPLSSMFEYEEEDPLLESIKQISEDVNDEVDDIFDEKEECLVAFARIYSGTLRVGQEISVLGPKYDPKCPEEHIETAIITHLYLFMGKELVPLDVCPSGNIVGIRGLAGKVLKSGTLIEKGVQGVNLAGVNFHFTPIVRVAVEPANPVEMSKLVRGLKLLDQADPCVHTYVENTGEHILCTAGELHLERCLKDLTERFAGIEITHSEPAIPYRETFLSASDMNPPQNSQLGRGVHELLLSQYKITFRTFPLSGKVTDFLSQHQNSIKNILKTSTSSMDPVIESTGSSFLDKKSLLVAFEEVINQEEKSRELLSGFKVKLAGFGPSRVGCNILLSQDNLLGSLFEGTPAAFEYSDSIKNGFQLAVSEGPLANEPVQGMCVLVESVHKMSQDEIESIEDPRYQQHIVDLSGRLITSTRDAIHEAFLDWSPRIMWAIYSCDIQTSVDVLGKVYAVILQRHGKIISEEMKEGTPFFQIEAHVPVVEAFGLSEDIRKRTSGAAQPQLVFSGFECIDLDPFWVPTTEEELEELGDTADRENIARKHMNAIRRRKGLFIEEKVVENAEKQRTLKKN | |
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 |
---|---|---|---|---|---|
157 | Acetylation | KPILVLNKIDRLITE HHEEEHHHHHHHHHH | 41.65 | 24489116 | |
275 | Acetylation | GDFYMDPKTKKIINN CCCCCCHHHHHHHCC | 69.57 | 24489116 | |
430 | Phosphorylation | VESKRIASSDELMER CCCHHHCCHHHHHHH | 35.63 | 22369663 | |
431 | Phosphorylation | ESKRIASSDELMERS CCHHHCCHHHHHHHH | 26.53 | 22369663 | |
475 | Ubiquitination | KNTSDLYKRAKDTVM CCHHHHHHHHHHCCC | 53.85 | 21427232 | |
480 | Phosphorylation | LYKRAKDTVMTPEVG HHHHHHHCCCCCCCC | 16.09 | 29136822 | |
483 | Phosphorylation | RAKDTVMTPEVGEQT HHHHCCCCCCCCCCC | 16.38 | 29136822 | |
797 | Phosphorylation | FPLSGKVTDFLSQHQ ECCCCHHHHHHHHHH | 25.23 | 19823750 | |
801 | Phosphorylation | GKVTDFLSQHQNSIK CHHHHHHHHHHHHHH | 26.13 | 19823750 | |
806 | Phosphorylation | FLSQHQNSIKNILKT HHHHHHHHHHHHHHH | 28.50 | 19823750 | |
813 | Phosphorylation | SIKNILKTSTSSMDP HHHHHHHHCCCCCCH | 33.52 | 19823750 | |
814 | Phosphorylation | IKNILKTSTSSMDPV HHHHHHHCCCCCCHH | 25.38 | 19823750 | |
815 | Phosphorylation | KNILKTSTSSMDPVI HHHHHHCCCCCCHHH | 30.01 | 19823750 | |
816 | Phosphorylation | NILKTSTSSMDPVIE HHHHHCCCCCCHHHH | 24.35 | 19823750 | |
817 | Phosphorylation | ILKTSTSSMDPVIES HHHHCCCCCCHHHHC | 27.56 | 19823750 |
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 RIA1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIA1_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 RIA1_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-430 AND SER-431, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, AND MASSSPECTROMETRY. |