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

Peroxidasin homolog

Gene

PXDN

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

Functioni

Displays low peroxidase activity and is likely to participate in H2O2 metabolism and peroxidative reactions in the cardiovascular system. Plays a role in extracellular matrix formation.2 Publications

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per subunit.

Kineticsi

  1. KM=0.15 mM for H2O21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei826 – 8261Heme (covalent; via 2 links)By similarity
    Active sitei827 – 8271Proton acceptorPROSITE-ProRule annotation
    Metal bindingi828 – 8281CalciumPROSITE-ProRule annotation
    Metal bindingi907 – 9071CalciumPROSITE-ProRule annotation
    Metal bindingi909 – 9091Calcium; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi911 – 9111CalciumPROSITE-ProRule annotation
    Metal bindingi913 – 9131CalciumPROSITE-ProRule annotation
    Sitei977 – 9771Transition state stabilizerPROSITE-ProRule annotation
    Binding sitei980 – 9801Heme (covalent; via 2 links)By similarity
    Metal bindingi1074 – 10741Iron (heme axial ligand)PROSITE-ProRule annotation

    GO - Molecular functioni

    • extracellular matrix structural constituent Source: UniProtKB
    • heme binding Source: UniProtKB
    • interleukin-1 receptor antagonist activity Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW
    • peroxidase activity Source: UniProtKB

    GO - Biological processi

    • extracellular matrix organization Source: UniProtKB
    • hydrogen peroxide catabolic process Source: UniProtKB
    • immune response Source: UniProtKB
    • negative regulation of cytokine-mediated signaling pathway Source: GOC
    • oxidation-reduction process Source: UniProtKB
    • response to oxidative stress Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.11.1.7. 2681.

    Protein family/group databases

    PeroxiBasei3355. HsPxd01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxidasin homolog (EC:1.11.1.7)
    Alternative name(s):
    Melanoma-associated antigen MG50
    Vascular peroxidase 1
    p53-responsive gene 2 protein
    Gene namesi
    Name:PXDN
    Synonyms:KIAA0230, MG50, PRG2, VPO, VPO1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14966. PXDN.

    Subcellular locationi

    GO - Cellular componenti

    • endoplasmic reticulum Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • extracellular matrix Source: UniProtKB
    • extracellular space Source: UniProtKB
    • proteinaceous extracellular matrix Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Corneal opacification with other ocular anomalies (COPOA)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAn ocular disease characterized by sclerocornea associated with other ocular anomalies, such as cataract, microcornea, microphthalmia, and anterior segment dysgenesis. Sclerocornea is a primary anomaly in which scleralization of a peripheral part of the cornea, or the entire corneal tissue, occurs. In the peripheral type of sclerocornea, the affected area is vascularized with regular arcades of superficial scleral vessels. In total sclerocornea, the entire cornea is opaque and vascularized.

    See also OMIM:269400
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti880 – 8801R → C in COPOA. 1 Publication
    VAR_071389

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi269400. phenotype.
    Orphaneti289499. Congenital cataract microcornea with corneal opacity.
    PharmGKBiPA128394535.

    Polymorphism and mutation databases

    BioMutaiPXDN.
    DMDMi172045828.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 14791453Peroxidasin homologPRO_0000319619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi267 ↔ 317By similarity
    Disulfide bondi363 ↔ 412By similarity
    Disulfide bondi454 ↔ 502By similarity
    Disulfide bondi546 ↔ 594By similarity
    Glycosylationi640 – 6401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi699 – 6991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi719 – 7191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi731 – 7311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi732 ↔ 748By similarity
    Disulfide bondi847 ↔ 857By similarity
    Disulfide bondi851 ↔ 875By similarity
    Glycosylationi865 – 8651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi959 ↔ 970By similarity
    Modified residuei1176 – 11761Phosphotyrosine1 Publication
    Disulfide bondi1177 ↔ 1234By similarity
    Glycosylationi1178 – 11781N-linked (GlcNAc...)1 Publication
    Modified residuei1180 – 11801Phosphoserine1 Publication
    Disulfide bondi1275 ↔ 1301By similarity
    Glycosylationi1280 – 12801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1368 – 13681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1425 – 14251N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ92626.
    PaxDbiQ92626.
    PRIDEiQ92626.

    PTM databases

    PhosphoSiteiQ92626.

    Expressioni

    Tissue specificityi

    Expressed at higher levels in heart, lung, ovary, spleen, intestine and placenta, and at lower levels in liver, colon, pancreas, kidney, thymus, skeletal muscle and prostate. Expressed in tumors such as melanoma, breast cancer, ovarian cancer and glioblastoma. A shorter form probably lacking the signal sequence is found in testis and in EB1 cells undergoing p53/TP53-dependent apoptosis.4 Publications

    Developmental stagei

    Expressed in fetal liver and spleen.1 Publication

    Inductioni

    By TGFB1 in fibroblasts and up-regulated in apoptotic cells.2 Publications

    Gene expression databases

    BgeeiQ92626.
    CleanExiHS_PRG2.
    HS_PXDN.
    ExpressionAtlasiQ92626. baseline and differential.
    GenevisibleiQ92626. HS.

    Organism-specific databases

    HPAiHPA012375.

    Interactioni

    Protein-protein interaction databases

    BioGridi113596. 9 interactions.
    IntActiQ92626. 1 interaction.
    MINTiMINT-4931004.
    STRINGi9606.ENSP00000252804.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92626.
    SMRiQ92626. Positions 34-676, 738-1314.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 6337LRRNTAdd
    BLAST
    Repeati87 – 10822LRR 1Add
    BLAST
    Repeati111 – 13222LRR 2Add
    BLAST
    Repeati135 – 15622LRR 3Add
    BLAST
    Repeati159 – 18022LRR 4Add
    BLAST
    Domaini192 – 24554LRRCTAdd
    BLAST
    Domaini246 – 33287Ig-like C2-type 1Add
    BLAST
    Domaini342 – 42887Ig-like C2-type 2Add
    BLAST
    Domaini433 – 52088Ig-like C2-type 3Add
    BLAST
    Domaini521 – 61090Ig-like C2-type 4Add
    BLAST
    Domaini1413 – 147159VWFCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation
    Contains 4 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated
    Contains 1 VWFC domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG262194.
    GeneTreeiENSGT00550000074325.
    HOGENOMiHOG000016084.
    HOVERGENiHBG108312.
    InParanoidiQ92626.
    OMAiEPVITWN.
    OrthoDBiEOG7D2FD6.
    PhylomeDBiQ92626.
    TreeFamiTF314316.

    Family and domain databases

    Gene3Di1.10.640.10. 2 hits.
    2.60.40.10. 4 hits.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF03098. An_peroxidase. 1 hit.
    PF07679. I-set. 4 hits.
    PF13855. LRR_8. 1 hit.
    PF00093. VWC. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SMARTiSM00408. IGc2. 4 hits.
    SM00369. LRR_TYP. 4 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50835. IG_LIKE. 4 hits.
    PS51450. LRR. 5 hits.
    PS50292. PEROXIDASE_3. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

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

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q92626-1) [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
    MAKRSRGPGR RCLLALVLFC AWGTLAVVAQ KPGAGCPSRC LCFRTTVRCM
    60 70 80 90 100
    HLLLEAVPAV APQTSILDLR FNRIREIQPG AFRRLRNLNT LLLNNNQIKR
    110 120 130 140 150
    IPSGAFEDLE NLKYLYLYKN EIQSIDRQAF KGLASLEQLY LHFNQIETLD
    160 170 180 190 200
    PDSFQHLPKL ERLFLHNNRI THLVPGTFNH LESMKRLRLD SNTLHCDCEI
    210 220 230 240 250
    LWLADLLKTY AESGNAQAAA ICEYPRRIQG RSVATITPEE LNCERPRITS
    260 270 280 290 300
    EPQDADVTSG NTVYFTCRAE GNPKPEIIWL RNNNELSMKT DSRLNLLDDG
    310 320 330 340 350
    TLMIQNTQET DQGIYQCMAK NVAGEVKTQE VTLRYFGSPA RPTFVIQPQN
    360 370 380 390 400
    TEVLVGESVT LECSATGHPP PRISWTRGDR TPLPVDPRVN ITPSGGLYIQ
    410 420 430 440 450
    NVVQGDSGEY ACSATNNIDS VHATAFIIVQ ALPQFTVTPQ DRVVIEGQTV
    460 470 480 490 500
    DFQCEAKGNP PPVIAWTKGG SQLSVDRRHL VLSSGTLRIS GVALHDQGQY
    510 520 530 540 550
    ECQAVNIIGS QKVVAHLTVQ PRVTPVFASI PSDTTVEVGA NVQLPCSSQG
    560 570 580 590 600
    EPEPAITWNK DGVQVTESGK FHISPEGFLT INDVGPADAG RYECVARNTI
    610 620 630 640 650
    GSASVSMVLS VNVPDVSRNG DPFVATSIVE AIATVDRAIN STRTHLFDSR
    660 670 680 690 700
    PRSPNDLLAL FRYPRDPYTV EQARAGEIFE RTLQLIQEHV QHGLMVDLNG
    710 720 730 740 750
    TSYHYNDLVS PQYLNLIANL SGCTAHRRVN NCSDMCFHQK YRTHDGTCNN
    760 770 780 790 800
    LQHPMWGASL TAFERLLKSV YENGFNTPRG INPHRLYNGH ALPMPRLVST
    810 820 830 840 850
    TLIGTETVTP DEQFTHMLMQ WGQFLDHDLD STVVALSQAR FSDGQHCSNV
    860 870 880 890 900
    CSNDPPCFSV MIPPNDSRAR SGARCMFFVR SSPVCGSGMT SLLMNSVYPR
    910 920 930 940 950
    EQINQLTSYI DASNVYGSTE HEARSIRDLA SHRGLLRQGI VQRSGKPLLP
    960 970 980 990 1000
    FATGPPTECM RDENESPIPC FLAGDHRANE QLGLTSMHTL WFREHNRIAT
    1010 1020 1030 1040 1050
    ELLKLNPHWD GDTIYYETRK IVGAEIQHIT YQHWLPKILG EVGMRTLGEY
    1060 1070 1080 1090 1100
    HGYDPGINAG IFNAFATAAF RFGHTLVNPL LYRLDENFQP IAQDHLPLHK
    1110 1120 1130 1140 1150
    AFFSPFRIVN EGGIDPLLRG LFGVAGKMRV PSQLLNTELT ERLFSMAHTV
    1160 1170 1180 1190 1200
    ALDLAAINIQ RGRDHGIPPY HDYRVYCNLS AAHTFEDLKN EIKNPEIREK
    1210 1220 1230 1240 1250
    LKRLYGSTLN IDLFPALVVE DLVPGSRLGP TLMCLLSTQF KRLRDGDRLW
    1260 1270 1280 1290 1300
    YENPGVFSPA QLTQIKQTSL ARILCDNADN ITRVQSDVFR VAEFPHGYGS
    1310 1320 1330 1340 1350
    CDEIPRVDLR VWQDCCEDCR TRGQFNAFSY HFRGRRSLEF SYQEDKPTKK
    1360 1370 1380 1390 1400
    TRPRKIPSVG RQGEHLSNST SAFSTRSDAS GTNDFREFVL EMQKTITDLR
    1410 1420 1430 1440 1450
    TQIKKLESRL STTECVDAGG ESHANNTKWK KDACTICECK DGQVTCFVEA
    1460 1470
    CPPATCAVPV NIPGACCPVC LQKRAEEKP
    Length:1,479
    Mass (Da):165,275
    Last modified:February 26, 2008 - v2
    Checksum:i7A75F533D89C6AAD
    GO
    Isoform 2 (identifier: Q92626-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         703-727: YHYNDLVSPQYLNLIANLSGCTAHR → QCQSLFFLLHGLSNGVEHASVKSHS
         728-1479: Missing.

    Show »
    Length:727
    Mass (Da):80,329
    Checksum:i16391EA8B7F61878
    GO

    Sequence cautioni

    The sequence AAF06354.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAA13219.1 differs from that shown. Reason: Erroneous initiation. Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti880 – 8801R → C in COPOA. 1 Publication
    VAR_071389
    Natural varianti1198 – 11981R → Q.
    Corresponds to variant rs6723697 [ dbSNP | Ensembl ].
    VAR_050487
    Natural varianti1261 – 12611Q → R.
    Corresponds to variant rs6723697 [ dbSNP | Ensembl ].
    VAR_039048

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei703 – 72725YHYND…CTAHR → QCQSLFFLLHGLSNGVEHAS VKSHS in isoform 2. 1 PublicationVSP_031516Add
    BLAST
    Alternative sequencei728 – 1479752Missing in isoform 2. 1 PublicationVSP_031517Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200348 mRNA. Translation: AAF06354.1. Different initiation.
    EF090903 mRNA. Translation: ABO25865.1.
    D86983 mRNA. Translation: BAA13219.1. Different initiation.
    CH471053 Genomic DNA. Translation: EAX01084.1.
    CH471053 Genomic DNA. Translation: EAX01085.1.
    BC098579 mRNA. Translation: AAH98579.1.
    CCDSiCCDS46221.1. [Q92626-1]
    RefSeqiNP_036425.1. NM_012293.2. [Q92626-1]
    UniGeneiHs.332197.

    Genome annotation databases

    EnsembliENST00000252804; ENSP00000252804; ENSG00000130508. [Q92626-1]
    GeneIDi7837.
    KEGGihsa:7837.
    UCSCiuc002qxa.3. human. [Q92626-1]
    uc002qxb.1. human. [Q92626-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF200348 mRNA. Translation: AAF06354.1. Different initiation.
    EF090903 mRNA. Translation: ABO25865.1.
    D86983 mRNA. Translation: BAA13219.1. Different initiation.
    CH471053 Genomic DNA. Translation: EAX01084.1.
    CH471053 Genomic DNA. Translation: EAX01085.1.
    BC098579 mRNA. Translation: AAH98579.1.
    CCDSiCCDS46221.1. [Q92626-1]
    RefSeqiNP_036425.1. NM_012293.2. [Q92626-1]
    UniGeneiHs.332197.

    3D structure databases

    ProteinModelPortaliQ92626.
    SMRiQ92626. Positions 34-676, 738-1314.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi113596. 9 interactions.
    IntActiQ92626. 1 interaction.
    MINTiMINT-4931004.
    STRINGi9606.ENSP00000252804.

    Protein family/group databases

    PeroxiBasei3355. HsPxd01.

    PTM databases

    PhosphoSiteiQ92626.

    Polymorphism and mutation databases

    BioMutaiPXDN.
    DMDMi172045828.

    Proteomic databases

    MaxQBiQ92626.
    PaxDbiQ92626.
    PRIDEiQ92626.

    Protocols and materials databases

    DNASUi7837.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000252804; ENSP00000252804; ENSG00000130508. [Q92626-1]
    GeneIDi7837.
    KEGGihsa:7837.
    UCSCiuc002qxa.3. human. [Q92626-1]
    uc002qxb.1. human. [Q92626-2]

    Organism-specific databases

    CTDi7837.
    GeneCardsiGC02M001635.
    HGNCiHGNC:14966. PXDN.
    HPAiHPA012375.
    MIMi269400. phenotype.
    605158. gene.
    neXtProtiNX_Q92626.
    Orphaneti289499. Congenital cataract microcornea with corneal opacity.
    PharmGKBiPA128394535.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG262194.
    GeneTreeiENSGT00550000074325.
    HOGENOMiHOG000016084.
    HOVERGENiHBG108312.
    InParanoidiQ92626.
    OMAiEPVITWN.
    OrthoDBiEOG7D2FD6.
    PhylomeDBiQ92626.
    TreeFamiTF314316.

    Enzyme and pathway databases

    BRENDAi1.11.1.7. 2681.

    Miscellaneous databases

    ChiTaRSiPXDN. human.
    GeneWikiiPXDN.
    GenomeRNAii7837.
    NextBioi30238.
    PROiQ92626.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ92626.
    CleanExiHS_PRG2.
    HS_PXDN.
    ExpressionAtlasiQ92626. baseline and differential.
    GenevisibleiQ92626. HS.

    Family and domain databases

    Gene3Di1.10.640.10. 2 hits.
    2.60.40.10. 4 hits.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR001007. VWF_C.
    [Graphical view]
    PfamiPF03098. An_peroxidase. 1 hit.
    PF07679. I-set. 4 hits.
    PF13855. LRR_8. 1 hit.
    PF00093. VWC. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SMARTiSM00408. IGc2. 4 hits.
    SM00369. LRR_TYP. 4 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    SM00214. VWC. 1 hit.
    [Graphical view]
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50835. IG_LIKE. 4 hits.
    PS51450. LRR. 5 hits.
    PS50292. PEROXIDASE_3. 1 hit.
    PS01208. VWFC_1. 1 hit.
    PS50184. VWFC_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation of differentially expressed cDNAs from p53-dependent apoptotic cells: activation of the human homologue of the Drosophila peroxidasin gene."
      Horikoshi N., Cong J., Kley N., Shenk T.
      Biochem. Biophys. Res. Commun. 261:864-869(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY.
    2. "A novel melanoma gene (MG50) encoding the interleukin 1 receptor antagonist and six epitopes recognized by human cytolytic T lymphocytes."
      Mitchell M.S., Kan-Mitchell J., Minev B., Edman C., Deans R.J.
      Cancer Res. 60:6448-6456(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    3. "Identification and characterization of VPO1, a new animal heme-containing peroxidase."
      Cheng G., Salerno J.C., Cao Z., Pagano P.J., Lambeth J.D.
      Free Radic. Biol. Med. 45:1682-1694(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 3D-STRUCTURE MODELING, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, HEME COFACTOR, TISSUE SPECIFICITY.
    4. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] OF 6-1479 (ISOFORM 2).
      Tissue: Chondrosarcoma.
    7. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1176 AND SER-1180, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. Cheng G.
      Unpublished observations (FEB-2008)
      Cited for: SUBCELLULAR LOCATION.
    9. "Peroxidasin is secreted and incorporated into the extracellular matrix of myofibroblasts and fibrotic kidney."
      Peterfi Z., Donko A., Orient A., Sum A., Prokai A., Molnar B., Vereb Z., Rajnavolgyi E., Kovacs K.J., Muller V., Szabo A.J., Geiszt M.
      Am. J. Pathol. 175:725-735(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY TGFB1.
    10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1178.
      Tissue: Liver.
    11. Cited for: INVOLVEMENT IN COPOA, VARIANT COPOA CYS-880.

    Entry informationi

    Entry nameiPXDN_HUMAN
    AccessioniPrimary (citable) accession number: Q92626
    Secondary accession number(s): A8QM65, D6W4Y0, Q4KMG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 26, 2008
    Last sequence update: February 26, 2008
    Last modified: June 24, 2015
    This is version 142 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

    Complete proteome, 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. 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.