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O14638

- ENPP3_HUMAN

UniProt

O14638 - ENPP3_HUMAN

Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

ENPP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (23 Sep 2008)
      Previous versions | rss
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    Functioni

    Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD.By similarity

    Catalytic activityi

    Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.
    A dinucleotide + H2O = 2 mononucleotides.

    Cofactori

    Binds 2 divalent metal cations per subunit.Curated

    Enzyme regulationi

    At low concentrations of ATP, a phosphorylated active site intermediate is formed which inhibits further ATP hydrolysis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi167 – 1671Zinc 1; catalyticBy similarity
    Active sitei205 – 2051AMP-threonine intermediateBy similarity
    Metal bindingi205 – 2051Zinc 1; catalyticBy similarity
    Binding sitei226 – 2261SubstrateBy similarity
    Binding sitei320 – 3201SubstrateBy similarity
    Metal bindingi325 – 3251Zinc 2; catalyticBy similarity
    Metal bindingi329 – 3291Zinc 2; via tele nitrogen; catalyticBy similarity
    Metal bindingi372 – 3721Zinc 1; catalyticBy similarity
    Metal bindingi373 – 3731Zinc 1; via tele nitrogen; catalyticBy similarity
    Metal bindingi483 – 4831Zinc 2; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. NADH pyrophosphatase activity Source: UniProtKB-EC
    3. nucleic acid binding Source: InterPro
    4. nucleoside-triphosphate diphosphatase activity Source: BHF-UCL
    5. nucleotide diphosphatase activity Source: ProtInc
    6. phosphodiesterase I activity Source: ProtInc
    7. polysaccharide binding Source: InterPro
    8. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. immune response Source: InterPro
    2. nucleic acid phosphodiester bond hydrolysis Source: GOC
    3. nucleoside triphosphate catabolic process Source: BHF-UCL
    4. phosphate-containing compound metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
    Short name:
    E-NPP 3
    Alternative name(s):
    Phosphodiesterase I beta
    Short name:
    PD-Ibeta
    Phosphodiesterase I/nucleotide pyrophosphatase 3
    CD_antigen: CD203c
    Including the following 2 domains:
    Alkaline phosphodiesterase I (EC:3.1.4.1)
    Nucleotide pyrophosphatase (EC:3.6.1.9)
    Short name:
    NPPase
    Gene namesi
    Name:ENPP3
    Synonyms:PDNP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:3358. ENPP3.

    Subcellular locationi

    Membrane Curated; Single-pass type II membrane protein Curated. Secreted 2 Publications
    Note: Located to the apical surface in intestinal and kidney epithelial cells. Located to the cell surface of basophils, and to the apical plasma membrane of bile duct cells. Secreted in serum, and in lumen of epithelial cells.

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27793.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875Ectonucleotide pyrophosphatase/phosphodiesterase family member 3PRO_0000188570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 71PROSITE-ProRule annotation
    Disulfide bondi58 ↔ 89PROSITE-ProRule annotation
    Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
    Disulfide bondi75 ↔ 81PROSITE-ProRule annotation
    Disulfide bondi98 ↔ 115PROSITE-ProRule annotation
    Disulfide bondi103 ↔ 133PROSITE-ProRule annotation
    Disulfide bondi113 ↔ 126PROSITE-ProRule annotation
    Disulfide bondi119 ↔ 125PROSITE-ProRule annotation
    Disulfide bondi144 ↔ 190PROSITE-ProRule annotation
    Disulfide bondi152 ↔ 364PROSITE-ProRule annotation
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi380 ↔ 478PROSITE-ProRule annotation
    Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi429 ↔ 818PROSITE-ProRule annotation
    Glycosylationi533 – 5331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi575 ↔ 679PROSITE-ProRule annotation
    Disulfide bondi577 ↔ 664PROSITE-ProRule annotation
    Glycosylationi582 – 5821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi687 – 6871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi699 – 6991N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi787 ↔ 797PROSITE-ProRule annotation
    Glycosylationi789 – 7891N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO14638.
    PaxDbiO14638.
    PRIDEiO14638.

    PTM databases

    PhosphoSiteiO14638.

    Expressioni

    Tissue specificityi

    Expressed in bile ducts, prostate, uterus and colon. Exclusively expressed on basophils, mast cells and their progenitors.2 Publications

    Inductioni

    Up-regulated by stimulation by allergen or by cross-linking with IgE. The IgE-mediated activation is enhanced by tetradecanoyl phorbol acetate (TPA), a stimulator of the PKC pathway, and inhibited by the P13 kinase inhibitors, LY294002 and wortmannin. Up-regulated in invasive bile duct cancers.1 Publication

    Gene expression databases

    ArrayExpressiO14638.
    BgeeiO14638.
    CleanExiHS_ENPP3.
    GenevestigatoriO14638.

    Organism-specific databases

    HPAiHPA043772.

    Interactioni

    Protein-protein interaction databases

    BioGridi111195. 2 interactions.
    IntActiO14638. 1 interaction.
    MINTiMINT-6610326.
    STRINGi9606.ENSP00000350265.

    Structurei

    3D structure databases

    ProteinModelPortaliO14638.
    SMRiO14638. Positions 52-872.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini31 – 875845ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 3019Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 9344SMB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini94 – 13845SMB 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni140 – 510371PhosphodiesteraseAdd
    BLAST
    Regioni605 – 875271NucleaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi78 – 803Cell attachment siteSequence Analysis

    Sequence similaritiesi

    Contains 2 SMB (somatomedin-B) domains.Curated

    Keywords - Domaini

    Repeat, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1524.
    HOGENOMiHOG000037439.
    HOVERGENiHBG051484.
    InParanoidiO14638.
    KOiK01513.
    OMAiTSDSQYD.
    OrthoDBiEOG7XM2X4.
    PhylomeDBiO14638.
    TreeFamiTF330032.

    Family and domain databases

    Gene3Di3.40.570.10. 1 hit.
    3.40.720.10. 1 hit.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR001604. DNA/RNA_non-sp_Endonuclease.
    IPR024873. E-NPP.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR001212. Somatomedin_B_dom.
    [Graphical view]
    PANTHERiPTHR10151. PTHR10151. 1 hit.
    PfamiPF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view]
    SMARTiSM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O14638-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESTLTLATE QPVKKNTLKK YKIACIVLLA LLVIMSLGLG LGLGLRKLEK    50
    QGSCRKKCFD ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNK 100
    FRCGETRLEA SLCSCSDDCL QRKDCCADYK SVCQGETSWL EENCDTAQQS 150
    QCPEGFDLPP VILFSMDGFR AEYLYTWDTL MPNINKLKTC GIHSKYMRAM 200
    YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VNLNKNFSLS SKEQNNPAWW 250
    HGQPMWLTAM YQGLKAATYF WPGSEVAING SFPSIYMPYN GSVPFEERIS 300
    TLLKWLDLPK AERPRFYTMY FEEPDSSGHA GGPVSARVIK ALQVVDHAFG 350
    MLMEGLKQRN LHNCVNIILL ADHGMDQTYC NKMEYMTDYF PRINFFYMYE 400
    GPAPRIRAHN IPHDFFSFNS EEIVRNLSCR KPDQHFKPYL TPDLPKRLHY 450
    AKNVRIDKVH LFVDQQWLAV RSKSNTNCGG GNHGYNNEFR SMEAIFLAHG 500
    PSFKEKTEVE PFENIEVYNL MCDLLRIQPA PNNGTHGSLN HLLKVPFYEP 550
    SHAEEVSKFS VCGFANPLPT ESLDCFCPHL QNSTQLEQVN QMLNLTQEEI 600
    TATVKVNLPF GRPRVLQKNV DHCLLYHREY VSGFGKAMRM PMWSSYTVPQ 650
    LGDTSPLPPT VPDCLRADVR VPPSESQKCS FYLADKNITH GFLYPPASNR 700
    TSDSQYDALI TSNLVPMYEE FRKMWDYFHS VLLIKHATER NGVNVVSGPI 750
    FDYNYDGHFD APDEITKHLA NTDVPIPTHY FVVLTSCKNK SHTPENCPGW 800
    LDVLPFIIPH RPTNVESCPE GKPEALWVEE RFTAHIARVR DVELLTGLDF 850
    YQDKVQPVSE ILQLKTYLPT FETTI 875
    Length:875
    Mass (Da):100,124
    Last modified:September 23, 2008 - v2
    Checksum:i629D2E33B4C45196
    GO

    Sequence cautioni

    The sequence AAD05192.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti122 – 1221R → K in AAC51813. (PubMed:9344668)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti620 – 6201V → M.
    Corresponds to variant rs9321309 [ dbSNP | Ensembl ].
    VAR_018516
    Natural varianti744 – 7441N → H.
    Corresponds to variant rs36094194 [ dbSNP | Ensembl ].
    VAR_046538
    Natural varianti786 – 7861S → N.
    Corresponds to variant rs17601580 [ dbSNP | Ensembl ].
    VAR_031253

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005632 mRNA. Translation: AAC51813.1.
    EF560735 mRNA. Translation: ABQ59045.1.
    AC005587 Genomic DNA. Translation: AAD05192.1. Sequence problems.
    AL121575, AC005587, AL355150 Genomic DNA. Translation: CAI23322.1.
    AL355150, AC005587, AL121575 Genomic DNA. Translation: CAI40481.1.
    CH471051 Genomic DNA. Translation: EAW48045.1.
    CCDSiCCDS5148.1.
    RefSeqiNP_005012.2. NM_005021.3.
    UniGeneiHs.486489.

    Genome annotation databases

    EnsembliENST00000357639; ENSP00000350265; ENSG00000154269.
    ENST00000414305; ENSP00000406261; ENSG00000154269.
    GeneIDi5169.
    KEGGihsa:5169.
    UCSCiuc003qcu.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005632 mRNA. Translation: AAC51813.1 .
    EF560735 mRNA. Translation: ABQ59045.1 .
    AC005587 Genomic DNA. Translation: AAD05192.1 . Sequence problems.
    AL121575 , AC005587 , AL355150 Genomic DNA. Translation: CAI23322.1 .
    AL355150 , AC005587 , AL121575 Genomic DNA. Translation: CAI40481.1 .
    CH471051 Genomic DNA. Translation: EAW48045.1 .
    CCDSi CCDS5148.1.
    RefSeqi NP_005012.2. NM_005021.3.
    UniGenei Hs.486489.

    3D structure databases

    ProteinModelPortali O14638.
    SMRi O14638. Positions 52-872.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111195. 2 interactions.
    IntActi O14638. 1 interaction.
    MINTi MINT-6610326.
    STRINGi 9606.ENSP00000350265.

    Chemistry

    ChEMBLi CHEMBL5580.

    PTM databases

    PhosphoSitei O14638.

    Proteomic databases

    MaxQBi O14638.
    PaxDbi O14638.
    PRIDEi O14638.

    Protocols and materials databases

    DNASUi 5169.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357639 ; ENSP00000350265 ; ENSG00000154269 .
    ENST00000414305 ; ENSP00000406261 ; ENSG00000154269 .
    GeneIDi 5169.
    KEGGi hsa:5169.
    UCSCi uc003qcu.4. human.

    Organism-specific databases

    CTDi 5169.
    GeneCardsi GC06P132000.
    HGNCi HGNC:3358. ENPP3.
    HPAi HPA043772.
    MIMi 602182. gene.
    neXtProti NX_O14638.
    PharmGKBi PA27793.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1524.
    HOGENOMi HOG000037439.
    HOVERGENi HBG051484.
    InParanoidi O14638.
    KOi K01513.
    OMAi TSDSQYD.
    OrthoDBi EOG7XM2X4.
    PhylomeDBi O14638.
    TreeFami TF330032.

    Miscellaneous databases

    GeneWikii ENPP3.
    GenomeRNAii 5169.
    NextBioi 20000.
    PROi O14638.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14638.
    Bgeei O14638.
    CleanExi HS_ENPP3.
    Genevestigatori O14638.

    Family and domain databases

    Gene3Di 3.40.570.10. 1 hit.
    3.40.720.10. 1 hit.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR001604. DNA/RNA_non-sp_Endonuclease.
    IPR024873. E-NPP.
    IPR020821. Extracellular_endonuc_su_A.
    IPR002591. Phosphodiest/P_Trfase.
    IPR001212. Somatomedin_B_dom.
    [Graphical view ]
    PANTHERi PTHR10151. PTHR10151. 1 hit.
    Pfami PF01223. Endonuclease_NS. 1 hit.
    PF01663. Phosphodiest. 1 hit.
    PF01033. Somatomedin_B. 2 hits.
    [Graphical view ]
    SMARTi SM00892. Endonuclease_NS. 1 hit.
    SM00477. NUC. 1 hit.
    SM00201. SO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00524. SMB_1. 2 hits.
    PS50958. SMB_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes."
      Piao J.-H., Goding J.W., Nakamura H., Sano K.
      Genomics 45:412-415(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Prostate.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Endometrium.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3."
      Buehring H.J., Seiffert M., Giesert C., Marxer A., Kanz L., Valent P., Sano K.
      Blood 97:3303-3305(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 393-405, IDENTIFICATION AS CD203C, SUBCELLULAR LOCATION.
    6. "Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases."
      Yano Y., Hayashi Y., Sano K., Nagano H., Nakaji M., Seo Y., Ninomiya T., Yoon S., Yokozaki H., Kasuga M.
      Cancer Lett. 207:139-147(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis."
      Buehring H.J., Streble A., Valent P.
      Int. Arch. Allergy Immunol. 133:317-329(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, POSSIBLE APPLICATION IN ALLERGY DIAGNOSIS.

    Entry informationi

    Entry nameiENPP3_HUMAN
    AccessioniPrimary (citable) accession number: O14638
    Secondary accession number(s): Q5JTL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 130 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3