UniProt ID | FES1_YEAST | |
---|---|---|
UniProt AC | P38260 | |
Protein Name | Hsp70 nucleotide exchange factor FES1 | |
Gene Name | FES1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 290 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Involved in protein translation, propagation of [PSI+] prions, and polyamine tolerance. Functions as a nucleotide exchange factor (NEF), which accelerates the release of ADP, for the cytosolic Hsp70 chaperone SSA1 and the ribosome-associated Hsp70 chaperone SSB1. Required for fully efficient Hsp70-mediated folding of proteins.. | |
Protein Sequence | MEKLLQWSIANSQGDKEAMARAGQPDPKLLQQLFGGGGPDDPTLMKESMAVIMNPEVDLETKLVAFDNFEMLIENLDNANNIENLKLWEPLLDVLVQTKDEELRAAALSIIGTAVQNNLDSQNNFMKYDNGLRSLIEIASDKTKPLDVRTKAFYALSNLIRNHKDISEKFFKLNGLDCIAPVLSDNTAKPKLKMRAIALLTAYLSSVKIDENIISVLRKDGVIESTIECLSDESNLNIIDRVLSFLSHLISSGIKFNEQELHKLNEGYKHIEPLKDRLNEDDYLAVKYVL | |
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 |
---|---|---|---|---|---|
3 | Ubiquitination | -----MEKLLQWSIA -----CHHHHHHHHH | 53.88 | 24961812 | |
12 | Phosphorylation | LQWSIANSQGDKEAM HHHHHHCCCCCHHHH | 26.90 | 25752575 | |
16 | Acetylation | IANSQGDKEAMARAG HHCCCCCHHHHHHCC | 54.95 | 24489116 | |
16 | Ubiquitination | IANSQGDKEAMARAG HHCCCCCHHHHHHCC | 54.95 | 23749301 | |
28 | Ubiquitination | RAGQPDPKLLQQLFG HCCCCCHHHHHHHHC | 70.03 | 23749301 | |
45 | Sulfoxidation | GPDDPTLMKESMAVI CCCCCHHHHHHCCHH | 5.08 | 31806703 | |
49 | Sulfoxidation | PTLMKESMAVIMNPE CHHHHHHCCHHCCCC | 3.46 | 31806703 | |
53 | Sulfoxidation | KESMAVIMNPEVDLE HHHCCHHCCCCCCCC | 5.71 | 31806703 | |
142 | Acetylation | LIEIASDKTKPLDVR HHHHHCCCCCCCCHH | 56.82 | 24489116 | |
143 | Phosphorylation | IEIASDKTKPLDVRT HHHHCCCCCCCCHHH | 42.77 | 28889911 | |
151 | Acetylation | KPLDVRTKAFYALSN CCCCHHHHHHHHHHH | 26.40 | 24489116 | |
157 | Phosphorylation | TKAFYALSNLIRNHK HHHHHHHHHHHHCCC | 22.78 | 19779198 | |
169 | Acetylation | NHKDISEKFFKLNGL CCCCHHHHHHHHCCC | 49.67 | 24489116 | |
225 | Phosphorylation | RKDGVIESTIECLSD HHCCCCHHHHHHCCC | 24.46 | 28889911 | |
231 | Phosphorylation | ESTIECLSDESNLNI HHHHHHCCCCCCCHH | 51.49 | 28889911 | |
234 | Phosphorylation | IECLSDESNLNIIDR HHHCCCCCCCHHHHH | 52.16 | 28889911 | |
263 | Acetylation | FNEQELHKLNEGYKH CCHHHHHHHCCCCCC | 66.68 | 24489116 | |
269 | Acetylation | HKLNEGYKHIEPLKD HHHCCCCCCCCCHHH | 49.30 | 24489116 |
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 FES1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FES1_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 FES1_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-12, AND MASSSPECTROMETRY. |