| UniProt ID | MRD1_YEAST | |
|---|---|---|
| UniProt AC | Q06106 | |
| Protein Name | Multiple RNA-binding domain-containing protein 1 | |
| Gene Name | MRD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 887 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Involved in pre-rRNA processing. Required for maintaining steady-state levels of 40S ribosomal subunit. Required for the initial processing of pre-rRNA at the A0 to A2 sites, leading to the processing of the 23S pre-rRNA intermediate to the 18S rRNA.. | |
| Protein Sequence | MSRIIVKGLPVYLTDDNLREHFTKRLRQKHSHQAVNGSGPDLITDVKILRDRNGESRRFGFIGYRNEEDAFDAVEYFNGSFINTSKIEVSMAKSFADPRVPQPMKEKRREALKRFREKEEKLLQEENRKKKKVDENKHSNIDDEIRKNKQLQEFMETMKPSSQVTSWEKVGIDKSIEDEKLKREEEDSSVQGNSLLAHALALKEENNKDEAPNLVIENESDDEYSALNRNRDEDQEDAGEEEKMISISNLKDTDIGLVNDDANSDEKENEKRRNLAQDEKVSDLDWFKQRRVRIKESEAETREKSSSYATEQNESLDTKKEEQPERAVPQKTDEELAIEKINQTGRLFLRNILYTSKEEDFRKLFSPFGELEEVHVALDTRTGQSKGFAYVLFKDSKNAVNAYVELDKQIFQGRLLHILPGEEKKSHRLDEFDLKNMPLKKQKELKRKAAASRQTFSWNSLYMNQDAVLGSVAAKLGLEKSQLIDAENSSSAVKQALAEAHVIGDVRKYFESKGVDLTKFSQLKSTNQRDDKVILVKNFPFGTTREELGEMFLPYGKLERLLMPPAGTIAIVQFRDTTSARAAFTKLSYKRFKDGIIYLERGPKDCFTKPAEADDLINNTSAKEEENPVEVKPSSNDLMEANKDVTEGSSNAHDEDVIDGPTVSIFIKNLNFSTTNQNLTDRFKVFTGFVVAQVKTKPDPKHQGKTLSMGFGFVEFRTKEQANAVIAAMDGTVIDGHKIQLKLSHRQASQSGNTKTKSNKKSGKIIVKNLPFEATRKDVFELFNSFGQLKSVRVPKKFDKSARGFAFVEFLLPKEAENAMDQLHGVHLLGRRLVMQYAEEDAVDAEEEIARMTKKVRKQVATNEMAALRNGGGRKKLDVDDEENEGF | |
| 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 | Phosphorylation | ------MSRIIVKGL ------CCCEEEECC | 31.99 | 19795423 | |
| 31 | Phosphorylation | KRLRQKHSHQAVNGS HHHHHHHHHHCCCCC | 25.08 | 27017623 | |
| 38 | Phosphorylation | SHQAVNGSGPDLITD HHHCCCCCCCCCEEE | 41.78 | 27017623 | |
| 105 | Acetylation | PRVPQPMKEKRREAL CCCCCCCHHHHHHHH | 67.76 | 25381059 | |
| 161 | Phosphorylation | FMETMKPSSQVTSWE HHHHCCCHHHCCCHH | 28.08 | 19779198 | |
| 162 | Phosphorylation | METMKPSSQVTSWEK HHHCCCHHHCCCHHH | 36.88 | 27717283 | |
| 165 | Phosphorylation | MKPSSQVTSWEKVGI CCCHHHCCCHHHCCC | 22.08 | 27717283 | |
| 166 | Phosphorylation | KPSSQVTSWEKVGID CCHHHCCCHHHCCCC | 34.09 | 30377154 | |
| 174 | Acetylation | WEKVGIDKSIEDEKL HHHCCCCCCCCCHHH | 51.95 | 25381059 | |
| 175 | Phosphorylation | EKVGIDKSIEDEKLK HHCCCCCCCCCHHHH | 27.71 | 21440633 | |
| 188 | Phosphorylation | LKREEEDSSVQGNSL HHHHHHCCCHHHHHH | 35.37 | 21551504 | |
| 189 | Phosphorylation | KREEEDSSVQGNSLL HHHHHCCCHHHHHHH | 30.68 | 21440633 | |
| 220 | Phosphorylation | NLVIENESDDEYSAL CEEEECCCHHHHHHH | 63.04 | 22369663 | |
| 224 | Phosphorylation | ENESDDEYSALNRNR ECCCHHHHHHHHCCC | 13.26 | 22890988 | |
| 225 | Phosphorylation | NESDDEYSALNRNRD CCCHHHHHHHHCCCC | 25.00 | 22890988 | |
| 246 | Phosphorylation | GEEEKMISISNLKDT CHHHHEEEECCCCCC | 19.23 | 21440633 | |
| 248 | Phosphorylation | EEKMISISNLKDTDI HHHEEEECCCCCCCE | 29.35 | 21440633 | |
| 253 | Phosphorylation | SISNLKDTDIGLVND EECCCCCCCEEEECC | 28.12 | 27017623 | |
| 264 | Phosphorylation | LVNDDANSDEKENEK EECCCCCCCHHHHHH | 49.20 | 22369663 | |
| 267 | Acetylation | DDANSDEKENEKRRN CCCCCCHHHHHHHHH | 71.48 | 24489116 | |
| 271 | Acetylation | SDEKENEKRRNLAQD CCHHHHHHHHHHHHH | 69.14 | 24489116 | |
| 280 | Acetylation | RNLAQDEKVSDLDWF HHHHHHHCCCCHHHH | 56.16 | 24489116 | |
| 282 | Phosphorylation | LAQDEKVSDLDWFKQ HHHHHCCCCHHHHHH | 43.45 | 30377154 | |
| 288 | Acetylation | VSDLDWFKQRRVRIK CCCHHHHHHHCCCCC | 38.34 | 24489116 | |
| 297 | Phosphorylation | RRVRIKESEAETREK HCCCCCCCHHHHHHH | 36.78 | 30377154 | |
| 305 | Phosphorylation | EAETREKSSSYATEQ HHHHHHHHHCHHHHC | 21.55 | 28889911 | |
| 306 | Phosphorylation | AETREKSSSYATEQN HHHHHHHHCHHHHCC | 38.14 | 29136822 | |
| 307 | Phosphorylation | ETREKSSSYATEQNE HHHHHHHCHHHHCCC | 26.36 | 21551504 | |
| 308 | Phosphorylation | TREKSSSYATEQNES HHHHHHCHHHHCCCC | 21.35 | 29136822 | |
| 310 | Phosphorylation | EKSSSYATEQNESLD HHHHCHHHHCCCCCC | 29.85 | 29136822 | |
| 315 | Phosphorylation | YATEQNESLDTKKEE HHHHCCCCCCCCCCC | 38.81 | 28889911 | |
| 354 | Phosphorylation | LFLRNILYTSKEEDF HHHHHHHHCCCHHHH | 12.74 | 28889911 | |
| 394 | Acetylation | GFAYVLFKDSKNAVN CEEEEEEECCCCHHH | 57.86 | 24489116 | |
| 403 | Phosphorylation | SKNAVNAYVELDKQI CCCHHHHHHHHHHHH | 6.83 | 21440633 | |
| 424 | Acetylation | HILPGEEKKSHRLDE EECCCCCHHCCCCCC | 56.10 | 24489116 | |
| 435 | Acetylation | RLDEFDLKNMPLKKQ CCCCCCCCCCCHHHH | 53.71 | 24489116 | |
| 455 | Phosphorylation | KAAASRQTFSWNSLY HHHHHCCCCCHHHHC | 20.66 | 30377154 | |
| 480 | Acetylation | AAKLGLEKSQLIDAE HHHHCCCHHHCCCCC | 48.85 | 24489116 | |
| 509 | Phosphorylation | VIGDVRKYFESKGVD HHHHHHHHHHHCCCC | 11.30 | 19823750 | |
| 512 | Phosphorylation | DVRKYFESKGVDLTK HHHHHHHHCCCCHHH | 25.47 | 19823750 | |
| 513 | Acetylation | VRKYFESKGVDLTKF HHHHHHHCCCCHHHH | 56.61 | 24489116 | |
| 518 | Phosphorylation | ESKGVDLTKFSQLKS HHCCCCHHHHHHCCC | 26.11 | 19823750 | |
| 519 | Acetylation | SKGVDLTKFSQLKST HCCCCHHHHHHCCCC | 50.76 | 24489116 | |
| 557 | Acetylation | EMFLPYGKLERLLMP HHCCCHHHHHHHHCC | 41.13 | 24489116 | |
| 620 | Phosphorylation | ADDLINNTSAKEEEN HHHHCCCCCCCCCCC | 26.10 | 28889911 | |
| 621 | Phosphorylation | DDLINNTSAKEEENP HHHCCCCCCCCCCCC | 39.19 | 21551504 | |
| 635 | Phosphorylation | PVEVKPSSNDLMEAN CCCCCCCHHHHHHHC | 42.78 | 28889911 | |
| 649 | Phosphorylation | NKDVTEGSSNAHDED CCCCCCCCCCCCCCC | 17.74 | 21551504 | |
| 650 | Phosphorylation | KDVTEGSSNAHDEDV CCCCCCCCCCCCCCC | 49.22 | 21551504 | |
| 662 | Phosphorylation | EDVIDGPTVSIFIKN CCCCCCCEEEEEEEC | 32.20 | 21551504 | |
| 768 | Acetylation | KSGKIIVKNLPFEAT CCCCEEEECCCCCCC | 42.21 | 22865919 | |
| 785 | Phosphorylation | DVFELFNSFGQLKSV HHHHHHHHCCCCCEE | 24.34 | 30377154 | |
| 800 | Acetylation | RVPKKFDKSARGFAF ECCCCCCCCCCCEEE | 49.50 | 25381059 | |
| 837 | Phosphorylation | GRRLVMQYAEEDAVD HHHHHHHHHHHCCCC | 9.63 | 19779198 | |
| 875 | Acetylation | LRNGGGRKKLDVDDE HHCCCCCCCCCCCCC | 62.05 | 25381059 |
| 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 MRD1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MRD1_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 MRD1_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 SER-189; SER-220; TYR-224;SER-264 AND SER-315, 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-220 AND SER-264, ANDMASS SPECTROMETRY. | |
| "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-264, AND MASSSPECTROMETRY. | |
