| UniProt ID | YRA1_YEAST | |
|---|---|---|
| UniProt AC | Q12159 | |
| Protein Name | RNA annealing protein YRA1 | |
| Gene Name | YRA1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 226 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | RNA-binding RNA annealing protein. May have a role in pre-mRNA metabolism. Component the TREX complex, which operates in coupling transcription elongation to mRNA export.. | |
| Protein Sequence | MSANLDKSLDEIIGSNKAGSNRARVGGTRGNGPRRVGKQVGSQRRSLPNRRGPIRKNTRAPPNAVARVAKLLDTTREVKVNVEGLPRDIKQDAVREFFASQVGGVQRVLLSYNERGQSTGMANITFKNGELARRAVERFNGSPIDGGRSRLRLNLIVDPNQRPVKSLADRIKAMPQKGGNAPRPVKRGPNRKAAMAKSQNKPKREKPAKKSLEDLDKEMADYFEKK | |
| 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 | Acetylation | ------MSANLDKSL ------CCCCCCHHH | 26.34 | 22814378 | |
| 2 | Phosphorylation | ------MSANLDKSL ------CCCCCCHHH | 26.34 | 29136822 | |
| 7 | Ubiquitination | -MSANLDKSLDEIIG -CCCCCCHHHHHHHC | 56.96 | 24961812 | |
| 8 | Phosphorylation | MSANLDKSLDEIIGS CCCCCCHHHHHHHCC | 40.49 | 22369663 | |
| 15 | Phosphorylation | SLDEIIGSNKAGSNR HHHHHHCCCCCCCCC | 25.42 | 22890988 | |
| 17 | Ubiquitination | DEIIGSNKAGSNRAR HHHHCCCCCCCCCCC | 56.68 | 24961812 | |
| 17 | Acetylation | DEIIGSNKAGSNRAR HHHHCCCCCCCCCCC | 56.68 | 22865919 | |
| 20 | Phosphorylation | IGSNKAGSNRARVGG HCCCCCCCCCCCCCC | 28.18 | 23749301 | |
| 38 | Acetylation | NGPRRVGKQVGSQRR CCCCCCHHHHCCCCC | 38.66 | 25381059 | |
| 58 | Phosphorylation | RGPIRKNTRAPPNAV CCCCCCCCCCCCCHH | 31.10 | 28889911 | |
| 70 | Acetylation | NAVARVAKLLDTTRE CHHHHHHHHHHCCCE | 46.88 | 24489116 | |
| 70 | Ubiquitination | NAVARVAKLLDTTRE CHHHHHHHHHHCCCE | 46.88 | 23749301 | |
| 74 | Phosphorylation | RVAKLLDTTREVKVN HHHHHHHCCCEEEEC | 27.93 | 21126336 | |
| 79 | Acetylation | LDTTREVKVNVEGLP HHCCCEEEECCCCCC | 24.28 | 24489116 | |
| 79 | 2-Hydroxyisobutyrylation | LDTTREVKVNVEGLP HHCCCEEEECCCCCC | 24.28 | - | |
| 90 | 2-Hydroxyisobutyrylation | EGLPRDIKQDAVREF CCCCCCHHHHHHHHH | 46.55 | - | |
| 100 | Phosphorylation | AVREFFASQVGGVQR HHHHHHHHHHCCHHE | 21.90 | 25752575 | |
| 111 | Phosphorylation | GVQRVLLSYNERGQS CHHEEEEEECCCCCC | 23.04 | 30377154 | |
| 118 | Phosphorylation | SYNERGQSTGMANIT EECCCCCCCCCEEEE | 29.74 | 27017623 | |
| 127 | Ubiquitination | GMANITFKNGELARR CCEEEEEECCHHHHH | 56.23 | 24961812 | |
| 127 | Acetylation | GMANITFKNGELARR CCEEEEEECCHHHHH | 56.23 | 24489116 | |
| 142 | Phosphorylation | AVERFNGSPIDGGRS HHHHHCCCCCCCCCC | 21.56 | 22369663 | |
| 149 | Phosphorylation | SPIDGGRSRLRLNLI CCCCCCCCCEEEEEE | 38.65 | 22369663 | |
| 165 | Acetylation | DPNQRPVKSLADRIK CCCCCCHHHHHHHHH | 42.29 | 24489116 | |
| 165 | Ubiquitination | DPNQRPVKSLADRIK CCCCCCHHHHHHHHH | 42.29 | 24961812 | |
| 166 | Phosphorylation | PNQRPVKSLADRIKA CCCCCHHHHHHHHHH | 29.08 | 19795423 | |
| 172 | Ubiquitination | KSLADRIKAMPQKGG HHHHHHHHHCCCCCC | 39.25 | 22817900 | |
| 177 | Ubiquitination | RIKAMPQKGGNAPRP HHHHCCCCCCCCCCC | 64.02 | 22817900 | |
| 210 | Acetylation | KREKPAKKSLEDLDK CCCCCCCHHHHHHHH | 63.48 | 22865919 | |
| 211 | Phosphorylation | REKPAKKSLEDLDKE CCCCCCHHHHHHHHH | 35.96 | 25521595 | |
| 217 | Acetylation | KSLEDLDKEMADYFE HHHHHHHHHHHHHHH | 57.60 | 24489116 | |
| 225 | Acetylation | EMADYFEKK------ HHHHHHHCC------ | 54.61 | 24489116 | |
| 225 | Succinylation | EMADYFEKK------ HHHHHHHCC------ | 54.61 | 23954790 |
| 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 YRA1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YRA1_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 YRA1_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-100, AND MASSSPECTROMETRY. | |
