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 | ||
* 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 | ||||||
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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-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. |