UniProt ID | TRM44_YEAST | |
---|---|---|
UniProt AC | Q02648 | |
Protein Name | tRNA (uracil-O(2)-)-methyltransferase | |
Gene Name | TRM44 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 567 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | tRNA (uracil-O(2)-)-methyltransferase, which catalyzes the formation of O(2)-methyluracil at position 44 (Um44) in tRNA(Ser).. | |
Protein Sequence | MTGDGSAHISKNNQNQHKDRFKFIVNDKSILGPQWLSLYQTDGKVTFAKSHFEQAMMNVIREPNINSTVILRADILKEINHAAEAGSEPKFDESVLKKFEIDNGNESGEEDVKKINIEDLNIRSCETSESLKLSPVHEFVRRIIPRNFYKDAIINQTCLILNSKDPNFQETSLIVYTPHINSEKDCPFYIPRTQSVGILLHQSVLSVHYIPFPEDKTAFTDESERVVRTAYRLLQTANKHSKGVMQGYEKRVNHDQVVNKVNFQNTYIVLKKKYSKFLVENWAESTDPKKHVFEDIAIAAFLIELWIKVYGPDFRSKMQFRDLGCGNGALCYILLSESIKGLGIDARKRKSWSIYPPEVQSSLKEQVIIPSILLRPHPALKRQVPHLEHNGRFFPVKVTHEVIAPATVVYSSEDLLKSPQVNTAEFPPDTFIIGNHSDELTCWIPLLGHPYMVIPCCSHNFSGQRVRFNVRKRSPRSNEIKNQNNSKSTYSGLVDHVEYISSRVGWKVEKEMLRIPSTRNAAIIGVENATLKHFPTQAVYDMIWEDGGAEGWIQNTMSLLKRNPRNH | |
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 |
---|---|---|---|---|---|
22 | Acetylation | NQHKDRFKFIVNDKS CCCCCCEEEEECCCC | 34.77 | 24489116 | |
87 | Phosphorylation | NHAAEAGSEPKFDES HHHHHCCCCCCCCHH | 58.75 | 30377154 | |
107 | Phosphorylation | EIDNGNESGEEDVKK EECCCCCCCCHHHHH | 56.35 | 22369663 |
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 TRM44_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRM44_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 TRM44_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-107, AND MASSSPECTROMETRY. | |
"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-107, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASSSPECTROMETRY. |