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Q53FA7 (QORX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Quinone oxidoreductase PIG3

EC=1.-.-.-
Alternative name(s):
Tumor protein p53-inducible protein 3
p53-induced gene 3 protein
Gene names
Name:TP53I3
Synonyms:PIG3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.11

Subunit structure

Homodimer. Ref.11

Induction

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

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=215 µM for 1,2-naphthoquinone Ref.11

Sequence caution

The sequence AAC39535.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: UV radiation favors the production of isoform 2.
Isoform 1 (identifier: Q53FA7-1)

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.
Note: Major isoform under normal light conditions.
Isoform 2 (identifier: Q53FA7-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 332332Quinone oxidoreductase PIG3
PRO_0000160917

Regions

Nucleotide binding148 – 1547NADP
Nucleotide binding173 – 1775NADP
Nucleotide binding264 – 2663NADP

Sites

Binding site411NADP
Binding site1921NADP
Binding site3221NADP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9

Natural variations

Alternative sequence207 – 24842GAGVN…GDING → VQANAGECFHGANSASLLHG GPPTSAAGSGQNLPSDRNPG GP in isoform 2.
VSP_015783
Alternative sequence249 – 33284Missing in isoform 2.
VSP_015784
Natural variant1801M → K in a breast cancer sample; somatic mutation. Ref.12
VAR_033032
Natural variant2231E → K.
Corresponds to variant rs35176319 [ dbSNP | Ensembl ].
VAR_048201

Experimental info

Mutagenesis511Y → A: Loss of enzyme activity. Ref.11
Mutagenesis511Y → F: Increased enzyme activity. Ref.11
Mutagenesis1511S → V: Loss of enzyme activity. Ref.11
Sequence conflict361A → AA in AAC39535. Ref.1
Sequence conflict2631T → A in BAD97102. Ref.4
Sequence conflict315 – 33218KYMEA…LELPQ → STWRPTRT in AAC39528. Ref.1

Secondary structure

.............................................................. 332
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: C5A33C46B3F96473

FASTA33235,536
        10         20         30         40         50         60 
MLAVHFDKPG GPENLYVKEV AKPSPGEGEV LLKVAASALN RADLMQRQGQ YDPPPGASNI 

        70         80         90        100        110        120 
LGLEASGHVA ELGPGCQGHW KIGDTAMALL PGGGQAQYVT VPEGLLMPIP EGLTLTQAAA 

       130        140        150        160        170        180 
IPEAWLTAFQ LLHLVGNVQA GDYVLIHAGL SGVGTAAIQL TRMAGAIPLV TAGSQKKLQM 

       190        200        210        220        230        240 
AEKLGAAAGF NYKKEDFSEA TLKFTKGAGV NLILDCIGGS YWEKNVNCLA LDGRWVLYGL 

       250        260        270        280        290        300 
MGGGDINGPL FSKLLFKRGS LITSLLRSRD NKYKQMLVNA FTEQILPHFS TEGPQRLLPV 

       310        320        330 
LDRIYPVTEI QEAHKYMEAN KNIGKIVLEL PQ 

« Hide

Isoform 2 (PIG3AS) [UniParc].

Checksum: 8899613C763DDDDC
Show »

FASTA24825,402

References

« Hide 'large scale' references
[1]"A model for p53-induced apoptosis."
Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B.
Nature 389:300-306(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), INDUCTION BY TP53.
Tissue: Colon cancer.
[2]"UV-dependent alternative splicing uncouples p53 activity and PIG3 gene function through rapid proteolytic degradation."
Nicholls C.D., Shields M.A., Lee P.W.K., Robbins S.M., Beattie T.L.
J. Biol. Chem. 279:24171-24178(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Mammary tumor.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Gastric mucosa.
[5]NIEHS SNPs program
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[9]Bienvenut W.V., Vousden K.H., Lukashchuk N.
Submitted (MAR-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-33; 163-176; 184-203; 259-267; 297-303 AND 326-332, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Three-dimensional structure and enzymatic function of proapoptotic human p53-inducible quinone oxidoreductase PIG3."
Porte S., Valencia E., Yakovtseva E.A., Borras E., Shafqat N., Debreczeny J.E., Pike A.C.W., Oppermann U., Farres J., Fita I., Pares X.
J. Biol. Chem. 284:17194-17205(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-51 AND SER-151.
[12]"Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.
Breast Cancer Res. 9:R5-R5(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-180.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001193731.1. NM_001206802.2.
NP_004872.2. NM_004881.4.
NP_671713.1. NM_147184.3.
UniGeneHs.50649.
Hs.733381.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J8ZX-ray2.50A1-332[»]
2OBYX-ray3.00A/B/C/D/E1-332[»]
ProteinModelPortalQ53FA7.
SMRQ53FA7. Positions 1-332.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114915. 9 interactions.
IntActQ53FA7. 4 interactions.
STRING9606.ENSP00000238721.

PTM databases

PhosphoSiteQ53FA7.

Polymorphism databases

DMDM76789665.

Proteomic databases

PaxDbQ53FA7.
PeptideAtlasQ53FA7.
PRIDEQ53FA7.

Protocols and materials databases

DNASU9540.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238721; ENSP00000238721; ENSG00000115129. [Q53FA7-1]
ENST00000313482; ENSP00000322298; ENSG00000115129. [Q53FA7-2]
ENST00000335934; ENSP00000337834; ENSG00000115129. [Q53FA7-1]
ENST00000407482; ENSP00000384414; ENSG00000115129. [Q53FA7-2]
GeneID9540.
KEGGhsa:9540.
UCSCuc002rex.2. human. [Q53FA7-2]
uc002rey.2. human. [Q53FA7-1]

Organism-specific databases

CTD9540.
GeneCardsGC02M024300.
HGNCHGNC:19373. TP53I3.
HPACAB017479.
HPA022012.
HPA028742.
MIM605171. gene.
neXtProtNX_Q53FA7.
PharmGKBPA134923704.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0604.
HOGENOMHOG000294672.
HOVERGENHBG097584.
InParanoidQ53FA7.
KOK10133.
OMASSAHIGK.
OrthoDBEOG7Z69CN.
PhylomeDBQ53FA7.
TreeFamTF300079.

Gene expression databases

ArrayExpressQ53FA7.
BgeeQ53FA7.
CleanExHS_TP53I3.
GenevestigatorQ53FA7.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR014189. Quinone_OxRdtase_PIG3.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
TIGRFAMsTIGR02824. quinone_pig3. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ53FA7.
GeneWikiTP53I3.
GenomeRNAi9540.
NextBio35770.
PROQ53FA7.
SOURCESearch...

Entry information

Entry nameQORX_HUMAN
AccessionPrimary (citable) accession number: Q53FA7
Secondary accession number(s): D6W533 expand/collapse secondary AC list , O14679, O14685, Q38G78, Q6JLE7, Q9BWB8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM