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Reviewed, UniProtKB/Swiss-Prot Q53FA7 (QORX_HUMAN)

Last modified June 16, 2009. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative quinone oxidoreductase
    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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in the generation of reactive oxygen species (ROS).

Induction

Isoforms 1 and 2 are both activated by TP53/p53, 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.

Sequence caution

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

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processinduction of apoptosis by oxidative stress

Non-traceable author statement. Source: UniProtKB

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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 – 332332Putative quinone oxidoreductase
PRO_0000160917

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

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.9
VAR_033032
Natural variant2231E → K: dbSNP rs35176319.
VAR_048201

Experimental info

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).

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: 9305847] [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: 15067011] [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: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Muscle.
[8]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, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[9]"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: 17224074] [Abstract]
Cited for: VARIANT LYS-180.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

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.
BC000474 mRNA. Translation: AAH00474.1.
IPIIPI00384643.
IPI00418440.
RefSeqNP_004872.2.
NP_671713.1.
UniGeneHs.50649

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2J8ZX-ray2.50A1-332[»]
2OBYX-ray3.00A/B/C/D/E1-332[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ53FA7. 4 interactions.

PTM databases

PhosphoSiteQ53FA7.

Proteomic databases

PeptideAtlasQ53FA7.
PRIDEQ53FA7.

Genome annotation databases

EnsemblENSG00000115129. Homo sapiens. [Contig view]
GeneID9540.
KEGGhsa:9540.

Organism-specific databases

GeneCardsGC02M024211.
HGNCHGNC:19373. TP53I3.
MIM605171. gene.
PharmGKBPA134923704.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ53FA7.
HOVERGENQ53FA7.
OMAQ53FA7. SEATLKF.

Gene expression databases

ArrayExpressQ53FA7.
BgeeQ53FA7.
CleanExHS_TP53I3.
GermOnlineENSG00000115129. Homo sapiens.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR016040. NAD(P)-bd_dom.
IPR002364. Quin_OxRdtase/zeta-crystal_CS.
IPR014189. Quinone_OxRdtase_PIG3.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PTHR11695:SF28. Quinone_oxidored_PIG3. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR02824. quinone_pig3. 1 hit.
PROSITEPS01162. QOR_ZETA_CRYSTAL. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio35770.
SOURCESearch...

Entry information

Entry nameQORX_HUMAN
AccessionPrimary (citable) accession number: Q53FA7
Secondary accession number(s): O14679 expand/collapse secondary AC list , O14685, Q38G78, Q6JLE7, Q9BWB8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents