| UniProt ID | IF2G_YEAST | |
|---|---|---|
| UniProt AC | P32481 | |
| Protein Name | Eukaryotic translation initiation factor 2 subunit gamma | |
| Gene Name | GCD11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 527 | |
| Subcellular Localization | ||
| Protein Description | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.. | |
| Protein Sequence | MSDLQDQEPSIIINGNLEPVGEPDIVEETEVVAQETQETQDADKPKKKVAFTGLEEDGETEEEKRKREFEEGGGLPEQPLNPDFSKLNPLSAEIINRQATINIGTIGHVAHGKSTVVRAISGVQTVRFKDELERNITIKLGYANAKIYKCQEPTCPEPDCYRSFKSDKEISPKCQRPGCPGRYKLVRHVSFVDCPGHDILMSTMLSGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHVIILQNKVDLMREESALEHQKSILKFIRGTIADGAPIVPISAQLKYNIDAVNEFIVKTIPVPPRDFMISPRLIVIRSFDVNKPGAEIEDLKGGVAGGSILNGVFKLGDEIEIRPGIVTKDDKGKIQCKPIFSNIVSLFAEQNDLKFAVPGGLIGVGTKVDPTLCRADRLVGQVVGAKGHLPNIYTDIEINYFLLRRLLGVKTDGQKQAKVRKLEPNEVLMVNIGSTATGARVVAVKADMARLQLTSPACTEINEKIALSRRIEKHWRLIGWATIKKGTTLEPIA | |
| 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 |
|---|---|---|---|---|---|
| 48 | Ubiquitination | DADKPKKKVAFTGLE CCCCCCCEEEEECCC | 44.94 | 17644757 | |
| 60 | Phosphorylation | GLEEDGETEEEKRKR CCCCCCCCHHHHHHH | 54.98 | 22369663 | |
| 64 | Acetylation | DGETEEEKRKREFEE CCCCHHHHHHHHHHC | 67.51 | 24489116 | |
| 64 | Ubiquitination | DGETEEEKRKREFEE CCCCHHHHHHHHHHC | 67.51 | 23749301 | |
| 66 | Ubiquitination | ETEEEKRKREFEEGG CCHHHHHHHHHHCCC | 68.31 | 17644757 | |
| 86 | Ubiquitination | PLNPDFSKLNPLSAE CCCCCHHHCCCCCHH | 52.88 | 17644757 | |
| 86 | Acetylation | PLNPDFSKLNPLSAE CCCCCHHHCCCCCHH | 52.88 | 24489116 | |
| 121 | Phosphorylation | STVVRAISGVQTVRF HHHHHHHCCCEEEEE | 31.74 | 28889911 | |
| 129 | Acetylation | GVQTVRFKDELERNI CCEEEEECHHHHHCE | 39.46 | 24489116 | |
| 129 | Ubiquitination | GVQTVRFKDELERNI CCEEEEECHHHHHCE | 39.46 | 23749301 | |
| 146 | Ubiquitination | KLGYANAKIYKCQEP EEECCCCEEEECCCC | 46.50 | 22817900 | |
| 146 | Succinylation | KLGYANAKIYKCQEP EEECCCCEEEECCCC | 46.50 | 23954790 | |
| 149 | Ubiquitination | YANAKIYKCQEPTCP CCCCEEEECCCCCCC | 32.68 | 23749301 | |
| 165 | Ubiquitination | PDCYRSFKSDKEISP CCHHHHCCCCCCCCC | 60.02 | 22817900 | |
| 168 | Ubiquitination | YRSFKSDKEISPKCQ HHHCCCCCCCCCCCC | 65.13 | 22817900 | |
| 168 | Acetylation | YRSFKSDKEISPKCQ HHHCCCCCCCCCCCC | 65.13 | 24489116 | |
| 173 | Ubiquitination | SDKEISPKCQRPGCP CCCCCCCCCCCCCCC | 35.89 | 22817900 | |
| 258 | Phosphorylation | VDLMREESALEHQKS HHHHHHHHHHHHHHH | 33.14 | 17287358 | |
| 264 | Acetylation | ESALEHQKSILKFIR HHHHHHHHHHHHHHH | 41.18 | 24489116 | |
| 268 | Acetylation | EHQKSILKFIRGTIA HHHHHHHHHHHCCCC | 36.76 | 24489116 | |
| 288 | Ubiquitination | VPISAQLKYNIDAVN CEEEEEEEECHHHCC | 24.95 | 17644757 | |
| 300 | Acetylation | AVNEFIVKTIPVPPR HCCEEEEEECCCCCC | 35.60 | 24489116 | |
| 312 | Phosphorylation | PPRDFMISPRLIVIR CCCCCEECCEEEEEE | 7.68 | 28889911 | |
| 325 | Acetylation | IRSFDVNKPGAEIED EEEECCCCCCCCHHH | 44.68 | 22865919 | |
| 325 | Ubiquitination | IRSFDVNKPGAEIED EEEECCCCCCCCHHH | 44.68 | 23749301 | |
| 334 | Ubiquitination | GAEIEDLKGGVAGGS CCCHHHCCCCCCCHH | 66.97 | 23749301 | |
| 348 | Ubiquitination | SILNGVFKLGDEIEI HHHCEEEECCCEEEE | 49.51 | 17644757 | |
| 362 | Succinylation | IRPGIVTKDDKGKIQ ECCCEEECCCCCCEE | 53.70 | 23954790 | |
| 362 | Acetylation | IRPGIVTKDDKGKIQ ECCCEEECCCCCCEE | 53.70 | 24489116 | |
| 367 | Ubiquitination | VTKDDKGKIQCKPIF EECCCCCCEECEECC | 35.03 | 17644757 | |
| 371 | Ubiquitination | DKGKIQCKPIFSNIV CCCCEECEECCHHHH | 25.44 | 17644757 | |
| 388 | Ubiquitination | FAEQNDLKFAVPGGL HHHHCCCCEEECCCE | 33.85 | 17644757 | |
| 400 | Phosphorylation | GGLIGVGTKVDPTLC CCEECCCCCCCHHHH | 26.03 | 19795423 | |
| 401 | Ubiquitination | GLIGVGTKVDPTLCR CEECCCCCCCHHHHH | 38.42 | 17644757 | |
| 420 | Ubiquitination | VGQVVGAKGHLPNIY HHHHHCCCCCCCCCC | 40.72 | 17644757 | |
| 444 | 2-Hydroxyisobutyrylation | LRRLLGVKTDGQKQA HHHHHCCCCCCCCEE | 38.82 | - | |
| 455 | Acetylation | QKQAKVRKLEPNEVL CCEEEEECCCCCCEE | 61.26 | 24489116 | |
| 479 | Ubiquitination | GARVVAVKADMARLQ CCEEEEEECCHHHCC | 29.00 | 22817900 | |
| 498 | Ubiquitination | ACTEINEKIALSRRI HHHHHHHHHHHHHHH | 28.88 | 17644757 | |
| 498 | Acetylation | ACTEINEKIALSRRI HHHHHHHHHHHHHHH | 28.88 | 24489116 | |
| 507 | Ubiquitination | ALSRRIEKHWRLIGW HHHHHHHHHHHEEEE | 46.20 | 22817900 |
| 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 IF2G_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF2G_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 IF2G_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 THR-60 AND SER-258, AND MASSSPECTROMETRY. | |
| "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-258, AND MASSSPECTROMETRY. | |
