| UniProt ID | PEX25_YEAST | |
|---|---|---|
| UniProt AC | Q02969 | |
| Protein Name | Peroxisomal membrane protein PEX25 | |
| Gene Name | PEX25 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 394 | |
| Subcellular Localization |
Peroxisome membrane Single-pass membrane protein . |
|
| Protein Description | Required for regulation of peroxisome size and maintenance. Has a role in the import of peroxisomal matrix proteins. Imports RHO1 into the peroxisome. Also promotes peroxisome division and biogenesis.. | |
| Protein Sequence | MSQFGTTDIVSGSETPPYSGASYQDAQDDNTHPHSSDAGAEKFSAGSGSESHTESSRSDDEDSQAKTKMVDNITILKYILDSLSGRDKLAKIIKYALDILKLFIEKSKRNLTVLDPSVLTYYTKILKNLTVKVALRHPITVIKVLLLSLLRNFDKKIDFISQQLSTFRYILRFGGTPFRVCSFLGKFNKTRKCNFQIDQIKKIWFNEASLREFLDLYYGIFDELDLLYKLKIWTNKSFYSFVSRQESLAWQYDILLSLKDHWLNLQSLQKRQLELEVQLKVQNNALLLSPILMHQAHKDDGSQSPIRKQLLNDLNVNNDAEVLIHKQLKAIKDEKTLVYLDIARLSFDCMANTSDILNLKTPKGTYAVLSLGSGLTGLVKLWITTKRSLCSSKD | |
| 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 | ------MSQFGTTDI ------CCCCCCCCC | 33.93 | 19823750 | |
| 6 | Phosphorylation | --MSQFGTTDIVSGS --CCCCCCCCCCCCC | 23.68 | 19823750 | |
| 7 | Phosphorylation | -MSQFGTTDIVSGSE -CCCCCCCCCCCCCC | 24.90 | 19823750 | |
| 11 | Phosphorylation | FGTTDIVSGSETPPY CCCCCCCCCCCCCCC | 36.61 | 19823750 | |
| 13 | Phosphorylation | TTDIVSGSETPPYSG CCCCCCCCCCCCCCC | 30.69 | 19823750 | |
| 15 | Phosphorylation | DIVSGSETPPYSGAS CCCCCCCCCCCCCCC | 31.12 | 19823750 | |
| 18 | Phosphorylation | SGSETPPYSGASYQD CCCCCCCCCCCCCCC | 22.42 | 19823750 | |
| 19 | Phosphorylation | GSETPPYSGASYQDA CCCCCCCCCCCCCCC | 33.39 | 19823750 | |
| 22 | Phosphorylation | TPPYSGASYQDAQDD CCCCCCCCCCCCCCC | 27.18 | 19823750 | |
| 23 | Phosphorylation | PPYSGASYQDAQDDN CCCCCCCCCCCCCCC | 15.18 | 19823750 | |
| 44 | Phosphorylation | DAGAEKFSAGSGSES HHCCCCCCCCCCCCC | 42.67 | 22890988 | |
| 47 | Phosphorylation | AEKFSAGSGSESHTE CCCCCCCCCCCCCCC | 38.57 | 22890988 | |
| 49 | Phosphorylation | KFSAGSGSESHTESS CCCCCCCCCCCCCCC | 37.31 | 22890988 | |
| 51 | Phosphorylation | SAGSGSESHTESSRS CCCCCCCCCCCCCCC | 37.09 | 22890988 | |
| 53 | Phosphorylation | GSGSESHTESSRSDD CCCCCCCCCCCCCCC | 47.01 | 22890988 | |
| 55 | Phosphorylation | GSESHTESSRSDDED CCCCCCCCCCCCCCC | 32.01 | 22890988 | |
| 56 | Phosphorylation | SESHTESSRSDDEDS CCCCCCCCCCCCCCH | 29.57 | 22890988 | |
| 58 | Phosphorylation | SHTESSRSDDEDSQA CCCCCCCCCCCCHHH | 51.89 | 19823750 | |
| 63 | Phosphorylation | SRSDDEDSQAKTKMV CCCCCCCHHHHHHHC | 29.95 | 19823750 | |
| 107 | Phosphorylation | LKLFIEKSKRNLTVL HHHHHHHHCCCCEEC | 24.86 | 29688323 | |
| 112 | Phosphorylation | EKSKRNLTVLDPSVL HHHCCCCEECCHHHH | 23.67 | 29688323 | |
| 117 | Phosphorylation | NLTVLDPSVLTYYTK CCEECCHHHHHHHHH | 29.44 | 29688323 | |
| 120 | Phosphorylation | VLDPSVLTYYTKILK ECCHHHHHHHHHHHH | 16.60 | 29688323 | |
| 122 | Phosphorylation | DPSVLTYYTKILKNL CHHHHHHHHHHHHCC | 9.05 | 29688323 | |
| 123 | Phosphorylation | PSVLTYYTKILKNLT HHHHHHHHHHHHCCC | 10.95 | 29688323 | |
| 130 | Phosphorylation | TKILKNLTVKVALRH HHHHHCCCHHHHHCC | 27.89 | 21440633 | |
| 289 | Phosphorylation | QNNALLLSPILMHQA HCCHHHHHHHHHHHH | 15.18 | 17330950 | |
| 302 | Phosphorylation | QAHKDDGSQSPIRKQ HHHCCCCCCCHHHHH | 34.18 | 21440633 | |
| 304 | Phosphorylation | HKDDGSQSPIRKQLL HCCCCCCCHHHHHHH | 24.80 | 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 PEX25_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PEX25_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 PEX25_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-289 AND SER-304, ANDMASS 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-304, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-63 AND SER-304,AND MASS SPECTROMETRY. | |