| UniProt ID | BMS1_YEAST | |
|---|---|---|
| UniProt AC | Q08965 | |
| Protein Name | Ribosome biogenesis protein BMS1 | |
| Gene Name | BMS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1183 | |
| Subcellular Localization | Cytoplasm . Nucleus, nucleolus . | |
| Protein Description | May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits.. | |
| Protein Sequence | MEQSNKQHRKAKEKNTAKKKLHTQGHNAKAFAVAAPGKMARTMQRSSDVNERKLHVPMVDRTPEDDPPPFIVAVVGPPGTGKTTLIRSLVRRMTKSTLNDIQGPITVVSGKHRRLTFLECPADDLNAMIDIAKIADLVLLLIDGNFGFEMETMEFLNIAQHHGMPRVLGVATHLDLFKSQSTLRASKKRLKHRFWTEVYQGAKLFYLSGVINGRYPDREILNLSRFISVMKFRPLKWRNEHPYMLADRFTDLTHPELIETQGLQIDRKVAIYGYLHGTPLPSAPGTRVHIAGVGDFSVAQIEKLPDPCPTPFYQQKLDDFEREKMKEEAKANGEITTASTTRRRKRLDDKDKLIYAPMSDVGGVLMDKDAVYIDIGKKNEEPSFVPGQERGEGEKLMTGLQSVEQSIAEKFDGVGLQLFSNGTELHEVADHEGMDVESGEESIEDDEGKSKGRTSLRKPRIYGKPVQEEDADIDNLPSDEEPYTNDDDVQDSEPRMVEIDFNNTGEQGAEKLALETDSEFEESEDEFSWERTAANKLKKTESKKRTWNIGKLIYMDNISPEECIRRWRGEDDDSKDESDIEEDVDDDFFRKKDGTVTKEGNKDHAVDLEKFVPYFDTFEKLAKKWKSVDAIKERFLGAGILGNDNKTKSDSNEGGEELYGDFEDLEDGNPSEQAEDNSDKESEDEDENEDTNGDDDNSFTNFDAEEKKDLTMEQEREMNAAKKEKLRAQFEIEEGENFKEDDENNEYDTWYELQKAKISKQLEINNIEYQEMTPEQRQRIEGFKAGSYVRIVFEKVPMEFVKNFNPKFPIVMGGLLPTEIKFGIVKARLRRHRWHKKILKTNDPLVLSLGWRRFQTLPIYTTTDSRTRTRMLKYTPEHTYCNAAFYGPLCSPNTPFCGVQIVANSDTGNGFRIAATGIVEEIDVNIEIVKKLKLVGFPYKIFKNTAFIKDMFSSAMEVARFEGAQIKTVSGIRGEIKRALSKPEGHYRAAFEDKILMSDIVILRSWYPVRVKKFYNPVTSLLLKEKTEWKGLRLTGQIRAAMNLETPSNPDSAYHKIERVERHFNGLKVPKAVQKELPFKSQIHQMKPQKKKTYMAKRAVVLGGDEKKARSFIQKVLTISKAKDSKRKEQKASQRKERLKKLAKMEEEKSQRDKEKKKEYFAQNGKRTTMGGDDESRPRKMRR | |
| 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 |
|---|---|---|---|---|---|
| 29 | Acetylation | HTQGHNAKAFAVAAP HHCCCCHHEEEEECC | 49.72 | 25381059 | |
| 111 | Acetylation | PITVVSGKHRRLTFL CEEEECCCCCEEEEE | 26.82 | 24489116 | |
| 310 | Phosphorylation | KLPDPCPTPFYQQKL CCCCCCCCCHHHHCH | 32.52 | 17287358 | |
| 340 | Phosphorylation | GEITTASTTRRRKRL CCCCCCHHHCCHHCC | 23.12 | 30377154 | |
| 402 | Phosphorylation | KLMTGLQSVEQSIAE HHHHHHHHHHHHHHH | 32.44 | 30377154 | |
| 420 | Phosphorylation | GVGLQLFSNGTELHE CCEEEEECCCCEEEE | 42.83 | 29688323 | |
| 423 | Phosphorylation | LQLFSNGTELHEVAD EEEECCCCEEEEECC | 39.36 | 21440633 | |
| 438 | Phosphorylation | HEGMDVESGEESIED CCCCCCCCCCCCCCC | 51.89 | 20377248 | |
| 442 | Phosphorylation | DVESGEESIEDDEGK CCCCCCCCCCCCCCC | 27.29 | 21440633 | |
| 462 | Phosphorylation | SLRKPRIYGKPVQEE CCCCCCCCCCCCCCC | 22.00 | 19779198 | |
| 478 | Phosphorylation | ADIDNLPSDEEPYTN CCCCCCCCCCCCCCC | 61.90 | 22369663 | |
| 483 | Phosphorylation | LPSDEEPYTNDDDVQ CCCCCCCCCCCCCCC | 22.81 | 22369663 | |
| 484 | Phosphorylation | PSDEEPYTNDDDVQD CCCCCCCCCCCCCCC | 42.77 | 22369663 | |
| 492 | Phosphorylation | NDDDVQDSEPRMVEI CCCCCCCCCCCEEEE | 32.20 | 29136822 | |
| 504 | Phosphorylation | VEIDFNNTGEQGAEK EEEECCCCCCCHHHH | 43.11 | 28152593 | |
| 516 | Phosphorylation | AEKLALETDSEFEES HHHEEEECCCCCCCC | 45.75 | 20377248 | |
| 518 | Phosphorylation | KLALETDSEFEESED HEEEECCCCCCCCCC | 52.16 | 20377248 | |
| 523 | Phosphorylation | TDSEFEESEDEFSWE CCCCCCCCCCCCCHH | 43.05 | 20377248 | |
| 559 | Phosphorylation | LIYMDNISPEECIRR EEEECCCCHHHHHHH | 32.29 | 28889911 | |
| 574 | Phosphorylation | WRGEDDDSKDESDIE HCCCCCCCCCHHHCC | 49.34 | 22369663 | |
| 578 | Phosphorylation | DDDSKDESDIEEDVD CCCCCCHHHCCCCCC | 54.76 | 22369663 | |
| 620 | Acetylation | PYFDTFEKLAKKWKS HHHHHHHHHHHHCCC | 49.94 | 24489116 | |
| 646 | Acetylation | GILGNDNKTKSDSNE EECCCCCCCCCCCCC | 61.26 | 24489116 | |
| 698 | Phosphorylation | TNGDDDNSFTNFDAE CCCCCCCCCCCCCHH | 40.20 | 28889911 | |
| 773 | Phosphorylation | NIEYQEMTPEQRQRI CEEEECCCHHHHHHH | 23.95 | 27214570 | |
| 802 | Acetylation | KVPMEFVKNFNPKFP ECCHHHHHHCCCCCC | 62.23 | 24489116 | |
| 856 | Phosphorylation | LGWRRFQTLPIYTTT ECCCEECCCCEEEEC | 31.61 | 28889911 | |
| 860 | Phosphorylation | RFQTLPIYTTTDSRT EECCCCEEEECCCCC | 8.97 | 28889911 | |
| 861 | Phosphorylation | FQTLPIYTTTDSRTR ECCCCEEEECCCCCC | 24.76 | 28889911 | |
| 862 | Phosphorylation | QTLPIYTTTDSRTRT CCCCEEEECCCCCCC | 16.19 | 28889911 | |
| 863 | Phosphorylation | TLPIYTTTDSRTRTR CCCEEEECCCCCCCE | 24.95 | 28889911 | |
| 865 | Phosphorylation | PIYTTTDSRTRTRML CEEEECCCCCCCEEC | 33.20 | 28889911 | |
| 940 | Acetylation | KLVGFPYKIFKNTAF EECCCCHHHHCCCHH | 41.74 | 24489116 | |
| 967 | Ubiquitination | RFEGAQIKTVSGIRG HHCCCEEEEEECCHH | 30.69 | 23749301 | |
| 1024 | Acetylation | PVTSLLLKEKTEWKG CHHHHHHCCCCCCCC | 58.07 | 24489116 | |
| 1056 | Acetylation | NPDSAYHKIERVERH CCCHHHHHHHHHHHH | 33.32 | 24489116 | |
| 1068 | Acetylation | ERHFNGLKVPKAVQK HHHHCCCCCCHHHHC | 58.87 | 24489116 | |
| 1075 | Acetylation | KVPKAVQKELPFKSQ CCCHHHHCCCCCCHH | 55.40 | 22865919 | |
| 1115 | Acetylation | KARSFIQKVLTISKA HHHHHHHHHHHHHHH | 34.10 | 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 BMS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BMS1_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 BMS1_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-438; SER-478; TYR-483;SER-559; SER-578 AND SER-698, 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-578, AND MASSSPECTROMETRY. | |
| "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 SER-578, AND MASSSPECTROMETRY. | |
| "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 THR-310, AND MASSSPECTROMETRY. | |
