| UniProt ID | PDR1_YEAST | |
|---|---|---|
| UniProt AC | P12383 | |
| Protein Name | Transcription factor PDR1 | |
| Gene Name | PDR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1068 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Positive regulator of proteins involved in permeability. PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.. | |
| Protein Sequence | MRGLTPKNGVHIETGPDTESSADSSNFSTGFSGKIRKPRSKVSKACDNCRKRKIKCNGKFPCASCEIYSCECTFSTRQGGARIKNLHKTSLEGTTVQVKEETDSSSTSFSNPQRCTDGPCAVEQPTKFFENFKLGGRSSGDNSGSDGKNDDDVNRNGFYEDDSESQATLTSLQTTLKNLKEMAHLGTHVTSAIESIELQISDLLKRWEPKVRTKELATTKFYPNKSIETQLMKNKYCDVVHLTRYAAWSNNKKDQDTSSQPLIDEIFGLYSPFQFLSLQGIGKCFQNYRSKSKCEIFPRTAKETIYIMLRFFDVCFHHINQGCVSIANPLENYLQKMNLLPSTPSSISSAGSPNTAHTKSHVALVINHLPQPFVRNITGISNSELLSEMNNDISMFGILLKMLDMHKNSYQNFLMEITSNPSVAKNTQSIDVLQEFIHYCQAGEALIALCYSYYNSTLYNYVDFTCDITHLEQLLYFLDLLFWLSEIYGFEKVLNVAVHFVSRVGLSRWEFYVGLDENFAERRRNLWWKAFYFEKTLASKLGYPSNIDDSKINCLLPKNFRDVGFLDNRDFIENVHLVRRSEAFDNMCISDLKYYGELAVLQIVSHFSSSVLFNEKFTSIRNTSKPSVVREKLLFEVLEIFNETEMKYDAIKEQTGKLFDIAFSKDSTELKVSREDKIMASKFVLFYEHHFCRMVNESDNIVARLCVHRRPSILIENLKIYLHKIYKSWTDMNKILLDFDNDYSVYRSFAHYSISCIILVSQAFSVAEFIKVNDVVNMIRVFKRFLDIKIFSENETNEHVFNSQSFKDYTRAFSFLTIVTRIMLLAYGESSSTNLDVISKYIDENAPDLKGIIELVLDTNSCAYRFLLEPVQKSGFHLTVSQMLKNRKFQEPLMSNEDNKQMKHNSGKNLNPDLPSLKTGTSCLLNGIESPQLPFNGRSAPSPVRNNSLPEFAQLPSFRSLSVSDMINPDYAQPTNGQNNTQVQSNKPINAQQQIPTSVQVPFMNTNEINNNNNNNNNNKNNINNINNNNSNNFSATSFNLGTLDEFVNNGDLEDLYSILWSDVYPDS | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MRGLTPKNGVHI ---CCCCCCCCCCCC | 34.73 | 21440633 | |
| 20 | Phosphorylation | ETGPDTESSADSSNF CCCCCCCCCCCCCCC | 32.68 | 19779198 | |
| 21 | Phosphorylation | TGPDTESSADSSNFS CCCCCCCCCCCCCCC | 29.84 | 28889911 | |
| 34 | Acetylation | FSTGFSGKIRKPRSK CCCCCCCCCCCCHHH | 37.83 | 25381059 | |
| 89 | Phosphorylation | RIKNLHKTSLEGTTV EEEEEEECCCCCCEE | 28.00 | 21551504 | |
| 90 | Phosphorylation | IKNLHKTSLEGTTVQ EEEEEECCCCCCEEE | 29.27 | 19779198 | |
| 102 | Phosphorylation | TVQVKEETDSSSTSF EEEEEECCCCCCCCC | 42.12 | 30377154 | |
| 104 | Phosphorylation | QVKEETDSSSTSFSN EEEECCCCCCCCCCC | 33.34 | 30377154 | |
| 105 | Phosphorylation | VKEETDSSSTSFSNP EEECCCCCCCCCCCC | 40.21 | 30377154 | |
| 106 | Phosphorylation | KEETDSSSTSFSNPQ EECCCCCCCCCCCCC | 31.83 | 30377154 | |
| 108 | Phosphorylation | ETDSSSTSFSNPQRC CCCCCCCCCCCCCCC | 28.73 | 25752575 | |
| 110 | Phosphorylation | DSSSTSFSNPQRCTD CCCCCCCCCCCCCCC | 47.57 | 28889911 | |
| 138 | Phosphorylation | NFKLGGRSSGDNSGS CCCCCCCCCCCCCCC | 41.78 | 17563356 | |
| 145 | Phosphorylation | SSGDNSGSDGKNDDD CCCCCCCCCCCCCCC | 42.90 | 28889911 | |
| 342 | Phosphorylation | QKMNLLPSTPSSISS HHCCCCCCCCCCCCC | 53.58 | 22369663 | |
| 343 | Phosphorylation | KMNLLPSTPSSISSA HCCCCCCCCCCCCCC | 25.83 | 22369663 | |
| 345 | Phosphorylation | NLLPSTPSSISSAGS CCCCCCCCCCCCCCC | 40.15 | 22369663 | |
| 346 | Phosphorylation | LLPSTPSSISSAGSP CCCCCCCCCCCCCCC | 27.91 | 22369663 | |
| 348 | Phosphorylation | PSTPSSISSAGSPNT CCCCCCCCCCCCCCC | 18.98 | 22369663 | |
| 349 | Phosphorylation | STPSSISSAGSPNTA CCCCCCCCCCCCCCC | 34.67 | 22369663 | |
| 352 | Phosphorylation | SSISSAGSPNTAHTK CCCCCCCCCCCCCCC | 18.07 | 22369663 | |
| 355 | Phosphorylation | SSAGSPNTAHTKSHV CCCCCCCCCCCCHHH | 24.17 | 22369663 | |
| 358 | Phosphorylation | GSPNTAHTKSHVALV CCCCCCCCCHHHHHH | 31.60 | 22369663 | |
| 881 | Phosphorylation | SGFHLTVSQMLKNRK CCCEEEHHHHHHCCC | 12.49 | 30377154 | |
| 919 | Phosphorylation | PDLPSLKTGTSCLLN CCCCCCCCCCCHHHC | 51.49 | 30377154 | |
| 930 | Phosphorylation | CLLNGIESPQLPFNG HHHCCCCCCCCCCCC | 18.94 | 28152593 | |
| 939 | Phosphorylation | QLPFNGRSAPSPVRN CCCCCCCCCCCCCCC | 46.02 | 22369663 | |
| 942 | Phosphorylation | FNGRSAPSPVRNNSL CCCCCCCCCCCCCCC | 35.43 | 22369663 | |
| 948 | Phosphorylation | PSPVRNNSLPEFAQL CCCCCCCCCHHHHCC | 49.18 | 22369663 | |
| 957 | Phosphorylation | PEFAQLPSFRSLSVS HHHHCCCCCCCCCHH | 41.71 | 29136822 |
| 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 PDR1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDR1_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 PDR1_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-21; SER-110; SER-348;SER-948 AND SER-957, 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-138 AND SER-942, ANDMASS SPECTROMETRY. | |
| "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 SER-948, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942, AND MASSSPECTROMETRY. | |