QORX_HUMAN - dbPTM
QORX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
24PhosphorylationVKEVAKPSPGEGEVL
EEEEECCCCCCCHHH
44.8428857561
85PhosphorylationGHWKIGDTAMALLPG
CCCEECCEEEEECCC
17.08-
100PhosphorylationGGQAQYVTVPEGLLM
CCCCEEEECCCCCEE
25.96-
171PhosphorylationAGAIPLVTAGSQKKL
HCCCCEEECCCHHHH
32.7421406692
174PhosphorylationIPLVTAGSQKKLQMA
CCEEECCCHHHHHHH
36.0421406692
1762-HydroxyisobutyrylationLVTAGSQKKLQMAEK
EEECCCHHHHHHHHH
58.09-
176MalonylationLVTAGSQKKLQMAEK
EEECCCHHHHHHHHH
58.0926320211
180SulfoxidationGSQKKLQMAEKLGAA
CCHHHHHHHHHHCCC
8.2430846556
1932-HydroxyisobutyrylationAAAGFNYKKEDFSEA
CCCCCCCCCCCCCHH
51.28-
194UbiquitinationAAGFNYKKEDFSEAT
CCCCCCCCCCCCHHH
52.75-
194MalonylationAAGFNYKKEDFSEAT
CCCCCCCCCCCCHHH
52.7526320211
203UbiquitinationDFSEATLKFTKGAGV
CCCHHHHHHCCCCCC
46.78-
252PhosphorylationDINGPLFSKLLFKRG
CCCCHHHHHHHHHHC
30.0324719451
260PhosphorylationKLLFKRGSLITSLLR
HHHHHHCHHHHHHHH
22.1923927012
263PhosphorylationFKRGSLITSLLRSRD
HHHCHHHHHHHHCCC
20.7223927012
264PhosphorylationKRGSLITSLLRSRDN
HHCHHHHHHHHCCCH
20.5723927012
321AcetylationHKYMEANKNIGKIVL
HHHHHHCCCCCCHHC
57.9219608861
321MalonylationHKYMEANKNIGKIVL
HHHHHHCCCCCCHHC
57.9226320211

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of QORX_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FUND2_HUMANFUNDC2physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
UBR1_HUMANUBR1physical
16169070
U119A_HUMANUNC119physical
16169070
H2AX_HUMANH2AFXphysical
20023697
TP53B_HUMANTP53BP1physical
20023697
HEM3_HUMANHMBSphysical
26344197
GPX3_HUMANGPX3physical
22461624

Drug and Disease Associations
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.
Regulatory Network of QORX_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.

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