| UniProt ID | YRB2_YEAST | |
|---|---|---|
| UniProt AC | P40517 | |
| Protein Name | Ran-specific GTPase-activating protein 2 | |
| Gene Name | YRB2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 327 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1.. | |
| Protein Sequence | MSETNGGNAARENSEVKQTAVENPIDKLDGTPKRPREKDQDEQAEETSDKSEAPNKNDEEKKEEGKKDQEPSHKKIKVDDGKTVESGIVEDDKKEDKFVFGAASKFGTGFGVAKKDTKDGDATTSTESLPASDSKTKKPFAFGSGLSFGSGFNILKNKTENNSESEKKATDVDKDKVHSGSEQLANASEDTKDKPKPLKLQKQEVKSGEESEECIYQVNAKLYQLSNIKEGWKERGVGIIKINKSKDDVEKTRIVMRSRGILKVILNIQLVKGFTVQKGFTGSLQSEKFIRLLAVDDNGDPAQYAIKTGKKETTDELYNIIVKSVPK | |
| 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 | ------MSETNGGNA ------CCCCCCCCH | 53.80 | 22369663 | |
| 4 | Phosphorylation | ----MSETNGGNAAR ----CCCCCCCCHHH | 31.68 | 22369663 | |
| 14 | Phosphorylation | GNAARENSEVKQTAV CCHHHCCCHHHHHHH | 38.73 | 22369663 | |
| 17 | Acetylation | ARENSEVKQTAVENP HHCCCHHHHHHHHCC | 37.57 | 24489116 | |
| 19 | Phosphorylation | ENSEVKQTAVENPID CCCHHHHHHHHCCHH | 27.27 | 19795423 | |
| 27 | Acetylation | AVENPIDKLDGTPKR HHHCCHHHCCCCCCC | 49.55 | 24489116 | |
| 31 | Phosphorylation | PIDKLDGTPKRPREK CHHHCCCCCCCCCCC | 25.88 | 22369663 | |
| 47 | Phosphorylation | QDEQAEETSDKSEAP HHHHHHHHCCCCCCC | 33.46 | 19795423 | |
| 48 | Phosphorylation | DEQAEETSDKSEAPN HHHHHHHCCCCCCCC | 46.45 | 29136822 | |
| 51 | Phosphorylation | AEETSDKSEAPNKND HHHHCCCCCCCCCCH | 43.94 | 21551504 | |
| 74 | Acetylation | KDQEPSHKKIKVDDG CCCCCCCCCEECCCC | 61.61 | 25381059 | |
| 105 | Acetylation | FVFGAASKFGTGFGV EEEEHHHHCCCCEEE | 42.98 | 25381059 | |
| 117 | Phosphorylation | FGVAKKDTKDGDATT EEEEECCCCCCCCCC | 39.66 | 19779198 | |
| 123 | Phosphorylation | DTKDGDATTSTESLP CCCCCCCCCCCCCCC | 26.48 | 22369663 | |
| 124 | Phosphorylation | TKDGDATTSTESLPA CCCCCCCCCCCCCCC | 35.06 | 22369663 | |
| 125 | Phosphorylation | KDGDATTSTESLPAS CCCCCCCCCCCCCCC | 26.31 | 22369663 | |
| 126 | Phosphorylation | DGDATTSTESLPASD CCCCCCCCCCCCCCC | 27.74 | 22369663 | |
| 128 | Phosphorylation | DATTSTESLPASDSK CCCCCCCCCCCCCCC | 39.48 | 22369663 | |
| 132 | Phosphorylation | STESLPASDSKTKKP CCCCCCCCCCCCCCC | 40.24 | 29136822 | |
| 144 | Phosphorylation | KKPFAFGSGLSFGSG CCCCCCCCCCCCCCC | 30.06 | 24961812 | |
| 147 | Phosphorylation | FAFGSGLSFGSGFNI CCCCCCCCCCCCCHH | 30.96 | 24961812 | |
| 150 | Phosphorylation | GSGLSFGSGFNILKN CCCCCCCCCCHHHCC | 37.90 | 21440633 | |
| 170 | Phosphorylation | SESEKKATDVDKDKV CHHHHHCCCCCHHHC | 45.49 | 28889911 | |
| 179 | Phosphorylation | VDKDKVHSGSEQLAN CCHHHCCCCHHHHHC | 47.18 | 22369663 | |
| 181 | Phosphorylation | KDKVHSGSEQLANAS HHHCCCCHHHHHCCC | 25.78 | 22369663 | |
| 188 | Phosphorylation | SEQLANASEDTKDKP HHHHHCCCCCCCCCC | 35.49 | 22890988 | |
| 191 | Phosphorylation | LANASEDTKDKPKPL HHCCCCCCCCCCCCC | 36.77 | 22890988 | |
| 207 | Phosphorylation | LQKQEVKSGEESEEC HHHEEHHCCCCCHHH | 57.52 | 23749301 | |
| 216 | Phosphorylation | EESEECIYQVNAKLY CCCHHHHHHHHHHHH | 20.33 | 27017623 | |
| 221 | Acetylation | CIYQVNAKLYQLSNI HHHHHHHHHHHHHCC | 42.39 | 24489116 | |
| 229 | Acetylation | LYQLSNIKEGWKERG HHHHHCCCHHHHHCC | 55.19 | 24489116 | |
| 288 | Acetylation | TGSLQSEKFIRLLAV CCCCCCHHEEEEEEE | 51.87 | 24489116 | |
| 307 | Acetylation | DPAQYAIKTGKKETT CHHHHHHHCCCCCCH | 42.95 | 24489116 | |
| 323 | Acetylation | ELYNIIVKSVPK--- HHHHHHHHCCCC--- | 35.01 | 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 YRB2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YRB2_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 YRB2_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-14; THR-31; SER-125;SER-179 AND SER-181, 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-14; THR-31; SER-179 ANDSER-181, AND MASS SPECTROMETRY. | |