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P24158

- PRTN3_HUMAN

UniProt

P24158 - PRTN3_HUMAN

Protein

Myeloblastin

Gene

PRTN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Polymorphonuclear leukocyte serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) and causes emphysema when administered by tracheal insufflation to hamsters.

    Catalytic activityi

    Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-|-Xaa- > -Val-|-Xaa-.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711Charge relay system
    Active sitei118 – 1181Charge relay system
    Active sitei203 – 2031Charge relay system

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. serine-type endopeptidase activity Source: InterPro
    3. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. mature dendritic cell differentiation Source: UniProtKB
    3. negative regulation of phagocytosis Source: UniProtKB
    4. positive regulation of cell proliferation Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Collagen degradation

    Enzyme and pathway databases

    BRENDAi3.4.21.76. 2681.

    Protein family/group databases

    MEROPSiS01.134.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myeloblastin (EC:3.4.21.76)
    Alternative name(s):
    AGP7
    C-ANCA antigen
    Leukocyte proteinase 3
    Short name:
    PR-3
    Short name:
    PR3
    Neutrophil proteinase 4
    Short name:
    NP-4
    P29
    Wegener autoantigen
    Gene namesi
    Name:PRTN3
    Synonyms:MBN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9495. PRTN3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. plasma membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti900. Granulomatosis with polyangiitis.
    PharmGKBiPA33842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Propeptidei26 – 272PRO_0000027707
    Chaini28 – 248221MyeloblastinPRO_0000027708Add
    BLAST
    Propeptidei249 – 2568PRO_0000027709

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 72
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi152 ↔ 209
    Glycosylationi174 – 1741N-linked (GlcNAc...)
    Disulfide bondi182 ↔ 188
    Disulfide bondi199 ↔ 224

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP24158.
    PeptideAtlasiP24158.
    PRIDEiP24158.

    Expressioni

    Gene expression databases

    BgeeiP24158.
    CleanExiHS_PRTN3.
    GenevestigatoriP24158.

    Organism-specific databases

    HPAiCAB017558.
    HPA005938.

    Interactioni

    Protein-protein interaction databases

    BioGridi111638. 6 interactions.
    IntActiP24158. 2 interactions.
    MINTiMINT-4054660.

    Structurei

    Secondary structure

    1
    256
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 476
    Beta strandi56 – 627
    Beta strandi65 – 684
    Helixi70 – 734
    Beta strandi74 – 763
    Helixi78 – 803
    Beta strandi81 – 866
    Beta strandi98 – 10710
    Turni112 – 1154
    Beta strandi120 – 1267
    Beta strandi151 – 16010
    Beta strandi162 – 1643
    Beta strandi171 – 1788
    Beta strandi186 – 1905
    Beta strandi192 – 1954
    Beta strandi206 – 2094
    Beta strandi212 – 2198
    Beta strandi221 – 2233
    Beta strandi227 – 2293
    Beta strandi231 – 2355
    Helixi236 – 2394
    Helixi240 – 2478

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FUJX-ray2.20A/B/C/D28-248[»]
    ProteinModelPortaliP24158.
    SMRiP24158. Positions 28-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24158.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 248221Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Elastase subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOVERGENiHBG013304.
    InParanoidiP24158.
    KOiK01350.
    OMAiHFSVAQV.
    OrthoDBiEOG7MKW6Q.
    PhylomeDBiP24158.
    TreeFamiTF335284.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24158-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHRPPSPAL ASVLLALLLS GAARAAEIVG GHEAQPHSRP YMASLQMRGN    50
    PGSHFCGGTL IHPSFVLTAA HCLRDIPQRL VNVVLGAHNV RTQEPTQQHF 100
    SVAQVFLNNY DAENKLNDVL LIQLSSPANL SASVATVQLP QQDQPVPHGT 150
    QCLAMGWGRV GAHDPPAQVL QELNVTVVTF FCRPHNICTF VPRRKAGICF 200
    GDSGGPLICD GIIQGIDSFV IWGCATRLFP DFFTRVALYV DWIRSTLRRV 250
    EAKGRP 256
    Length:256
    Mass (Da):27,807
    Last modified:December 15, 1998 - v3
    Checksum:iCBECA36D8C4B2A40
    GO

    Sequence cautioni

    The sequence AAA36342.1 differs from that shown. Reason: Frameshift at positions 34 and 39.
    The sequence CAA39598.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → R in CAA39203. (PubMed:2258701)Curated
    Sequence conflicti38 – 381S → I AA sequence (PubMed:1688612)Curated
    Sequence conflicti40 – 401P → PI AA sequence (PubMed:1688612)Curated
    Sequence conflicti46 – 461Q → E AA sequence (PubMed:2404977)Curated
    Sequence conflicti46 – 461Q → E AA sequence (PubMed:2501794)Curated
    Sequence conflicti48 – 481R → A AA sequence (PubMed:2121162)Curated
    Sequence conflicti64 – 641S → D AA sequence (PubMed:2033050)Curated
    Sequence conflicti70 – 701A → P in AAA59558. (PubMed:1681549)Curated
    Sequence conflicti255 – 2551Missing in CAA39203. (PubMed:2258701)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191V → I.7 Publications
    Corresponds to variant rs351111 [ dbSNP | Ensembl ].
    VAR_011691
    Natural varianti135 – 1351A → T.4 Publications
    Corresponds to variant rs1042281 [ dbSNP | Ensembl ].
    VAR_011713
    Natural varianti136 – 1361T → S.4 Publications
    Corresponds to variant rs1042282 [ dbSNP | Ensembl ].
    VAR_011714

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75154 mRNA. Translation: AAA59558.1.
    AC004799 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW69591.1.
    BC096183 mRNA. Translation: AAH96183.1.
    BC096184 mRNA. Translation: AAH96184.1.
    BC096185 mRNA. Translation: AAH96185.1.
    BC096186 mRNA. Translation: AAH96186.1.
    M96628 Genomic DNA. Translation: AAB59364.1.
    AH005293 Genomic DNA. Translation: AAB59493.1.
    M97911 Genomic DNA. No translation available.
    AH007523 Genomic DNA. Translation: AAD21524.1.
    X56606 mRNA. Translation: CAA39943.1.
    X55668 mRNA. Translation: CAA39203.1.
    M29142 mRNA. Translation: AAA36342.1. Frameshift.
    X56132 mRNA. Translation: CAA39597.1.
    X56132 mRNA. Translation: CAA39598.1. Different initiation.
    CCDSiCCDS32860.1.
    PIRiA45080. PRHU3.
    RefSeqiNP_002768.3. NM_002777.3.
    UniGeneiHs.928.

    Genome annotation databases

    EnsembliENST00000234347; ENSP00000234347; ENSG00000196415.
    GeneIDi5657.
    KEGGihsa:5657.
    UCSCiuc002lqa.1. human.

    Polymorphism databases

    DMDMi6174926.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Proteinase 3 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M75154 mRNA. Translation: AAA59558.1 .
    AC004799 Genomic DNA. No translation available.
    CH471139 Genomic DNA. Translation: EAW69591.1 .
    BC096183 mRNA. Translation: AAH96183.1 .
    BC096184 mRNA. Translation: AAH96184.1 .
    BC096185 mRNA. Translation: AAH96185.1 .
    BC096186 mRNA. Translation: AAH96186.1 .
    M96628 Genomic DNA. Translation: AAB59364.1 .
    AH005293 Genomic DNA. Translation: AAB59493.1 .
    M97911 Genomic DNA. No translation available.
    AH007523 Genomic DNA. Translation: AAD21524.1 .
    X56606 mRNA. Translation: CAA39943.1 .
    X55668 mRNA. Translation: CAA39203.1 .
    M29142 mRNA. Translation: AAA36342.1 . Frameshift.
    X56132 mRNA. Translation: CAA39597.1 .
    X56132 mRNA. Translation: CAA39598.1 . Different initiation.
    CCDSi CCDS32860.1.
    PIRi A45080. PRHU3.
    RefSeqi NP_002768.3. NM_002777.3.
    UniGenei Hs.928.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FUJ X-ray 2.20 A/B/C/D 28-248 [» ]
    ProteinModelPortali P24158.
    SMRi P24158. Positions 28-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111638. 6 interactions.
    IntActi P24158. 2 interactions.
    MINTi MINT-4054660.

    Chemistry

    BindingDBi P24158.
    ChEMBLi CHEMBL3900.

    Protein family/group databases

    MEROPSi S01.134.

    Polymorphism databases

    DMDMi 6174926.

    Proteomic databases

    PaxDbi P24158.
    PeptideAtlasi P24158.
    PRIDEi P24158.

    Protocols and materials databases

    DNASUi 5657.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234347 ; ENSP00000234347 ; ENSG00000196415 .
    GeneIDi 5657.
    KEGGi hsa:5657.
    UCSCi uc002lqa.1. human.

    Organism-specific databases

    CTDi 5657.
    GeneCardsi GC19P000840.
    HGNCi HGNC:9495. PRTN3.
    HPAi CAB017558.
    HPA005938.
    MIMi 177020. gene.
    neXtProti NX_P24158.
    Orphaneti 900. Granulomatosis with polyangiitis.
    PharmGKBi PA33842.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG013304.
    InParanoidi P24158.
    KOi K01350.
    OMAi HFSVAQV.
    OrthoDBi EOG7MKW6Q.
    PhylomeDBi P24158.
    TreeFami TF335284.

    Enzyme and pathway databases

    BRENDAi 3.4.21.76. 2681.

    Miscellaneous databases

    EvolutionaryTracei P24158.
    GeneWikii Proteinase_3.
    GenomeRNAii 5657.
    NextBioi 21988.
    PROi P24158.
    SOURCEi Search...

    Gene expression databases

    Bgeei P24158.
    CleanExi HS_PRTN3.
    Genevestigatori P24158.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Wegener autoantigen and myeloblastin are encoded by a single mRNA."
      Labbaye C., Musette P., Cayre Y.E.
      Proc. Natl. Acad. Sci. U.S.A. 88:9253-9256(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-119; THR-135 AND SER-136.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ILE-119.
    4. "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], VARIANT ILE-119.
    5. "Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter."
      Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.
      Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20 AND 22-256.
    6. "Structure, chromosomal assignment, and expression of the gene for proteinase-3. The Wegener's granulomatosis autoantigen."
      Sturrock A.B., Franklin K.F., Rao G., Marshall B.C., Rebentisch M.B., Lemons R.S., Hoidal J.R.
      J. Biol. Chem. 267:21193-21199(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-254, VARIANTS THR-135 AND SER-136.
    7. "Donor-recipient polymorphism of the proteinase 3 gene: a potential target for T-cell alloresponses to myeloid leukemia."
      Clave E., Molldrem J., Hensel N., Raptis A., Barrett A.J.
      J. Immunother. 22:1-6(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200, VARIANT ILE-119.
    8. "Wegener's autoantigen and leukemia."
      Musette P., Labbaye C., Dorner M.H., Cayre Y.E., Casanova J.-L., Kourilsky P.
      Blood 77:1398-1399(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-42.
    9. "Cloning of cDNA for proteinase 3: a serine protease, antibiotic, and autoantigen from human neutrophils."
      Campanelli D., Melchior M., Fu Y., Nakata M., Shuman H., Nathan C., Gabay J.E.
      J. Exp. Med. 172:1709-1715(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-256, PROTEIN SEQUENCE OF 28-71; 156-181 AND 196-219.
    10. "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells."
      Bories D., Raynal M.-C., Solomon D.H., Darzynkiewicz Z., Cayre Y.E.
      Cell 59:959-968(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, VARIANTS ILE-119; THR-135 AND SER-136.
    11. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-256, PROTEIN SEQUENCE OF 28-48, VARIANTS ILE-119; THR-135 AND SER-136, IDENTITY OF WEGENER'S AUTOANTIGEN WITH PR-3.
    12. "Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties."
      Rao N.V., Wehner N.G., Marshall B.C., Gray W.R., Gray B.H., Hoidal J.R.
      J. Biol. Chem. 266:9540-9548(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-67 AND 228-244.
    13. "Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase."
      Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.
      J. Biol. Chem. 265:2038-2041(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-47 AND 196-219.
    14. "Monoclonal antibodies specific for neutrophil proteinase 4. Production and use for isolation of the enzyme."
      Ohlsson K., Linder C., Rosengren M.
      Biol. Chem. Hoppe-Seyler 371:549-555(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-52.
    15. "The relation of 29 kD C-ANCA antigen to proteinase 3."
      Goldschmeding R., Dolman K.M., van den Ende M.E., van der Meer-Gerritsen C.H., Sonnenberg A., von dem Borne A.E.
      APMIS Suppl. 19:26-27(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-48.
    16. "Wegener's granulomatosis autoantigen is a novel neutrophil serine proteinase."
      Niles J.L., McCluskey R.T., Ahmad M.F., Arnaout M.A.
      Blood 74:1888-1893(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-47.
    17. Cited for: PROTEIN SEQUENCE OF 28-47.
    18. "Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis."
      Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.
      J. Immunol. Methods 180:25-33(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-47, CATALYTIC ACTIVITY.
      Tissue: Neutrophil.
    19. "Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme."
      Ludemann J., Utecht B., Gross W.L.
      J. Exp. Med. 171:357-362(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-43.
    20. "A novel form of dipeptidylpeptidase IV found in human serum. Isolation, characterization, and comparison with T lymphocyte membrane dipeptidylpeptidase IV (CD26)."
      Duke-Cohan J.S., Morimoto C., Rocker J.A., Schlossman S.F.
      J. Biol. Chem. 270:14107-14114(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 110-121, VARIANT ILE-119.
      Tissue: Serum.
    21. "Identity of Wegener's autoantigen (p29) with proteinase 3 and myeloblastin."
      Gupta S.K., Niles J.L., McCluskey R.T., Arnaout M.A.
      Blood 76:2162-2162(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTITY OF WEGENER'S AUTOANTIGEN WITH PROTEINASE 3.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The crystal structure of PR3, a neutrophil serine proteinase antigen of Wegener's granulomatosis antibodies."
      Fujinaga M., Charnaia M.M., Halenbeck R., Koths K., James M.N.G.
      J. Mol. Biol. 261:267-278(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiPRTN3_HUMAN
    AccessioniPrimary (citable) accession number: P24158
    Secondary accession number(s): P15637
    , P18078, Q4VB08, Q4VB09, Q6LBM7, Q6LBN2, Q9UD25, Q9UQD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 161 of the entry and version 3 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 19
      Human chromosome 19: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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