UniProt ID | FNTB_YEAST | |
---|---|---|
UniProt AC | P22007 | |
Protein Name | Protein farnesyltransferase subunit beta | |
Gene Name | RAM1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 431 | |
Subcellular Localization | ||
Protein Description | Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins such as a-factor and RAS. The beta subunit is responsible for peptide-binding.. | |
Protein Sequence | MRQRVGRSIARAKFINTALLGRKRPVMERVVDIAHVDSSKAIQPLMKELETDTTEARYKVLQSVLEIYDDEKNIEPALTKEFHKMYLDVAFEISLPPQMTALDASQPWMLYWIANSLKVMDRDWLSDDTKRKIVDKLFTISPSGGPFGGGPGQLSHLASTYAAINALSLCDNIDGCWDRIDRKGIYQWLISLKEPNGGFKTCLEVGEVDTRGIYCALSIATLLNILTEELTEGVLNYLKNCQNYEGGFGSCPHVDEAHGGYTFCATASLAILRSMDQINVEKLLEWSSARQLQEERGFCGRSNKLVDGCYSFWVGGSAAILEAFGYGQCFNKHALRDYILYCCQEKEQPGLRDKPGAHSDFYHTNYCLLGLAVAESSYSCTPNDSPHNIKCTPDRLIGSSKLTDVNPVYGLPIENVRKIIHYFKSNLSSPS | |
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 |
---|---|---|---|---|---|
17 | Phosphorylation | ARAKFINTALLGRKR HHHHHHHHHHHCCCC | 17.54 | 28889911 | |
38 | Phosphorylation | VDIAHVDSSKAIQPL EEEHHCCCHHHHHHH | 32.42 | 22369663 | |
39 | Phosphorylation | DIAHVDSSKAIQPLM EEHHCCCHHHHHHHH | 22.95 | 22369663 | |
40 | Acetylation | IAHVDSSKAIQPLMK EHHCCCHHHHHHHHH | 54.16 | 24489116 | |
424 | Acetylation | RKIIHYFKSNLSSPS HHHHHHHHHCCCCCC | 31.13 | 24489116 | |
429 | Phosphorylation | YFKSNLSSPS----- HHHHCCCCCC----- | 32.12 | 25521595 |
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 FNTB_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FNTB_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 FNTB_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-17 AND SER-38, AND MASSSPECTROMETRY. |