| UniProt ID | EED_HUMAN | |
|---|---|---|
| UniProt AC | O75530 | |
| Protein Name | Polycomb protein EED {ECO:0000305} | |
| Gene Name | EED {ECO:0000312|HGNC:HGNC:3188} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 441 | |
| Subcellular Localization | Nucleus. Chromosome. Transiently colocalizes with XIST at inactive X chromosomes. | |
| Protein Description | Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. 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 and CDKN2A.. | |
| Protein Sequence | MSEREVSTAPAGTDMPAAKKQKLSSDENSNPDLSGDENDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVSKDHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSEREVSTA ------CCCCCCCCC | 45.41 | 22199227 | |
| 2 | Acetylation | ------MSEREVSTA ------CCCCCCCCC | 45.41 | 19413330 | |
| 7 | Phosphorylation | -MSEREVSTAPAGTD -CCCCCCCCCCCCCC | 17.69 | 22199227 | |
| 8 | Phosphorylation | MSEREVSTAPAGTDM CCCCCCCCCCCCCCC | 41.66 | 23186163 | |
| 15 | Sulfoxidation | TAPAGTDMPAAKKQK CCCCCCCCCHHHHHC | 2.15 | 21406390 | |
| 19 (in isoform 3) | Ubiquitination | - | 58.82 | 21890473 | |
| 19 (in isoform 2) | Ubiquitination | - | 58.82 | 21890473 | |
| 19 | Acetylation | GTDMPAAKKQKLSSD CCCCCHHHHHCCCCC | 58.82 | 25953088 | |
| 19 (in isoform 1) | Ubiquitination | - | 58.82 | 21890473 | |
| 19 | Ubiquitination | GTDMPAAKKQKLSSD CCCCCHHHHHCCCCC | 58.82 | - | |
| 24 | Phosphorylation | AAKKQKLSSDENSNP HHHHHCCCCCCCCCC | 42.66 | 25022875 | |
| 25 | Phosphorylation | AKKQKLSSDENSNPD HHHHCCCCCCCCCCC | 60.42 | 30278072 | |
| 29 | Phosphorylation | KLSSDENSNPDLSGD CCCCCCCCCCCCCCC | 47.92 | 23898821 | |
| 34 | Phosphorylation | ENSNPDLSGDENDDA CCCCCCCCCCCCCCC | 52.13 | 30278072 | |
| 43 | Phosphorylation | DENDDAVSIESGTNT CCCCCCEEECCCCCC | 23.51 | 30278072 | |
| 46 | Phosphorylation | DDAVSIESGTNTERP CCCEEECCCCCCCCC | 49.61 | 25022875 | |
| 48 | Phosphorylation | AVSIESGTNTERPDT CEEECCCCCCCCCCC | 48.52 | 30576142 | |
| 50 | Phosphorylation | SIESGTNTERPDTPT EECCCCCCCCCCCCC | 32.96 | 30278072 | |
| 55 | Phosphorylation | TNTERPDTPTNTPNA CCCCCCCCCCCCCCC | 34.39 | 30278072 | |
| 57 | Phosphorylation | TERPDTPTNTPNAPG CCCCCCCCCCCCCCC | 54.54 | 30278072 | |
| 59 | Phosphorylation | RPDTPTNTPNAPGRK CCCCCCCCCCCCCCC | 22.01 | 30576142 | |
| 66 | "N6,N6,N6-trimethyllysine" | TPNAPGRKSWGKGKW CCCCCCCCCCCCCCC | 57.38 | - | |
| 66 | Methylation | TPNAPGRKSWGKGKW CCCCCCCCCCCCCCC | 57.38 | 20974918 | |
| 81 | Phosphorylation | KSKKCKYSFKCVNSL CCCCCCCEEEEHHHC | 12.06 | 29496963 | |
| 83 | Ubiquitination | KKCKYSFKCVNSLKE CCCCCEEEEHHHCCC | 31.19 | - | |
| 83 | Acetylation | KKCKYSFKCVNSLKE CCCCCEEEEHHHCCC | 31.19 | 25953088 | |
| 115 | Phosphorylation | GDPLVFATVGSNRVT CCCEEEEEECCCEEE | 17.59 | 20068231 | |
| 118 | Phosphorylation | LVFATVGSNRVTLYE EEEEEECCCEEEEEE | 19.68 | 21406692 | |
| 197 | Ubiquitination | GNAINELKFHPRDPN CHHHCEECCCCCCCC | 35.13 | 20974918 | |
| 197 (in isoform 2) | Ubiquitination | - | 35.13 | - | |
| 197 | "N6,N6,N6-trimethyllysine" | GNAINELKFHPRDPN CHHHCEECCCCCCCC | 35.13 | - | |
| 197 | Methylation | GNAINELKFHPRDPN CHHHCEECCCCCCCC | 35.13 | 20974918 | |
| 208 | Phosphorylation | RDPNLLLSVSKDHAL CCCCEEEEEEHHHHH | 25.06 | 24719451 | |
| 211 | Acetylation | NLLLSVSKDHALRLW CEEEEEEHHHHHHHH | 51.91 | 26051181 | |
| 211 (in isoform 2) | Ubiquitination | - | 51.91 | - | |
| 211 | Ubiquitination | NLLLSVSKDHALRLW CEEEEEEHHHHHHHH | 51.91 | - | |
| 224 | Phosphorylation | LWNIQTDTLVAIFGG HHCCCCCCEEEEECC | 26.90 | 24275569 | |
| 253 | Phosphorylation | LLGEKIMSCGMDHSL HHHHHHHHCCCCHHH | 15.82 | 22210691 | |
| 259 | Phosphorylation | MSCGMDHSLKLWRIN HHCCCCHHHHHHHCC | 23.96 | 22210691 | |
| 267 | Phosphorylation | LKLWRINSKRMMNAI HHHHHCCHHHHHHHH | 21.19 | 24260401 | |
| 268 | Methylation | KLWRINSKRMMNAIK HHHHCCHHHHHHHHH | 39.56 | 20974918 | |
| 268 | "N6,N6,N6-trimethyllysine" | KLWRINSKRMMNAIK HHHHCCHHHHHHHHH | 39.56 | - | |
| 275 | Ubiquitination | KRMMNAIKESYDYNP HHHHHHHHHHHCCCC | 37.89 | - | |
| 275 (in isoform 2) | Ubiquitination | - | 37.89 | 21890473 | |
| 275 (in isoform 3) | Ubiquitination | - | 37.89 | 21890473 | |
| 275 (in isoform 1) | Ubiquitination | - | 37.89 | 21890473 | |
| 277 | Phosphorylation | MMNAIKESYDYNPNK HHHHHHHHHCCCCCC | 20.50 | - | |
| 278 | Phosphorylation | MNAIKESYDYNPNKT HHHHHHHHCCCCCCC | 24.44 | - | |
| 280 | Phosphorylation | AIKESYDYNPNKTNR HHHHHHCCCCCCCCC | 25.04 | - | |
| 284 (in isoform 2) | Ubiquitination | - | 48.73 | 21890473 | |
| 284 (in isoform 1) | Ubiquitination | - | 48.73 | 21890473 | |
| 284 | "N6,N6,N6-trimethyllysine" | SYDYNPNKTNRPFIS HHCCCCCCCCCCCCC | 48.73 | - | |
| 284 (in isoform 3) | Ubiquitination | - | 48.73 | 21890473 | |
| 284 | Ubiquitination | SYDYNPNKTNRPFIS HHCCCCCCCCCCCCC | 48.73 | 20974918 | |
| 284 | Methylation | SYDYNPNKTNRPFIS HHCCCCCCCCCCCCC | 48.73 | 20974918 | |
| 293 | Acetylation | NRPFISQKIHFPDFS CCCCCCCEECCCCCC | 31.21 | 26051181 | |
| 332 | Acetylation | ENAIVCWKPGKMEDD CCEEEEECCCCCHHC | 38.47 | 26051181 | |
| 340 (in isoform 2) | Phosphorylation | - | 10.07 | 20860994 | |
| 344 (in isoform 3) | Ubiquitination | - | 48.51 | 21890473 | |
| 344 (in isoform 1) | Ubiquitination | - | 48.51 | 21890473 | |
| 344 | Ubiquitination | EDDIDKIKPSESNVT HHCHHHCCCCCCCEE | 48.51 | - | |
| 348 (in isoform 2) | Phosphorylation | - | 40.72 | 25850435 | |
| 369 (in isoform 2) | Ubiquitination | - | 13.69 | 21890473 | |
| 398 | Ubiquitination | LEVEDPHKAKCTTLT CCCCCCCCCCCEECC | 55.73 | - | |
| 398 | Acetylation | LEVEDPHKAKCTTLT CCCCCCCCCCCEECC | 55.73 | 25953088 | |
| 408 | Ubiquitination | CTTLTHHKCGAAIRQ CEECCCCCCCHHHHC | 27.10 | - | |
| 433 (in isoform 2) | Ubiquitination | - | 29.67 | - | |
| 433 | Phosphorylation | IAVCDDASIWRWDRL EEEECCCCCCCCHHC | 29.67 | 24719451 |
| 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 EED_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 26 | K | Methylation |
| 20974918 |
* 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 EED_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| 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 |
| "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 SER-34; THR-55 AND THR-57,AND MASS SPECTROMETRY. | |