| UniProt ID | BRO1_YEAST | |
|---|---|---|
| UniProt AC | P48582 | |
| Protein Name | Vacuolar-sorting protein BRO1 | |
| Gene Name | BRO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 844 | |
| Subcellular Localization | Cytoplasm. Endosome. | |
| Protein Description | Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. Fusion between endosomes and the vacuole will then target the cargo proteins to the vacuolar lumen. Acts as an adapter that recruits the DOA4 deubiquitinase to the endosomes, leading to deubiquitination of cargo proteins prior to the lumenal sequestration. Its association to the endosomes depends on SNF7 and its dissociation requires VPS4. Interacts functionally with the Pkc1p-mitogen-activated protein kinase pathway.. | |
| Protein Sequence | MKPYLFDLKLKDTEKLDWKKGLSSYLKKSYGSSQWRTFYDEKATSELDHLRNNANGELAPSSLSEQNLKYYSFLEHLYFRLGSKGSRLKMDFTWYDAEYSSAQKGLKYTQHTLAFEKSCTLFNIAVIFTQIARENINEDYKNSIANLTKAFSCFEYLSENFLNSPSVDLQSENTRFLANICHAEAQELFVLKLLNDQISSKQYTLISKLSRATCNLFQKCHDFMKEIDDDVAIYGEPKWKTTVTCKLHFYKSLSAYYHGLHLEEENRVGEAIAFLDFSMQQLISSLPFKTWLVEFIDFDGFKETLEKKQKELIKDNDFIYHESVPAVVQVDSIKALDAIKSPTWEKILEPYMQDVANKCDSLYRGIIPLDVYEKESIYSEEKATLLRKQVEETETANLEYSSFIEFTNLPRLLSDLEKQFSDGNIFSNTDTQGQLMRDQIQTWCKFIQTNEFRDIEEQMNKIVFKRKQILEILSALPNDQKENVTKLKSSLVAASNSDEKLFACVKPHIVEINLLNDNGKIWKKFDEFNRNTPPQPSLLDIDDTKNDKILELLKQVKGHAEDLRTLKEERSRNLSELRDEINNDDITKLLIINKGKSDVELKDLFEVELEKFEPLSTRIEATIYKQSSMIDDIKAKLDEIFHLSNFKDKSSGEEKFLEDRKNFFDKLQEAVKSFSIFASDLPKGIEFYDSLFNMSRDLAERVRVAKQTEDSTANSPAPPLPPLDSKASVVGGPPLLPQKSAAFQSLSRQGLNLGDQFQNLKISAGSDLPQGPGIPPRTYEASPYAATPTMAAPPVPPKQSQEDMYDLRRRKAVENEERELQENPTSFYNRPSVFDENMYSKYSS | |
| 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 |
|---|---|---|---|---|---|
| 23 | Phosphorylation | LDWKKGLSSYLKKSY CCHHHHHHHHHHHHH | 26.13 | 27017623 | |
| 24 | Phosphorylation | DWKKGLSSYLKKSYG CHHHHHHHHHHHHHC | 39.26 | 27017623 | |
| 28 | Ubiquitination | GLSSYLKKSYGSSQW HHHHHHHHHHCCCHH | 46.44 | 23749301 | |
| 42 | Acetylation | WRTFYDEKATSELDH HHHHCCHHHHHHHHH | 54.81 | 24489116 | |
| 70 | Phosphorylation | LSEQNLKYYSFLEHL CCHHHHHHHHHHHHH | 13.91 | 23607784 | |
| 71 | Phosphorylation | SEQNLKYYSFLEHLY CHHHHHHHHHHHHHH | 7.43 | 23607784 | |
| 72 | Phosphorylation | EQNLKYYSFLEHLYF HHHHHHHHHHHHHHH | 21.92 | 23607784 | |
| 78 | Phosphorylation | YSFLEHLYFRLGSKG HHHHHHHHHHCCCCC | 6.64 | 23607784 | |
| 83 | Phosphorylation | HLYFRLGSKGSRLKM HHHHHCCCCCCCEEE | 38.13 | 23607784 | |
| 141 | Acetylation | ENINEDYKNSIANLT HCCCHHHHHHHHHHH | 57.45 | 24489116 | |
| 208 | Acetylation | KQYTLISKLSRATCN CHHHHHHHHHHHHHH | 43.41 | 24489116 | |
| 289 | Ubiquitination | LISSLPFKTWLVEFI HHHCCCCCEEEEEEE | 36.53 | 19722269 | |
| 414 | Phosphorylation | TNLPRLLSDLEKQFS CCHHHHHHHHHHHCC | 44.75 | 30377154 | |
| 532 | Phosphorylation | FDEFNRNTPPQPSLL HHHHCCCCCCCCCCC | 32.86 | 29136822 | |
| 537 | Phosphorylation | RNTPPQPSLLDIDDT CCCCCCCCCCCCCCC | 36.00 | 28889911 | |
| 554 | Acetylation | DKILELLKQVKGHAE HHHHHHHHHHCCCHH | 66.71 | 24489116 | |
| 597 | Phosphorylation | LIINKGKSDVELKDL EEEECCCCCCCHHHH | 56.40 | 30377154 | |
| 647 | Acetylation | IFHLSNFKDKSSGEE HHHHHCCCCCCCCCH | 69.38 | 24489116 | |
| 666 | Acetylation | DRKNFFDKLQEAVKS HHHHHHHHHHHHHHH | 47.08 | 24489116 | |
| 708 | Phosphorylation | RVRVAKQTEDSTANS HHHHHHHCCCCCCCC | 40.84 | 29136822 | |
| 711 | Phosphorylation | VAKQTEDSTANSPAP HHHHCCCCCCCCCCC | 24.16 | 24961812 | |
| 712 | Phosphorylation | AKQTEDSTANSPAPP HHHCCCCCCCCCCCC | 42.03 | 24961812 | |
| 715 | Phosphorylation | TEDSTANSPAPPLPP CCCCCCCCCCCCCCC | 21.70 | 29136822 | |
| 728 | Phosphorylation | PPLDSKASVVGGPPL CCCCCCCCCCCCCCC | 22.52 | 28889911 | |
| 740 | Phosphorylation | PPLLPQKSAAFQSLS CCCCCCCHHHHHHHH | 21.41 | 25752575 | |
| 745 | Phosphorylation | QKSAAFQSLSRQGLN CCHHHHHHHHHCCCC | 23.12 | 21440633 | |
| 747 | Phosphorylation | SAAFQSLSRQGLNLG HHHHHHHHHCCCCHH | 28.01 | 21440633 | |
| 787 | Phosphorylation | EASPYAATPTMAAPP CCCCCCCCCCCCCCC | 15.89 | 27017623 | |
| 800 | Phosphorylation | PPVPPKQSQEDMYDL CCCCCCCCHHHHHHH | 41.48 | 27017623 | |
| 805 | Phosphorylation | KQSQEDMYDLRRRKA CCCHHHHHHHHHHHH | 24.93 | 27017623 | |
| 843 | Phosphorylation | ENMYSKYSS------ CCHHHHCCC------ | 33.05 | 27017623 |
| 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 BRO1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BRO1_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 BRO1_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-728 AND SER-740, ANDMASS SPECTROMETRY. | |
