| UniProt ID | MTR4_YEAST | |
|---|---|---|
| UniProt AC | P47047 | |
| Protein Name | ATP-dependent RNA helicase DOB1 | |
| Gene Name | MTR4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1073 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | ATP-dependent RNA helicase required for the 3'-end formation of 5.8S RNA. Cofactor for the exosome complex that unwinds secondary structure in pre-rRNA. Required for nucleocytoplasmic transport of mRNA. May serve as a chaperone which translocates or normalizes the structure of mRNAs in preparation for export. Component of the TRAMP complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates.. | |
| Protein Sequence | MDSTDLFDVFEETPVELPTDSNGEKNADTNVGDTPDHTQDKKHGLEEEKEEHEENNSENKKIKSNKSKTEDKNKKVVVPVLADSFEQEASREVDASKGLTNSETLQVEQDGKVRLSHQVRHQVALPPNYDYTPIAEHKRVNEARTYPFTLDPFQDTAISCIDRGESVLVSAHTSAGKTVVAEYAIAQSLKNKQRVIYTSPIKALSNQKYRELLAEFGDVGLMTGDITINPDAGCLVMTTEILRSMLYRGSEVMREVAWVIFDEVHYMRDKERGVVWEETIILLPDKVRYVFLSATIPNAMEFAEWICKIHSQPCHIVYTNFRPTPLQHYLFPAHGDGIYLVVDEKSTFREENFQKAMASISNQIGDDPNSTDSRGKKGQTYKGGSAKGDAKGDIYKIVKMIWKKKYNPVIVFSFSKRDCEELALKMSKLDFNSDDEKEALTKIFNNAIALLPETDRELPQIKHILPLLRRGIGIHHSGLLPILKEVIEILFQEGFLKVLFATETFSIGLNMPAKTVVFTSVRKWDGQQFRWVSGGEYIQMSGRAGRRGLDDRGIVIMMIDEKMEPQVAKGMVKGQADRLDSAFHLGYNMILNLMRVEGISPEFMLEHSFFQFQNVISVPVMEKKLAELKKDFDGIEVEDEENVKEYHEIEQAIKGYREDVRQVVTHPANALSFLQPGRLVEISVNGKDNYGWGAVVDFAKRINKRNPSAVYTDHESYIVNVVVNTMYIDSPVNLLKPFNPTLPEGIRPAEEGEKSICAVIPITLDSIKSIGNLRLYMPKDIRASGQKETVGKSLREVNRRFPDGIPVLDPVKNMKIEDEDFLKLMKKIDVLNTKLSSNPLTNSMRLEELYGKYSRKHDLHEDMKQLKRKISESQAVIQLDDLRRRKRVLRRLGFCTPNDIIELKGRVACEISSGDELLLTELIFNGNFNELKPEQAAALLSCFAFQERCKEAPRLKPELAEPLKAMREIAAKIAKIMKDSKIEVVEKDYVESFRHELMEVVYEWCRGATFTQICKMTDVYEGSLIRMFKRLEELVKELVDVANTIGNSSLKEKMEAVLKLIHRDIVSAGSLYL | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MDSTDLFDVF -----CCCCCCCHHH | 35.36 | 30377154 | |
| 4 | Phosphorylation | ----MDSTDLFDVFE ----CCCCCCCHHHC | 49.40 | 30377154 | |
| 13 | Phosphorylation | LFDVFEETPVELPTD CCHHHCCCCCCCCCC | 25.99 | 30377154 | |
| 19 | Phosphorylation | ETPVELPTDSNGEKN CCCCCCCCCCCCCCC | 65.76 | 30377154 | |
| 21 | Phosphorylation | PVELPTDSNGEKNAD CCCCCCCCCCCCCCC | 49.57 | 28152593 | |
| 29 | Phosphorylation | NGEKNADTNVGDTPD CCCCCCCCCCCCCCC | 29.41 | 22890988 | |
| 34 | Phosphorylation | ADTNVGDTPDHTQDK CCCCCCCCCCHHHCH | 25.37 | 22369663 | |
| 38 | Phosphorylation | VGDTPDHTQDKKHGL CCCCCCHHHCHHCCC | 45.93 | 22369663 | |
| 75 | Ubiquitination | KTEDKNKKVVVPVLA CCCCCCCCEEEEEEC | 50.05 | 17644757 | |
| 84 | Phosphorylation | VVPVLADSFEQEASR EEEEECHHHHHHHHC | 25.69 | 22369663 | |
| 90 | Phosphorylation | DSFEQEASREVDASK HHHHHHHHCCCCCCC | 28.37 | 22369663 | |
| 96 | Phosphorylation | ASREVDASKGLTNSE HHCCCCCCCCCCCCC | 23.85 | 22369663 | |
| 97 | Ubiquitination | SREVDASKGLTNSET HCCCCCCCCCCCCCE | 60.71 | 17644757 | |
| 97 | Acetylation | SREVDASKGLTNSET HCCCCCCCCCCCCCE | 60.71 | 22865919 | |
| 100 | Phosphorylation | VDASKGLTNSETLQV CCCCCCCCCCCEEEE | 45.42 | 30377154 | |
| 102 | Phosphorylation | ASKGLTNSETLQVEQ CCCCCCCCCEEEEEE | 27.07 | 30377154 | |
| 104 | Phosphorylation | KGLTNSETLQVEQDG CCCCCCCEEEEEECC | 23.47 | 30377154 | |
| 112 | Acetylation | LQVEQDGKVRLSHQV EEEEECCEEEEEEEE | 32.26 | 24489116 | |
| 132 | Phosphorylation | LPPNYDYTPIAEHKR CCCCCCCCCHHHCCC | 12.81 | 21551504 | |
| 183 | Phosphorylation | GKTVVAEYAIAQSLK CCHHHHHHHHHHHHC | 8.12 | 25533186 | |
| 202 | Ubiquitination | VIYTSPIKALSNQKY EEECCHHHHHCCHHH | 46.81 | 24961812 | |
| 355 | Ubiquitination | FREENFQKAMASISN CCHHHHHHHHHHHHH | 35.67 | 17644757 | |
| 399 | Acetylation | GDIYKIVKMIWKKKY CCHHHHHHHHHHHCC | 28.30 | 24489116 | |
| 425 | Acetylation | DCEELALKMSKLDFN HHHHHHHHHHHCCCC | 35.20 | 24489116 | |
| 428 | Acetylation | ELALKMSKLDFNSDD HHHHHHHHCCCCCCH | 48.88 | 24489116 | |
| 433 | Phosphorylation | MSKLDFNSDDEKEAL HHHCCCCCCHHHHHH | 46.57 | 23749301 | |
| 437 | Acetylation | DFNSDDEKEALTKIF CCCCCHHHHHHHHHH | 56.11 | 24489116 | |
| 462 | Acetylation | DRELPQIKHILPLLR CCCCHHHHHHHHHHH | 21.24 | 24489116 | |
| 779 | Acetylation | NLRLYMPKDIRASGQ CEEEECCCCHHCCCC | 49.62 | 24489116 | |
| 815 | Acetylation | LDPVKNMKIEDEDFL CCCCCCCCCCCHHHH | 52.95 | 24489116 | |
| 823 | Acetylation | IEDEDFLKLMKKIDV CCCHHHHHHHHHHHH | 46.67 | 24489116 | |
| 834 | Acetylation | KIDVLNTKLSSNPLT HHHHHCCCCCCCCCC | 45.35 | 24489116 | |
| 843 | Phosphorylation | SSNPLTNSMRLEELY CCCCCCHHHHHHHHH | 10.47 | 28889911 | |
| 852 | Acetylation | RLEELYGKYSRKHDL HHHHHHHHHHHCCCH | 26.88 | 24489116 | |
| 864 | Acetylation | HDLHEDMKQLKRKIS CCHHHHHHHHHHHHC | 65.87 | 24489116 | |
| 871 | Phosphorylation | KQLKRKISESQAVIQ HHHHHHHCHHHHHHC | 33.94 | 28889911 | |
| 873 | Phosphorylation | LKRKISESQAVIQLD HHHHHCHHHHHHCHH | 19.35 | 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 MTR4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MTR4_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 MTR4_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 THR-29; THR-34; THR-38;SER-84; SER-843 AND SER-871, 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-84, 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 THR-34, AND MASSSPECTROMETRY. | |
