| UniProt ID | REB1_YEAST | |
|---|---|---|
| UniProt AC | P21538 | |
| Protein Name | DNA-binding protein REB1 | |
| Gene Name | REB1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 810 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | DNA-binding protein that recognizes sites within both the enhancer and the promoter of rRNA transcription, as well as upstream of many genes transcribed by RNA polymerase II. It is essential for cell growth. May stimulate or inhibit transcription. Specifically recognizes the sequence 5'-CCGGGTA-3' or 5'-CGGGTRR-3' (where R is any purine). A member of the general regulatory factors (GRFs) which act as genome partitioners. Acts as a chromatin insulator which are known as STARs (Subtelomeric anti-silencing region). STARs prevent negative or positive transcription influence by extending across chromotin to a promoter.. | |
| Protein Sequence | MPSGHNDKNANQESVEEAVLKYVGVGLDHQNHDPQLHTKDLENKHSKKQNIVESSSDVDVNNNDDSNRNEDNNDDSENISALNANESSSNVDHANSNEQHNAVMDWYLRQTAHNQQDDEDDENNNNTDNGNDSNNHFSQSDIVVDDDDDKNKKDAGVGVDDDHQSMAMAAVAAAYTLSKNNNNNNSIANDSNSRKRQHDNGNNHENSQKKRKNNNDDDDRQIGNVDPELTTLGDADDNDTNNDVIDRDQLVHKAIIDADSITQHPDFQQYLNTAADTDDNEKLKHIKDHLMRTHGLNHQNKNHNDDTDDLSNSTKQYSELQKDSMLDSSLNKSRNYMEVLPKVISQDTQPHQQKSPSHDNEAGSVDNSEISQLLQSAATKASSLVSLSSSSATPSTSRSNNSKAFDKAEDAALERFINEYEAIERLTRQQVCERIWSSDRPKDNFWNNIYKVLPYRSSSSIYKHMRRKYHIFEQRGKWTAEEEQELAKLCAEKEGQWAEIGKTLGRMPEDCRDRWRNYVKCGTNRASNRWSVEEEELLKKVISDMLEEAQQQQSQLHPNLLEEEQHLLQDDQNDHRNNDEDDDDTASAAAAAAAAIQEQQQLLQQKQQDDDDAIAAAAAAASSSLGDNKDEDKPHDSLGIQLDDNSQNSMVPAPSATSTHSKSLSNTIRRHNNKLRKSLMGNGKLDFKDIINWTIVSERMGGTRSRIQCRYKWNKLVKREAIAKIQTVKDDDMLWIFEKLRDLGITEDSQVDWDELAALKPGMKLNGLELKLCYERMKKKVKGYKQKSINEISKELVDYFSSNISMKTEN | |
| 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 |
|---|---|---|---|---|---|
| 8 | Ubiquitination | MPSGHNDKNANQESV CCCCCCCCCCCHHHH | 64.38 | 15699485 | |
| 14 | Phosphorylation | DKNANQESVEEAVLK CCCCCHHHHHHHHHH | 25.68 | 22369663 | |
| 21 | Ubiquitination | SVEEAVLKYVGVGLD HHHHHHHHHHCCCCC | 31.15 | 15699485 | |
| 21 | Acetylation | SVEEAVLKYVGVGLD HHHHHHHHHHCCCCC | 31.15 | 24489116 | |
| 39 | Acetylation | HDPQLHTKDLENKHS CCCCCCHHHCCCCHH | 49.95 | 24489116 | |
| 44 | Acetylation | HTKDLENKHSKKQNI CHHHCCCCHHHCCCC | 39.62 | 25381059 | |
| 54 | Phosphorylation | KKQNIVESSSDVDVN HCCCCCCCCCCCCCC | 25.01 | 25704821 | |
| 55 | Phosphorylation | KQNIVESSSDVDVNN CCCCCCCCCCCCCCC | 19.63 | 25704821 | |
| 56 | Phosphorylation | QNIVESSSDVDVNNN CCCCCCCCCCCCCCC | 51.43 | 23749301 | |
| 175 | Phosphorylation | MAAVAAAYTLSKNNN HHHHHHHHHHHCCCC | 11.95 | 21440633 | |
| 186 | Phosphorylation | KNNNNNNSIANDSNS CCCCCCCCCCCCCCH | 25.79 | 23749301 | |
| 191 | Phosphorylation | NNSIANDSNSRKRQH CCCCCCCCCHHHCCC | 36.19 | 23749301 | |
| 193 | Phosphorylation | SIANDSNSRKRQHDN CCCCCCCHHHCCCCC | 43.03 | 21440633 | |
| 230 | Phosphorylation | GNVDPELTTLGDADD CCCCHHHCCCCCCCC | 20.50 | 21551504 | |
| 240 | Phosphorylation | GDADDNDTNNDVIDR CCCCCCCCCCCCCCH | 42.02 | 21440633 | |
| 260 | Phosphorylation | KAIIDADSITQHPDF HHHCCCHHHCCCCCH | 29.29 | 22369663 | |
| 262 | Phosphorylation | IIDADSITQHPDFQQ HCCCHHHCCCCCHHH | 25.44 | 22369663 | |
| 270 | Phosphorylation | QHPDFQQYLNTAADT CCCCHHHHHHHCCCC | 7.37 | 22369663 | |
| 273 | Phosphorylation | DFQQYLNTAADTDDN CHHHHHHHCCCCCCH | 22.19 | 22369663 | |
| 277 | Phosphorylation | YLNTAADTDDNEKLK HHHHCCCCCCHHHHH | 40.29 | 20377248 | |
| 282 | Acetylation | ADTDDNEKLKHIKDH CCCCCHHHHHHHHHH | 69.92 | 24489116 | |
| 287 | Acetylation | NEKLKHIKDHLMRTH HHHHHHHHHHHHHHH | 38.52 | 25381059 | |
| 311 | Phosphorylation | NDDTDDLSNSTKQYS CCCCCCCCHHHHHHH | 35.41 | 21551504 | |
| 313 | Phosphorylation | DTDDLSNSTKQYSEL CCCCCCHHHHHHHHH | 33.34 | 28889911 | |
| 318 | Phosphorylation | SNSTKQYSELQKDSM CHHHHHHHHHHHHHH | 29.36 | 30377154 | |
| 322 | Acetylation | KQYSELQKDSMLDSS HHHHHHHHHHHHHHH | 65.48 | 24489116 | |
| 328 | Phosphorylation | QKDSMLDSSLNKSRN HHHHHHHHHHCCCCC | 32.53 | 30377154 | |
| 329 | Phosphorylation | KDSMLDSSLNKSRNY HHHHHHHHHCCCCCH | 35.31 | 30377154 | |
| 332 | Acetylation | MLDSSLNKSRNYMEV HHHHHHCCCCCHHHH | 56.96 | 25381059 | |
| 333 | Phosphorylation | LDSSLNKSRNYMEVL HHHHHCCCCCHHHHH | 25.37 | 30377154 | |
| 336 | Phosphorylation | SLNKSRNYMEVLPKV HHCCCCCHHHHHHHH | 8.11 | 21440633 | |
| 342 | Acetylation | NYMEVLPKVISQDTQ CHHHHHHHHHCCCCC | 48.30 | 22865919 | |
| 345 | Phosphorylation | EVLPKVISQDTQPHQ HHHHHHHCCCCCCCC | 25.62 | 22369663 | |
| 348 | Phosphorylation | PKVISQDTQPHQQKS HHHHCCCCCCCCCCC | 36.04 | 22369663 | |
| 355 | Phosphorylation | TQPHQQKSPSHDNEA CCCCCCCCCCCCCCC | 27.57 | 22369663 | |
| 357 | Phosphorylation | PHQQKSPSHDNEAGS CCCCCCCCCCCCCCC | 51.03 | 22369663 | |
| 364 | Phosphorylation | SHDNEAGSVDNSEIS CCCCCCCCCCHHHHH | 33.09 | 22369663 | |
| 368 | Phosphorylation | EAGSVDNSEISQLLQ CCCCCCHHHHHHHHH | 31.66 | 22890988 | |
| 371 | Phosphorylation | SVDNSEISQLLQSAA CCCHHHHHHHHHHHH | 15.66 | 22890988 | |
| 376 | Phosphorylation | EISQLLQSAATKASS HHHHHHHHHHHHHHH | 21.60 | 22890988 | |
| 379 | Phosphorylation | QLLQSAATKASSLVS HHHHHHHHHHHHHHH | 27.19 | 22890988 | |
| 382 | Phosphorylation | QSAATKASSLVSLSS HHHHHHHHHHHHHCC | 26.26 | 22369663 | |
| 383 | Phosphorylation | SAATKASSLVSLSSS HHHHHHHHHHHHCCC | 37.34 | 22369663 | |
| 386 | Phosphorylation | TKASSLVSLSSSSAT HHHHHHHHHCCCCCC | 28.03 | 22369663 | |
| 388 | Phosphorylation | ASSLVSLSSSSATPS HHHHHHHCCCCCCCC | 22.22 | 22369663 | |
| 389 | Phosphorylation | SSLVSLSSSSATPST HHHHHHCCCCCCCCC | 33.34 | 22369663 | |
| 390 | Phosphorylation | SLVSLSSSSATPSTS HHHHHCCCCCCCCCC | 22.18 | 22369663 | |
| 391 | Phosphorylation | LVSLSSSSATPSTSR HHHHCCCCCCCCCCC | 37.80 | 22369663 | |
| 393 | Phosphorylation | SLSSSSATPSTSRSN HHCCCCCCCCCCCCC | 21.51 | 22369663 | |
| 395 | Phosphorylation | SSSSATPSTSRSNNS CCCCCCCCCCCCCCC | 34.36 | 22369663 | |
| 396 | Phosphorylation | SSSATPSTSRSNNSK CCCCCCCCCCCCCCH | 29.39 | 22369663 | |
| 397 | Phosphorylation | SSATPSTSRSNNSKA CCCCCCCCCCCCCHH | 37.74 | 22369663 | |
| 403 | Acetylation | TSRSNNSKAFDKAED CCCCCCCHHCHHHHH | 56.02 | 24489116 | |
| 407 | Acetylation | NNSKAFDKAEDAALE CCCHHCHHHHHHHHH | 47.42 | 24489116 | |
| 455 | Phosphorylation | NIYKVLPYRSSSSIY HHHHHCCCCCCHHHH | 20.97 | 21440633 | |
| 459 | Phosphorylation | VLPYRSSSSIYKHMR HCCCCCCHHHHHHHH | 23.23 | 21551504 | |
| 460 | Phosphorylation | LPYRSSSSIYKHMRR CCCCCCHHHHHHHHH | 31.70 | 21551504 | |
| 468 | Acetylation | IYKHMRRKYHIFEQR HHHHHHHHHHHHHHC | 30.71 | 25381059 | |
| 477 | Acetylation | HIFEQRGKWTAEEEQ HHHHHCCCCCHHHHH | 43.49 | 24489116 | |
| 493 | Acetylation | LAKLCAEKEGQWAEI HHHHHHHHHCCHHHH | 48.93 | 24489116 | |
| 585 | Phosphorylation | NDEDDDDTASAAAAA CCCCCHHHHHHHHHH | 29.52 | 19779198 | |
| 587 | Phosphorylation | EDDDDTASAAAAAAA CCCHHHHHHHHHHHH | 22.12 | 19779198 | |
| 665 | Phosphorylation | STHSKSLSNTIRRHN CCCCHHHHHHHHHHC | 38.73 | 27214570 | |
| 674 | Acetylation | TIRRHNNKLRKSLMG HHHHHCHHHHHHHHC | 55.79 | 25381059 | |
| 678 | Phosphorylation | HNNKLRKSLMGNGKL HCHHHHHHHHCCCCC | 19.70 | 21440633 | |
| 799 | Phosphorylation | ISKELVDYFSSNISM HHHHHHHHHHHHCCC | 9.62 | 21551504 | |
| 801 | Phosphorylation | KELVDYFSSNISMKT HHHHHHHHHHCCCCC | 19.08 | 21551504 | |
| 805 | Phosphorylation | DYFSSNISMKTEN-- HHHHHHCCCCCCC-- | 20.62 | 30377154 | |
| 807 | Sumoylation | FSSNISMKTEN---- HHHHCCCCCCC---- | 45.99 | - | |
| 807 | Sumoylation | FSSNISMKTEN---- HHHHCCCCCCC---- | 45.99 | 15542864 | |
| 807 | Ubiquitination | FSSNISMKTEN---- HHHHCCCCCCC---- | 45.99 | 15542864 |
| 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 REB1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of REB1_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 REB1_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-355; SER-383 ANDSER-386, 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-355, 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-355, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASSSPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "A proteomic strategy for gaining insights into protein sumoylation inyeast."; Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.; Mol. Cell. Proteomics 4:246-254(2005). Cited for: PROTEIN SEQUENCE OF 795-810, SUMOYLATION [LARGE SCALE ANALYSIS] ATLYS-807, AND MASS SPECTROMETRY. | |
