UniProt ID | SLF1_YEAST | |
---|---|---|
UniProt AC | Q12034 | |
Protein Name | Protein SLF1 | |
Gene Name | SLF1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 447 | |
Subcellular Localization | ||
Protein Description | Regulates the copper-dependent mineralization of copper sulfide complexes on the cell surface in cells cultured in medium containing copper salts.. | |
Protein Sequence | MSSQNLNDNPKNTSSAAEDKKKQTSSLKLAPIPTTSPWKSSSPDSNTVIPVEELRDISKTAKPSKNGSGSIKLTSNTKWTPITPSVIISGSKDTNSKSGKNSKNSKTNKKMKKRGKYNNDINKKDFNGQTNSTSEISNVSNLESKPLDANAKVNIHSSSGATANGNIKRITNNNNSTNGRQSRNYQNRNGKTRYNNNSRHSQAANNAISFPNNYQARPEYIPNASHWLNNNSRNSYKQLSYFRQQQYYNNINYQQQLQTPYYYSMEPIFKSIESIKNQIEFYFSEENLKTDEFLRSKFKKANDGFIPMSLIGKFYRMVNLSLGGDPNLILASMREVLQHKETNHLEIALGSIEGAQKNMADDFNPLENYFIRRENWAEYAMESNFDENDDETEKYNIEKLLGPNDLDNYSYMGYPNFFPSNENGKKSQSYDQGEISRQFEQNLQIND | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSSQNLNDN ------CCCCCCCCC | 40.40 | 30377154 | |
40 | Phosphorylation | PTTSPWKSSSPDSNT CCCCCCCCCCCCCCC | 31.98 | 22369663 | |
41 | Phosphorylation | TTSPWKSSSPDSNTV CCCCCCCCCCCCCCE | 42.01 | 22369663 | |
42 | Phosphorylation | TSPWKSSSPDSNTVI CCCCCCCCCCCCCEE | 39.56 | 22369663 | |
45 | Phosphorylation | WKSSSPDSNTVIPVE CCCCCCCCCCEEEHH | 37.47 | 22369663 | |
47 | Phosphorylation | SSSPDSNTVIPVEEL CCCCCCCCEEEHHHH | 24.62 | 22369663 | |
133 | Phosphorylation | FNGQTNSTSEISNVS CCCCCCCCHHCCCCC | 32.23 | 28889911 | |
134 | Phosphorylation | NGQTNSTSEISNVSN CCCCCCCHHCCCCCC | 32.52 | 28889911 | |
176 | Phosphorylation | RITNNNNSTNGRQSR ECCCCCCCCCCCCCC | 25.93 | 21551504 | |
182 | Phosphorylation | NSTNGRQSRNYQNRN CCCCCCCCCCCCCCC | 22.57 | 21551504 | |
427 | Phosphorylation | SNENGKKSQSYDQGE CCCCCCCCCCCCHHH | 28.04 | 23749301 | |
429 | Phosphorylation | ENGKKSQSYDQGEIS CCCCCCCCCCHHHHH | 37.45 | 28889911 |
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 SLF1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLF1_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 SLF1_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-40; SER-42; SER-45 ANDSER-427, AND MASS SPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY. |