| UniProt ID | BZZ1_YEAST | |
|---|---|---|
| UniProt AC | P38822 | |
| Protein Name | Protein BZZ1 | |
| Gene Name | BZZ1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 633 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, actin patch . localizes in cortical actin patches in a LAS17-dependent manner. | |
| Protein Description | Plays a role in endocytosis and trafficking to the vacuole. Functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress.. | |
| Protein Sequence | MSADLSIGNEIKDSFKETHKWVQNNLKWLKDIEQFYRERAKLEKDYSERLSRLSAEYFNKKSSTSVPISVGDTPTTTPGSIEAAGVVAWNEILSQTDMISKDHDQLSTDFENHVANQLSGLFTKLDMTLSKINGFNNDMVNKKDNIYHELEKAKKDYDEACSTMEMARNRYTKASNDRNKKKLDEKEMEMNKCKNEYLIKINQANRTKDKYYFQDVPEVLDLLQDVNEAKTLFLNDLWLKAASVENDLGANVSKRLQAANSVVKQNKPSLNTAIFIKHNLKNWKEPQDFVYKPSPVWHDDEKFAVPSSLEVEDLRIKLAKAENDYNSLQDKTQNELSKLSTLNKIKHEMKTNEDNINATKFYDTLKEYLNVVSPFTSHETLKLQAEVQIESIQNNVPEEYDLSTDNIDLSKTKKKSGIFSKFKHNILNVDSKPSSGGSTGNGNGGPLHITSLFNTSRRTRLGSAPNNAGEDSDNNSIRTTSTNNTKKTTQNSSDDGKNKVLYAYVQKDDDEITITPGDKISLVARDTGSGWTKINNDTTGETGLVPTTYIRISSAATVKANDRGPAPEVPPPRRSTLPVRTMEAIYAYEAQGDDEISIDPGDIITVIRGDDGSGWTYGECDGLKGLFPTSYCK | |
| 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 |
|---|---|---|---|---|---|
| 30 | Acetylation | QNNLKWLKDIEQFYR HHHHHHHHHHHHHHH | 56.39 | 24489116 | |
| 152 | Acetylation | NIYHELEKAKKDYDE HHHHHHHHHHCCHHH | 77.47 | 24489116 | |
| 277 | Ubiquitination | LNTAIFIKHNLKNWK CCHHHHHHCCCCCCC | 18.72 | 22817900 | |
| 281 | Ubiquitination | IFIKHNLKNWKEPQD HHHHCCCCCCCCCCC | 67.11 | 22817900 | |
| 284 | Ubiquitination | KHNLKNWKEPQDFVY HCCCCCCCCCCCCCC | 69.75 | 22817900 | |
| 307 | Phosphorylation | DEKFAVPSSLEVEDL CCCCCCCCCCCHHHH | 40.74 | 24961812 | |
| 308 | Phosphorylation | EKFAVPSSLEVEDLR CCCCCCCCCCHHHHH | 23.60 | 24961812 | |
| 325 | Phosphorylation | LAKAENDYNSLQDKT HHHHHCCHHHHCHHH | 20.45 | 22369663 | |
| 327 | Phosphorylation | KAENDYNSLQDKTQN HHHCCHHHHCHHHHH | 22.60 | 22369663 | |
| 331 | Acetylation | DYNSLQDKTQNELSK CHHHHCHHHHHHHHH | 38.76 | 24489116 | |
| 331 | Ubiquitination | DYNSLQDKTQNELSK CHHHHCHHHHHHHHH | 38.76 | 23749301 | |
| 338 | Acetylation | KTQNELSKLSTLNKI HHHHHHHHHHHHHHH | 60.11 | 24489116 | |
| 400 | Phosphorylation | QNNVPEEYDLSTDNI HHCCCCCCCCCCCCC | 22.11 | 27017623 | |
| 416 | Phosphorylation | LSKTKKKSGIFSKFK CCCCCHHCCCCHHHC | 46.10 | 24909858 | |
| 420 | Phosphorylation | KKKSGIFSKFKHNIL CHHCCCCHHHCCCEE | 34.95 | 19823750 | |
| 421 | Acetylation | KKSGIFSKFKHNILN HHCCCCHHHCCCEEC | 47.91 | 24489116 | |
| 463 | Phosphorylation | SRRTRLGSAPNNAGE CCCCCCCCCCCCCCC | 45.18 | 22369663 | |
| 472 | Phosphorylation | PNNAGEDSDNNSIRT CCCCCCCCCCCCCEE | 37.63 | 22369663 | |
| 476 | Phosphorylation | GEDSDNNSIRTTSTN CCCCCCCCCEECCCC | 21.50 | 22369663 | |
| 479 | Phosphorylation | SDNNSIRTTSTNNTK CCCCCCEECCCCCCE | 24.35 | 22369663 | |
| 480 | Phosphorylation | DNNSIRTTSTNNTKK CCCCCEECCCCCCEE | 24.57 | 22369663 | |
| 481 | Phosphorylation | NNSIRTTSTNNTKKT CCCCEECCCCCCEEC | 28.64 | 22369663 | |
| 482 | Phosphorylation | NSIRTTSTNNTKKTT CCCEECCCCCCEECC | 30.32 | 22369663 | |
| 485 | Phosphorylation | RTTSTNNTKKTTQNS EECCCCCCEECCCCC | 35.67 | 21440633 | |
| 493 | Phosphorylation | KKTTQNSSDDGKNKV EECCCCCCCCCCCEE | 47.47 | 21440633 | |
| 521 | Phosphorylation | ITPGDKISLVARDTG ECCCCEEEEEEEECC | 23.64 | 22369663 | |
| 538 | Phosphorylation | WTKINNDTTGETGLV CEEECCCCCCCCCEE | 38.53 | 27017623 | |
| 539 | Phosphorylation | TKINNDTTGETGLVP EEECCCCCCCCCEEE | 35.56 | 27017623 | |
| 553 | Phosphorylation | PTTYIRISSAATVKA ECEEEEECCCEEECC | 12.22 | 21440633 | |
| 554 | Phosphorylation | TTYIRISSAATVKAN CEEEEECCCEEECCC | 21.39 | 20377248 | |
| 575 | Phosphorylation | EVPPPRRSTLPVRTM CCCCCCCCCCCCEEH | 35.26 | 28889911 | |
| 576 | Phosphorylation | VPPPRRSTLPVRTME CCCCCCCCCCCEEHH | 33.02 | 17563356 |
| 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 BZZ1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BZZ1_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 BZZ1_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-327; SER-463; SER-472AND SER-476, 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 THR-576, AND MASSSPECTROMETRY. | |
