UniProt ID | RLI1_YEAST | |
---|---|---|
UniProt AC | Q03195 | |
Protein Name | Translation initiation factor RLI1 | |
Gene Name | RLI1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 608 | |
Subcellular Localization | Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm. | |
Protein Description | Component of the multifactor complex (MFC) involved in translation initiation. Required for the binding of MFC to the 40S ribosome. Required for the processing and nuclear export of the 60S and 40S ribosomal subunits.. | |
Protein Sequence | MSDKNSRIAIVSADKCKPKKCRQECKRSCPVVKTGKLCIEVTPTSKIAFISEILCIGCGICVKKCPFDAIQIINLPTNLEAHVTHRYSANSFKLHRLPTPRPGQVLGLVGTNGIGKSTALKILAGKQKPNLGRFDDPPEWQEIIKYFRGSELQNYFTKMLEDDIKAIIKPQYVDNIPRAIKGPVQKVGELLKLRMEKSPEDVKRYIKILQLENVLKRDIEKLSGGELQRFAIGMSCVQEADVYMFDEPSSYLDVKQRLNAAQIIRSLLAPTKYVICVEHDLSVLDYLSDFVCIIYGVPSVYGVVTLPASVREGINIFLDGHIPAENLRFRTEALQFRIADATEDLQNDSASRAFSYPSLKKTQGDFVLNVEEGEFSDSEILVMMGENGTGKTTLIKLLAGALKPDEGQDIPKLNVSMKPQKIAPKFPGTVRQLFFKKIRGQFLNPQFQTDVVKPLRIDDIIDQEVQHLSGGELQRVAIVLALGIPADIYLIDEPSAYLDSEQRIICSKVIRRFILHNKKTAFIVEHDFIMATYLADKVIVFEGIPSKNAHARAPESLLTGCNRFLKNLNVTFRRDPNSFRPRINKLDSQMDKEQKSSGNYFFLDNTGI | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MSDKNSRIAIVSA --CCCCCCCEEEEEC | 30.70 | 27717283 | |
12 | Phosphorylation | NSRIAIVSADKCKPK CCCEEEEECCCCCCH | 25.33 | 27717283 | |
36 | Acetylation | CPVVKTGKLCIEVTP CCEEECCCEEEEECC | 45.47 | 24489116 | |
121 | Acetylation | IGKSTALKILAGKQK CCHHHHHHHHCCCCC | 32.96 | 22865919 | |
165 | Acetylation | KMLEDDIKAIIKPQY HHHHHHHHHHHCHHH | 40.29 | 24489116 | |
186 | Acetylation | AIKGPVQKVGELLKL HHCCHHHHHHHHHHH | 53.06 | 24489116 | |
192 | Acetylation | QKVGELLKLRMEKSP HHHHHHHHHHCCCCH | 46.82 | 24489116 | |
207 | Acetylation | EDVKRYIKILQLENV HHHHHHHHHHHHHHH | 28.56 | 24489116 | |
216 | Acetylation | LQLENVLKRDIEKLS HHHHHHHHHHHHHHC | 43.68 | 24489116 | |
221 | Acetylation | VLKRDIEKLSGGELQ HHHHHHHHHCCCCCC | 48.57 | 24489116 | |
221 | Ubiquitination | VLKRDIEKLSGGELQ HHHHHHHHHCCCCCC | 48.57 | 23749301 | |
342 | Phosphorylation | QFRIADATEDLQNDS EEECCCCCHHHCCCC | 30.49 | 28889911 | |
349 | Phosphorylation | TEDLQNDSASRAFSY CHHHCCCCCCHHCCC | 35.38 | 22369663 | |
351 | Phosphorylation | DLQNDSASRAFSYPS HHCCCCCCHHCCCHH | 28.26 | 22369663 | |
355 | Phosphorylation | DSASRAFSYPSLKKT CCCCHHCCCHHHCCC | 34.84 | 27214570 | |
396 | Acetylation | TGKTTLIKLLAGALK CCHHHHHHHHHCCCC | 40.33 | 24489116 | |
403 | Acetylation | KLLAGALKPDEGQDI HHHHCCCCCCCCCCC | 50.30 | 24489116 | |
425 | Acetylation | KPQKIAPKFPGTVRQ CHHHCCCCCCHHHHH | 55.99 | 24489116 | |
508 | Ubiquitination | EQRIICSKVIRRFIL HHHHHHHHHHHHHHH | 36.95 | 23749301 | |
566 | Acetylation | TGCNRFLKNLNVTFR HHHHHHHHHCCCEEC | 57.59 | 22865919 |
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 RLI1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RLI1_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 RLI1_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 THR-342; SER-349 ANDSER-351, AND MASS SPECTROMETRY. |