| UniProt ID | ERF3_YEAST | |
|---|---|---|
| UniProt AC | P05453 | |
| Protein Name | Eukaryotic peptide chain release factor GTP-binding subunit | |
| Gene Name | SUP35 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 685 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides. Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs. Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.. | |
| Protein Sequence | MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE | |
| 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 | ------MSDSNQGNN ------CCCCCCCCC | 50.15 | 22814378 | |
| 2 | Phosphorylation | ------MSDSNQGNN ------CCCCCCCCC | 50.15 | 22369663 | |
| 4 | Phosphorylation | ----MSDSNQGNNQQ ----CCCCCCCCCHH | 24.60 | 22369663 | |
| 13 | Phosphorylation | QGNNQQNYQQYSQNG CCCCHHHHHHHHCCC | 7.83 | 29136822 | |
| 16 | Phosphorylation | NQQNYQQYSQNGNQQ CHHHHHHHHCCCCCC | 9.19 | 29136822 | |
| 17 | Phosphorylation | QQNYQQYSQNGNQQQ HHHHHHHHCCCCCCC | 16.90 | 29136822 | |
| 102 | Acetylation | QGGRGNYKNFNYNNN CCCCCCCCCCCCCCC | 60.09 | 24489116 | |
| 121 | Phosphorylation | QAGFQPQSQGMSLND CCCCCCCCCCCCHHH | 35.07 | 30377154 | |
| 125 | Phosphorylation | QPQSQGMSLNDFQKQ CCCCCCCCHHHHHHH | 30.74 | 21551504 | |
| 131 | Acetylation | MSLNDFQKQQKQAAP CCHHHHHHHHHHCCC | 55.48 | 24489116 | |
| 142 | Acetylation | QAAPKPKKTLKLVSS HCCCCCCCEEEEEHH | 68.56 | 25381059 | |
| 145 | Acetylation | PKPKKTLKLVSSSGI CCCCCEEEEEHHCCC | 52.66 | 25381059 | |
| 148 | Phosphorylation | KKTLKLVSSSGIKLA CCEEEEEHHCCCHHH | 29.26 | 22369663 | |
| 149 | Phosphorylation | KTLKLVSSSGIKLAN CEEEEEHHCCCHHHH | 25.71 | 22369663 | |
| 150 | Phosphorylation | TLKLVSSSGIKLANA EEEEEHHCCCHHHHC | 36.71 | 22369663 | |
| 153 | Acetylation | LVSSSGIKLANATKK EEHHCCCHHHHCCHH | 45.10 | 24489116 | |
| 159 | Acetylation | IKLANATKKVGTKPA CHHHHCCHHCCCCCC | 42.95 | 25381059 | |
| 221 | Phosphorylation | KVEDLKISESTHNTN CHHHCEECCCCCCCC | 24.73 | 22369663 | |
| 223 | Phosphorylation | EDLKISESTHNTNNA HHCEECCCCCCCCCC | 28.33 | 22369663 | |
| 224 | Phosphorylation | DLKISESTHNTNNAN HCEECCCCCCCCCCC | 18.33 | 22369663 | |
| 227 | Phosphorylation | ISESTHNTNNANVTS ECCCCCCCCCCCCCH | 23.42 | 21440633 | |
| 233 | Phosphorylation | NTNNANVTSADALIK CCCCCCCCHHHHHHH | 20.29 | 24961812 | |
| 234 | Phosphorylation | TNNANVTSADALIKE CCCCCCCHHHHHHHH | 21.62 | 29136822 | |
| 274 | Phosphorylation | GHVDAGKSTMGGNLL EECCCCCCCCCCCEE | 23.78 | 19823750 | |
| 275 | Phosphorylation | HVDAGKSTMGGNLLY ECCCCCCCCCCCEEE | 24.26 | 19823750 | |
| 282 | Phosphorylation | TMGGNLLYLTGSVDK CCCCCEEEEECCCCH | 12.84 | 19823750 | |
| 284 | Phosphorylation | GGNLLYLTGSVDKRT CCCEEEEECCCCHHH | 17.54 | 19823750 | |
| 286 | Phosphorylation | NLLYLTGSVDKRTIE CEEEEECCCCHHHHH | 23.16 | 19823750 | |
| 289 | Acetylation | YLTGSVDKRTIEKYE EEECCCCHHHHHHHH | 49.65 | 24489116 | |
| 294 | Acetylation | VDKRTIEKYEREAKD CCHHHHHHHHHHHHH | 48.86 | 24489116 | |
| 294 | 2-Hydroxyisobutyrylation | VDKRTIEKYEREAKD CCHHHHHHHHHHHHH | 48.86 | - | |
| 330 | Acetylation | GKTIEVGKAYFETEK CCEEEECCEEEECCC | 45.12 | 24489116 | |
| 330 | Succinylation | GKTIEVGKAYFETEK CCEEEECCEEEECCC | 45.12 | 23954790 | |
| 341 | Phosphorylation | ETEKRRYTILDAPGH ECCCCEEEEEECCCC | 17.16 | 28889911 | |
| 400 | Ubiquitination | AKTQGVNKMVVVVNK HHCCCCCEEEEEEEC | 30.57 | 23749301 | |
| 407 | Acetylation | KMVVVVNKMDDPTVN EEEEEEECCCCCCCC | 31.90 | 24489116 | |
| 417 | Ubiquitination | DPTVNWSKERYDQCV CCCCCCCHHHHHHHH | 37.51 | 23749301 | |
| 417 | Acetylation | DPTVNWSKERYDQCV CCCCCCCHHHHHHHH | 37.51 | 24489116 | |
| 456 | Acetylation | GYSGANLKDHVDPKE CCCCCCHHHCCCCCC | 45.66 | 24489116 | |
| 508 | Acetylation | LGTIVEGKIESGHIK CCEEEEEEEECCCCC | 29.78 | 24489116 | |
| 556 | Ubiquitination | EQVKLRIKGVEEEDI CEEEEEECCCCHHHC | 50.93 | 17644757 | |
| 556 | Acetylation | EQVKLRIKGVEEEDI CEEEEEECCCCHHHC | 50.93 | 24489116 | |
| 564 | Phosphorylation | GVEEEDISPGFVLTS CCCHHHCCCCEEEEC | 31.15 | 30377154 | |
| 570 | Phosphorylation | ISPGFVLTSPKNPIK CCCCEEEECCCCCHH | 37.37 | 25521595 | |
| 571 | Phosphorylation | SPGFVLTSPKNPIKS CCCEEEECCCCCHHH | 29.71 | 25521595 | |
| 573 | Ubiquitination | GFVLTSPKNPIKSVT CEEEECCCCCHHHHH | 75.11 | 17644757 | |
| 629 | Phosphorylation | EKGTNRKSKKPPAFA HHCCCCCCCCCCHHH | 42.55 | 19795423 | |
| 641 | Ubiquitination | AFAKKGMKVIAVLET HHHCCCCEEEEEEEC | 38.88 | 17644757 | |
| 679 | 2-Hydroxyisobutyrylation | GTTIAIGKIVKIAE- CCEEEEEEEEEECC- | 37.91 | - | |
| 679 | Ubiquitination | GTTIAIGKIVKIAE- CCEEEEEEEEEECC- | 37.91 | 23749301 | |
| 679 | Acetylation | GTTIAIGKIVKIAE- CCEEEEEEEEEECC- | 37.91 | 24489116 | |
| 682 | Ubiquitination | IAIGKIVKIAE---- EEEEEEEEECC---- | 39.41 | 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 ERF3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERF3_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 ERF3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-221 AND SER-571, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND MASSSPECTROMETRY. | |
| "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-571, AND MASSSPECTROMETRY. | |
