UniProt ID | ECM1_YEAST | |
---|---|---|
UniProt AC | P39715 | |
Protein Name | Shuttling pre-60S factor ECM1 | |
Gene Name | ECM1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 212 | |
Subcellular Localization | Nucleus, nucleolus. Nucleus. Cytoplasm. Shuttles between the nucleus and the cytoplasm and is re-imported by the KAP123 karyopherin. | |
Protein Description | Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus.. | |
Protein Sequence | MWEQRRQKVVFSLTILVRYRLKQSMAKKISKNSRAARQSDALEPEVKDLSELPRAEKTDLTNILIRTAAKNEALLEAKISKKANKSKRGKKLNKKALEDKLANSISSMDRDRLVKALNFTNRLDGKIAKSISRAKYIQNTRKAGWDSTNETIKKELAFLNGGLSVQAKSASEGNAEKEDEEIPEVFDSLAEDNTVQKTPTNRFGVLPDDVEE | |
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 |
---|---|---|---|---|---|
33 | Phosphorylation | AKKISKNSRAARQSD HHHHHHCHHHHHHHH | 27.34 | 19823750 | |
39 | Phosphorylation | NSRAARQSDALEPEV CHHHHHHHHCCCHHH | 21.21 | 21440633 | |
57 | Acetylation | SELPRAEKTDLTNIL HHCCCCCCCCHHHHH | 46.48 | 22865919 | |
70 | Acetylation | ILIRTAAKNEALLEA HHHHHHHHCHHHHHH | 53.51 | 22865919 | |
104 | Phosphorylation | LEDKLANSISSMDRD HHHHHHHHHHHCCHH | 20.45 | 30377154 | |
106 | Phosphorylation | DKLANSISSMDRDRL HHHHHHHHHCCHHHH | 21.30 | 30377154 | |
107 | Phosphorylation | KLANSISSMDRDRLV HHHHHHHHCCHHHHH | 24.04 | 30377154 | |
115 | Acetylation | MDRDRLVKALNFTNR CCHHHHHHHHHHHHC | 52.31 | 25381059 | |
126 | Acetylation | FTNRLDGKIAKSISR HHHCCCHHHHHHHHH | 38.87 | 25381059 | |
129 | Acetylation | RLDGKIAKSISRAKY CCCHHHHHHHHHHHH | 52.36 | 25381059 | |
135 | Acetylation | AKSISRAKYIQNTRK HHHHHHHHHHHHHHH | 41.60 | 25381059 | |
147 | Phosphorylation | TRKAGWDSTNETIKK HHHCCCCCCCHHHHH | 26.99 | 21440633 | |
148 | Phosphorylation | RKAGWDSTNETIKKE HHCCCCCCCHHHHHH | 34.30 | 27717283 | |
151 | Phosphorylation | GWDSTNETIKKELAF CCCCCCHHHHHHHHH | 39.92 | 27717283 | |
164 | Phosphorylation | AFLNGGLSVQAKSAS HHHCCCEEEEEECCC | 18.56 | 30377154 | |
169 | Phosphorylation | GLSVQAKSASEGNAE CEEEEEECCCCCCCC | 39.79 | 19779198 | |
171 | Phosphorylation | SVQAKSASEGNAEKE EEEEECCCCCCCCCC | 53.80 | 21440633 | |
177 | Acetylation | ASEGNAEKEDEEIPE CCCCCCCCCHHCHHH | 68.97 | 24489116 | |
188 | Phosphorylation | EIPEVFDSLAEDNTV CHHHHHHHHHCCCCC | 20.29 | 17563356 | |
194 | Phosphorylation | DSLAEDNTVQKTPTN HHHHCCCCCCCCCCC | 36.31 | 28132839 | |
198 | Phosphorylation | EDNTVQKTPTNRFGV CCCCCCCCCCCCCCC | 20.46 | 28132839 |
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 ECM1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ECM1_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 ECM1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-188, AND MASSSPECTROMETRY. |