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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411NADP1 Publication
    Binding sitei192 – 1921NADP1 Publication
    Binding sitei322 – 3221NADP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi148 – 1547NADP1 Publication
    Nucleotide bindingi173 – 1775NADP1 Publication
    Nucleotide bindingi264 – 2663NADP1 Publication

    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
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-1143-MONOMER.

    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
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:19373. TP53I3.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi51 – 511Y → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi51 – 511Y → F: Increased enzyme activity. 1 Publication
    Mutagenesisi151 – 1511S → V: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134923704.

    Polymorphism and mutation databases

    BioMutaiTP53I3.
    DMDMi76789665.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 332332Quinone oxidoreductase PIG3PRO_0000160917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ53FA7.
    PaxDbiQ53FA7.
    PeptideAtlasiQ53FA7.
    PRIDEiQ53FA7.

    PTM databases

    PhosphoSiteiQ53FA7.

    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

    BgeeiQ53FA7.
    CleanExiHS_TP53I3.
    ExpressionAtlasiQ53FA7. baseline and differential.
    GenevisibleiQ53FA7. HS.

    Organism-specific databases

    HPAiCAB017479.
    HPA022012.
    HPA028742.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi114915. 9 interactions.
    IntActiQ53FA7. 4 interactions.
    STRINGi9606.ENSP00000238721.

    Structurei

    Secondary structure

    332
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 88Combined sources
    Helixi12 – 143Combined sources
    Beta strandi15 – 217Combined sources
    Beta strandi29 – 3810Combined sources
    Helixi41 – 477Combined sources
    Beta strandi59 – 613Combined sources
    Beta strandi63 – 7210Combined sources
    Beta strandi78 – 803Combined sources
    Beta strandi85 – 895Combined sources
    Beta strandi95 – 1028Combined sources
    Helixi103 – 1053Combined sources
    Beta strandi106 – 1083Combined sources
    Helixi115 – 1184Combined sources
    Helixi122 – 13211Combined sources
    Turni133 – 1353Combined sources
    Beta strandi143 – 1486Combined sources
    Helixi152 – 16312Combined sources
    Beta strandi167 – 1737Combined sources
    Helixi175 – 18410Combined sources
    Beta strandi187 – 1915Combined sources
    Turni192 – 1943Combined sources
    Helixi197 – 2048Combined sources
    Turni205 – 2073Combined sources
    Beta strandi210 – 2178Combined sources
    Helixi219 – 2213Combined sources
    Helixi222 – 2287Combined sources
    Beta strandi229 – 2379Combined sources
    Beta strandi246 – 2483Combined sources
    Helixi250 – 2567Combined sources
    Beta strandi260 – 2634Combined sources
    Helixi271 – 28414Combined sources
    Helixi286 – 2894Combined sources
    Beta strandi301 – 3066Combined sources
    Helixi307 – 3093Combined sources
    Helixi310 – 3189Combined sources
    Beta strandi323 – 3297Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J8ZX-ray2.50A1-332[»]
    2OBYX-ray3.00A/B/C/D/E1-332[»]
    ProteinModelPortaliQ53FA7.
    SMRiQ53FA7. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ53FA7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00550000074483.
    HOGENOMiHOG000294672.
    HOVERGENiHBG097584.
    InParanoidiQ53FA7.
    KOiK10133.
    OMAiAKDGCLS.
    OrthoDBiEOG7Z69CN.
    PhylomeDBiQ53FA7.
    TreeFamiTF300079.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. 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]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 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 AAC39535.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361A → AA in AAC39535 (PubMed:9305847).Curated
    Sequence conflicti263 – 2631T → A in BAD97102 (Ref. 4) Curated
    Sequence conflicti315 – 33218KYMEA…LELPQ → STWRPTRT in AAC39528 (PubMed:9305847).CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti180 – 1801M → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_033032
    Natural varianti223 – 2231E → K.
    Corresponds to variant rs35176319 [ dbSNP | Ensembl ].
    VAR_048201

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei207 – 24842GAGVN…GDING → VQANAGECFHGANSASLLHG GPPTSAAGSGQNLPSDRNPG GP in isoform 2. 1 PublicationVSP_015783Add
    BLAST
    Alternative sequencei249 – 33284Missing in isoform 2. 1 PublicationVSP_015784Add
    BLAST

    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.2. human. [Q53FA7-2]
    uc002rey.2. 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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2J8ZX-ray2.50A1-332[»]
    2OBYX-ray3.00A/B/C/D/E1-332[»]
    ProteinModelPortaliQ53FA7.
    SMRiQ53FA7. Positions 1-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114915. 9 interactions.
    IntActiQ53FA7. 4 interactions.
    STRINGi9606.ENSP00000238721.

    PTM databases

    PhosphoSiteiQ53FA7.

    Polymorphism and mutation databases

    BioMutaiTP53I3.
    DMDMi76789665.

    Proteomic databases

    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.2. human. [Q53FA7-2]
    uc002rey.2. human. [Q53FA7-1]

    Organism-specific databases

    CTDi9540.
    GeneCardsiGC02M024300.
    HGNCiHGNC:19373. TP53I3.
    HPAiCAB017479.
    HPA022012.
    HPA028742.
    MIMi605171. gene.
    neXtProtiNX_Q53FA7.
    PharmGKBiPA134923704.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00550000074483.
    HOGENOMiHOG000294672.
    HOVERGENiHBG097584.
    InParanoidiQ53FA7.
    KOiK10133.
    OMAiAKDGCLS.
    OrthoDBiEOG7Z69CN.
    PhylomeDBiQ53FA7.
    TreeFamiTF300079.

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-1143-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiQ53FA7.
    GeneWikiiTP53I3.
    GenomeRNAii9540.
    NextBioi35770.
    PROiQ53FA7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ53FA7.
    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_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR014189. Quinone_OxRdtase_PIG3.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    TIGRFAMsiTIGR02824. quinone_pig3. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. 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.
      , 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. 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. 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.

    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: June 24, 2015
    This is version 99 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

    External Data

    Dasty 3

    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 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.