| UniProt ID | SET_MOUSE | |
|---|---|---|
| UniProt AC | Q9EQU5 | |
| Protein Name | Protein SET | |
| Gene Name | Set | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 289 | |
| Subcellular Localization | Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus, nucleoplasm. In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavag | |
| Protein Description | Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher (By similarity).. | |
| Protein Sequence | MAPKRQSAILPQPKKPRPAAAPKLEDKSASPGLPKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEAEDDDDDDEEEEGLEDIDEEGDEDEGEEDDDEDEGEEGEEDEGEDD | |
| 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 | Methylation | ------MAPKRQSAI ------CCCCCCCCC | 20.51 | 20668449 | |
| 7 | Phosphorylation | -MAPKRQSAILPQPK -CCCCCCCCCCCCCC | 22.70 | 14729942 | |
| 9 (in isoform 2) | Phosphorylation | - | 7.55 | - | |
| 11 (in isoform 2) | Acetylation | - | 42.17 | - | |
| 15 (in isoform 2) | Phosphorylation | - | 53.60 | 22324799 | |
| 23 | Malonylation | PRPAAAPKLEDKSAS CCCCCCCCCCCCCCC | 60.84 | 26320211 | |
| 23 | Acetylation | PRPAAAPKLEDKSAS CCCCCCCCCCCCCCC | 60.84 | 23806337 | |
| 23 (in isoform 2) | Phosphorylation | - | 60.84 | 22802335 | |
| 24 (in isoform 2) | Phosphorylation | - | 11.36 | 26824392 | |
| 27 | Acetylation | AAPKLEDKSASPGLP CCCCCCCCCCCCCCC | 38.25 | 23806337 | |
| 27 | Succinylation | AAPKLEDKSASPGLP CCCCCCCCCCCCCCC | 38.25 | 23806337 | |
| 27 | Ubiquitination | AAPKLEDKSASPGLP CCCCCCCCCCCCCCC | 38.25 | - | |
| 28 | Phosphorylation | APKLEDKSASPGLPK CCCCCCCCCCCCCCC | 46.42 | 27087446 | |
| 30 | Phosphorylation | KLEDKSASPGLPKGE CCCCCCCCCCCCCCH | 26.96 | 27087446 | |
| 38 | Acetylation | PGLPKGEKEQQEAIE CCCCCCHHHHHHHHH | 70.28 | 23806337 | |
| 38 | Ubiquitination | PGLPKGEKEQQEAIE CCCCCCHHHHHHHHH | 70.28 | - | |
| 62 | Phosphorylation | DRLNEQASEEILKVE HHHHHHHHHHHHHHH | 35.14 | 27087446 | |
| 67 | Acetylation | QASEEILKVEQKYNK HHHHHHHHHHHHHHH | 49.76 | 23806337 | |
| 70 (in isoform 2) | Ubiquitination | - | 57.42 | - | |
| 82 (in isoform 2) | Ubiquitination | - | 53.38 | 22790023 | |
| 82 | Ubiquitination | LRQPFFQKRSELIAK HHCCHHHHHHHHHHH | 53.38 | 22790023 | |
| 89 | Ubiquitination | KRSELIAKIPNFWVT HHHHHHHHCCCEEEE | 52.26 | - | |
| 119 (in isoform 2) | Ubiquitination | - | 1.39 | - | |
| 131 | Ubiquitination | VTEFEDIKSGYRIDF EEEEECCCCCEEEEE | 50.58 | 22790023 | |
| 131 | Acetylation | VTEFEDIKSGYRIDF EEEEECCCCCEEEEE | 50.58 | 23236377 | |
| 131 (in isoform 2) | Ubiquitination | - | 50.58 | 22790023 | |
| 132 | Phosphorylation | TEFEDIKSGYRIDFY EEEECCCCCEEEEEE | 41.20 | 21183079 | |
| 134 | Phosphorylation | FEDIKSGYRIDFYFD EECCCCCEEEEEEEC | 16.10 | 21082442 | |
| 137 (in isoform 2) | Ubiquitination | - | 24.16 | - | |
| 141 (in isoform 2) | Ubiquitination | - | 43.30 | - | |
| 145 | Phosphorylation | FYFDENPYFENKVLS EEECCCCCHHCCEEC | 34.80 | 22817900 | |
| 149 (in isoform 2) | Ubiquitination | - | 37.04 | 22790023 | |
| 149 | Ubiquitination | ENPYFENKVLSKEFH CCCCHHCCEECEEEE | 37.04 | 22790023 | |
| 149 | Acetylation | ENPYFENKVLSKEFH CCCCHHCCEECEEEE | 37.04 | 23954790 | |
| 153 (in isoform 2) | Ubiquitination | - | 61.30 | 22790023 | |
| 153 | Ubiquitination | FENKVLSKEFHLNES HHCCEECEEEECCCC | 61.30 | 22790023 | |
| 154 (in isoform 2) | Ubiquitination | - | 34.62 | - | |
| 159 (in isoform 2) | Ubiquitination | - | 63.56 | - | |
| 160 | Phosphorylation | KEFHLNESGDPSSKS EEEECCCCCCCCCCC | 47.63 | 25266776 | |
| 164 | Phosphorylation | LNESGDPSSKSTEIK CCCCCCCCCCCCEEE | 55.95 | 22345495 | |
| 165 | Phosphorylation | NESGDPSSKSTEIKW CCCCCCCCCCCEEEE | 35.69 | 25338131 | |
| 166 | Ubiquitination | ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC | 66.78 | 22790023 | |
| 166 (in isoform 2) | Ubiquitination | - | 66.78 | 22790023 | |
| 167 | Phosphorylation | SGDPSSKSTEIKWKS CCCCCCCCCEEEECC | 32.97 | 25338131 | |
| 171 | Malonylation | SSKSTEIKWKSGKDL CCCCCEEEECCCCCH | 42.19 | 26320211 | |
| 171 | Ubiquitination | SSKSTEIKWKSGKDL CCCCCEEEECCCCCH | 42.19 | - | |
| 171 | Acetylation | SSKSTEIKWKSGKDL CCCCCEEEECCCCCH | 42.19 | - | |
| 171 (in isoform 2) | Ubiquitination | - | 42.19 | 22790023 | |
| 176 | Acetylation | EIKWKSGKDLTKRSS EEEECCCCCHHHHHH | 57.57 | 23201123 | |
| 180 | Acetylation | KSGKDLTKRSSQTQN CCCCCHHHHHHHHHC | 58.54 | 23201123 | |
| 182 | Phosphorylation | GKDLTKRSSQTQNKA CCCHHHHHHHHHCHH | 28.49 | 29514104 | |
| 183 | Phosphorylation | KDLTKRSSQTQNKAS CCHHHHHHHHHCHHH | 41.08 | 27087446 |
| 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 SET_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SET_MOUSE !! | ||||||
* 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 SET_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Methylation | |
| Reference | PubMed |
| "NRMT is an alpha-N-methyltransferase that methylates RCC1 andretinoblastoma protein."; Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.; Nature 466:1125-1128(2010). Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT ALA-2, ANDMUTAGENESIS OF LYS-4. | |
| Phosphorylation | |
| Reference | PubMed |
| "Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY. | |
| "Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASSSPECTROMETRY. | |
