| UniProt ID | UFD1_YEAST | |
|---|---|---|
| UniProt AC | P53044 | |
| Protein Name | Ubiquitin fusion degradation protein 1 | |
| Gene Name | UFD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 361 | |
| Subcellular Localization | ||
| Protein Description | Functions at a post-ubiquitation step in the ubiquitin fusion degradation (UFD) pathway. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD.. | |
| Protein Sequence | MFSGFSSFGGGNGFVNMPQTFEEFFRCYPIAMMNDRIRKDDANFGGKIFLPPSALSKLSMLNIRYPMLFKLTANETGRVTHGGVLEFIAEEGRVYLPQWMMETLGIQPGSLLQISSTDVPLGQFVKLEPQSVDFLDISDPKAVLENVLRNFSTLTVDDVIEISYNGKTFKIKILEVKPESSSKSICVIETDLVTDFAPPVGYVEPDYKALKAQQDKEKKNSFGKGQVLDPSVLGQGSMSTRIDYAGIANSSRNKLSKFVGQGQNISGKAPKAEPKQDIKDMKITFDGEPAKLDLPEGQLFFGFPMVLPKEDEESAAGSKSSEQNFQGQGISLRKSNKRKTKSDHDSSKSKAPKSPEVIEID | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MFSGFSSFGG -----CCCCCCCCCC | 37.32 | 30377154 | |
| 6 | Phosphorylation | --MFSGFSSFGGGNG --CCCCCCCCCCCCC | 28.43 | 30377154 | |
| 7 | Phosphorylation | -MFSGFSSFGGGNGF -CCCCCCCCCCCCCC | 26.16 | 30377154 | |
| 28 | Phosphorylation | FEEFFRCYPIAMMND HHHHHHHHHHHHHCC | 8.07 | 30377154 | |
| 59 | Phosphorylation | PSALSKLSMLNIRYP HHHHHHHHHHCCCCC | 25.59 | 30377154 | |
| 70 | Ubiquitination | IRYPMLFKLTANETG CCCCEEEEEECCCCC | 40.75 | 23749301 | |
| 172 | Ubiquitination | NGKTFKIKILEVKPE CCEEEEEEEEEECCC | 41.66 | 22817900 | |
| 177 | Ubiquitination | KIKILEVKPESSSKS EEEEEEECCCCCCCC | 33.42 | 23749301 | |
| 219 | Ubiquitination | AQQDKEKKNSFGKGQ HHHHHHHHCCCCCCC | 59.94 | 22817900 | |
| 224 | Ubiquitination | EKKNSFGKGQVLDPS HHHCCCCCCCCCCHH | 44.13 | 23749301 | |
| 250 | Phosphorylation | DYAGIANSSRNKLSK CCCEECCCCCCHHHH | 22.96 | 22369663 | |
| 251 | Phosphorylation | YAGIANSSRNKLSKF CCEECCCCCCHHHHH | 39.41 | 22369663 | |
| 257 | Acetylation | SSRNKLSKFVGQGQN CCCCHHHHHHCCCCC | 55.28 | 24489116 | |
| 257 | Ubiquitination | SSRNKLSKFVGQGQN CCCCHHHHHHCCCCC | 55.28 | 23749301 | |
| 268 | Ubiquitination | QGQNISGKAPKAEPK CCCCCCCCCCCCCCC | 55.51 | 23749301 | |
| 318 | Phosphorylation | DEESAAGSKSSEQNF CCCCCCCCCCCCHHH | 25.33 | 28889911 | |
| 319 | Ubiquitination | EESAAGSKSSEQNFQ CCCCCCCCCCCHHHC | 58.02 | 23749301 | |
| 320 | Phosphorylation | ESAAGSKSSEQNFQG CCCCCCCCCCHHHCC | 40.58 | 28889911 | |
| 321 | Phosphorylation | SAAGSKSSEQNFQGQ CCCCCCCCCHHHCCC | 47.11 | 27214570 | |
| 342 | Phosphorylation | SNKRKTKSDHDSSKS CCCCCCCCCCCCCCC | 45.46 | 27017623 | |
| 346 | Phosphorylation | KTKSDHDSSKSKAPK CCCCCCCCCCCCCCC | 35.92 | 27017623 | |
| 349 | Phosphorylation | SDHDSSKSKAPKSPE CCCCCCCCCCCCCCC | 35.68 | 22369663 | |
| 354 | Phosphorylation | SKSKAPKSPEVIEID CCCCCCCCCCCEECC | 25.82 | 22369663 |
| 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 UFD1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UFD1_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 UFD1_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-251; SER-321 ANDSER-354, 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-354, 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 SER-354, 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-354, AND MASSSPECTROMETRY. | |
