| UniProt ID | DBP2_YEAST | |
|---|---|---|
| UniProt AC | P24783 | |
| Protein Name | ATP-dependent RNA helicase DBP2 | |
| Gene Name | DBP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 546 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing.. | |
| Protein Sequence | MTYGGRDQQYNKTNYKSRGGDFRGGRNSDRNSYNDRPQGGNYRGGFGGRSNYNQPQELIKPNWDEELPKLPTFEKNFYVEHESVRDRSDSEIAQFRKENEMTISGHDIPKPITTFDEAGFPDYVLNEVKAEGFDKPTGIQCQGWPMALSGRDMVGIAATGSGKTLSYCLPGIVHINAQPLLAPGDGPIVLVLAPTRELAVQIQTECSKFGHSSRIRNTCVYGGVPKSQQIRDLSRGSEIVIATPGRLIDMLEIGKTNLKRVTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVKQLAADYLNDPIQVQVGSLELSASHNITQIVEVVSDFEKRDRLNKYLETASQDNEYKTLIFASTKRMCDDITKYLREDGWPALAIHGDKDQRERDWVLQEFRNGRSPIMVATDVAARGIDVKGINYVINYDMPGNIEDYVHRIGRTGRAGATGTAISFFTEQNKGLGAKLISIMREANQNIPPELLKYDRRSYGGGHPRYGGGRGGRGGYGRRGGYGGGRGGYGGNRQRDGGWGNRGRSNY | |
| 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 |
|---|---|---|---|---|---|
| 12 | Acetylation | GRDQQYNKTNYKSRG CCCCCCCCCCCCCCC | 32.96 | 22865919 | |
| 50 | Phosphorylation | RGGFGGRSNYNQPQE CCCCCCCCCCCCCHH | 47.11 | 30377154 | |
| 60 | Ubiquitination | NQPQELIKPNWDEEL CCCHHHCCCCCCCCC | 44.94 | 23749301 | |
| 60 | Acetylation | NQPQELIKPNWDEEL CCCHHHCCCCCCCCC | 44.94 | 24489116 | |
| 75 | Acetylation | PKLPTFEKNFYVEHE CCCCCCCCCEEECCC | 48.44 | 24489116 | |
| 83 | Phosphorylation | NFYVEHESVRDRSDS CEEECCCCCCCCCHH | 25.10 | 24961812 | |
| 88 | Phosphorylation | HESVRDRSDSEIAQF CCCCCCCCHHHHHHH | 50.18 | 22369663 | |
| 90 | Phosphorylation | SVRDRSDSEIAQFRK CCCCCCHHHHHHHHH | 31.95 | 22369663 | |
| 135 | Acetylation | VKAEGFDKPTGIQCQ HHCCCCCCCCCCEEC | 42.07 | 24489116 | |
| 208 | Acetylation | QIQTECSKFGHSSRI HHHHHHHHCCCCHHH | 68.00 | 24489116 | |
| 218 | Phosphorylation | HSSRIRNTCVYGGVP CCHHHCCCEEECCCC | 8.10 | 29136822 | |
| 221 | Phosphorylation | RIRNTCVYGGVPKSQ HHCCCEEECCCCHHH | 15.43 | 29136822 | |
| 226 | Ubiquitination | CVYGGVPKSQQIRDL EEECCCCHHHHHHHH | 59.50 | 23749301 | |
| 227 | Phosphorylation | VYGGVPKSQQIRDLS EECCCCHHHHHHHHH | 22.65 | 23749301 | |
| 255 | Acetylation | IDMLEIGKTNLKRVT EEHHHHCCCCCEEEE | 39.64 | 24489116 | |
| 283 | Acetylation | GFEPQIRKIVDQIRP CCHHHHHHHHHHHCC | 49.03 | 22865919 | |
| 303 | Acetylation | MWSATWPKEVKQLAA EEECCCCHHHHHHHH | 67.70 | 24489116 | |
| 350 | Acetylation | EKRDRLNKYLETASQ HHHHHHHHHHHHHCC | 56.66 | 24489116 | |
| 356 | Phosphorylation | NKYLETASQDNEYKT HHHHHHHCCCCCHHH | 45.55 | 27017623 | |
| 362 | Acetylation | ASQDNEYKTLIFAST HCCCCCHHHHEEECH | 30.58 | 24489116 | |
| 363 | Phosphorylation | SQDNEYKTLIFASTK CCCCCHHHHEEECHH | 24.96 | 19795423 | |
| 368 | Phosphorylation | YKTLIFASTKRMCDD HHHHEEECHHHHHHH | 24.58 | 19823750 | |
| 369 | Phosphorylation | KTLIFASTKRMCDDI HHHEEECHHHHHHHH | 21.17 | 19823750 | |
| 370 | Acetylation | TLIFASTKRMCDDIT HHEEECHHHHHHHHH | 35.32 | 25381059 | |
| 378 | Acetylation | RMCDDITKYLREDGW HHHHHHHHHHHHHCC | 42.49 | 24489116 | |
| 451 | Phosphorylation | YVHRIGRTGRAGATG HHHHHCCCCCCCCCC | 26.30 | 27017623 | |
| 459 | Phosphorylation | GRAGATGTAISFFTE CCCCCCCCCHHHHHH | 19.23 | 27017623 | |
| 462 | Phosphorylation | GATGTAISFFTEQNK CCCCCCHHHHHHCCC | 16.31 | 27017623 | |
| 469 | Ubiquitination | SFFTEQNKGLGAKLI HHHHHCCCCHHHHHH | 56.03 | 22817900 | |
| 474 | Ubiquitination | QNKGLGAKLISIMRE CCCCHHHHHHHHHHH | 44.55 | 23749301 | |
| 474 | Acetylation | QNKGLGAKLISIMRE CCCCHHHHHHHHHHH | 44.55 | 24489116 | |
| 492 | Acetylation | NIPPELLKYDRRSYG CCCHHHHHCCCCCCC | 58.70 | 24489116 | |
| 497 | Phosphorylation | LLKYDRRSYGGGHPR HHHCCCCCCCCCCCC | 29.08 | 28889911 |
| 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 DBP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DBP2_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 DBP2_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-88 AND SER-90, 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-88 AND SER-90, 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-90, 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-90, AND MASSSPECTROMETRY. | |