| UniProt ID | EZH2_HUMAN | |
|---|---|---|
| UniProt AC | Q15910 | |
| Protein Name | Histone-lysine N-methyltransferase EZH2 {ECO:0000305} | |
| Gene Name | EZH2 {ECO:0000312|HGNC:HGNC:3527} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 746 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. [PubMed: 22323599 Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-ARNTL/BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription.] | |
| Protein Sequence | MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKSMFSSNRQKILERTEILNQEWKQRRIQPVHILTSVSSLRGTRECSVTSDLDFPTQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPEEREEKQKDLEDHRDDKESRPPRKFPSDKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTINVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPAPAEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP | |
| 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 |
|---|---|---|---|---|---|
| 7 | Acetylation | -MGQTGKKSEKGPVC -CCCCCCCCCCCCCC | 66.25 | 25953088 | |
| 7 | Ubiquitination | -MGQTGKKSEKGPVC -CCCCCCCCCCCCCC | 66.25 | - | |
| 8 | Phosphorylation | MGQTGKKSEKGPVCW CCCCCCCCCCCCCCC | 48.29 | - | |
| 10 | Acetylation | QTGKKSEKGPVCWRK CCCCCCCCCCCCCHH | 75.50 | 25953088 | |
| 10 | Ubiquitination | QTGKKSEKGPVCWRK CCCCCCCCCCCCCHH | 75.50 | - | |
| 10 (in isoform 2) | Malonylation | - | 75.50 | 32601280 | |
| 21 | Phosphorylation | CWRKRVKSEYMRLRQ CCHHHHHHHHHHHHH | 30.97 | 16224021 | |
| 23 | Phosphorylation | RKRVKSEYMRLRQLK HHHHHHHHHHHHHHH | 8.47 | - | |
| 39 | Ubiquitination | FRRADEVKSMFSSNR HHCHHHHHHHHCHHH | 33.87 | - | |
| 39 (in isoform 2) | Ubiquitination | - | 33.87 | - | |
| 43 | Phosphorylation | DEVKSMFSSNRQKIL HHHHHHHCHHHHHHH | 20.33 | 20860994 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 2189047 | |
| 61 (in isoform 2) | Ubiquitination | - | 32.92 | - | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 61 | Ubiquitination | EILNQEWKQRRIQPV HHHCHHHHHCCCCCE | 32.92 | 21890473 | |
| 73 | O-linked_Glycosylation | QPVHILTSVSSLRGT CCEEEEEEHHHCCCC | 19.29 | 29941599 | |
| 75 | O-linked_Glycosylation | VHILTSVSSLRGTRE EEEEEEHHHCCCCCE | 24.34 | 24474760 | |
| 75 | Phosphorylation | VHILTSVSSLRGTRE EEEEEEHHHCCCCCE | 24.34 | 24719451 | |
| 76 | O-linked_Glycosylation | HILTSVSSLRGTREC EEEEEHHHCCCCCEE | 21.67 | 62173233 | |
| 76 | Phosphorylation | HILTSVSSLRGTREC EEEEEHHHCCCCCEE | 21.67 | 23186163 | |
| 83 | Glutathionylation | SLRGTRECSVTSDLD HCCCCCEEEECCCCC | 3.41 | 22555962 | |
| 84 | O-linked_Glycosylation | LRGTRECSVTSDLDF CCCCCEEEECCCCCC | 24.55 | 29941599 | |
| 87 | O-linked_Glycosylation | TRECSVTSDLDFPTQ CCEEEECCCCCCCCC | 33.74 | 29941599 | |
| 212 | Phosphorylation | DHRDDKESRPPRKFP HCCCCCCCCCCCCCC | 56.69 | 23312004 | |
| 220 | Phosphorylation | RPPRKFPSDKIFEAI CCCCCCCCHHHHHHH | 55.45 | - | |
| 234 | Acetylation | ISSMFPDKGTAEELK HHHHCCCCCCHHHHH | 59.40 | 23749302 | |
| 234 | Ubiquitination | ISSMFPDKGTAEELK HHHHCCCCCCHHHHH | 59.40 | - | |
| 241 | Acetylation | KGTAEELKEKYKELT CCCHHHHHHHHHHHH | 56.28 | 25953088 | |
| 244 | Phosphorylation | AEELKEKYKELTEQQ HHHHHHHHHHHHHHH | 15.70 | - | |
| 261 | Phosphorylation | GALPPECTPNIDGPN CCCCCCCCCCCCCCC | 20.08 | - | |
| 277 | Phosphorylation | KSVQREQSLHSFHTL CHHHHHHHHHHHHHH | 24.24 | 30108239 | |
| 280 | Phosphorylation | QREQSLHSFHTLFCR HHHHHHHHHHHHHHH | 24.82 | 30108239 | |
| 292 | Phosphorylation | FCRRCFKYDCFLHPF HHHHHHCCCCCCCCC | 9.55 | 23312004 | |
| 302 | Phosphorylation | FLHPFHATPNTYKRK CCCCCCCCCCCCCCC | 14.43 | 25159151 | |
| 305 | Phosphorylation | PFHATPNTYKRKNTE CCCCCCCCCCCCCCC | 31.46 | 22617229 | |
| 306 | Phosphorylation | FHATPNTYKRKNTET CCCCCCCCCCCCCCC | 18.55 | 23186163 | |
| 311 | Phosphorylation | NTYKRKNTETALDNK CCCCCCCCCCHHCCC | 37.43 | - | |
| 313 | O-linked_Glycosylation | YKRKNTETALDNKPC CCCCCCCCHHCCCCC | 30.40 | 29941599 | |
| 318 | Acetylation | TETALDNKPCGPQCY CCCHHCCCCCCHHHH | 41.15 | 26051181 | |
| 318 | Ubiquitination | TETALDNKPCGPQCY CCCHHCCCCCCHHHH | 41.15 | - | |
| 339 | Phosphorylation | KEFAAALTAERIKTP HHHHHHHHHHHCCCC | 23.03 | 21712546 | |
| 345 | Phosphorylation | LTAERIKTPPKRPGG HHHHHCCCCCCCCCC | 42.31 | 23927012 | |
| 348 | Acetylation | ERIKTPPKRPGGRRR HHCCCCCCCCCCCCC | 72.87 | 80954805 | |
| 350 (in isoform 2) | Phosphorylation | - | 56.57 | 24719451 | |
| 362 | Phosphorylation | RGRLPNNSSRPSTPT CCCCCCCCCCCCCCE | 34.07 | 29255136 | |
| 363 | Phosphorylation | GRLPNNSSRPSTPTI CCCCCCCCCCCCCEE | 50.78 | 29255136 | |
| 366 | Phosphorylation | PNNSSRPSTPTINVL CCCCCCCCCCEEEEE | 46.00 | 29255136 | |
| 367 | Phosphorylation | NNSSRPSTPTINVLE CCCCCCCCCEEEEEE | 27.43 | 19664994 | |
| 367 (in isoform 2) | Phosphorylation | - | 27.43 | 27251275 | |
| 368 (in isoform 2) | Phosphorylation | - | 35.30 | 24719451 | |
| 369 | Phosphorylation | SSRPSTPTINVLESK CCCCCCCEEEEEECC | 25.85 | 30266825 | |
| 371 (in isoform 2) | Phosphorylation | - | 34.50 | 24719451 | |
| 372 (in isoform 2) | Phosphorylation | - | 5.77 | 27251275 | |
| 375 | Phosphorylation | PTINVLESKDTDSDR CEEEEEECCCCCCCC | 31.50 | 23927012 | |
| 378 | Phosphorylation | NVLESKDTDSDREAG EEEECCCCCCCCCCC | 40.93 | 23663014 | |
| 380 | Phosphorylation | LESKDTDSDREAGTE EECCCCCCCCCCCCC | 40.43 | 25159151 | |
| 386 | Phosphorylation | DSDREAGTETGGENN CCCCCCCCCCCCCCC | 37.10 | 30576142 | |
| 388 | Phosphorylation | DREAGTETGGENNDK CCCCCCCCCCCCCCH | 50.77 | 30576142 | |
| 404 | Phosphorylation | EEEKKDETSSSSEAN HHHHHCCCCCHHHHH | 44.00 | 26074081 | |
| 405 | Phosphorylation | EEKKDETSSSSEANS HHHHCCCCCHHHHHH | 26.61 | 30576142 | |
| 406 | Phosphorylation | EKKDETSSSSEANSR HHHCCCCCHHHHHHH | 45.35 | 22496350 | |
| 407 | Phosphorylation | KKDETSSSSEANSRC HHCCCCCHHHHHHHC | 31.78 | 30576142 | |
| 408 | Phosphorylation | KDETSSSSEANSRCQ HCCCCCHHHHHHHCC | 42.55 | 30576142 | |
| 412 | Phosphorylation | SSSSEANSRCQTPIK CCHHHHHHHCCCCCC | 41.29 | 25159151 | |
| 416 | Phosphorylation | EANSRCQTPIKMKPN HHHHHCCCCCCCCCC | 30.52 | 25159151 | |
| 421 (in isoform 2) | Phosphorylation | - | 29.88 | 24719451 | |
| 460 | Phosphorylation | AIARLIGTKTCRQVY HHHHHHCCCCCCEEE | 19.04 | - | |
| 461 | Ubiquitination | IARLIGTKTCRQVYE HHHHHCCCCCCEEEE | 40.18 | - | |
| 472 | Ubiquitination | QVYEFRVKESSIIAP EEEEEEECCCCEEEC | 47.85 | - | |
| 474 | Phosphorylation | YEFRVKESSIIAPAP EEEEECCCCEEECCC | 22.56 | 23927012 | |
| 475 | Phosphorylation | EFRVKESSIIAPAPA EEEECCCCEEECCCH | 21.07 | 23927012 | |
| 477 (in isoform 2) | Ubiquitination | - | 3.97 | - | |
| 487 | Phosphorylation | APAEDVDTPPRKKKR CCHHHCCCCCCCHHH | 34.73 | 19664994 | |
| 492 (in isoform 2) | Phosphorylation | - | 60.12 | 24719451 | |
| 505 | "N6,N6-dimethyllysine" | LWAAHCRKIQLKKDG HHHHHHEEEEEECCC | 39.95 | - | |
| 505 | Methylation | LWAAHCRKIQLKKDG HHHHHHEEEEEECCC | 39.95 | 24129315 | |
| 509 | "N6,N6-dimethyllysine" | HCRKIQLKKDGSSNH HHEEEEEECCCCCCC | 32.23 | - | |
| 509 | Methylation | HCRKIQLKKDGSSNH HHEEEEEECCCCCCC | 32.23 | - | |
| 510 | "N6,N6-dimethyllysine" | CRKIQLKKDGSSNHV HEEEEEECCCCCCCC | 75.75 | - | |
| 510 | Methylation | CRKIQLKKDGSSNHV HEEEEEECCCCCCCC | 75.75 | 24129315 | |
| 514 | Phosphorylation | QLKKDGSSNHVYNYQ EEECCCCCCCCEECC | 36.16 | 28555341 | |
| 569 | Acetylation | CKAQCNTKQCPCYLA EECCCCCCCCCEEEE | 35.59 | 25953088 | |
| 569 | Ubiquitination | CKAQCNTKQCPCYLA EECCCCCCCCCEEEE | 35.59 | - | |
| 574 (in isoform 2) | Ubiquitination | - | 5.26 | - | |
| 597 | Ubiquitination | AADHWDSKNVSCKNC CCCCCCCCCCCCCCC | 59.92 | - | |
| 602 | Ubiquitination | DSKNVSCKNCSIQRG CCCCCCCCCCEEECC | 54.18 | - | |
| 602 (in isoform 2) | Ubiquitination | - | 54.18 | - | |
| 607 (in isoform 2) | Ubiquitination | - | 27.64 | - | |
| 629 | Ubiquitination | AGWGIFIKDPVQKNE CCCEEEECCHHHCCH | 45.27 | - | |
| 634 | Sumoylation | FIKDPVQKNEFISEY EECCHHHCCHHHHHH | 59.69 | 28112733 | |
| 634 | Ubiquitination | FIKDPVQKNEFISEY EECCHHHCCHHHHHH | 59.69 | - | |
| 634 (in isoform 2) | Ubiquitination | - | 59.69 | - | |
| 641 | Phosphorylation | KNEFISEYCGEIISQ CCHHHHHHHHHHHCC | 10.04 | - | |
| 647 | Phosphorylation | EYCGEIISQDEADRR HHHHHHHCCHHHHHC | 36.92 | - | |
| 652 (in isoform 2) | Phosphorylation | - | 38.47 | - | |
| 684 | Ubiquitination | ATRKGNKIRFANHSV CCCCCCEEEECCCCC | 5.20 | 21890473 | |
| 690 | Phosphorylation | KIRFANHSVNPNCYA EEEECCCCCCCCCEE | 24.32 | 18452278 | |
| 696 | Ubiquitination | HSVNPNCYAKVMMVN CCCCCCCEEEEEEEC | 18.98 | 21890473 | |
| 696 | Ubiquitination | HSVNPNCYAKVMMVN CCCCCCCEEEEEEEC | 18.98 | 21890473 | |
| 696 | Phosphorylation | HSVNPNCYAKVMMVN CCCCCCCEEEEEEEC | 18.98 | - | |
| 698 | Acetylation | VNPNCYAKVMMVNGD CCCCCEEEEEEECCC | 12.28 | 26051181 | |
| 713 | Acetylation | HRIGIFAKRAIQTGE CEEEEEEHHHHHCCC | 31.45 | 25953088 | |
| 713 | Ubiquitination | HRIGIFAKRAIQTGE CEEEEEEHHHHHCCC | 31.45 | - | |
| 718 | Phosphorylation | FAKRAIQTGEELFFD EEHHHHHCCCHHHEE | 40.21 | 24719451 | |
| 723 (in isoform 2) | Phosphorylation | - | 5.04 | 24719451 | |
| 726 | Ubiquitination | GEELFFDYRYSQADA CCHHHEEECCCHHHH | 13.29 | 21890473 | |
| 728 | Phosphorylation | ELFFDYRYSQADALK HHHEEECCCHHHHHH | 10.02 | 20068231 | |
| 729 | O-linked_Glycosylation | LFFDYRYSQADALKY HHEEECCCHHHHHHH | 15.19 | 29941599 | |
| 729 | Phosphorylation | LFFDYRYSQADALKY HHEEECCCHHHHHHH | 15.19 | 20068231 | |
| 734 (in isoform 2) | Phosphorylation | - | 4.18 | - | |
| 735 | Methylation | YSQADALKYVGIERE CCHHHHHHHHCCCCC | 39.34 | 24129315 | |
| 735 | Ubiquitination | YSQADALKYVGIERE CCHHHHHHHHCCCCC | 39.34 | 21890473 | |
| 740 | Ubiquitination | ALKYVGIEREMEIP- HHHHHCCCCCCCCC- | 36.34 | 21890473 | |
| 740 (in isoform 2) | Ubiquitination | - | 36.34 | - | |
| 740 | Ubiquitination | ALKYVGIEREMEIP- HHHHHCCCCCCCCC- | 36.34 | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 21 | S | Phosphorylation | Kinase | AKT1 | P31749 | Uniprot |
| 220 | S | Phosphorylation | Kinase | MELK | Q14680 | PSP |
| 244 | Y | Phosphorylation | Kinase | JAK3 | P52333 | PSP |
| 311 | T | Phosphorylation | Kinase | PRKAA1 | Q13131 | GPS |
| 345 | T | Phosphorylation | Kinase | CDK1 | P06493 | Uniprot |
| 345 | T | Phosphorylation | Kinase | CDK2 | P24941 | Uniprot |
| 345 | T | Phosphorylation | Kinase | PRKCI | P41743 | GPS |
| 363 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
| 367 | T | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
| 367 | T | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
| 416 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 487 | T | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 487 | T | Phosphorylation | Kinase | PRKCI | P41743 | GPS |
| 641 | Y | Phosphorylation | Kinase | JAK2 | O60674 | PSP |
| 690 | S | Phosphorylation | Kinase | PRKCI | P41743 | GPS |
| 734 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
| - | K | Ubiquitination | E3 ubiquitin ligase | PJA1 | Q8NG27 | PMID:21513699 |
* 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 EZH2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 277590 | Weaver syndrome (WVS) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND THR-487, ANDMASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-339; SER-366; THR-367AND THR-487, AND MASS SPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND MASSSPECTROMETRY. | |
| "Cyclin-dependent kinases regulate epigenetic gene silencing throughphosphorylation of EZH2."; Chen S., Bohrer L.R., Rai A.N., Pan Y., Gan L., Zhou X., Bagchi A.,Simon J.A., Huang H.; Nat. Cell Biol. 12:1108-1114(2010). Cited for: FUNCTION, PHOSPHORYLATION AT THR-345 BY CDK1 AND CDK2, AND MUTAGENESISOF THR-345. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
| "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-487, AND MASSSPECTROMETRY. | |
