| UniProt ID | EI2BG_YEAST | |
|---|---|---|
| UniProt AC | P09032 | |
| Protein Name | Translation initiation factor eIF-2B subunit gamma | |
| Gene Name | GCD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 578 | |
| Subcellular Localization | ||
| Protein Description | Acts as essential component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD1 stabilizes the interaction between eIF-2 and GCD6 and stimulates the catalytic activity in vitro.. | |
| Protein Sequence | MSIQAFVFCGKGSNLAPFTQPDFPFQTQNKDSTAATSGDKLNELVNSALDSTVINEFMQHSTRLPKALLPIGNRPMIEYVLDWCDQADFKEISVVAPVDEIELIESGLTSFLSLRKQQFELIYKALSNSNHSHHLQDPKKINFIPSKANSTGESLQKELLPRINGDFVILPCDFVTDIPPQVLVDQFRNRDDNNLAMTIYYKNSLDSSIDKKQQQKQKQQQFFTVYSENEDSERQPILLDVYSQRDVTKTKYLQIRSHLLWNYPNLTVSTKLLNSFIYFCSFELCQLLKLGPQSMSRQASFKDPFTGNQQQQNPPTTDDDEDRNHDDDDDYKPSATSIQPTYFKKKNDLILDPINCNKSLSKVFRDLSRRSWQHSKPREPIGIFILPNETLFIRANNLNAYMDANRFVLKIKSQTMFTKNIQIQSAAIGADAIVDPKCQISAHSNVKMSVLGTQANIGSRCRVAGSLLFPGVHLGDEVILENCIIGPMAKIGSKCKLSNCYIEGHYVVEPKNNFKGETLANVYLDEDEEDELIYDDSVIAGESEIAEETDSDDRSDEDSDDSEYTDEYEYEDDGLFER | |
| 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 |
|---|---|---|---|---|---|
| 32 | Phosphorylation | FQTQNKDSTAATSGD CCCCCCCCCCCCCHH | 22.89 | 22369663 | |
| 33 | Phosphorylation | QTQNKDSTAATSGDK CCCCCCCCCCCCHHH | 30.37 | 22369663 | |
| 36 | Phosphorylation | NKDSTAATSGDKLNE CCCCCCCCCHHHHHH | 30.67 | 22369663 | |
| 37 | Phosphorylation | KDSTAATSGDKLNEL CCCCCCCCHHHHHHH | 40.02 | 22369663 | |
| 47 | Phosphorylation | KLNELVNSALDSTVI HHHHHHHHHHHHHHH | 23.80 | 22369663 | |
| 51 | Phosphorylation | LVNSALDSTVINEFM HHHHHHHHHHHHHHH | 25.98 | 29136822 | |
| 52 | Phosphorylation | VNSALDSTVINEFMQ HHHHHHHHHHHHHHH | 25.68 | 29136822 | |
| 61 | Phosphorylation | INEFMQHSTRLPKAL HHHHHHHCCCCCHHH | 9.79 | 22369663 | |
| 62 | Phosphorylation | NEFMQHSTRLPKALL HHHHHHCCCCCHHHC | 33.82 | 22369663 | |
| 294 | Phosphorylation | LLKLGPQSMSRQASF HHHHCCCCCCCCCCC | 23.12 | 22369663 | |
| 296 | Phosphorylation | KLGPQSMSRQASFKD HHCCCCCCCCCCCCC | 26.87 | 22369663 | |
| 300 | Phosphorylation | QSMSRQASFKDPFTG CCCCCCCCCCCCCCC | 25.21 | 17287358 | |
| 306 | Phosphorylation | ASFKDPFTGNQQQQN CCCCCCCCCCCCCCC | 40.38 | 28889911 | |
| 316 | Phosphorylation | QQQQNPPTTDDDEDR CCCCCCCCCCCCCCC | 44.08 | 20377248 | |
| 317 | Phosphorylation | QQQNPPTTDDDEDRN CCCCCCCCCCCCCCC | 43.11 | 20377248 | |
| 331 | Phosphorylation | NHDDDDDYKPSATSI CCCCCCCCCCCCCCC | 31.62 | 19823750 | |
| 334 | Phosphorylation | DDDDYKPSATSIQPT CCCCCCCCCCCCCCC | 39.77 | 19823750 | |
| 336 | Phosphorylation | DDYKPSATSIQPTYF CCCCCCCCCCCCCCC | 30.60 | 19823750 | |
| 337 | Phosphorylation | DYKPSATSIQPTYFK CCCCCCCCCCCCCCC | 20.95 | 19823750 | |
| 341 | Phosphorylation | SATSIQPTYFKKKND CCCCCCCCCCCCCCC | 25.80 | 19823750 | |
| 342 | Phosphorylation | ATSIQPTYFKKKNDL CCCCCCCCCCCCCCE | 21.78 | 19823750 |
| 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 EI2BG_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EI2BG_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 EI2BG_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-32; SER-37 AND SER-296,AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-300, ANDMASS 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-296, AND MASSSPECTROMETRY. | |
