UniProt ID | DRS1_YEAST | |
---|---|---|
UniProt AC | P32892 | |
Protein Name | ATP-dependent RNA helicase DRS1 | |
Gene Name | DRS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 752 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | ATP-binding RNA helicase involved in ribosome assembly.. | |
Protein Sequence | MVVGTKKYSNLDFVPTISDSEDDVPILDSSDDEKVEAKKTTKKRKGKNNKKKVSEGDNLDEDVHEDLDAGFKFDLDADDTTSNFQGWNFLAEGESNKDDAEAFVKKDVDLDKIIRRKGGLVKMAHIDSKQEEETEKEKVEKENDSDDEELAMDGFGMGAPMNNGDENQSEEEEEEEEKEEEEEEEEEQEEMTLEKGGKDDEIDEEDDSEEAKADFYAPETEGDEAKKQMYENFNSLSLSRPVLKGLASLGYVKPSPIQSATIPIALLGKDIIAGAVTGSGKTAAFMIPIIERLLYKPAKIASTRVIVLLPTRELAIQVADVGKQIARFVSGITFGLAVGGLNLRQQEQMLKSRPDIVIATPGRFIDHIRNSASFNVDSVEILVMDEADRMLEEGFQDELNEIMGLLPSNRQNLLFSATMNSKIKSLVSLSLKKPVRIMIDPPKKAATKLTQEFVRIRKRDHLKPALLFNLIRKLDPTGQKRIVVFVARKETAHRLRIIMGLLGMSVGELHGSLTQEQRLDSVNKFKNLEVPVLICTDLASRGLDIPKIEVVINYDMPKSYEIYLHRVGRTARAGREGRSVTFVGESSQDRSIVRAAIKSVEENKSLTQGKALGRNVDWVQIEETNKLVESMNDTIEDILVEEKEEKEILRAEMQLRKGENMLKHKKEIQARPRRTWFQSESDKKNSKVLGALSRNKKVTNSKKRKREEAKADGNGARSYRKTKTDRIADQERTFKKQKSTNSNKKKGFKSRR | |
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 |
---|---|---|---|---|---|
16 | Phosphorylation | SNLDFVPTISDSEDD CCCCCCCCCCCCCCC | 28.01 | 28889911 | |
18 | Phosphorylation | LDFVPTISDSEDDVP CCCCCCCCCCCCCCC | 37.25 | 21440633 | |
20 | Phosphorylation | FVPTISDSEDDVPIL CCCCCCCCCCCCCCC | 35.81 | 28889911 | |
29 | Phosphorylation | DDVPILDSSDDEKVE CCCCCCCCCCCHHHH | 32.02 | 21440633 | |
30 | Phosphorylation | DVPILDSSDDEKVEA CCCCCCCCCCHHHHH | 49.07 | 21440633 | |
112 | Acetylation | KKDVDLDKIIRRKGG HHCCCHHHHHHHCCC | 47.53 | 24489116 | |
128 | Phosphorylation | VKMAHIDSKQEEETE EEEEECCHHHHHHHH | 35.32 | 28889911 | |
208 | Phosphorylation | EIDEEDDSEEAKADF CCCCCCCCHHHHHHH | 50.05 | 25521595 | |
299 | Acetylation | RLLYKPAKIASTRVI HHHCCCCHHCCCEEE | 47.54 | 24489116 | |
302 | Phosphorylation | YKPAKIASTRVIVLL CCCCHHCCCEEEEEE | 21.88 | 27017623 | |
432 | Acetylation | SLVSLSLKKPVRIMI HHHHCCCCCCEEEEE | 52.21 | 22865919 | |
657 | Acetylation | RAEMQLRKGENMLKH HHHHHHHCCHHHHHH | 78.24 | 25381059 | |
663 | Acetylation | RKGENMLKHKKEIQA HCCHHHHHHHHHHHC | 42.48 | 25381059 | |
687 | Acetylation | ESDKKNSKVLGALSR HHHHHCHHHHHHHHC | 51.37 | 22865919 | |
693 | Phosphorylation | SKVLGALSRNKKVTN HHHHHHHHCCCCCCC | 33.02 | 30377154 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of DRS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DRS1_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 DRS1_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-208, 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-208, AND MASSSPECTROMETRY. |