| UniProt ID | IF6_YEAST | |
|---|---|---|
| UniProt AC | Q12522 | |
| Protein Name | Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132} | |
| Gene Name | TIF6 {ECO:0000255|HAMAP-Rule:MF_03132} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 245 | |
| Subcellular Localization | Cytoplasm. Nucleus, nucleolus. Shuttles between cytoplasm and nucleus/nucleolus. | |
| Protein Description | Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1. Also required for pre-rRNA processing.. | |
| Protein Sequence | MATRTQFENSNEIGVFSKLTNTYCLVAVGGSENFYSAFEAELGDAIPIVHTTIAGTRIIGRMTAGNRRGLLVPTQTTDQELQHLRNSLPDSVKIQRVEERLSALGNVICCNDYVALVHPDIDRETEELISDVLGVEVFRQTISGNILVGSYCSLSNQGGLVHPQTSVQDQEELSSLLQVPLVAGTVNRGSSVVGAGMVVNDYLAVTGLDTTAPELSVIESIFRLQDAQPESISGNLRDTLIETYS | |
| 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 |
|---|---|---|---|---|---|
| 87 | Phosphorylation | ELQHLRNSLPDSVKI HHHHHHHCCCCCHHH | 34.54 | 28889911 | |
| 91 | Phosphorylation | LRNSLPDSVKIQRVE HHHCCCCCHHHHHHH | 24.30 | 28889911 | |
| 174 | Phosphorylation | VQDQEELSSLLQVPL CCCHHHHHHHHCCCE | 23.40 | 18256024 | |
| 175 | Phosphorylation | QDQEELSSLLQVPLV CCHHHHHHHHCCCEE | 45.80 | 18256024 | |
| 231 | Phosphorylation | LQDAQPESISGNLRD CCCCCCCCCCCCHHH | 28.83 | 22369663 | |
| 233 | Phosphorylation | DAQPESISGNLRDTL CCCCCCCCCCHHHHH | 30.79 | 22369663 | |
| 239 | Phosphorylation | ISGNLRDTLIETYS- CCCCHHHHHHHHCC- | 24.17 | 22369663 | |
| 243 | Phosphorylation | LRDTLIETYS----- HHHHHHHHCC----- | 23.28 | 22369663 | |
| 244 | Phosphorylation | RDTLIETYS------ HHHHHHHCC------ | 10.29 | 22369663 | |
| 245 | Phosphorylation | DTLIETYS------- HHHHHHCC------- | 40.96 | 22369663 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 174 | S | Phosphorylation | Kinase | CK1 | - | Uniprot |
| 175 | S | Phosphorylation | Kinase | CK1 | - | Uniprot |
* 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 IF6_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-231 AND SER-233, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY. | |
