| UniProt ID | ULS1_YEAST | |
|---|---|---|
| UniProt AC | Q08562 | |
| Protein Name | ATP-dependent helicase ULS1 | |
| Gene Name | ULS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1619 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ATP-dependent helicase involved mating type switching and in silencing interference through its interaction with the silencing regulator SIR4. Cooperates with UBC4 and UBC5 to mediate ubiquitination of SUMO conjugates.. | |
| Protein Sequence | MAAVPTIDLTLADSDNEDIFHSFSSSTSVDKIDIRKENGKLRMAGLEVAQSNDDAARQAFHVFKTNISNNETFDTILSKSKTITDSTFNNEKSSNEVKQQQVLKEETMGSSNDEKKTQESSPSAEMIKLFYENDDVPLSDSFKQKEEGKRINQDEQVKENICGISSSYVSKDYDGVEDDFEPNTCQDSNLDFQEEKLNLNNKPSQQQFSDPETKDNSLKSENKDQIKGVTTTSYRDLPIESSAFQDSETQNNSKNTIPNIVNEKRTPALPSNLSSVESSLKNETAKVEGKTTVRLPGLQNNVALLEQEQSELFKHFSEQPVDISDFGRKIKRKHSGDFADNKILKRPILPSKNMDHTTHNSHDSEQKNSSIIILSDEDESGAGINDIESPLKVSEPNTADALRSSVPEVISLLDLPNIDLNNSVIKEASGSNSIPTSETDAQSSSSSVLQGTIMTEQATQSSQHECNSSLDTLKKNHQKLLKDLNSRESELRNALSCCKTNSEILRRKLSRREKEVSDAEKHWQLLLTSMARGGRTISSTQQILVDEAENQLNKLKEKRQLTKSKLDSINLKMYNYNEQWKSFVHSKNINLQKSLAALERSARDSKASATVNKRNECLAEKEKLDQMLKEGTLSFSTYKQLTGEIQQKLNDLKLGDQRTTDINSVLPIVRQPLAKRDLFIKSIDTAKDLLAKNTSRTEMTKRILYRHLDNLVSYKNFFEDGRSLIDINRRHVAHESAQILFTNGVKMPIVFETLQDYGIKFSNPAIVNPDRRAQYFKSIEVARDLISKSTRSEDAKRKITRFLNIIEEFRKDIDTGFPPTPLKREGVGKAVVGLRQQGLKMDRLYENLRRYKIPITSEELLQQSYLFPVNADQRPPSNWNIVENTEDTSSTANDLSMQDEFHISNMHAAEDQEQIRALLENVKQSESIIDGEALTPEDMTVNLLKHQRLGLHWLLQVENSAKKGGLLADDMGLGKTIQAIALMLANRSEESKCKTNLIVAPVSVLRVWKGELETKVKKRAKFTTFIFGGSGNGKVKHWRDLARYDAVLVSYQTLANEFKKHWPKKLDGEQNQLPAVPHIQALNRLKTSNEYYSPFFCNDSTFYRILLDEGQNIKNKNTRASKACCTINGMYRWVLSGTPIQNSMDELYSLIRFLRIPPYHKEQRFKLDIGRFFQRNKQYQYDNEDRKNALRKVRVLLNAIMLRRSKADKIDGKPLLELPPKIVEVDESRLKGEELKFYTALESKNQALAKKLLNNSTRGSYSSVLTLLLRLRQACCHSELVVMGEKKAEGTKVANGKSFEDDWLRLYYKITHMSGEAQAQVITSMNSMTCFWCMEQLEPEAMSVLTGCGHLICDTCIEPFIEESSMLPQAKKTKGGAFAIPCKDCQRLTNEKDIVSHKLYDQVINQGFTEEDLHAEYLSEMEKQKIQQKNVYVPNFESLEPSTKIEQCIQVIQRVFDESATEKIIIFSQFTTFFEILEHFLKNKLNFPYLKYIGSMNAQRRSDVINEFYRDPEKRILLISMKAGNSGLTLTCANHVVIVDPFWNPYVEEQAQDRCYRISQTKKVQVHKLFIKDSVEDRISELQKRKKEMVDSAMDPGKIKEVNSLGRRELGFLFGLNAL | |
| 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 |
|---|---|---|---|---|---|
| 111 | Phosphorylation | KEETMGSSNDEKKTQ HHHHCCCCCCHHHHH | 42.44 | 28889911 | |
| 117 | Phosphorylation | SSNDEKKTQESSPSA CCCCHHHHHCCCCCH | 48.95 | 21440633 | |
| 120 | Phosphorylation | DEKKTQESSPSAEMI CHHHHHCCCCCHHHH | 37.42 | 22369663 | |
| 121 | Phosphorylation | EKKTQESSPSAEMIK HHHHHCCCCCHHHHH | 23.32 | 22369663 | |
| 123 | Phosphorylation | KTQESSPSAEMIKLF HHHCCCCCHHHHHHH | 38.52 | 22369663 | |
| 139 | Phosphorylation | ENDDVPLSDSFKQKE HCCCCCCCHHHCCHH | 25.74 | 28152593 | |
| 141 | Phosphorylation | DDVPLSDSFKQKEEG CCCCCCHHHCCHHHC | 30.85 | 28152593 | |
| 204 | Phosphorylation | LNLNNKPSQQQFSDP HCCCCCCCCCCCCCC | 42.08 | 22369663 | |
| 209 | Phosphorylation | KPSQQQFSDPETKDN CCCCCCCCCCCCCCC | 48.17 | 22369663 | |
| 213 | Phosphorylation | QQFSDPETKDNSLKS CCCCCCCCCCCCCCC | 49.43 | 22369663 | |
| 217 | Phosphorylation | DPETKDNSLKSENKD CCCCCCCCCCCCCHH | 47.51 | 28889911 | |
| 231 | Phosphorylation | DQIKGVTTTSYRDLP HHCCCCEECEECCCC | 16.02 | 30377154 | |
| 317 | Phosphorylation | SELFKHFSEQPVDIS HHHHHHHHCCCCCHH | 34.73 | 21440633 | |
| 335 | Phosphorylation | RKIKRKHSGDFADNK HHHHHHCCCCCCCCC | 42.99 | 19795423 | |
| 370 | Phosphorylation | DSEQKNSSIIILSDE CCCCCCCEEEEEECC | 27.48 | 19779198 | |
| 375 | Phosphorylation | NSSIIILSDEDESGA CCEEEEEECCCCCCC | 28.66 | 28889911 | |
| 380 | Phosphorylation | ILSDEDESGAGINDI EEECCCCCCCCCCCC | 46.39 | 30377154 | |
| 634 | Phosphorylation | MLKEGTLSFSTYKQL HHHHCCCCHHHHHHH | 19.59 | 27214570 | |
| 778 | Phosphorylation | RRAQYFKSIEVARDL HHHHHHHHHHHHHHH | 17.68 | 27017623 | |
| 787 | Phosphorylation | EVARDLISKSTRSED HHHHHHHHHCCCCHH | 28.05 | 27017623 | |
| 1023 | Phosphorylation | VKKRAKFTTFIFGGS HHHHCCEEEEEECCC | 21.79 | 19823750 | |
| 1024 | Phosphorylation | KKRAKFTTFIFGGSG HHHCCEEEEEECCCC | 20.19 | 19823750 | |
| 1030 | Phosphorylation | TTFIFGGSGNGKVKH EEEEECCCCCCCCCH | 29.48 | 19795423 |
| 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 ULS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ULS1_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 ULS1_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-121 AND SER-209, ANDMASS SPECTROMETRY. | |