| UniProt ID | PUR4_YEAST | |
|---|---|---|
| UniProt AC | P38972 | |
| Protein Name | Phosphoribosylformylglycinamidine synthase | |
| Gene Name | ADE6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1358 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (By similarity).. | |
| Protein Sequence | MTDYILPGPKALSQFRVDNLIKDINSYTNSTSVINELRSCYIHYVNGIAQNLSEQDTKLLEVLLTYDSALDIANDPLARQLNDAVANNLPSSALGEDTYLIRVVPRSGTISPWSSKATNIAHVCGLQDKVQRIERGLALLIKTVPGFPLLENLNDISLKCVYDRMTQQLYLTEPPNTMSIFTHEEPKPLVHVPLTPKDTKQSPKDILSKANTELGLALDSGEMEYLIHAFVETMKRDPTDVELFMFAQVNSEHCRHKIFNADWTIDGIKQQFTLFQMIRNTHKLNPEYTISAYSDNAAVLDSENDAFFFAPNSTTKEWTSTKERIPLLIKVETHNHPTAVSPFPGAATGSGGEIRDEGATGRGSKTKCGLSGFSVSDLLIPGNEQPWELNIGKPYHIASALDIMIEAPLGSAAFNNEFGRPCINGYFRTLTTKVLNHQGKEEIRGFHKPIMIAGGFGTVRPQFALKNTPITPGSCLIVLGGQSMLIGLGGGAASSVASGEGSADLDFASVQRGNPEMERRCQQVIDACVALGNNNPIQSIHDVGAGGLSNALPELVHDNDLGAKFDIRKVLSLEPGMSPMEIWCNESQERYVLGVSPQDLSIFEEICKRERAPFAVVGHATAEQKLIVEDPLLKTTPIDLEMPILFGKPPKMSRETITEALNLPEANLSEIPSLQDAIQRVLNLPSVGSKSFLITIGDRSVTGLIDRDQFVGPWQVPVADVGVTGTSLGETIISTGEAMAMGEKPVNALISASASAKLSVAESLLNIFAADVKSLNHIKLSANWMSPASHQGEGSKLYEAVQALGLDLCPALGVAIPVGKDSMSMKMKWDDKEVTAPLSLNITAFAPVFNTSKTWTPLLNRNTDDSVLVLVDLSAKQETKSLGASALLQVYNQVGNKSPTVYDNAILKGFLESLIQLHQQKEDIVLAYHDRSDGGLLITLLEMAFASRCGLEINIDGGDLESQLTNLFNEELGAVFQISAKNLSKFEKILNENGVAKEYISIVGKPSFQSQEIKIINSTTNDVIYANSRSELEQTWSKTSYEMQKLRDNPKTAEEEFASITDDRDPGLQYALTYNPADDMKIGLELSSQRPKVAILREQGVNGQMEMAWCFQQAGFNSVDVTMTDLLEGRFHLDDFIGLAACGGFSYGDVLGAGAGWAKSVLYHEGVRSQFSKFFNERQDTFAFGACNGCQFLSRLKDIIPGCENWPSFERNVSEQYEARVCMVQISQEKDNSSEESVFLNGMAGSKLPIAVAHGEGKATFSKSAEQLEKFEKDGLCCIRYVDNYGNVTERFPFNPNGSTNGIAGIKSPNGRVLAMMPHPERVCRLEANSWYPEGKYEEWGGYGPWIRLFRSARRWVG | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MTDYILPGP ------CCCCCCCCH | 49.14 | 22814378 | |
| 10 | Ubiquitination | DYILPGPKALSQFRV CCCCCCHHHHHHHCH | 68.80 | 24961812 | |
| 13 | Phosphorylation | LPGPKALSQFRVDNL CCCHHHHHHHCHHHH | 31.94 | 21440633 | |
| 22 | Ubiquitination | FRVDNLIKDINSYTN HCHHHHHHHHHHCCC | 56.58 | 24961812 | |
| 107 | Phosphorylation | LIRVVPRSGTISPWS EEEEECCCCCCCCCC | 33.93 | 22369663 | |
| 109 | Phosphorylation | RVVPRSGTISPWSSK EEECCCCCCCCCCCC | 21.38 | 22369663 | |
| 111 | Phosphorylation | VPRSGTISPWSSKAT ECCCCCCCCCCCCCH | 21.83 | 22369663 | |
| 114 | Phosphorylation | SGTISPWSSKATNIA CCCCCCCCCCCHHHH | 25.91 | 22369663 | |
| 115 | Phosphorylation | GTISPWSSKATNIAH CCCCCCCCCCHHHHH | 23.57 | 22369663 | |
| 116 | Ubiquitination | TISPWSSKATNIAHV CCCCCCCCCHHHHHH | 54.43 | 23749301 | |
| 129 | Ubiquitination | HVCGLQDKVQRIERG HHCCCHHHHHHHHHH | 27.57 | 17644757 | |
| 129 | Acetylation | HVCGLQDKVQRIERG HHCCCHHHHHHHHHH | 27.57 | 24489116 | |
| 195 | Phosphorylation | PLVHVPLTPKDTKQS CCEECCCCCCCCCCC | 23.40 | 29734811 | |
| 257 | Acetylation | NSEHCRHKIFNADWT CCHHHCCHHHCCCCC | 29.64 | 24489116 | |
| 257 | Ubiquitination | NSEHCRHKIFNADWT CCHHHCCHHHCCCCC | 29.64 | 23749301 | |
| 330 | Acetylation | ERIPLLIKVETHNHP CCCCEEEEEEECCCC | 33.71 | 24489116 | |
| 333 | Phosphorylation | PLLIKVETHNHPTAV CEEEEEEECCCCCCC | 30.85 | 29136822 | |
| 338 | Phosphorylation | VETHNHPTAVSPFPG EEECCCCCCCCCCCC | 31.94 | 29136822 | |
| 341 | Phosphorylation | HNHPTAVSPFPGAAT CCCCCCCCCCCCCCC | 20.54 | 29136822 | |
| 360 | Phosphorylation | EIRDEGATGRGSKTK EECCCCCCCCCCCCC | 37.96 | 28889911 | |
| 364 | Phosphorylation | EGATGRGSKTKCGLS CCCCCCCCCCCCCCC | 35.47 | 28889911 | |
| 433 | Ubiquitination | YFRTLTTKVLNHQGK HHHHHHHHHHCCCCH | 39.22 | 22817900 | |
| 440 | Acetylation | KVLNHQGKEEIRGFH HHHCCCCHHHHCCCC | 45.67 | 22865919 | |
| 448 | Ubiquitination | EEIRGFHKPIMIAGG HHHCCCCCCEEEECC | 33.70 | 22817900 | |
| 448 | Acetylation | EEIRGFHKPIMIAGG HHHCCCCCCEEEECC | 33.70 | 24489116 | |
| 578 | Phosphorylation | LSLEPGMSPMEIWCN HCCCCCCCCCEEEEC | 27.32 | 28152593 | |
| 596 | Phosphorylation | ERYVLGVSPQDLSIF CEEECCCCHHHHHHH | 18.29 | 22369663 | |
| 625 | Ubiquitination | GHATAEQKLIVEDPL CCCCHHCEEEECCCC | 31.52 | 17644757 | |
| 634 | Ubiquitination | IVEDPLLKTTPIDLE EECCCCCCCCCCCCC | 59.02 | 17644757 | |
| 648 | Acetylation | EMPILFGKPPKMSRE CCCHHCCCCCCCCHH | 51.30 | 24489116 | |
| 648 | Ubiquitination | EMPILFGKPPKMSRE CCCHHCCCCCCCCHH | 51.30 | 17644757 | |
| 651 | Ubiquitination | ILFGKPPKMSRETIT HHCCCCCCCCHHHHH | 59.02 | 17644757 | |
| 757 | Ubiquitination | ISASASAKLSVAESL HHCCHHHCHHHHHHH | 38.51 | 17644757 | |
| 773 | Ubiquitination | NIFAADVKSLNHIKL HHHHHCHHHCCCEEE | 50.18 | 17644757 | |
| 786 | Phosphorylation | KLSANWMSPASHQGE EEEECCCCCCCCCCC | 14.66 | 23749301 | |
| 822 | Phosphorylation | AIPVGKDSMSMKMKW EEECCCCCCCCEECC | 19.08 | 27017623 | |
| 824 | Phosphorylation | PVGKDSMSMKMKWDD ECCCCCCCCEECCCC | 21.14 | 27017623 | |
| 835 | Phosphorylation | KWDDKEVTAPLSLNI CCCCCCCCCCEEEEE | 24.53 | 22369663 | |
| 839 | Phosphorylation | KEVTAPLSLNITAFA CCCCCCEEEEEEEEE | 20.50 | 22369663 | |
| 843 | Phosphorylation | APLSLNITAFAPVFN CCEEEEEEEEECCCC | 18.04 | 22369663 | |
| 851 | Phosphorylation | AFAPVFNTSKTWTPL EEECCCCCCCCCCCC | 21.82 | 22369663 | |
| 852 | Phosphorylation | FAPVFNTSKTWTPLL EECCCCCCCCCCCCC | 29.23 | 22369663 | |
| 854 | Phosphorylation | PVFNTSKTWTPLLNR CCCCCCCCCCCCCCC | 34.05 | 22369663 | |
| 856 | Phosphorylation | FNTSKTWTPLLNRNT CCCCCCCCCCCCCCC | 14.86 | 22369663 | |
| 880 | Ubiquitination | LSAKQETKSLGASAL CCCCHHHHCCCHHHH | 42.82 | 17644757 | |
| 897 | Ubiquitination | VYNQVGNKSPTVYDN HHHHHCCCCCCHHHH | 52.46 | 17644757 | |
| 921 | Acetylation | LIQLHQQKEDIVLAY HHHHHHCCCCEEEEE | 51.27 | 24489116 | |
| 985 | Acetylation | ISAKNLSKFEKILNE EECCCHHHHHHHHCC | 61.79 | 24489116 | |
| 988 | Acetylation | KNLSKFEKILNENGV CCHHHHHHHHCCCCC | 56.47 | 24489116 | |
| 1038 | Ubiquitination | ELEQTWSKTSYEMQK HHHHHHHHHHHHHHH | 32.81 | 23749301 | |
| 1081 | Ubiquitination | YNPADDMKIGLELSS ECCHHHCEEEEEECC | 40.39 | 19722269 | |
| 1160 | Phosphorylation | AGAGWAKSVLYHEGV CCCCCHHHHHHHHHH | 15.03 | 21440633 | |
| 1173 | 2-Hydroxyisobutyrylation | GVRSQFSKFFNERQD HHHHHHHHHHHHCCC | 56.09 | - | |
| 1173 | Acetylation | GVRSQFSKFFNERQD HHHHHHHHHHHHCCC | 56.09 | 24489116 | |
| 1197 | Ubiquitination | CQFLSRLKDIIPGCE HHHHHHHHHHCCCCC | 45.85 | 22817900 | |
| 1237 | Phosphorylation | KDNSSEESVFLNGMA CCCCCCCEEECCCCC | 17.70 | 27017623 | |
| 1246 | Phosphorylation | FLNGMAGSKLPIAVA ECCCCCCCCCCEEEE | 22.83 | 27017623 | |
| 1247 | Ubiquitination | LNGMAGSKLPIAVAH CCCCCCCCCCEEEEE | 58.32 | 24961812 | |
| 1258 | Ubiquitination | AVAHGEGKATFSKSA EEEECCCEECCCCCH | 39.69 | 22817900 | |
| 1263 | Acetylation | EGKATFSKSAEQLEK CCEECCCCCHHHHHH | 49.87 | 24489116 | |
| 1263 | Ubiquitination | EGKATFSKSAEQLEK CCEECCCCCHHHHHH | 49.87 | 22817900 | |
| 1263 | 2-Hydroxyisobutyrylation | EGKATFSKSAEQLEK CCEECCCCCHHHHHH | 49.87 | - | |
| 1307 | Ubiquitination | TNGIAGIKSPNGRVL CCCCCCCCCCCCCEE | 59.97 | 23749301 | |
| 1336 | Ubiquitination | NSWYPEGKYEEWGGY CCCCCCCCCCCCCCC | 48.07 | 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 PUR4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUR4_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 PUR4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-333, AND MASSSPECTROMETRY. | |