UniProt ID | DED1_YEAST | |
---|---|---|
UniProt AC | P06634 | |
Protein Name | ATP-dependent RNA helicase DED1 | |
Gene Name | DED1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 604 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes. Has weak ATP-dependent affinity for dsRNA, but strong ATP-dependent affinity for ssRNA. Acts as a virus host factor involved in the replication of the MBV and the L-A viruses by promoting the negative-strand RNA synthesis. May be involved in recognition of the preinitiation complex and DNA binding of the RNA polymerase III and play a role in mRNA splicing.. | |
Protein Sequence | MAELSEQVQNLSINDNNENGYVPPHLRGKPRSARNNSSNYNNNNGGYNGGRGGGSFFSNNRRGGYGNGGFFGGNNGGSRSNGRSGGRWIDGKHVPAPRNEKAEIAIFGVPEDPNFQSSGINFDNYDDIPVDASGKDVPEPITEFTSPPLDGLLLENIKLARFTKPTPVQKYSVPIVANGRDLMACAQTGSGKTGGFLFPVLSESFKTGPSPQPESQGSFYQRKAYPTAVIMAPTRELATQIFDEAKKFTYRSWVKACVVYGGSPIGNQLREIERGCDLLVATPGRLNDLLERGKISLANVKYLVLDEADRMLDMGFEPQIRHIVEDCDMTPVGERQTLMFSATFPADIQHLARDFLSDYIFLSVGRVGSTSENITQKVLYVENQDKKSALLDLLSASTDGLTLIFVETKRMADQLTDFLIMQNFRATAIHGDRTQSERERALAAFRSGAATLLVATAVAARGLDIPNVTHVINYDLPSDVDDYVHRIGRTGRAGNTGLATAFFNSENSNIVKGLHEILTEANQEVPSFLKDAMMSAPGSRSNSRRGGFGRNNNRDYRKAGGASAGGWGSSRSRDNSFRGGSGWGSDSKSSGWGNSGGSNNSSWW | |
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 | ------MAELSEQVQ ------CCHHHHHHH | 26.83 | 22814378 | |
5 | Phosphorylation | ---MAELSEQVQNLS ---CCHHHHHHHCCC | 19.93 | 30377154 | |
12 | Phosphorylation | SEQVQNLSINDNNEN HHHHHCCCCCCCCCC | 27.22 | 30377154 | |
37 | Phosphorylation | PRSARNNSSNYNNNN CCCCCCCCCCCCCCC | 24.41 | 24909858 | |
38 | Phosphorylation | RSARNNSSNYNNNNG CCCCCCCCCCCCCCC | 45.52 | 24909858 | |
40 | Phosphorylation | ARNNSSNYNNNNGGY CCCCCCCCCCCCCCC | 22.63 | 22369663 | |
47 | Phosphorylation | YNNNNGGYNGGRGGG CCCCCCCCCCCCCCC | 16.42 | 22369663 | |
55 | Phosphorylation | NGGRGGGSFFSNNRR CCCCCCCCCCCCCCC | 26.79 | 24909858 | |
58 | Phosphorylation | RGGGSFFSNNRRGGY CCCCCCCCCCCCCCC | 31.05 | 21440633 | |
62 | Methylation | SFFSNNRRGGYGNGG CCCCCCCCCCCCCCC | 45.04 | 23865587 | |
92 | Acetylation | GGRWIDGKHVPAPRN CCCCCCCCCCCCCCC | 37.37 | 24489116 | |
117 | Phosphorylation | PEDPNFQSSGINFDN CCCCCCCCCCCCCCC | 26.79 | 30377154 | |
118 | Phosphorylation | EDPNFQSSGINFDNY CCCCCCCCCCCCCCC | 32.67 | 30377154 | |
135 | Ubiquitination | IPVDASGKDVPEPIT CCCCCCCCCCCCCCC | 53.72 | 17644757 | |
142 | Phosphorylation | KDVPEPITEFTSPPL CCCCCCCCCCCCCCC | 35.44 | 27017623 | |
145 | Phosphorylation | PEPITEFTSPPLDGL CCCCCCCCCCCCCCC | 33.81 | 27017623 | |
146 | Phosphorylation | EPITEFTSPPLDGLL CCCCCCCCCCCCCCH | 29.82 | 28747907 | |
158 | Ubiquitination | GLLLENIKLARFTKP CCHHCCCEEEECCCC | 47.91 | 22106047 | |
164 | Acetylation | IKLARFTKPTPVQKY CEEEECCCCCCCCCC | 44.15 | 22865919 | |
170 | Ubiquitination | TKPTPVQKYSVPIVA CCCCCCCCCEEEEEE | 39.46 | 23749301 | |
170 | Acetylation | TKPTPVQKYSVPIVA CCCCCCCCCEEEEEE | 39.46 | 24489116 | |
192 | Ubiquitination | CAQTGSGKTGGFLFP EECCCCCCCCCCCHH | 45.77 | 17644757 | |
193 | Phosphorylation | AQTGSGKTGGFLFPV ECCCCCCCCCCCHHH | 46.17 | 21440633 | |
202 | Phosphorylation | GFLFPVLSESFKTGP CCCHHHHCCCCCCCC | 31.28 | 30377154 | |
206 | Ubiquitination | PVLSESFKTGPSPQP HHHCCCCCCCCCCCC | 62.95 | 17644757 | |
207 | Phosphorylation | VLSESFKTGPSPQPE HHCCCCCCCCCCCCC | 52.92 | 27214570 | |
210 | Phosphorylation | ESFKTGPSPQPESQG CCCCCCCCCCCCCCC | 37.20 | 20377248 | |
215 | Phosphorylation | GPSPQPESQGSFYQR CCCCCCCCCCCCCCC | 46.66 | 21440633 | |
218 | Phosphorylation | PQPESQGSFYQRKAY CCCCCCCCCCCCCCC | 17.10 | 21440633 | |
220 | Phosphorylation | PESQGSFYQRKAYPT CCCCCCCCCCCCCCC | 14.76 | 30377154 | |
223 | Ubiquitination | QGSFYQRKAYPTAVI CCCCCCCCCCCCEEE | 36.43 | 17644757 | |
246 | Ubiquitination | TQIFDEAKKFTYRSW HHHHHHHHHCCHHHH | 46.50 | 17644757 | |
246 | Acetylation | TQIFDEAKKFTYRSW HHHHHHHHHCCHHHH | 46.50 | 24489116 | |
246 | Succinylation | TQIFDEAKKFTYRSW HHHHHHHHHCCHHHH | 46.50 | 23954790 | |
247 | Ubiquitination | QIFDEAKKFTYRSWV HHHHHHHHCCHHHHH | 50.41 | 17644757 | |
255 | Ubiquitination | FTYRSWVKACVVYGG CCHHHHHHHHEEECC | 29.79 | 17644757 | |
263 | Phosphorylation | ACVVYGGSPIGNQLR HHEEECCCCHHHHHH | 14.69 | 21082442 | |
301 | Ubiquitination | KISLANVKYLVLDEA CCCHHCCEEEEEEHH | 32.45 | 24961812 | |
369 | Phosphorylation | LSVGRVGSTSENITQ EEECCCCCCCCCCCE | 26.38 | 25704821 | |
370 | Phosphorylation | SVGRVGSTSENITQK EECCCCCCCCCCCEE | 33.85 | 27214570 | |
371 | Phosphorylation | VGRVGSTSENITQKV ECCCCCCCCCCCEEE | 30.28 | 27214570 | |
377 | Acetylation | TSENITQKVLYVENQ CCCCCCEEEEEEECC | 26.09 | 24489116 | |
386 | 2-Hydroxyisobutyrylation | LYVENQDKKSALLDL EEEECCCHHHHHHHH | 38.57 | - | |
386 | Succinylation | LYVENQDKKSALLDL EEEECCCHHHHHHHH | 38.57 | 23954790 | |
436 | Phosphorylation | IHGDRTQSERERALA CCCCCCHHHHHHHHH | 37.70 | 28889911 | |
451 | Phosphorylation | AFRSGAATLLVATAV HHHHHHHHHHHHHHH | 21.79 | 28889911 | |
456 | Phosphorylation | AATLLVATAVAARGL HHHHHHHHHHHHCCC | 17.74 | 28889911 | |
478 | Phosphorylation | VINYDLPSDVDDYVH EEECCCCCCHHHHHH | 58.52 | 21440633 | |
505 | Phosphorylation | LATAFFNSENSNIVK EEEEEECCCCCCHHH | 32.76 | 30377154 | |
508 | Phosphorylation | AFFNSENSNIVKGLH EEECCCCCCHHHHHH | 24.71 | 27214570 | |
512 | Ubiquitination | SENSNIVKGLHEILT CCCCCHHHHHHHHHH | 52.54 | 17644757 | |
527 | Phosphorylation | EANQEVPSFLKDAMM HHHHHCCHHHHHHHH | 48.68 | 21440633 | |
530 | Ubiquitination | QEVPSFLKDAMMSAP HHCCHHHHHHHHHCC | 41.24 | 23749301 | |
535 | Phosphorylation | FLKDAMMSAPGSRSN HHHHHHHHCCCCCCC | 20.44 | 22369663 | |
539 | Phosphorylation | AMMSAPGSRSNSRRG HHHHCCCCCCCCCCC | 31.32 | 22369663 | |
541 | Phosphorylation | MSAPGSRSNSRRGGF HHCCCCCCCCCCCCC | 40.63 | 22369663 | |
543 | Phosphorylation | APGSRSNSRRGGFGR CCCCCCCCCCCCCCC | 25.30 | 22369663 | |
558 | Ubiquitination | NNNRDYRKAGGASAG CCCCCHHHCCCCCCC | 45.19 | 23749301 | |
563 | Phosphorylation | YRKAGGASAGGWGSS HHHCCCCCCCCCCCC | 30.62 | 21440633 | |
569 | Phosphorylation | ASAGGWGSSRSRDNS CCCCCCCCCCCCCCC | 18.97 | 22369663 | |
570 | Phosphorylation | SAGGWGSSRSRDNSF CCCCCCCCCCCCCCC | 30.27 | 22369663 | |
572 | Phosphorylation | GGWGSSRSRDNSFRG CCCCCCCCCCCCCCC | 46.03 | 22369663 | |
576 | Phosphorylation | SSRSRDNSFRGGSGW CCCCCCCCCCCCCCC | 22.17 | 22369663 | |
581 | Phosphorylation | DNSFRGGSGWGSDSK CCCCCCCCCCCCCCC | 33.91 | 24909858 | |
585 | Phosphorylation | RGGSGWGSDSKSSGW CCCCCCCCCCCCCCC | 32.00 | 22369663 | |
587 | Phosphorylation | GSGWGSDSKSSGWGN CCCCCCCCCCCCCCC | 35.81 | 22369663 | |
588 | Ubiquitination | SGWGSDSKSSGWGNS CCCCCCCCCCCCCCC | 54.34 | 23749301 | |
589 | Phosphorylation | GWGSDSKSSGWGNSG CCCCCCCCCCCCCCC | 37.73 | 30377154 | |
590 | Phosphorylation | WGSDSKSSGWGNSGG CCCCCCCCCCCCCCC | 42.15 | 21440633 | |
595 | Phosphorylation | KSSGWGNSGGSNNSS CCCCCCCCCCCCCCC | 40.36 | 21440633 | |
598 | Phosphorylation | GWGNSGGSNNSSWW- CCCCCCCCCCCCCC- | 36.04 | 10364207 | |
601 | Phosphorylation | NSGGSNNSSWW---- CCCCCCCCCCC---- | 31.42 | 30377154 | |
602 | Phosphorylation | SGGSNNSSWW----- CCCCCCCCCC----- | 34.74 | 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 DED1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DED1_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 DED1_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-210; SER-263; SER-535;SER-539; SER-541 AND SER-543, AND MASS 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-541, AND MASSSPECTROMETRY. | |
"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-535; SER-539; SER-543;SER-572 AND SER-576, AND MASS 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-535; SER-539 ANDSER-576, AND MASS SPECTROMETRY. |