UniProt ID | BAS1_YEAST | |
---|---|---|
UniProt AC | P22035 | |
Protein Name | Myb-like DNA-binding protein BAS1 | |
Gene Name | BAS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 811 | |
Subcellular Localization | Nucleus. | |
Protein Description | Activates HIS4 transcription only in combination with PHO2/BAS2. BAS1 is also involved in the regulation of the purine biosynthesis pathway.. | |
Protein Sequence | MSNISTKDIRKSKPKRGSGFDLLEVTESLGYQTHRKNGRNSWSKDDDNMLRSLVNESAKELGYENGLEDVKTIQQSNHLSKCIAWDVLATRFKHTVRTSKDVRKRWTGSLDPNLKKGKWTQEEDEQLLKAYEEHGPHWLSISMDIPGRTEDQCAKRYIEVLGPGSKGRLREWTLEEDLNLISKVKAYGTKWRKISSEMEFRPSLTCRNRWRKIITMVVRGQASEVITKAIKENKNIDMTDGKLRQHPIADSDIRSDSTPNKEEQLQLSQQNNPSLIKQDILNVKENESSKLPRLKDNDGPILNDSKPQALPPLKEISAPPPIRMTQVGQTHTSGSIRSKVSLPIEGLSQMNKQSPGGISDSPQTSLPPAFNPASLDEHMMNSNSISDSPKHAYSTVKTREPNSSSTQWKFTLKDGQGLSISNGTIDSTKLVKELVDQAKKYSLKISIHQHIHNHYVTSTDHPVSSNTGLSNIGNINGNPLLMDSFPHMGRQLGNGLPGLNSNSDTFNPEYRTSLDNMDSDFLSRTPNYNAFSLEATSHNPADNANELGSQSNRETNSPSVFYPQANTLIPTNSTATNNEIIQGNVSANSMSPNFNGTNGKAPSSTASYTTSGSEMPPDVGPNRIAHFNYLPPTIRPHLGSSDATRGADLNKLLNPSPNSVRSNGSKTKKKEKRKSESSQHHSSSSVTTNKFNHIDQSEISRTTSRSDTPLRDEDGLDFWETLRSLATTNPNPPVEKSAENDGAKPQVVHQGIGSHTEDSSLGSHSGGYDFFNELLDKKADTLHNEAKKTSEHDMTSGGSTDNGSVLPLNPS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
7 | Acetylation | -MSNISTKDIRKSKP -CCCCCHHHHHHCCC | 44.35 | 25381059 | |
18 | Phosphorylation | KSKPKRGSGFDLLEV HCCCCCCCCCCHHHH | 40.08 | 24961812 | |
57 | Phosphorylation | LRSLVNESAKELGYE HHHHHHHHHHHHCCC | 39.16 | 30377154 | |
166 | Acetylation | EVLGPGSKGRLREWT HHHCCCCCCCCCEEE | 54.70 | 25381059 | |
251 | Phosphorylation | RQHPIADSDIRSDST CCCCCCCCCCCCCCC | 26.39 | 24961812 | |
255 | Phosphorylation | IADSDIRSDSTPNKE CCCCCCCCCCCCCHH | 35.93 | 21440633 | |
257 | Phosphorylation | DSDIRSDSTPNKEEQ CCCCCCCCCCCHHHH | 47.19 | 24961812 | |
258 | Phosphorylation | SDIRSDSTPNKEEQL CCCCCCCCCCHHHHH | 35.55 | 21440633 | |
268 | Phosphorylation | KEEQLQLSQQNNPSL HHHHHHHHHHCCHHH | 19.43 | 23749301 | |
290 | Acetylation | VKENESSKLPRLKDN CCCCCCCCCCCCCCC | 72.32 | 25381059 | |
317 | Phosphorylation | LPPLKEISAPPPIRM CCCHHHCCCCCCEEE | 35.50 | 25752575 | |
354 | Phosphorylation | LSQMNKQSPGGISDS HHHHCCCCCCCCCCC | 27.41 | 21551504 | |
374 | Phosphorylation | PPAFNPASLDEHMMN CCCCCHHHHCHHHHC | 37.30 | 21551504 | |
388 | Phosphorylation | NSNSISDSPKHAYST CCCCCCCCCCHHCCC | 29.11 | 21440633 | |
419 | Phosphorylation | LKDGQGLSISNGTID EECCCCCEEECCEEC | 30.69 | 30377154 | |
421 | Phosphorylation | DGQGLSISNGTIDST CCCCCEEECCEECHH | 26.32 | 27017623 | |
424 | Phosphorylation | GLSISNGTIDSTKLV CCEEECCEECHHHHH | 26.34 | 27017623 | |
428 | Phosphorylation | SNGTIDSTKLVKELV ECCEECHHHHHHHHH | 25.34 | 27017623 | |
439 | Acetylation | KELVDQAKKYSLKIS HHHHHHHHHHCCEEE | 46.76 | 25381059 | |
503 | Phosphorylation | LPGLNSNSDTFNPEY CCCCCCCCCCCCHHH | 37.54 | 28152593 | |
512 | Phosphorylation | TFNPEYRTSLDNMDS CCCHHHHHCHHCCCH | 32.51 | 28889911 | |
525 | Phosphorylation | DSDFLSRTPNYNAFS CHHHHHCCCCCCEEC | 16.71 | 28889911 | |
537 | Phosphorylation | AFSLEATSHNPADNA EECCEECCCCCCCCH | 28.45 | 19779198 | |
549 | Phosphorylation | DNANELGSQSNRETN CCHHHHCCCCCCCCC | 42.96 | 25752575 | |
551 | Phosphorylation | ANELGSQSNRETNSP HHHHCCCCCCCCCCC | 39.28 | 27017623 | |
557 | Phosphorylation | QSNRETNSPSVFYPQ CCCCCCCCCCCCCCC | 26.44 | 28889911 | |
656 | Phosphorylation | LNKLLNPSPNSVRSN HHHHHCCCCCCCCCC | 35.32 | 22369663 | |
659 | Phosphorylation | LLNPSPNSVRSNGSK HHCCCCCCCCCCCCC | 23.45 | 22369663 | |
662 | Phosphorylation | PSPNSVRSNGSKTKK CCCCCCCCCCCCCCC | 43.30 | 22369663 | |
665 | Phosphorylation | NSVRSNGSKTKKKEK CCCCCCCCCCCCCHH | 41.21 | 22369663 | |
675 | Phosphorylation | KKKEKRKSESSQHHS CCCHHHHCCCCCCCC | 46.90 | 30377154 | |
677 | Phosphorylation | KEKRKSESSQHHSSS CHHHHCCCCCCCCCC | 42.25 | 30377154 | |
685 | Phosphorylation | SQHHSSSSVTTNKFN CCCCCCCCCCCCCCC | 25.98 | 30377154 | |
690 | Acetylation | SSSVTTNKFNHIDQS CCCCCCCCCCCCCHH | 45.51 | 22865919 | |
697 | Phosphorylation | KFNHIDQSEISRTTS CCCCCCHHHHCCCCC | 32.90 | 19795423 | |
700 | Phosphorylation | HIDQSEISRTTSRSD CCCHHHHCCCCCCCC | 21.37 | 25704821 | |
702 | Phosphorylation | DQSEISRTTSRSDTP CHHHHCCCCCCCCCC | 23.49 | 19779198 | |
703 | Phosphorylation | QSEISRTTSRSDTPL HHHHCCCCCCCCCCC | 22.49 | 19795423 | |
704 | Phosphorylation | SEISRTTSRSDTPLR HHHCCCCCCCCCCCC | 29.22 | 19795423 | |
706 | Phosphorylation | ISRTTSRSDTPLRDE HCCCCCCCCCCCCCC | 45.67 | 19795423 | |
708 | Phosphorylation | RTTSRSDTPLRDEDG CCCCCCCCCCCCCCC | 26.01 | 19795423 | |
759 | Phosphorylation | IGSHTEDSSLGSHSG CCCCCCCCCCCCCCC | 22.64 | 21551504 | |
760 | Phosphorylation | GSHTEDSSLGSHSGG CCCCCCCCCCCCCCC | 49.42 | 21440633 | |
765 | Phosphorylation | DSSLGSHSGGYDFFN CCCCCCCCCCHHHHH | 35.29 | 21440633 | |
789 | Phosphorylation | LHNEAKKTSEHDMTS HCHHHHHCCCCCCCC | 38.34 | 19779198 | |
795 | Phosphorylation | KTSEHDMTSGGSTDN HCCCCCCCCCCCCCC | 30.22 | 21440633 | |
796 | Phosphorylation | TSEHDMTSGGSTDNG CCCCCCCCCCCCCCC | 34.22 | 21440633 | |
799 | Phosphorylation | HDMTSGGSTDNGSVL CCCCCCCCCCCCCEE | 35.79 | 23749301 | |
800 | Phosphorylation | DMTSGGSTDNGSVLP CCCCCCCCCCCCEEC | 36.44 | 23749301 |
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 BAS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BAS1_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 BAS1_YEAST !! |
Kegg Drug | ||||||
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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-317; SER-557 ANDSER-656, AND MASS SPECTROMETRY. |