| UniProt ID | BRE5_YEAST | |
|---|---|---|
| UniProt AC | P53741 | |
| Protein Name | UBP3-associated protein BRE5 | |
| Gene Name | BRE5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 515 | |
| Subcellular Localization | ||
| Protein Description | Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of sec23.. | |
| Protein Sequence | MGVTVQDICFAFLQNYYERMRTDPSKLAYFYASTAELTHTNYQSKSTNEKDDVLPTVKVTGRENINKFFSRNDAKVRSLKLKLDTIDFQYTGHLHKSILIMATGEMFWTGTPVYKFCQTFILLPSSNGSTFDITNDIIRFISNSFKPYVLTDASLSQSNEENSVSAVEEDKIRHESGVEKEKEKEKSPEISKPKAKKETVKDTTAPTESSTQEKPIVDHSQPRAIPVTKESKIHTETVPSSTKGNHKQDEVSTEELGNVTKLNEKSHKAEKKAAPIKTKEGSVEAINAVNNSSLPNGKEVSDEKPVPGGVKEAETEIKPIEPQVSDAKESGNNASTPSSSPEPVANPPKMTWASKLMNENSDRISKNNTTVEYIRPETLPKKPTERKFEMGNRRDNASANSKNKKKPVFSTVNKDGFYPIYIRGTNGLREEKLRSALEKEFGKVMRITAADNFAVVDFETQKSQIDALEKKKKSIDGIEVCLERKTVKKPTSNNPPGIFTNGTRSHRKQPLKRKD | |
| 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 |
|---|---|---|---|---|---|
| 31 | Phosphorylation | PSKLAYFYASTAELT HHHHHHHHHHHHCCE | 6.23 | 19779198 | |
| 34 | Phosphorylation | LAYFYASTAELTHTN HHHHHHHHHCCEECC | 18.91 | 19779198 | |
| 50 | Succinylation | QSKSTNEKDDVLPTV CCCCCCCCCCCCCEE | 62.39 | 23954790 | |
| 50 | Acetylation | QSKSTNEKDDVLPTV CCCCCCCCCCCCCEE | 62.39 | 24489116 | |
| 176 | Phosphorylation | EDKIRHESGVEKEKE HHHHHHHHCCHHHHH | 41.85 | 25521595 | |
| 187 | Phosphorylation | KEKEKEKSPEISKPK HHHHHHCCCCCCCCH | 28.93 | 19823750 | |
| 191 | Phosphorylation | KEKSPEISKPKAKKE HHCCCCCCCCHHCCC | 41.04 | 24909858 | |
| 252 | Phosphorylation | NHKQDEVSTEELGNV CCCCCCCCHHHHHCH | 28.22 | 29136822 | |
| 253 | Phosphorylation | HKQDEVSTEELGNVT CCCCCCCHHHHHCHH | 38.36 | 28889911 | |
| 261 | Acetylation | EELGNVTKLNEKSHK HHHHCHHHHCHHCHH | 45.06 | 24489116 | |
| 278 | Phosphorylation | KKAAPIKTKEGSVEA HHCCCCCCCCCCHHH | 34.74 | 22369663 | |
| 282 | Phosphorylation | PIKTKEGSVEAINAV CCCCCCCCHHHHHHH | 20.20 | 22369663 | |
| 292 | Phosphorylation | AINAVNNSSLPNGKE HHHHHCCCCCCCCCC | 28.22 | 19823750 | |
| 293 | Phosphorylation | INAVNNSSLPNGKEV HHHHCCCCCCCCCCC | 50.39 | 29136822 | |
| 318 | Acetylation | KEAETEIKPIEPQVS CCEECEEECCCCCCC | 33.44 | 24489116 | |
| 325 | Phosphorylation | KPIEPQVSDAKESGN ECCCCCCCCCCCCCC | 26.97 | 23749301 | |
| 330 | Phosphorylation | QVSDAKESGNNASTP CCCCCCCCCCCCCCC | 46.22 | 22369663 | |
| 335 | Phosphorylation | KESGNNASTPSSSPE CCCCCCCCCCCCCCC | 42.87 | 25521595 | |
| 336 | Phosphorylation | ESGNNASTPSSSPEP CCCCCCCCCCCCCCC | 25.44 | 22369663 | |
| 338 | Phosphorylation | GNNASTPSSSPEPVA CCCCCCCCCCCCCCC | 43.46 | 22369663 | |
| 339 | Phosphorylation | NNASTPSSSPEPVAN CCCCCCCCCCCCCCC | 51.63 | 22369663 | |
| 340 | Phosphorylation | NASTPSSSPEPVANP CCCCCCCCCCCCCCC | 37.31 | 22369663 | |
| 355 | Acetylation | PKMTWASKLMNENSD CCCHHHHHHHHCCCH | 43.97 | 25381059 | |
| 361 | Phosphorylation | SKLMNENSDRISKNN HHHHHCCCHHHCCCC | 23.30 | 30377154 | |
| 398 | Phosphorylation | GNRRDNASANSKNKK CCCCCCCCCCCCCCC | 33.95 | 25521595 | |
| 401 | Phosphorylation | RDNASANSKNKKKPV CCCCCCCCCCCCCCC | 37.00 | 19823750 | |
| 473 | Acetylation | DALEKKKKSIDGIEV HHHHHHHHCCCCEEH | 62.62 | 24489116 |
| 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 BRE5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRE5_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 BRE5_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 THR-278; SER-282; THR-336;SER-338; SER-339 AND SER-340, 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-187; THR-278 ANDSER-282, AND MASS SPECTROMETRY. | |
| "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-187 AND SER-398, ANDMASS 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 THR-336 AND SER-339, 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 THR-336, AND MASSSPECTROMETRY. | |
