| UniProt ID | RTG2_YEAST | |
|---|---|---|
| UniProt AC | P32608 | |
| Protein Name | Retrograde regulation protein 2 | |
| Gene Name | RTG2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 588 | |
| Subcellular Localization | ||
| Protein Description | Required for a novel path of interorganelle communication between mitochondria, peroxisomes and the nucleus, thereby maintaining a functional metabolic interaction between the tricarboxylic acid and glyoxylate cycles. In particular, required for the retrograde expression of the peroxisomal isoform of citrate synthase, CIT2.. | |
| Protein Sequence | MSTLSDSDTETEVVSRNLCGIVDIGSNGIRFSISSKAAHHARIMPCVFKDRVGLSLYEVQYNTHTNAKCPIPRDIIKEVCSAMKRFKLICDDFGVPETSVRVIATEATRDAINADEFVNAVYGSTGWKVEILGQEDETRVGIYGVVSSFNTVRGLYLDVAGGSTQLSWVISSHGEVKQSSKPVSLPYGAGTLLRRMRTDDNRALFYEIKEAYKDAIEKIGIPQEMIDDAKKEGGFDLWTRGGGLRGMGHLLLYQSEGYPIQTIINGYACTYEEFSSMSDYLFLKQKIPGSSKEHKIFKVSDRRALQLPAVGLFMSAVFEAIPQIKAVHFSEGGVREGSLYSLLPKEIRAQDPLLIASRPYAPLLTEKYLYLLRTSIPQEDIPEIVNERIAPALCNLAFVHASYPKELQPTAALHVATRGIIAGCHGLSHRARALIGIALCSRWGGNIPESEEKYSQELEQVVLREGDKAEALRIVWWTKYIGTIMYVICGVHPGGNIRDNVFDFHVSKRSEVETSLKELIIDDANTTKVKEESTRKNRGYEVVVRISKDDLKTSASVRSRIITLQKKVRKLSRGSVERVKIGVQFYEE | |
| 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 | ------MSTLSDSDT ------CCCCCCCCC | 37.75 | 22369663 | |
| 3 | Phosphorylation | -----MSTLSDSDTE -----CCCCCCCCCC | 29.05 | 22369663 | |
| 5 | Phosphorylation | ---MSTLSDSDTETE ---CCCCCCCCCCHH | 34.85 | 22369663 | |
| 7 | Phosphorylation | -MSTLSDSDTETEVV -CCCCCCCCCCHHHC | 42.95 | 22369663 | |
| 9 | Phosphorylation | STLSDSDTETEVVSR CCCCCCCCCHHHCCC | 49.08 | 22369663 | |
| 11 | Phosphorylation | LSDSDTETEVVSRNL CCCCCCCHHHCCCCC | 35.85 | 22369663 | |
| 49 | Ubiquitination | RIMPCVFKDRVGLSL CEECEEECCCCCEEE | 24.99 | 23749301 | |
| 179 | Phosphorylation | SHGEVKQSSKPVSLP CCCCEEECCCCEECC | 34.31 | 22369663 | |
| 180 | Phosphorylation | HGEVKQSSKPVSLPY CCCEEECCCCEECCC | 38.19 | 22369663 | |
| 184 | Phosphorylation | KQSSKPVSLPYGAGT EECCCCEECCCCHHH | 31.96 | 22369663 | |
| 187 | Phosphorylation | SKPVSLPYGAGTLLR CCCEECCCCHHHHHH | 25.54 | 22369663 | |
| 191 | Phosphorylation | SLPYGAGTLLRRMRT ECCCCHHHHHHHHCC | 23.29 | 22369663 | |
| 345 | Acetylation | SLYSLLPKEIRAQDP CHHHHCCHHHHCCCC | 66.79 | 24489116 | |
| 405 | Acetylation | FVHASYPKELQPTAA EECCCCCCHHCCCHH | 63.92 | 24489116 | |
| 575 | Phosphorylation | VRKLSRGSVERVKIG HHHHHCCCCEEEEEE | 21.50 | 27017623 |
| 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 RTG2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RTG2_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 RTG2_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-5 AND SER-7, AND MASSSPECTROMETRY. | |
