| UniProt ID | DBP5_YEAST | |
|---|---|---|
| UniProt AC | P20449 | |
| Protein Name | ATP-dependent RNA helicase DBP5 | |
| Gene Name | DBP5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 482 | |
| Subcellular Localization |
Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane Peripheral membrane protein Cytoplasmic side. Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress. |
|
| Protein Description | ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.. | |
| Protein Sequence | MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADIQADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPEDASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDEADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDVLTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVLKD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDTKRDPA ------CCCCCCCHH | 54.72 | 22369663 | |
| 4 | Phosphorylation | ----MSDTKRDPADL ----CCCCCCCHHHH | 22.22 | 28132839 | |
| 5 | Acetylation | ---MSDTKRDPADLL ---CCCCCCCHHHHH | 60.85 | 24489116 | |
| 14 | Phosphorylation | DPADLLASLKIDNEK CHHHHHHHCCCCCCC | 30.11 | 19795423 | |
| 21 | Ubiquitination | SLKIDNEKEDTSEVS HCCCCCCCCCCCCCC | 68.12 | 23749301 | |
| 24 | Phosphorylation | IDNEKEDTSEVSTKE CCCCCCCCCCCCHHH | 28.07 | 23749301 | |
| 25 | Phosphorylation | DNEKEDTSEVSTKET CCCCCCCCCCCHHHH | 48.61 | 27717283 | |
| 28 | Phosphorylation | KEDTSEVSTKETVKS CCCCCCCCHHHHHHC | 29.70 | 25521595 | |
| 29 | Phosphorylation | EDTSEVSTKETVKSQ CCCCCCCHHHHHHCC | 37.77 | 24961812 | |
| 32 | Phosphorylation | SEVSTKETVKSQPEK CCCCHHHHHHCCCCC | 34.49 | 24961812 | |
| 43 | Phosphorylation | QPEKTADSIKPAEKL CCCCCCCCCCHHHHH | 30.01 | 23749301 | |
| 49 | Acetylation | DSIKPAEKLVPKVEE CCCCHHHHHHHHHHH | 57.82 | 24489116 | |
| 64 | Phosphorylation | KKTKQEDSNLISSEY HCCCHHHCCCCCCEE | 32.55 | 28889911 | |
| 68 | Phosphorylation | QEDSNLISSEYEVKV HHHCCCCCCEEEEEE | 21.93 | 24961812 | |
| 69 | Phosphorylation | EDSNLISSEYEVKVK HHCCCCCCEEEEEEE | 36.88 | 28152593 | |
| 71 | Phosphorylation | SNLISSEYEVKVKLA CCCCCCEEEEEEEEE | 28.15 | 21440633 | |
| 74 | Acetylation | ISSEYEVKVKLADIQ CCCEEEEEEEEECCC | 23.01 | 24489116 | |
| 76 | Acetylation | SEYEVKVKLADIQAD CEEEEEEEEECCCCC | 32.04 | 24489116 | |
| 86 | Phosphorylation | DIQADPNSPLYSAKS CCCCCCCCCCCCCCC | 22.97 | 17330950 | |
| 89 | Phosphorylation | ADPNSPLYSAKSFDE CCCCCCCCCCCCHHH | 15.23 | 26447709 | |
| 90 | Phosphorylation | DPNSPLYSAKSFDEL CCCCCCCCCCCHHHC | 36.58 | 24961812 | |
| 92 | Acetylation | NSPLYSAKSFDELGL CCCCCCCCCHHHCCC | 45.79 | 24489116 | |
| 93 | Phosphorylation | SPLYSAKSFDELGLA CCCCCCCCHHHCCCC | 37.33 | 21440633 | |
| 105 | Acetylation | GLAPELLKGIYAMKF CCCHHHHHHHHHHCC | 56.75 | 24489116 | |
| 111 | Acetylation | LKGIYAMKFQKPSKI HHHHHHHCCCCCCHH | 36.15 | 24489116 | |
| 145 | Phosphorylation | SQSGTGKTAAFSLTM CCCCCCCCCEEEEEE | 25.27 | 29650682 | |
| 154 | Phosphorylation | AFSLTMLTRVNPEDA EEEEEEEEECCCCCC | 23.04 | 29650682 | |
| 162 | Phosphorylation | RVNPEDASPQAICLA ECCCCCCCCCEEEEC | 29.84 | 28152593 | |
| 187 | Acetylation | EVVQEMGKFTKITSQ HHHHHHHHHCCCCCE | 48.85 | 24489116 | |
| 203 | Acetylation | IVPDSFEKNKQINAQ ECCCCHHCCCCCCEE | 68.39 | 24489116 | |
| 466 | Phosphorylation | IEMTRVPTDDWDEVE CEEEECCCCCHHHHH | 43.67 | 21440633 | |
| 474 | Acetylation | DDWDEVEKIVKKVLK CCHHHHHHHHHHHHC | 58.96 | 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 DBP5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DBP5_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 DBP5_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-69; SER-86 AND SER-162,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-86, AND MASSSPECTROMETRY. | |
