UniProt ID | EF1G1_YEAST | |
---|---|---|
UniProt AC | P29547 | |
Protein Name | Elongation factor 1-gamma 1 | |
Gene Name | CAM1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 415 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1.. | |
Protein Sequence | MSQGTLYANFRIRTWVPRGLVKALKLDVKVVTPDAAAEQFARDFPLKKVPAFVGPKGYKLTEAMAINYYLVKLSQDDKMKTQLLGADDDLNAQAQIIRWQSLANSDLCIQIANTIVPLKGGAPYNKKSVDSAMDAVDKIVDIFENRLKNYTYLATENISLADLVAASIFTRYFESLFGTEWRAQHPAIVRWFNTVRASPFLKDEYKDFKFADKPLSPPQKKKEKKAPAAAPAASKKKEEAKPAATETETSSKKPKHPLELLGKSTFVLDDWKRKYSNEDTRPVALPWFWEHYNPEEYSLWKVTYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDYVPAFDVAPDWESYDYAKLDPTNDDDKEFINNMWAWDKPVSVNGEPKEIVDGKVLK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MSQGTLYAN ------CCCCCEEEE | 37.00 | 22814378 | |
22 | 2-Hydroxyisobutyrylation | WVPRGLVKALKLDVK ECCHHHHHHHCCEEE | 53.71 | - | |
29 | Acetylation | KALKLDVKVVTPDAA HHHCCEEEEECCHHH | 30.56 | 24489116 | |
32 | Phosphorylation | KLDVKVVTPDAAAEQ CCEEEEECCHHHHHH | 20.59 | 25752575 | |
56 | Acetylation | VPAFVGPKGYKLTEA CCCCCCCCCCCHHHH | 69.78 | 24489116 | |
78 | 2-Hydroxyisobutyrylation | VKLSQDDKMKTQLLG EECCCCCHHHHHHCC | 51.06 | - | |
80 | 2-Hydroxyisobutyrylation | LSQDDKMKTQLLGAD CCCCCHHHHHHCCCC | 38.57 | - | |
80 | Ubiquitination | LSQDDKMKTQLLGAD CCCCCHHHHHHCCCC | 38.57 | 24961812 | |
127 | Acetylation | GGAPYNKKSVDSAMD CCCCCCCCCHHHHHH | 52.66 | 24489116 | |
202 | Succinylation | VRASPFLKDEYKDFK HCCCCCCCHHHCCCC | 49.22 | 23954790 | |
202 | Acetylation | VRASPFLKDEYKDFK HCCCCCCCHHHCCCC | 49.22 | 24489116 | |
206 | Acetylation | PFLKDEYKDFKFADK CCCCHHHCCCCCCCC | 55.42 | 24489116 | |
209 | Ubiquitination | KDEYKDFKFADKPLS CHHHCCCCCCCCCCC | 50.18 | 24961812 | |
213 | Acetylation | KDFKFADKPLSPPQK CCCCCCCCCCCCCHH | 44.41 | 24489116 | |
216 | Phosphorylation | KFADKPLSPPQKKKE CCCCCCCCCCHHHHH | 42.96 | 21440633 | |
234 | Phosphorylation | PAAAPAASKKKEEAK CCCCCHHHHCHHHCC | 47.30 | 28889911 | |
247 | Phosphorylation | AKPAATETETSSKKP CCCCCCCCCCCCCCC | 39.96 | 27717283 | |
249 | Phosphorylation | PAATETETSSKKPKH CCCCCCCCCCCCCCC | 45.80 | 28889911 | |
250 | Phosphorylation | AATETETSSKKPKHP CCCCCCCCCCCCCCH | 33.65 | 28889911 | |
251 | Phosphorylation | ATETETSSKKPKHPL CCCCCCCCCCCCCHH | 52.71 | 27717283 | |
263 | Ubiquitination | HPLELLGKSTFVLDD CHHHHCCCCEEEECC | 46.41 | 17644757 | |
264 | Phosphorylation | PLELLGKSTFVLDDW HHHHCCCCEEEECCH | 25.86 | 22369663 | |
265 | Phosphorylation | LELLGKSTFVLDDWK HHHCCCCEEEECCHH | 22.65 | 22369663 | |
272 | Acetylation | TFVLDDWKRKYSNED EEEECCHHHHCCCCC | 46.11 | 24489116 | |
272 | Ubiquitination | TFVLDDWKRKYSNED EEEECCHHHHCCCCC | 46.11 | 17644757 | |
272 | 2-Hydroxyisobutyrylation | TFVLDDWKRKYSNED EEEECCHHHHCCCCC | 46.11 | - | |
272 | Succinylation | TFVLDDWKRKYSNED EEEECCHHHHCCCCC | 46.11 | 23954790 | |
274 | Ubiquitination | VLDDWKRKYSNEDTR EECCHHHHCCCCCCC | 49.67 | 17644757 | |
276 | Phosphorylation | DDWKRKYSNEDTRPV CCHHHHCCCCCCCCC | 36.46 | 24961812 | |
280 | Phosphorylation | RKYSNEDTRPVALPW HHCCCCCCCCCCCCC | 30.60 | 24961812 | |
397 | Acetylation | NNMWAWDKPVSVNGE HHHCCCCCCCEECCC | 36.30 | 24489116 | |
400 | Phosphorylation | WAWDKPVSVNGEPKE CCCCCCCEECCCCCE | 20.56 | 22369663 | |
412 | Ubiquitination | PKEIVDGKVLK---- CCEECCCEECC---- | 39.67 | 23749301 | |
412 | Acetylation | PKEIVDGKVLK---- CCEECCCEECC---- | 39.67 | 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 EF1G1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EF1G1_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 EF1G1_YEAST !! |
Kegg Drug | ||||||
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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-32, AND MASSSPECTROMETRY. |