| UniProt ID | PTR2_YEAST | |
|---|---|---|
| UniProt AC | P32901 | |
| Protein Name | Peptide transporter PTR2 | |
| Gene Name | PTR2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 601 | |
| Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
| Protein Description | Uptake of small peptides.. | |
| Protein Sequence | MLNHPSQGSDDAQDEKQGDFPVIEEEKTQAVTLKDSYVSDDVANSTERYNLSPSPEDEDFEGPTEEEMQTLRHVGGKIPMRCWLIAIVELSERFSYYGLSAPFQNYMEYGPNDSPKGVLSLNSQGATGLSYFFQFWCYVTPVFGGYVADTFWGKYNTICCGTAIYIAGIFILFITSIPSVGNRDSAIGGFIAAIILIGIATGMIKANLSVLIADQLPKRKPSIKVLKSGERVIVDSNITLQNVFMFFYFMINVGSLSLMATTELEYHKGFWAAYLLPFCFFWIAVVTLIFGKKQYIQRPIGDKVIAKSFKVCWILTKNKFDFNAAKPSVHPEKNYPWNDKFVDEIKRALAACKVFIFYPIYWTQYGTMISSFITQASMMELHGIPNDFLQAFDSIALIIFIPIFEKFVYPFIRRYTPLKPITKIFFGFMFGSFAMTWAAVLQSFVYKAGPWYNEPLGHNTPNHVHVCWQIPAYVLISFSEIFASITGLEYAYSKAPASMKSFIMSIFLLTNAFGSAIGCALSPVTVDPKFTWLFTGLAVACFISGCLFWLCFRKYNDTEEEMNAMDYEEEDEFDLNPISAPKANDIEILEPMESLRSTTKY | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MLNHPSQGSDDAQ --CCCCCCCCCCCCC | 39.35 | 24909858 | |
| 9 | Phosphorylation | LNHPSQGSDDAQDEK CCCCCCCCCCCCCHH | 25.36 | 22369663 | |
| 16 | Ubiquitination | SDDAQDEKQGDFPVI CCCCCCHHCCCCCEE | 68.80 | 23793018 | |
| 27 | Ubiquitination | FPVIEEEKTQAVTLK CCEECCCCCCCEEEC | 49.57 | 23749301 | |
| 32 | Phosphorylation | EEKTQAVTLKDSYVS CCCCCCEEECCCCCC | 30.98 | 19779198 | |
| 34 | Ubiquitination | KTQAVTLKDSYVSDD CCCCEEECCCCCCHH | 34.95 | 23749301 | |
| 36 | Phosphorylation | QAVTLKDSYVSDDVA CCEEECCCCCCHHCC | 26.33 | 22890988 | |
| 37 | Phosphorylation | AVTLKDSYVSDDVAN CEEECCCCCCHHCCC | 17.69 | 22369663 | |
| 39 | Phosphorylation | TLKDSYVSDDVANST EECCCCCCHHCCCCC | 21.62 | 22369663 | |
| 45 | Phosphorylation | VSDDVANSTERYNLS CCHHCCCCCCCCCCC | 23.16 | 22369663 | |
| 46 | Phosphorylation | SDDVANSTERYNLSP CHHCCCCCCCCCCCC | 25.04 | 22369663 | |
| 49 | Phosphorylation | VANSTERYNLSPSPE CCCCCCCCCCCCCCC | 17.77 | 22890988 | |
| 52 | Phosphorylation | STERYNLSPSPEDED CCCCCCCCCCCCCCC | 21.50 | 19823750 | |
| 54 | Phosphorylation | ERYNLSPSPEDEDFE CCCCCCCCCCCCCCC | 37.23 | 22890988 | |
| 64 | Phosphorylation | DEDFEGPTEEEMQTL CCCCCCCCHHHHHHH | 67.87 | 19823750 | |
| 70 | Phosphorylation | PTEEEMQTLRHVGGK CCHHHHHHHHHCCCC | 25.17 | 19823750 | |
| 319 | Acetylation | CWILTKNKFDFNAAK EEEEECCCCCCCCCC | 48.11 | 24489116 | |
| 594 | Phosphorylation | EILEPMESLRSTTKY HHCCCHHHHHCCCCC | 23.88 | 22369663 | |
| 597 | Phosphorylation | EPMESLRSTTKY--- CCHHHHHCCCCC--- | 45.80 | 25521595 | |
| 598 | Phosphorylation | PMESLRSTTKY---- CHHHHHCCCCC---- | 22.37 | 22369663 | |
| 599 | Phosphorylation | MESLRSTTKY----- HHHHHCCCCC----- | 29.59 | 22369663 | |
| 600 | Ubiquitination | ESLRSTTKY------ HHHHCCCCC------ | 49.39 | 23749301 | |
| 601 | Phosphorylation | SLRSTTKY------- HHHCCCCC------- | 22.99 | 22890988 |
| 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 PTR2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTR2_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 PTR2_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-45, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-37; SER-39; SER-45 ANDSER-594, AND MASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-45; SER-594 ANDSER-597, AND MASS SPECTROMETRY. | |