| UniProt ID | NSG1_YEAST | |
|---|---|---|
| UniProt AC | P38837 | |
| Protein Name | Protein NSG1 | |
| Gene Name | NSG1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 291 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation.. | |
| Protein Sequence | MGKKKSKNQLNTGGVPNGVHNTKKEAALPPLGNKLGSASFTAINTLTKPALFSFYDDDITKNEGNVYDKALLSNASQLEMVPPSATARHERSLYAKIINTIAAFFILFIAGILFPMISECLFDNDQLAKGDIVSFLKHGIEIKNKIVAEPDMVPDWAVFGTEGVIFGSIVPFIDSFVRYQHQPKTRSSVYKNTLGSFIRCANTLLGLIFGIRKLEWSSSLQAAGAWSLLNIVLWLFFDGTLTVFFPGLVIGALSAFTCSQCFSQLSLALYFIDFYFFGFLMFSKLGRYLFN | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MGKKKSKNQLNTG --CCCCCCCCCCCCC | 45.80 | 30377154 | |
| 34 | Ubiquitination | ALPPLGNKLGSASFT CCCCCCCCCCCCCEE | 53.04 | 17644757 | |
| 37 | Phosphorylation | PLGNKLGSASFTAIN CCCCCCCCCCEEEHH | 31.04 | 22369663 | |
| 39 | Phosphorylation | GNKLGSASFTAINTL CCCCCCCCEEEHHCC | 25.48 | 22369663 | |
| 41 | Phosphorylation | KLGSASFTAINTLTK CCCCCCEEEHHCCCC | 24.92 | 22369663 | |
| 45 | Phosphorylation | ASFTAINTLTKPALF CCEEEHHCCCCCCHH | 29.68 | 22369663 | |
| 47 | Phosphorylation | FTAINTLTKPALFSF EEEHHCCCCCCHHCC | 32.70 | 22369663 | |
| 48 | Ubiquitination | TAINTLTKPALFSFY EEHHCCCCCCHHCCC | 31.26 | 17644757 | |
| 53 | Phosphorylation | LTKPALFSFYDDDIT CCCCCHHCCCCCCCC | 24.60 | 22369663 | |
| 55 | Phosphorylation | KPALFSFYDDDITKN CCCHHCCCCCCCCCC | 19.77 | 22369663 | |
| 60 | Phosphorylation | SFYDDDITKNEGNVY CCCCCCCCCCCCCHH | 34.51 | 22369663 | |
| 61 | Ubiquitination | FYDDDITKNEGNVYD CCCCCCCCCCCCHHH | 54.02 | 17644757 | |
| 67 | Phosphorylation | TKNEGNVYDKALLSN CCCCCCHHHHHHHCC | 18.74 | 22369663 | |
| 69 | Ubiquitination | NEGNVYDKALLSNAS CCCCHHHHHHHCCHH | 24.21 | 17644757 | |
| 73 | Phosphorylation | VYDKALLSNASQLEM HHHHHHHCCHHHCCC | 31.06 | 30377154 | |
| 76 | Phosphorylation | KALLSNASQLEMVPP HHHHCCHHHCCCCCC | 39.28 | 25752575 | |
| 84 | Phosphorylation | QLEMVPPSATARHER HCCCCCCCCCHHHHH | 31.98 | 27214570 | |
| 137 | Acetylation | GDIVSFLKHGIEIKN CCHHHHHHHCCEECC | 37.46 | 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 NSG1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NSG1_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 NSG1_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 SER-39 AND SER-76, AND MASSSPECTROMETRY. | |
| "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-39, AND MASSSPECTROMETRY. | |