UniProt ID | EAP1_YEAST | |
---|---|---|
UniProt AC | P36041 | |
Protein Name | Protein EAP1 | |
Gene Name | EAP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 632 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Can regulate translation through binding to eIF4E. Competes with eIF4G and p20 for binding to eIF4E in vivo and inhibits cap-dependent translation in vitro. Plays a role in cell growth and is implicated in the TOR signaling cascade. Functions independently of eIF4E to maintain genetic stability and to attenuate GCN4 translation upon TOR inactivation.. | |
Protein Sequence | MELNDPSIISSSQFSGELSDSDTAAATHKSQQAISNLFQKLAKKGREEKPIGSVESSTDSSNISVATSGNNKESNKKKNKKTAMLNFSSLTDPITNYKPMDLQYKTYAYSMNELYHLKPSLASASYEEDPLISELVRSLPKRKFWRLRMGPPDQKHANNHHFNGNNGGGSWKAGYKNGKNDERRMSRTKNMQGGKRRSQQDDEEKKIDQEMLEMDKNLQLGGDVGHSIADFEDWKAKMKELELKKLSKSKGISNSTAIAPRESASHETPTDLRPVIPRGPSSITDFLNLKRQDKKEESSQQTPGIPVGQPSLSKTSIEQVNELETNSDLGKSSSSRFSSFFNKSATSLPSLDNNNQVPSSNVSVVNNDGNSTPHQSGSRLMSFFKESRSSTPNAESQLLSASDKDNGKMQTLPQFQQQPQQMQPMAFTQHPPNNNAFFNGLLNKGKSETSTPPPPPPGLIAHQGPQFPVMGVPPNFPQRMMPPPPGLVQFQKDSKDVNKKEDRQLRQNKNPNGTRNSKGKQEETATPDLPQQQYMPPPPPPGFFPMHPNFPNGPMPPLPQGFPIPPNGMLPVTGQQPQPPYPNMMLQGNFPPNFQQGFGSNSPMPIPSIINANGKNVTNQLPPGLNSKKNIK | |
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 |
---|---|---|---|---|---|
7 | Phosphorylation | -MELNDPSIISSSQF -CCCCCHHHCCCCCC | 35.10 | 30377154 | |
15 | Phosphorylation | IISSSQFSGELSDSD HCCCCCCCCCCCCCH | 24.58 | 22369663 | |
19 | Phosphorylation | SQFSGELSDSDTAAA CCCCCCCCCCHHHHH | 30.66 | 22369663 | |
21 | Phosphorylation | FSGELSDSDTAAATH CCCCCCCCHHHHHHH | 33.22 | 22369663 | |
23 | Phosphorylation | GELSDSDTAAATHKS CCCCCCHHHHHHHHH | 23.34 | 22369663 | |
27 | Phosphorylation | DSDTAAATHKSQQAI CCHHHHHHHHHHHHH | 25.72 | 22369663 | |
30 | Phosphorylation | TAAATHKSQQAISNL HHHHHHHHHHHHHHH | 21.66 | 22369663 | |
40 | Acetylation | AISNLFQKLAKKGRE HHHHHHHHHHHCCCC | 42.98 | 24489116 | |
186 | Phosphorylation | KNDERRMSRTKNMQG CCHHHHHHHHHCCCC | 34.68 | 27717283 | |
188 | Phosphorylation | DERRMSRTKNMQGGK HHHHHHHHHCCCCCC | 21.33 | 27717283 | |
198 | Phosphorylation | MQGGKRRSQQDDEEK CCCCCCCCCCCHHHH | 35.91 | 28889911 | |
227 | Phosphorylation | LGGDVGHSIADFEDW CCCCCCCCHHCHHHH | 17.34 | 22369663 | |
263 | Phosphorylation | TAIAPRESASHETPT CEECCCCCCCCCCCC | 36.03 | 28132839 | |
265 | Phosphorylation | IAPRESASHETPTDL ECCCCCCCCCCCCCC | 31.00 | 28889911 | |
268 | Phosphorylation | RESASHETPTDLRPV CCCCCCCCCCCCCCC | 26.51 | 21440633 | |
270 | Phosphorylation | SASHETPTDLRPVIP CCCCCCCCCCCCCCC | 55.90 | 21440633 | |
281 | Phosphorylation | PVIPRGPSSITDFLN CCCCCCCCCHHHHHH | 36.88 | 22369663 | |
282 | Phosphorylation | VIPRGPSSITDFLNL CCCCCCCCHHHHHHH | 32.42 | 22369663 | |
284 | Phosphorylation | PRGPSSITDFLNLKR CCCCCCHHHHHHHHH | 23.73 | 22890988 | |
290 | Acetylation | ITDFLNLKRQDKKEE HHHHHHHHHCCCCHH | 47.11 | 24489116 | |
298 | Phosphorylation | RQDKKEESSQQTPGI HCCCCHHHCCCCCCC | 34.24 | 22369663 | |
299 | Phosphorylation | QDKKEESSQQTPGIP CCCCHHHCCCCCCCC | 29.59 | 28132839 | |
302 | Phosphorylation | KEESSQQTPGIPVGQ CHHHCCCCCCCCCCC | 18.82 | 22369663 | |
311 | Phosphorylation | GIPVGQPSLSKTSIE CCCCCCCCCCCCCHH | 37.07 | 21440633 | |
313 | Phosphorylation | PVGQPSLSKTSIEQV CCCCCCCCCCCHHHH | 37.92 | 22369663 | |
315 | Phosphorylation | GQPSLSKTSIEQVNE CCCCCCCCCHHHHHH | 31.40 | 29136822 | |
316 | Phosphorylation | QPSLSKTSIEQVNEL CCCCCCCCHHHHHHH | 28.06 | 29136822 | |
325 | Phosphorylation | EQVNELETNSDLGKS HHHHHHHCCCCCCCC | 53.28 | 22369663 | |
327 | Phosphorylation | VNELETNSDLGKSSS HHHHHCCCCCCCCCH | 41.45 | 22369663 | |
332 | Phosphorylation | TNSDLGKSSSSRFSS CCCCCCCCCHHHHHH | 33.38 | 23749301 | |
333 | Phosphorylation | NSDLGKSSSSRFSSF CCCCCCCCHHHHHHH | 35.50 | 22369663 | |
334 | Phosphorylation | SDLGKSSSSRFSSFF CCCCCCCHHHHHHHH | 32.40 | 22369663 | |
335 | Phosphorylation | DLGKSSSSRFSSFFN CCCCCCHHHHHHHHC | 39.01 | 22369663 | |
338 | Phosphorylation | KSSSSRFSSFFNKSA CCCHHHHHHHHCCCC | 25.73 | 22369663 | |
339 | Phosphorylation | SSSSRFSSFFNKSAT CCHHHHHHHHCCCCC | 31.01 | 22369663 | |
344 | Phosphorylation | FSSFFNKSATSLPSL HHHHHCCCCCCCCCC | 37.57 | 22369663 | |
346 | Phosphorylation | SFFNKSATSLPSLDN HHHCCCCCCCCCCCC | 37.58 | 22369663 | |
347 | Phosphorylation | FFNKSATSLPSLDNN HHCCCCCCCCCCCCC | 37.69 | 22369663 | |
350 | Phosphorylation | KSATSLPSLDNNNQV CCCCCCCCCCCCCCC | 54.36 | 22369663 | |
359 | Phosphorylation | DNNNQVPSSNVSVVN CCCCCCCCCCEEEEC | 35.37 | 22369663 | |
360 | Phosphorylation | NNNQVPSSNVSVVNN CCCCCCCCCEEEECC | 34.87 | 22369663 | |
363 | Phosphorylation | QVPSSNVSVVNNDGN CCCCCCEEEECCCCC | 25.29 | 22369663 | |
371 | Phosphorylation | VVNNDGNSTPHQSGS EECCCCCCCCCCCHH | 49.17 | 22369663 | |
372 | Phosphorylation | VNNDGNSTPHQSGSR ECCCCCCCCCCCHHH | 28.88 | 22369663 | |
376 | Phosphorylation | GNSTPHQSGSRLMSF CCCCCCCCHHHHHHH | 35.38 | 22369663 | |
378 | Phosphorylation | STPHQSGSRLMSFFK CCCCCCHHHHHHHHH | 27.73 | 22369663 | |
382 | Phosphorylation | QSGSRLMSFFKESRS CCHHHHHHHHHHHHC | 31.93 | 22369663 | |
385 | Acetylation | SRLMSFFKESRSSTP HHHHHHHHHHHCCCC | 53.41 | 24489116 | |
387 | Phosphorylation | LMSFFKESRSSTPNA HHHHHHHHHCCCCCH | 37.74 | 22369663 | |
389 | Phosphorylation | SFFKESRSSTPNAES HHHHHHHCCCCCHHH | 48.09 | 22369663 | |
390 | Phosphorylation | FFKESRSSTPNAESQ HHHHHHCCCCCHHHH | 46.93 | 22369663 | |
391 | Phosphorylation | FKESRSSTPNAESQL HHHHHCCCCCHHHHH | 23.08 | 22369663 | |
396 | Phosphorylation | SSTPNAESQLLSASD CCCCCHHHHHHHCCC | 24.58 | 22890988 | |
400 | Phosphorylation | NAESQLLSASDKDNG CHHHHHHHCCCCCCC | 34.03 | 22369663 | |
402 | Phosphorylation | ESQLLSASDKDNGKM HHHHHHCCCCCCCCC | 41.64 | 22369663 | |
447 | Phosphorylation | GLLNKGKSETSTPPP CCCCCCCCCCCCCCC | 55.57 | 21440633 | |
449 | Phosphorylation | LNKGKSETSTPPPPP CCCCCCCCCCCCCCC | 45.02 | 28132839 | |
450 | Phosphorylation | NKGKSETSTPPPPPP CCCCCCCCCCCCCCC | 34.56 | 29136822 | |
451 | Phosphorylation | KGKSETSTPPPPPPG CCCCCCCCCCCCCCC | 47.43 | 21440633 |
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 EAP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EAP1_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 EAP1_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 SER-30; SER-281; SER-282;THR-315; THR-325; SER-327; SER-344; SER-387 AND THR-391, AND MASSSPECTROMETRY. | |
"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-281; SER-282; SER-344;THR-346 AND SER-390, AND MASS 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-338, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281, AND MASSSPECTROMETRY. |