| UniProt ID | RUVB2_YEAST | |
|---|---|---|
| UniProt AC | Q12464 | |
| Protein Name | RuvB-like protein 2 | |
| Gene Name | RVB2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 471 | |
| Subcellular Localization | Nucleus, nucleoplasm . | |
| Protein Description | DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to 'Ser-129' phosphorylated H2A histones as a response to DNA damage. During transcription may recruit SPT15/TBP to the TATA-boxes of involved genes. Required for box C/D and box H/ACA snoRNA accumulation and involved in pre-rRNA processing.. | |
| Protein Sequence | MSIQTSDPNETSDLKSLSLIAAHSHITGLGLDENLQPRPTSEGMVGQLQARRAAGVILKMVQNGTIAGRAVLVAGPPSTGKTALAMGVSQSLGKDVPFTAIAGSEIFSLELSKTEALTQAFRKSIGIKIKEETELIEGEVVEIQIDRSITGGHKQGKLTIKTTDMETIYELGNKMIDGLTKEKVLAGDVISIDKASGKITKLGRSFARSRDYDAMGADTRFVQCPEGELQKRKTVVHTVSLHEIDVINSRTQGFLALFTGDTGEIRSEVRDQINTKVAEWKEEGKAEIVPGVLFIDEVHMLDIECFSFINRALEDEFAPIVMMATNRGVSKTRGTNYKSPHGLPLDLLDRSIIITTKSYNEQEIKTILSIRAQEEEVELSSDALDLLTKTGVETSLRYSSNLISVAQQIAMKRKNNTVEVEDVKRAYLLFLDSARSVKYVQENESQYIDDQGNVQISIAKSADPDAMDTTE | |
| 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 | ------MSIQTSDPN ------CCCCCCCCC | 24.33 | 24909858 | |
| 5 | Phosphorylation | ---MSIQTSDPNETS ---CCCCCCCCCCCC | 33.17 | 30377154 | |
| 6 | Phosphorylation | --MSIQTSDPNETSD --CCCCCCCCCCCCC | 34.39 | 28889911 | |
| 11 | Phosphorylation | QTSDPNETSDLKSLS CCCCCCCCCCHHHHH | 33.89 | 19823750 | |
| 12 | Phosphorylation | TSDPNETSDLKSLSL CCCCCCCCCHHHHHH | 34.46 | 19823750 | |
| 78 | Phosphorylation | VLVAGPPSTGKTALA EEEECCCCCCHHHHH | 53.58 | 22369663 | |
| 79 | Phosphorylation | LVAGPPSTGKTALAM EEECCCCCCHHHHHH | 48.77 | 22369663 | |
| 148 | Phosphorylation | VEIQIDRSITGGHKQ EEEEEECCCCCCCCC | 22.28 | 28889911 | |
| 150 | Phosphorylation | IQIDRSITGGHKQGK EEEECCCCCCCCCCE | 38.05 | 27214570 | |
| 174 | Ubiquitination | TIYELGNKMIDGLTK HHHHHCHHHCCCCCC | 35.12 | 23749301 | |
| 191 | Phosphorylation | VLAGDVISIDKASGK HHCCCEEEEECCCCC | 25.28 | 30377154 | |
| 209 | Phosphorylation | LGRSFARSRDYDAMG HCHHHHHCCCCCCCC | 26.52 | 30377154 | |
| 212 | Phosphorylation | SFARSRDYDAMGADT HHHHCCCCCCCCCCC | 12.42 | 28889911 | |
| 231 | Acetylation | CPEGELQKRKTVVHT CCCCHHHCCCEEEEE | 69.37 | 24489116 | |
| 338 | Acetylation | KTRGTNYKSPHGLPL CCCCCCCCCCCCCCH | 60.63 | 24489116 | |
| 339 | Phosphorylation | TRGTNYKSPHGLPLD CCCCCCCCCCCCCHH | 16.27 | 29734811 | |
| 358 | Phosphorylation | SIIITTKSYNEQEIK EEEEEECCCCHHHHH | 30.97 | 28889911 | |
| 395 | Phosphorylation | TKTGVETSLRYSSNL HHHCCHHHHHHHHHH | 9.42 | 27017623 | |
| 398 | Phosphorylation | GVETSLRYSSNLISV CCHHHHHHHHHHHHH | 23.03 | 27017623 | |
| 399 | Phosphorylation | VETSLRYSSNLISVA CHHHHHHHHHHHHHH | 13.30 | 27017623 | |
| 400 | Phosphorylation | ETSLRYSSNLISVAQ HHHHHHHHHHHHHHH | 27.07 | 27017623 | |
| 439 | Phosphorylation | DSARSVKYVQENESQ HCCCCCEEEECCCCC | 12.76 | 28132839 | |
| 461 | Phosphorylation | VQISIAKSADPDAMD EEEEEEECCCCCCCC | 28.96 | 28889911 | |
| 469 | Phosphorylation | ADPDAMDTTE----- CCCCCCCCCC----- | 21.53 | 25521595 | |
| 470 | Phosphorylation | DPDAMDTTE------ CCCCCCCCC------ | 35.12 | 25521595 |
| 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 RUVB2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RUVB2_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 RUVB2_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 TYR-212, AND MASSSPECTROMETRY. | |
