| UniProt ID | QORX_HUMAN | |
|---|---|---|
| UniProt AC | Q53FA7 | |
| Protein Name | Quinone oxidoreductase PIG3 | |
| Gene Name | TP53I3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 332 | |
| Subcellular Localization | ||
| Protein Description | May be involved in the generation of reactive oxygen species (ROS). Has low NADPH-dependent beta-naphthoquinone reductase activity, with a preference for 1,2-beta-naphthoquinone over 1,4-beta-naphthoquinone. Has low NADPH-dependent diamine reductase activity (in vitro).. | |
| Protein Sequence | MLAVHFDKPGGPENLYVKEVAKPSPGEGEVLLKVAASALNRADLMQRQGQYDPPPGASNILGLEASGHVAELGPGCQGHWKIGDTAMALLPGGGQAQYVTVPEGLLMPIPEGLTLTQAAAIPEAWLTAFQLLHLVGNVQAGDYVLIHAGLSGVGTAAIQLTRMAGAIPLVTAGSQKKLQMAEKLGAAAGFNYKKEDFSEATLKFTKGAGVNLILDCIGGSYWEKNVNCLALDGRWVLYGLMGGGDINGPLFSKLLFKRGSLITSLLRSRDNKYKQMLVNAFTEQILPHFSTEGPQRLLPVLDRIYPVTEIQEAHKYMEANKNIGKIVLELPQ | |
| 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 |
|---|---|---|---|---|---|
| 24 | Phosphorylation | VKEVAKPSPGEGEVL EEEEECCCCCCCHHH | 44.84 | 28857561 | |
| 85 | Phosphorylation | GHWKIGDTAMALLPG CCCEECCEEEEECCC | 17.08 | - | |
| 100 | Phosphorylation | GGQAQYVTVPEGLLM CCCCEEEECCCCCEE | 25.96 | - | |
| 171 | Phosphorylation | AGAIPLVTAGSQKKL HCCCCEEECCCHHHH | 32.74 | 21406692 | |
| 174 | Phosphorylation | IPLVTAGSQKKLQMA CCEEECCCHHHHHHH | 36.04 | 21406692 | |
| 176 | 2-Hydroxyisobutyrylation | LVTAGSQKKLQMAEK EEECCCHHHHHHHHH | 58.09 | - | |
| 176 | Malonylation | LVTAGSQKKLQMAEK EEECCCHHHHHHHHH | 58.09 | 26320211 | |
| 180 | Sulfoxidation | GSQKKLQMAEKLGAA CCHHHHHHHHHHCCC | 8.24 | 30846556 | |
| 193 | 2-Hydroxyisobutyrylation | AAAGFNYKKEDFSEA CCCCCCCCCCCCCHH | 51.28 | - | |
| 194 | Ubiquitination | AAGFNYKKEDFSEAT CCCCCCCCCCCCHHH | 52.75 | - | |
| 194 | Malonylation | AAGFNYKKEDFSEAT CCCCCCCCCCCCHHH | 52.75 | 26320211 | |
| 203 | Ubiquitination | DFSEATLKFTKGAGV CCCHHHHHHCCCCCC | 46.78 | - | |
| 252 | Phosphorylation | DINGPLFSKLLFKRG CCCCHHHHHHHHHHC | 30.03 | 24719451 | |
| 260 | Phosphorylation | KLLFKRGSLITSLLR HHHHHHCHHHHHHHH | 22.19 | 23927012 | |
| 263 | Phosphorylation | FKRGSLITSLLRSRD HHHCHHHHHHHHCCC | 20.72 | 23927012 | |
| 264 | Phosphorylation | KRGSLITSLLRSRDN HHCHHHHHHHHCCCH | 20.57 | 23927012 | |
| 321 | Acetylation | HKYMEANKNIGKIVL HHHHHHCCCCCCHHC | 57.92 | 19608861 | |
| 321 | Malonylation | HKYMEANKNIGKIVL HHHHHHCCCCCCHHC | 57.92 | 26320211 |
| 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 QORX_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of QORX_HUMAN !! | ||||||
* 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 QORX_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| FUND2_HUMAN | FUNDC2 | physical | 16169070 | |
| EF1G_HUMAN | EEF1G | physical | 16169070 | |
| UBR1_HUMAN | UBR1 | physical | 16169070 | |
| U119A_HUMAN | UNC119 | physical | 16169070 | |
| H2AX_HUMAN | H2AFX | physical | 20023697 | |
| TP53B_HUMAN | TP53BP1 | physical | 20023697 | |
| HEM3_HUMAN | HMBS | physical | 26344197 | |
| GPX3_HUMAN | GPX3 | physical | 22461624 |
| 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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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND MASS SPECTROMETRY. | |