| UniProt ID | DDI2_MOUSE | |
|---|---|---|
| UniProt AC | A2ADY9 | |
| Protein Name | Protein DDI1 homolog 2 {ECO:0000305} | |
| Gene Name | Ddi2 {ECO:0000312|MGI:MGI:1917244} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 399 | |
| Subcellular Localization | Cytoplasm, cytosol . | |
| Protein Description | Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane. Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1.. | |
| Protein Sequence | MLLTVYCVRRDLSEVTFSLQVDADFELHNFRALCELESGIPAAESQIVYAERPLTDNHRSLASYGLKDGDVVILRQKENADPRPAVQFSNLPRIDFSSIAVPGTSNPQQRQLPRTQAQHSSPGEMASSPQGLDNPALLRDMLLANPHELSLLKERNPPLAEALLSGDLEKFSRVLVEQQQDRARREQERIRLFSADPFDLEAQAKIEEDIRQQNIEENMTIAMEEAPESFGQVAMLYINCRVNGHPVKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGIAKGVGTQKIIGRVHLAQVQIEGDFLACSFSILEEQPMDMLLGLDMLKRHQCSIDLKKNVLVIGTTGSQTTFLPEGELPECARLAYGTGREDIRPEEIADQELAEAIQKSAEDAERQKP | |
| 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 |
|---|---|---|---|---|---|
| 67 | Ubiquitination | SLASYGLKDGDVVIL HHHHCCCCCCCEEEE | 56.13 | 22790023 | |
| 77 | Ubiquitination | DVVILRQKENADPRP CEEEEECCCCCCCCC | 46.64 | 22790023 | |
| 104 | Phosphorylation | SSIAVPGTSNPQQRQ CCEECCCCCCHHHCC | 21.18 | - | |
| 115 | Phosphorylation | QQRQLPRTQAQHSSP HHCCCCCCCCCCCCC | 26.73 | 24925903 | |
| 120 | Phosphorylation | PRTQAQHSSPGEMAS CCCCCCCCCCCCCCC | 26.58 | 25521595 | |
| 121 | Phosphorylation | RTQAQHSSPGEMASS CCCCCCCCCCCCCCC | 34.50 | 25521595 | |
| 125 | Oxidation | QHSSPGEMASSPQGL CCCCCCCCCCCCCCC | 5.63 | 17242355 | |
| 127 | Phosphorylation | SSPGEMASSPQGLDN CCCCCCCCCCCCCCC | 41.04 | 25521595 | |
| 128 | Phosphorylation | SPGEMASSPQGLDNP CCCCCCCCCCCCCCH | 16.23 | 24925903 | |
| 150 | Phosphorylation | LANPHELSLLKERNP HCCHHHHHHHHHHCC | 28.77 | 23984901 | |
| 153 | Ubiquitination | PHELSLLKERNPPLA HHHHHHHHHHCCHHH | 60.98 | 22790023 | |
| 170 | Ubiquitination | LLSGDLEKFSRVLVE HHHCCHHHHHHHHHH | 56.81 | 22790023 | |
| 194 | Phosphorylation | QERIRLFSADPFDLE HHHHHHEECCCCCHH | 36.03 | 26824392 | |
| 205 | Ubiquitination | FDLEAQAKIEEDIRQ CCHHHHHHHHHHHHH | 38.27 | 22790023 | |
| 283 | Ubiquitination | RRWAGIAKGVGTQKI HHHHCCCCCCCHHHE | 52.81 | 22790023 | |
| 289 | Ubiquitination | AKGVGTQKIIGRVHL CCCCCHHHEECEEEE | 35.81 | 22790023 | |
| 338 | Ubiquitination | QCSIDLKKNVLVIGT CCCCCCCCCEEEEEC | 60.63 | 22790023 | |
| 389 | Ubiquitination | ELAEAIQKSAEDAER HHHHHHHHHHHHHHH | 45.58 | 22790023 | |
| 390 | Phosphorylation | LAEAIQKSAEDAERQ HHHHHHHHHHHHHHH | 22.10 | 30635358 |
| 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 DDI2_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DDI2_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 DDI2_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DDI2_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-121 ANDSER-128, AND MASS SPECTROMETRY. | |