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Q92626

- PXDN_HUMAN

UniProt

Q92626 - PXDN_HUMAN

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Protein

Peroxidasin homolog

Gene

PXDN

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 calcium ion per subunit.By similarity
Binds 1 heme B (iron-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

  1. extracellular matrix structural constituent Source: UniProtKB
  2. heme binding Source: UniProtKB
  3. interleukin-1 receptor antagonist activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. peroxidase activity Source: UniProtKB

GO - Biological processi

  1. extracellular matrix organization Source: UniProtKB
  2. hydrogen peroxide catabolic process Source: UniProtKB
  3. immune response Source: UniProtKB
  4. negative regulation of cytokine-mediated signaling pathway Source: GOC
  5. oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

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: Chromosome 2

Organism-specific databases

HGNCiHGNC:14966. PXDN.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 2 Publications
Note: Enriched in the peritubular space of fibrotic kidneys.

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular matrix Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Corneal opacification with other ocular anomalies (COPOA) [MIM:269400]: An 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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.
GenevestigatoriQ92626.

Organism-specific databases

HPAiHPA012375.

Interactioni

Protein-protein interaction databases

BioGridi113596. 11 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. Align

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

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:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi172045828.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS46221.1. [Q92626-1 ]
RefSeqi NP_036425.1. NM_012293.2. [Q92626-1 ]
UniGenei Hs.332197.

3D structure databases

ProteinModelPortali Q92626.
SMRi Q92626. Positions 34-676, 738-1314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113596. 11 interactions.
IntActi Q92626. 1 interaction.
MINTi MINT-4931004.
STRINGi 9606.ENSP00000252804.

Protein family/group databases

PeroxiBasei 3355. HsPxd01.

PTM databases

PhosphoSitei Q92626.

Polymorphism databases

DMDMi 172045828.

Proteomic databases

MaxQBi Q92626.
PaxDbi Q92626.
PRIDEi Q92626.

Protocols and materials databases

DNASUi 7837.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252804 ; ENSP00000252804 ; ENSG00000130508 . [Q92626-1 ]
GeneIDi 7837.
KEGGi hsa:7837.
UCSCi uc002qxa.3. human. [Q92626-1 ]
uc002qxb.1. human. [Q92626-2 ]

Organism-specific databases

CTDi 7837.
GeneCardsi GC02M001635.
HGNCi HGNC:14966. PXDN.
HPAi HPA012375.
MIMi 269400. phenotype.
605158. gene.
neXtProti NX_Q92626.
Orphaneti 289499. Congenital cataract microcornea with corneal opacity.
PharmGKBi PA128394535.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG262194.
GeneTreei ENSGT00550000074325.
HOGENOMi HOG000016084.
HOVERGENi HBG108312.
InParanoidi Q92626.
OMAi EPVITWN.
OrthoDBi EOG7D2FD6.
PhylomeDBi Q92626.
TreeFami TF314316.

Miscellaneous databases

ChiTaRSi PXDN. human.
GeneWikii PXDN.
GenomeRNAii 7837.
NextBioi 30238.
PROi Q92626.
SOURCEi Search...

Gene expression databases

Bgeei Q92626.
CleanExi HS_PRG2.
HS_PXDN.
ExpressionAtlasi Q92626. baseline and differential.
Genevestigatori Q92626.

Family and domain databases

Gene3Di 1.10.640.10. 2 hits.
2.60.40.10. 4 hits.
InterProi IPR000483. 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 ]
Pfami PF03098. An_peroxidase. 1 hit.
PF07679. I-set. 4 hits.
PF13855. LRR_8. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view ]
PRINTSi PR00457. ANPEROXIDASE.
SMARTi SM00408. IGc2. 4 hits.
SM00369. LRR_TYP. 4 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
SUPFAMi SSF48113. SSF48113. 1 hit.
PROSITEi PS50835. 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 ]
ProtoNeti Search...

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: October 29, 2014
This is version 135 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