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 | ||
|
* 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. |