| UniProt ID | RKM4_YEAST | |
|---|---|---|
| UniProt AC | Q12504 | |
| Protein Name | Ribosomal lysine N-methyltransferase 4 {ECO:0000303|PubMed:18957409} | |
| Gene Name | RKM4 {ECO:0000303|PubMed:18957409} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 494 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L42 (RPL42A and RPL42B) at 'Lys-55'.. | |
| Protein Sequence | MDDFSRDTENFVCWLKTTAEIEVSPKIEIKDLCCDNQGRAVVATQKIKKDETLFKIPRSSVLSVTTSQLIKDYPSLKDKFLNETGSWEGLIICILYEMEVLQERSRWAPYFKVWNKPSDMNALIFWDDNELQLLKPSLVLERIGKKEAKEMHERIIKSIKQIGGEFSRVATSFEFDNFAYIASIILSYSFDLEMQDSSVNENEEEETSEEELENERYLKSMIPLADMLNADTSKCNANLTYDSNCLKMVALRDIEKNEQVYNIYGEHPNSELLRRYGYVEWDGSKYDFGEVLLENIVEALKETFETNTEFLDRCIDILRNNANIQEFLEGEEIVLDSYDCYNNGELLPQLILLVQILTILCQIPGLCKLDIKAMERQVERIVKKCLQLIEGARATTNCSATWKRCIMKRLADYPIKKCVSIEKPSKGNSLTREELRDVMARRVLKSEIDSLQVCEETIDKNYKVIPDEKLLTNILKRKLTEEEKSSVKRPCVKK | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | QGRAVVATQKIKKDE CCCEEEEEEEECCCC | 20.84 | 28889911 | |
| 55 | Acetylation | KKDETLFKIPRSSVL CCCCCCCCCCHHHHC | 55.71 | 22865919 | |
| 59 | Phosphorylation | TLFKIPRSSVLSVTT CCCCCCHHHHCEEEH | 21.31 | 19823750 | |
| 60 | Phosphorylation | LFKIPRSSVLSVTTS CCCCCHHHHCEEEHH | 28.49 | 19823750 | |
| 63 | Phosphorylation | IPRSSVLSVTTSQLI CCHHHHCEEEHHHHH | 18.43 | 19823750 | |
| 65 | Phosphorylation | RSSVLSVTTSQLIKD HHHHCEEEHHHHHHH | 19.84 | 19823750 | |
| 66 | Phosphorylation | SSVLSVTTSQLIKDY HHHCEEEHHHHHHHC | 16.60 | 19823750 | |
| 67 | Phosphorylation | SVLSVTTSQLIKDYP HHCEEEHHHHHHHCH | 17.39 | 19823750 | |
| 217 | Phosphorylation | EELENERYLKSMIPL HHHHHHHHHHHHHHH | 16.59 | 27017623 | |
| 220 | Phosphorylation | ENERYLKSMIPLADM HHHHHHHHHHHHHHH | 21.25 | 27017623 | |
| 233 | Phosphorylation | DMLNADTSKCNANLT HHHCCCCCCCCCCCC | 35.44 | 27017623 | |
| 469 | Acetylation | YKVIPDEKLLTNILK CCCCCCHHHHHHHHH | 57.06 | 24489116 | |
| 480 | Phosphorylation | NILKRKLTEEEKSSV HHHHHCCCHHHHHHC | 44.37 | 27214570 |
| 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 RKM4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RKM4_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 RKM4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-44, AND MASSSPECTROMETRY. | |