| UniProt ID | EFTU_YEAST | |
|---|---|---|
| UniProt AC | P02992 | |
| Protein Name | Elongation factor Tu, mitochondrial | |
| Gene Name | TUF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 437 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | G-protein that, in its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled before binding another molecule of aminoacyl-tRNA. Required for mitochondrial protein biosynthesis and maintenance of mitochondrial DNA.. | |
| Protein Sequence | MSALLPRLLTRTAFKASGKLLRLSSVISRTFSQTTTSYAAAFDRSKPHVNIGTIGHVDHGKTTLTAAITKTLAAKGGANFLDYAAIDKAPEERARGITISTAHVEYETAKRHYSHVDCPGHADYIKNMITGAAQMDGAIIVVAATDGQMPQTREHLLLARQVGVQHIVVFVNKVDTIDDPEMLELVEMEMRELLNEYGFDGDNAPIIMGSALCALEGRQPEIGEQAIMKLLDAVDEYIPTPERDLNKPFLMPVEDIFSISGRGTVVTGRVERGNLKKGEELEIVGHNSTPLKTTVTGIEMFRKELDSAMAGDNAGVLLRGIRRDQLKRGMVLAKPGTVKAHTKILASLYILSKEEGGRHSGFGENYRPQMFIRTADVTVVMRFPKEVEDHSMQVMPGDNVEMECDLIHPTPLEVGQRFNIREGGRTVGTGLITRIIE | |
| 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 |
|---|---|---|---|---|---|
| 25 | Phosphorylation | GKLLRLSSVISRTFS CHHHHHHHHHHHCCC | 28.23 | 30377154 | |
| 28 | Phosphorylation | LRLSSVISRTFSQTT HHHHHHHHHCCCCCC | 24.10 | 30377154 | |
| 30 | Phosphorylation | LSSVISRTFSQTTTS HHHHHHHCCCCCCCC | 22.35 | 30377154 | |
| 32 | Phosphorylation | SVISRTFSQTTTSYA HHHHHCCCCCCCCHH | 26.46 | 30377154 | |
| 62 | Phosphorylation | GHVDHGKTTLTAAIT EEECCCHHHHHHHHH | 31.46 | 22369663 | |
| 63 | Phosphorylation | HVDHGKTTLTAAITK EECCCHHHHHHHHHH | 26.12 | 22369663 | |
| 65 | Phosphorylation | DHGKTTLTAAITKTL CCCHHHHHHHHHHHH | 16.38 | 22369663 | |
| 69 | Phosphorylation | TTLTAAITKTLAAKG HHHHHHHHHHHHHCC | 17.16 | 22369663 | |
| 88 | Acetylation | LDYAAIDKAPEERAR ECHHHHCCCHHHHHC | 60.78 | 24489116 | |
| 100 | Phosphorylation | RARGITISTAHVEYE HHCCEEEEECEEEHH | 15.76 | 17287358 | |
| 101 | Phosphorylation | ARGITISTAHVEYET HCCEEEEECEEEHHH | 19.55 | 17287358 | |
| 247 | Acetylation | TPERDLNKPFLMPVE CCCCCCCCCCEEEHH | 44.43 | 24489116 | |
| 258 | Phosphorylation | MPVEDIFSISGRGTV EEHHHHEEECCCCEE | 19.04 | 22369663 | |
| 260 | Phosphorylation | VEDIFSISGRGTVVT HHHHEEECCCCEEEE | 22.65 | 22369663 | |
| 277 | Acetylation | VERGNLKKGEELEIV EECCCCCCCCEEEEE | 74.79 | 22865919 | |
| 288 | Phosphorylation | LEIVGHNSTPLKTTV EEEECCCCCCCCCHH | 26.23 | 20377248 | |
| 289 | Phosphorylation | EIVGHNSTPLKTTVT EEECCCCCCCCCHHH | 37.65 | 20377248 | |
| 296 | Phosphorylation | TPLKTTVTGIEMFRK CCCCCHHHHHHHHHH | 30.28 | 20377248 | |
| 337 | Phosphorylation | MVLAKPGTVKAHTKI CEECCCCCHHHHHHH | 27.62 | 22369663 | |
| 353 | Acetylation | ASLYILSKEEGGRHS HHHHHHCCCCCCCCC | 57.23 | 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 EFTU_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EFTU_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 EFTU_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-258 AND THR-296, ANDMASS 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-100 AND THR-101, ANDMASS SPECTROMETRY. | |
