Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Quinone oxidoreductase PIG3

Gene

TP53I3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Kineticsi

  1. KM=215 µM for 1,2-naphthoquinone1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei41NADP1 Publication1
    Binding sitei192NADP1 Publication1
    Binding sitei322NADP1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi148 – 154NADP1 Publication7
    Nucleotide bindingi173 – 177NADP1 Publication5
    Nucleotide bindingi264 – 266NADP1 Publication3

    GO - Molecular functioni

    • NADPH:quinone reductase activity Source: UniProtKB
    • NADPH binding Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • quinone binding Source: UniProtKB
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • NADP metabolic process Source: UniProtKB
    • regulation of apoptotic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciZFISH:HS03836-MONOMER.
    ReactomeiR-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Quinone oxidoreductase PIG3 (EC:1.-.-.-)
    Alternative name(s):
    Tumor protein p53-inducible protein 3
    p53-induced gene 3 protein
    Gene namesi
    Name:TP53I3
    Synonyms:PIG3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:19373. TP53I3.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi51Y → A: Loss of enzyme activity. 1 Publication1
    Mutagenesisi51Y → F: Increased enzyme activity. 1 Publication1
    Mutagenesisi151S → V: Loss of enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNETi9540.
    OpenTargetsiENSG00000115129.
    PharmGKBiPA134923704.

    Polymorphism and mutation databases

    BioMutaiTP53I3.
    DMDMi76789665.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001609171 – 332Quinone oxidoreductase PIG3Add BLAST332

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionine1 Publication1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    EPDiQ53FA7.
    MaxQBiQ53FA7.
    PaxDbiQ53FA7.
    PeptideAtlasiQ53FA7.
    PRIDEiQ53FA7.

    PTM databases

    iPTMnetiQ53FA7.
    PhosphoSitePlusiQ53FA7.

    Expressioni

    Inductioni

    Isoform 1 and isoform 2 are both activated by p53/TP53, doxorubicin, etoposide and ionizing radiation. Isoform 2 is highly activated by UV radiation.1 Publication

    Gene expression databases

    BgeeiENSG00000115129.
    CleanExiHS_TP53I3.
    ExpressionAtlasiQ53FA7. baseline and differential.
    GenevisibleiQ53FA7. HS.

    Organism-specific databases

    HPAiCAB017479.
    HPA022012.
    HPA028742.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi114915. 9 interactors.
    IntActiQ53FA7. 4 interactors.
    STRINGi9606.ENSP00000238721.

    Structurei

    Secondary structure

    1332
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi1 – 8Combined sources8
    Helixi12 – 14Combined sources3
    Beta strandi15 – 21Combined sources7
    Beta strandi29 – 38Combined sources10
    Helixi41 – 47Combined sources7
    Beta strandi59 – 61Combined sources3
    Beta strandi63 – 72Combined sources10
    Beta strandi78 – 80Combined sources3
    Beta strandi85 – 89Combined sources5
    Beta strandi95 – 102Combined sources8
    Helixi103 – 105Combined sources3
    Beta strandi106 – 108Combined sources3
    Helixi115 – 118Combined sources4
    Helixi122 – 132Combined sources11
    Turni133 – 135Combined sources3
    Beta strandi143 – 148Combined sources6
    Helixi152 – 163Combined sources12
    Beta strandi167 – 173Combined sources7
    Helixi175 – 184Combined sources10
    Beta strandi187 – 191Combined sources5
    Turni192 – 194Combined sources3
    Helixi197 – 204Combined sources8
    Turni205 – 207Combined sources3
    Beta strandi210 – 217Combined sources8
    Helixi219 – 221Combined sources3
    Helixi222 – 228Combined sources7
    Beta strandi229 – 237Combined sources9
    Beta strandi246 – 248Combined sources3
    Helixi250 – 256Combined sources7
    Beta strandi260 – 263Combined sources4
    Helixi271 – 284Combined sources14
    Helixi286 – 289Combined sources4
    Beta strandi301 – 306Combined sources6
    Helixi307 – 309Combined sources3
    Helixi310 – 318Combined sources9
    Beta strandi323 – 329Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J8ZX-ray2.50A1-332[»]
    2OBYX-ray3.00A/B/C/D/E1-332[»]
    ProteinModelPortaliQ53FA7.
    SMRiQ53FA7.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53FA7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1198. Eukaryota.
    COG0604. LUCA.
    GeneTreeiENSGT00550000074483.
    HOGENOMiHOG000294672.
    HOVERGENiHBG097584.
    InParanoidiQ53FA7.
    KOiK10133.
    OMAiGQYDPPP.
    OrthoDBiEOG091G0JZF.
    PhylomeDBiQ53FA7.
    TreeFamiTF300079.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    IPR014189. Quinone_OxRdtase_PIG3.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02824. quinone_pig3. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Note: UV radiation favors the production of isoform 2.
    Isoform 1 (identifier: Q53FA7-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MLAVHFDKPG GPENLYVKEV AKPSPGEGEV LLKVAASALN RADLMQRQGQ
    60 70 80 90 100
    YDPPPGASNI LGLEASGHVA ELGPGCQGHW KIGDTAMALL PGGGQAQYVT
    110 120 130 140 150
    VPEGLLMPIP EGLTLTQAAA IPEAWLTAFQ LLHLVGNVQA GDYVLIHAGL
    160 170 180 190 200
    SGVGTAAIQL TRMAGAIPLV TAGSQKKLQM AEKLGAAAGF NYKKEDFSEA
    210 220 230 240 250
    TLKFTKGAGV NLILDCIGGS YWEKNVNCLA LDGRWVLYGL MGGGDINGPL
    260 270 280 290 300
    FSKLLFKRGS LITSLLRSRD NKYKQMLVNA FTEQILPHFS TEGPQRLLPV
    310 320 330
    LDRIYPVTEI QEAHKYMEAN KNIGKIVLEL PQ
    Note: Major isoform under normal light conditions.
    Length:332
    Mass (Da):35,536
    Last modified:September 27, 2005 - v2
    Checksum:iC5A33C46B3F96473
    GO
    Isoform 2 (identifier: Q53FA7-2) [UniParc]FASTAAdd to basket
    Also known as: PIG3AS

    The sequence of this isoform differs from the canonical sequence as follows:
         207-248: GAGVNLILDC...GLMGGGDING → VQANAGECFH...LPSDRNPGGP
         249-332: Missing.

    Note: Major isoform under UV light exposure. Undergoes rapid proteolytic degradation by the proteasome.
    Show »
    Length:248
    Mass (Da):25,402
    Checksum:i8899613C763DDDDC
    GO

    Sequence cautioni

    The sequence AAC39535 differs from that shown. Reason: Erroneous gene model prediction.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti36A → AA in AAC39535 (PubMed:9305847).Curated1
    Sequence conflicti263T → A in BAD97102 (Ref. 4) Curated1
    Sequence conflicti315 – 332KYMEA…LELPQ → STWRPTRT in AAC39528 (PubMed:9305847).CuratedAdd BLAST18

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_033032180M → K in a breast cancer sample; somatic mutation. 1 Publication1
    Natural variantiVAR_048201223E → K.Corresponds to variant rs35176319dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_015783207 – 248GAGVN…GDING → VQANAGECFHGANSASLLHG GPPTSAAGSGQNLPSDRNPG GP in isoform 2. 1 PublicationAdd BLAST42
    Alternative sequenceiVSP_015784249 – 332Missing in isoform 2. 1 PublicationAdd BLAST84

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF010309 mRNA. Translation: AAC39528.1.
    AF010317 Genomic DNA. Translation: AAC39535.1. Sequence problems.
    AY371700 mRNA. Translation: AAQ90166.1.
    BT007149 mRNA. Translation: AAP35813.1.
    AK223382 mRNA. Translation: BAD97102.1.
    DQ232851 Genomic DNA. Translation: ABB02183.1.
    AC008073 Genomic DNA. Translation: AAY14665.1.
    CH471053 Genomic DNA. Translation: EAX00762.1.
    CH471053 Genomic DNA. Translation: EAX00763.1.
    CH471053 Genomic DNA. Translation: EAX00766.1.
    BC000474 mRNA. Translation: AAH00474.1.
    CCDSiCCDS1708.1. [Q53FA7-1]
    CCDS56112.1. [Q53FA7-2]
    RefSeqiNP_001193731.1. NM_001206802.2. [Q53FA7-2]
    NP_004872.2. NM_004881.4. [Q53FA7-1]
    NP_671713.1. NM_147184.3. [Q53FA7-1]
    XP_006712213.1. XM_006712150.2. [Q53FA7-2]
    UniGeneiHs.50649.
    Hs.733381.

    Genome annotation databases

    EnsembliENST00000238721; ENSP00000238721; ENSG00000115129. [Q53FA7-1]
    ENST00000335934; ENSP00000337834; ENSG00000115129. [Q53FA7-1]
    ENST00000407482; ENSP00000384414; ENSG00000115129. [Q53FA7-2]
    GeneIDi9540.
    KEGGihsa:9540.
    UCSCiuc002rex.3. human. [Q53FA7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF010309 mRNA. Translation: AAC39528.1.
    AF010317 Genomic DNA. Translation: AAC39535.1. Sequence problems.
    AY371700 mRNA. Translation: AAQ90166.1.
    BT007149 mRNA. Translation: AAP35813.1.
    AK223382 mRNA. Translation: BAD97102.1.
    DQ232851 Genomic DNA. Translation: ABB02183.1.
    AC008073 Genomic DNA. Translation: AAY14665.1.
    CH471053 Genomic DNA. Translation: EAX00762.1.
    CH471053 Genomic DNA. Translation: EAX00763.1.
    CH471053 Genomic DNA. Translation: EAX00766.1.
    BC000474 mRNA. Translation: AAH00474.1.
    CCDSiCCDS1708.1. [Q53FA7-1]
    CCDS56112.1. [Q53FA7-2]
    RefSeqiNP_001193731.1. NM_001206802.2. [Q53FA7-2]
    NP_004872.2. NM_004881.4. [Q53FA7-1]
    NP_671713.1. NM_147184.3. [Q53FA7-1]
    XP_006712213.1. XM_006712150.2. [Q53FA7-2]
    UniGeneiHs.50649.
    Hs.733381.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J8ZX-ray2.50A1-332[»]
    2OBYX-ray3.00A/B/C/D/E1-332[»]
    ProteinModelPortaliQ53FA7.
    SMRiQ53FA7.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114915. 9 interactors.
    IntActiQ53FA7. 4 interactors.
    STRINGi9606.ENSP00000238721.

    PTM databases

    iPTMnetiQ53FA7.
    PhosphoSitePlusiQ53FA7.

    Polymorphism and mutation databases

    BioMutaiTP53I3.
    DMDMi76789665.

    Proteomic databases

    EPDiQ53FA7.
    MaxQBiQ53FA7.
    PaxDbiQ53FA7.
    PeptideAtlasiQ53FA7.
    PRIDEiQ53FA7.

    Protocols and materials databases

    DNASUi9540.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000238721; ENSP00000238721; ENSG00000115129. [Q53FA7-1]
    ENST00000335934; ENSP00000337834; ENSG00000115129. [Q53FA7-1]
    ENST00000407482; ENSP00000384414; ENSG00000115129. [Q53FA7-2]
    GeneIDi9540.
    KEGGihsa:9540.
    UCSCiuc002rex.3. human. [Q53FA7-1]

    Organism-specific databases

    CTDi9540.
    DisGeNETi9540.
    GeneCardsiTP53I3.
    HGNCiHGNC:19373. TP53I3.
    HPAiCAB017479.
    HPA022012.
    HPA028742.
    MIMi605171. gene.
    neXtProtiNX_Q53FA7.
    OpenTargetsiENSG00000115129.
    PharmGKBiPA134923704.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1198. Eukaryota.
    COG0604. LUCA.
    GeneTreeiENSGT00550000074483.
    HOGENOMiHOG000294672.
    HOVERGENiHBG097584.
    InParanoidiQ53FA7.
    KOiK10133.
    OMAiGQYDPPP.
    OrthoDBiEOG091G0JZF.
    PhylomeDBiQ53FA7.
    TreeFamiTF300079.

    Enzyme and pathway databases

    BioCyciZFISH:HS03836-MONOMER.
    ReactomeiR-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.

    Miscellaneous databases

    EvolutionaryTraceiQ53FA7.
    GeneWikiiTP53I3.
    GenomeRNAii9540.
    PROiQ53FA7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000115129.
    CleanExiHS_TP53I3.
    ExpressionAtlasiQ53FA7. baseline and differential.
    GenevisibleiQ53FA7. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    IPR014189. Quinone_OxRdtase_PIG3.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02824. quinone_pig3. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiQORX_HUMAN
    AccessioniPrimary (citable) accession number: Q53FA7
    Secondary accession number(s): D6W533
    , O14679, O14685, Q38G78, Q6JLE7, Q9BWB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2005
    Last sequence update: September 27, 2005
    Last modified: November 2, 2016
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.