| UniProt ID | GCN20_YEAST | |
|---|---|---|
| UniProt AC | P43535 | |
| Protein Name | Protein GCN20 {ECO:0000305} | |
| Gene Name | GCN20 {ECO:0000312|SGD:S000001905} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 752 | |
| Subcellular Localization | ||
| Protein Description | Acts as a positive activator of the GCN2 protein kinase activity in response to amino acid starvation. [PubMed: 7621831 Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity] | |
| Protein Sequence | MASIGSQVRKAASSIDPIVTDYAVGYFNHLSGITFDAVQSKQVDLSTEVQFVSDLLIDAGASKAKVKELSESILKQLTTQLKENEAKLELTGDTSKRLLDINVLKSHNSKSDINVSLSMLGVNGDIEHTGRKMETRVDLKKLAKAEQKIAKKVAKRNNKFVKYEASKLINDQKEEDYDSFFLQINPLEFGSSAGKSKDIHIDTFDLYVGDGQRILSNAQLTLSFGHRYGLVGQNGIGKSTLLRALSRRELNVPKHVSILHVEQELRGDDTKALQSVLDADVWRKQLLSEEAKINERLKEMDVLRQEFEEDSLEVKKLDNEREDLDNHLIQISDKLVDMESDKAEARAASILYGLGFSTEAQQQPTNSFSGGWRMRLSLARALFCQPDLLLLDEPSNMLDVPSIAYLAEYLKTYPNTVLTVSHDRAFLNEVATDIIYQHNERLDYYRGQDFDTFYTTKEERRKNAQREYDNQMVYRKHLQEFIDKYRYNAAKSQEAQSRIKKLEKLPVLEPPEQDKTIDFKFPECDKLSPPIIQLQDVSFGYDENNLLLKDVNLDVQMDSRIALVGANGCGKTTLLKIMMEQLRPLKGFVSRNPRLRIGYFTQHHVDSMDLTTSAVDWMSKSFPGKTDEEYRRHLGSFGITGTLGLQKMQLLSGGQKSRVAFAALCLNNPHILVLDEPSNHLDTTGLDALVEALKNFNGGVLMVSHDISVIDSVCKEIWVSEQGTVKRFEGTIYDYRDYILQSADAAGVVKKH | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MASIGSQVR ------CCCHHHHHH | 15.17 | 22814378 | |
| 3 | Phosphorylation | -----MASIGSQVRK -----CCCHHHHHHH | 26.61 | 22369663 | |
| 6 | Phosphorylation | --MASIGSQVRKAAS --CCCHHHHHHHHHH | 24.67 | 22369663 | |
| 70 | Phosphorylation | KAKVKELSESILKQL HHHHHHHHHHHHHHH | 30.32 | 30377154 | |
| 72 | Phosphorylation | KVKELSESILKQLTT HHHHHHHHHHHHHHH | 29.82 | 30377154 | |
| 82 | Ubiquitination | KQLTTQLKENEAKLE HHHHHHHHHCHHHEE | 48.99 | 23749301 | |
| 91 | Phosphorylation | NEAKLELTGDTSKRL CHHHEEECCCHHHHH | 24.52 | 24961812 | |
| 94 | Phosphorylation | KLELTGDTSKRLLDI HEEECCCHHHHHEEE | 37.18 | 24961812 | |
| 95 | Phosphorylation | LELTGDTSKRLLDIN EEECCCHHHHHEEEE | 22.10 | 28889911 | |
| 105 | Acetylation | LLDINVLKSHNSKSD HEEEEEHHHCCCHHH | 45.44 | 24489116 | |
| 106 | Phosphorylation | LDINVLKSHNSKSDI EEEEEHHHCCCHHHC | 24.60 | 22369663 | |
| 109 | Phosphorylation | NVLKSHNSKSDINVS EEHHHCCCHHHCEEE | 28.28 | 22369663 | |
| 111 | Phosphorylation | LKSHNSKSDINVSLS HHHCCCHHHCEEEEH | 43.47 | 22369663 | |
| 116 | Phosphorylation | SKSDINVSLSMLGVN CHHHCEEEEHHHCCC | 15.39 | 22369663 | |
| 162 | Acetylation | KRNNKFVKYEASKLI HHCCCCHHHHHHHHH | 40.27 | 25381059 | |
| 238 | Acetylation | VGQNGIGKSTLLRAL CCCCCCCHHHHHHHH | 38.04 | 24489116 | |
| 342 | Ubiquitination | LVDMESDKAEARAAS HHCCCCHHHHHHHHH | 58.36 | 23749301 | |
| 457 | Acetylation | FDTFYTTKEERRKNA CCCCCCCHHHHHHHH | 50.18 | 24489116 | |
| 457 | Succinylation | FDTFYTTKEERRKNA CCCCCCCHHHHHHHH | 50.18 | 23954790 | |
| 484 | Acetylation | HLQEFIDKYRYNAAK HHHHHHHHHHHHHHH | 27.15 | 24489116 | |
| 491 | Ubiquitination | KYRYNAAKSQEAQSR HHHHHHHHCHHHHHH | 50.70 | 23749301 | |
| 576 | Acetylation | CGKTTLLKIMMEQLR CCHHHHHHHHHHHHH | 31.50 | 24489116 | |
| 656 | Ubiquitination | QLLSGGQKSRVAFAA HCCCCCCCHHHHHHH | 43.43 | 23749301 | |
| 656 | Methylation | QLLSGGQKSRVAFAA HCCCCCCCHHHHHHH | 43.43 | 20137074 | |
| 738 | Phosphorylation | TIYDYRDYILQSADA EEEEHHHHHCCCCHH | 8.43 | 27017623 | |
| 742 | Phosphorylation | YRDYILQSADAAGVV HHHHHCCCCHHHCCC | 25.35 | 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 GCN20_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GCN20_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 GCN20_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-95 AND SER-742, AND MASSSPECTROMETRY. | |
