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P05164

- PERM_HUMAN

UniProt

P05164 - PERM_HUMAN

Protein

Myeloperoxidase

Gene

MPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 175 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.

    Catalytic activityi

    Cl- + H2O2 + H+ = HClO + H2O.
    Cl- + H2O2 = HOCl + 2 H2O.

    Cofactori

    Binds 1 calcium ion per monomer.
    Binds 1 heme B (iron-protoporphyrin IX) group covalently per monomer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei260 – 2601Heme (covalent; via 3 links)
    Active sitei261 – 2611Proton acceptor
    Metal bindingi262 – 2621Calcium
    Metal bindingi334 – 3341Calcium
    Metal bindingi336 – 3361Calcium; via carbonyl oxygen
    Metal bindingi338 – 3381Calcium
    Metal bindingi340 – 3401Calcium
    Sitei405 – 4051Transition state stabilizer
    Binding sitei408 – 4081Heme (covalent; via 3 links)
    Binding sitei409 – 4091Heme (covalent; via 3 links)
    Metal bindingi502 – 5021Iron (heme axial ligand)

    GO - Molecular functioni

    1. chromatin binding Source: ProtInc
    2. heme binding Source: InterPro
    3. heparin binding Source: MGI
    4. metal ion binding Source: UniProtKB-KW
    5. peroxidase activity Source: BHF-UCL

    GO - Biological processi

    1. aging Source: Ensembl
    2. defense response Source: ProtInc
    3. defense response to fungus Source: Ensembl
    4. hydrogen peroxide catabolic process Source: BHF-UCL
    5. hypochlorous acid biosynthetic process Source: Ensembl
    6. low-density lipoprotein particle remodeling Source: BHF-UCL
    7. negative regulation of apoptotic process Source: ProtInc
    8. negative regulation of growth of symbiont in host Source: Ensembl
    9. oxidation-reduction process Source: BHF-UCL
    10. removal of superoxide radicals Source: Ensembl
    11. respiratory burst involved in defense response Source: Ensembl
    12. response to food Source: Ensembl
    13. response to lipopolysaccharide Source: Ensembl
    14. response to mechanical stimulus Source: Ensembl
    15. response to oxidative stress Source: UniProtKB
    16. response to yeast Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00140-MONOMER.

    Protein family/group databases

    PeroxiBasei3315. HsMPO.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myeloperoxidase (EC:1.11.2.2)
    Short name:
    MPO
    Cleaved into the following 5 chains:
    Gene namesi
    Name:MPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7218. MPO.

    Subcellular locationi

    GO - Cellular componenti

    1. azurophil granule Source: UniProtKB
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. lysosome Source: ProtInc
    5. mitochondrion Source: Ensembl
    6. nucleus Source: UniProt
    7. secretory granule Source: MGI

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Involvement in diseasei

    Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731Y → C in MPOD; affects proteolytic processing and secretion. 1 Publication
    Corresponds to variant rs78950939 [ dbSNP | Ensembl ].
    VAR_015377
    Natural varianti251 – 2511M → T in MPOD. 1 Publication
    Corresponds to variant rs56378716 [ dbSNP | Ensembl ].
    VAR_015378
    Natural varianti569 – 5691R → W in MPOD; suppress post-translational processing. 2 Publications
    VAR_015379

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi254600. phenotype.
    Orphaneti2587. Myeloperoxidase deficiency.
    PharmGKBiPA243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 48482 PublicationsAdd
    BLAST
    Chaini49 – 74569789 kDa myeloperoxidasePRO_0000023651Add
    BLAST
    Chaini155 – 74559184 kDa myeloperoxidasePRO_0000023653Add
    BLAST
    Chaini165 – 745581MyeloperoxidasePRO_0000023654Add
    BLAST
    Chaini165 – 278114Myeloperoxidase light chainPRO_0000023655Add
    BLAST
    Chaini279 – 745467Myeloperoxidase heavy chainPRO_0000023656Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
    Disulfide bondi167 ↔ 180
    Disulfide bondi281 ↔ 291
    Disulfide bondi285 ↔ 309
    Modified residuei316 – 3161Cysteine sulfenic acid (-SOH)1 Publication
    Disulfide bondi319 – 319Interchain
    Glycosylationi323 – 3231N-linked (GlcNAc...)2 Publications
    Glycosylationi355 – 3551N-linked (GlcNAc...)2 Publications
    Disulfide bondi387 ↔ 398
    Glycosylationi391 – 3911N-linked (GlcNAc...)2 Publications
    Glycosylationi483 – 4831N-linked (GlcNAc...)3 PublicationsCAR_000220
    Disulfide bondi606 ↔ 663
    Disulfide bondi704 ↔ 730
    Glycosylationi729 – 7291N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Oxidation

    Proteomic databases

    PaxDbiP05164.
    PRIDEiP05164.

    PTM databases

    PhosphoSiteiP05164.
    UniCarbKBiP05164.

    Miscellaneous databases

    PMAP-CutDBP05164.

    Expressioni

    Gene expression databases

    ArrayExpressiP05164.
    BgeeiP05164.
    CleanExiHS_MPO.
    GenevestigatoriP05164.

    Organism-specific databases

    HPAiCAB000059.
    HPA021147.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain.2 Publications

    Protein-protein interaction databases

    BioGridi110493. 2 interactions.
    IntActiP05164. 3 interactions.
    MINTiMINT-1522833.
    STRINGi9606.ENSP00000225275.

    Structurei

    Secondary structure

    1
    745
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi181 – 1855
    Turni186 – 1894
    Beta strandi191 – 1944
    Beta strandi206 – 2083
    Beta strandi218 – 2236
    Helixi227 – 2348
    Helixi239 – 2413
    Beta strandi244 – 2496
    Helixi250 – 26314
    Turni281 – 2833
    Beta strandi317 – 3193
    Beta strandi323 – 3253
    Beta strandi329 – 3313
    Beta strandi335 – 3384
    Helixi340 – 3434
    Helixi347 – 3537
    Beta strandi357 – 3604
    Beta strandi371 – 3744
    Helixi387 – 3904
    Turni392 – 3943
    Beta strandi401 – 4033
    Turni404 – 4074
    Helixi410 – 43324
    Helixi439 – 46022
    Helixi463 – 47513
    Helixi492 – 4976
    Helixi498 – 5047
    Beta strandi507 – 5104
    Beta strandi516 – 5183
    Beta strandi523 – 5264
    Helixi527 – 5293
    Turni530 – 5323
    Helixi534 – 5396
    Helixi543 – 55210
    Beta strandi553 – 5564
    Helixi566 – 5694
    Helixi574 – 5763
    Beta strandi577 – 5793
    Helixi583 – 59311
    Helixi599 – 6057
    Helixi614 – 6218
    Helixi624 – 63411
    Helixi637 – 6393
    Helixi642 – 6487
    Beta strandi655 – 6573
    Helixi659 – 67416
    Turni683 – 6853
    Helixi688 – 6947
    Helixi699 – 7068
    Beta strandi711 – 7133
    Turni717 – 7193
    Turni723 – 7264
    Beta strandi727 – 7293
    Helixi730 – 7323
    Helixi739 – 7413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CXPX-ray1.80A/B167-270[»]
    C/D279-744[»]
    1D2VX-ray1.75A/B167-270[»]
    C/D279-744[»]
    1D5LX-ray1.90A/B167-270[»]
    C/D279-744[»]
    1D7WX-ray1.90A/B167-270[»]
    C/D279-744[»]
    1DNUX-ray1.85A/B167-270[»]
    C/D279-744[»]
    1DNWX-ray1.90A/B167-270[»]
    C/D279-744[»]
    1MHLX-ray2.25A/B165-272[»]
    C/D279-744[»]
    1MYPX-ray3.00A/B165-272[»]
    C/D279-744[»]
    3F9PX-ray2.93A/B165-278[»]
    C/D279-745[»]
    3ZS0X-ray2.30A/B165-272[»]
    C/D279-745[»]
    3ZS1X-ray2.60A/B165-278[»]
    C/D279-745[»]
    4C1MX-ray2.00A/B165-272[»]
    C/D279-745[»]
    4DL1X-ray2.00A/B/E/F/I/J/M/N167-270[»]
    C/D/G/H/K/L/O/P279-744[»]
    4EJXX-ray4.69B165-278[»]
    D279-745[»]
    ProteinModelPortaliP05164.
    SMRiP05164. Positions 157-744.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05164.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG262194.
    HOGENOMiHOG000016084.
    HOVERGENiHBG000071.
    KOiK10789.
    OMAiQDKYRTI.
    OrthoDBiEOG7M0NQW.
    PhylomeDBiP05164.
    TreeFamiTF314316.

    Family and domain databases

    Gene3Di1.10.640.10. 2 hits.
    InterProiIPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR029609. MPO.
    [Graphical view]
    PANTHERiPTHR11475:SF46. PTHR11475:SF46. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform H17 (identifier: P05164-1) [UniParc]FASTAAdd to Basket

    Also known as: B

    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

    MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA    50
    PAVLGEVDTS LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS 100
    YFKQPVAATR TAVRAADYLH VALDLLERKL RSLWRRPFNV TDVLTPAQLN 150
    VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC NNRRSPTLGA SNRAFVRWLP 200
    AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD QLTPDQERSL 250
    MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND 300
    PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA 350
    RNLRNMSNQL GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL 400
    AGDTRSSEMP ELTSMHTLLL REHNRLATEL KSLNPRWDGE RLYQEARKIV 450
    GAMVQIITYR DYLPLVLGPT AMRKYLPTYR SYNDSVDPRI ANVFTNAFRY 500
    GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE GGIDPILRGL 550
    MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN 600
    AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP 650
    LKRKGRVGPL LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP 700
    RIICDNTGIT TVSKNNIFMS NSYPRDFVNC STLPALNLAS WREAS 745
    Length:745
    Mass (Da):83,869
    Last modified:August 13, 1987 - v1
    Checksum:i348B1CE0A11038B4
    GO
    Isoform H14 (identifier: P05164-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Show »
    Length:650
    Mass (Da):73,854
    Checksum:i7A29F89DFE6B4916
    GO
    Isoform H7 (identifier: P05164-3) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         182-182: N → NRCGWLGVAAGTGLREASRTPQASRCQRPVLPC

    Show »
    Length:777
    Mass (Da):87,248
    Checksum:iF15BC771A9C6F6A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti36 – 361L → V in CAA28565. (PubMed:3031585)Curated
    Sequence conflicti36 – 361L → V in CAA33438. (PubMed:2552418)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531V → F.1 Publication
    Corresponds to variant rs7208693 [ dbSNP | Ensembl ].
    VAR_023995
    Natural varianti173 – 1731Y → C in MPOD; affects proteolytic processing and secretion. 1 Publication
    Corresponds to variant rs78950939 [ dbSNP | Ensembl ].
    VAR_015377
    Natural varianti251 – 2511M → T in MPOD. 1 Publication
    Corresponds to variant rs56378716 [ dbSNP | Ensembl ].
    VAR_015378
    Natural varianti447 – 4471R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036517
    Natural varianti569 – 5691R → W in MPOD; suppress post-translational processing. 2 Publications
    VAR_015379
    Natural varianti604 – 6041R → C.1 Publication
    Corresponds to variant rs35670089 [ dbSNP | Ensembl ].
    VAR_023996
    Natural varianti683 – 6831E → Q.1 Publication
    Corresponds to variant rs35702888 [ dbSNP | Ensembl ].
    VAR_023997
    Natural varianti717 – 7171I → V.1 Publication
    Corresponds to variant rs2759 [ dbSNP | Ensembl ].
    VAR_012066

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9595Missing in isoform H14. 1 PublicationVSP_007206Add
    BLAST
    Alternative sequencei182 – 1821N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7. 1 PublicationVSP_007207

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02694 mRNA. Translation: AAA59896.1.
    M17176
    , M17170, M17171, M17172, M17173, M17174, M17175 Genomic DNA. Translation: AAA60346.1.
    X04876 mRNA. Translation: CAA28565.1.
    M19507 mRNA. Translation: AAA59863.1.
    M19508 Genomic DNA. Translation: AAA59864.1.
    M19508 Genomic DNA. Translation: AAA59865.1.
    X15377 Genomic DNA. Translation: CAA33438.1.
    S56200 mRNA. Translation: AAB25582.1.
    DQ088846 Genomic DNA. Translation: AAY68218.1.
    CH471109 Genomic DNA. Translation: EAW94470.1.
    BC130476 mRNA. Translation: AAI30477.1.
    D14466 Genomic DNA. Translation: BAA03362.1.
    CCDSiCCDS11604.1. [P05164-1]
    PIRiA29467. OPHUM.
    B28894.
    D28894.
    RefSeqiNP_000241.1. NM_000250.1. [P05164-1]
    UniGeneiHs.458272.

    Genome annotation databases

    EnsembliENST00000225275; ENSP00000225275; ENSG00000005381. [P05164-1]
    GeneIDi4353.
    KEGGihsa:4353.
    UCSCiuc002ivu.1. human. [P05164-1]

    Polymorphism databases

    DMDMi129825.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    MPObase

    MPO mutation db

    NIEHS-SNPs
    Wikipedia

    Myeloperoxidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02694 mRNA. Translation: AAA59896.1 .
    M17176
    , M17170 , M17171 , M17172 , M17173 , M17174 , M17175 Genomic DNA. Translation: AAA60346.1 .
    X04876 mRNA. Translation: CAA28565.1 .
    M19507 mRNA. Translation: AAA59863.1 .
    M19508 Genomic DNA. Translation: AAA59864.1 .
    M19508 Genomic DNA. Translation: AAA59865.1 .
    X15377 Genomic DNA. Translation: CAA33438.1 .
    S56200 mRNA. Translation: AAB25582.1 .
    DQ088846 Genomic DNA. Translation: AAY68218.1 .
    CH471109 Genomic DNA. Translation: EAW94470.1 .
    BC130476 mRNA. Translation: AAI30477.1 .
    D14466 Genomic DNA. Translation: BAA03362.1 .
    CCDSi CCDS11604.1. [P05164-1 ]
    PIRi A29467. OPHUM.
    B28894.
    D28894.
    RefSeqi NP_000241.1. NM_000250.1. [P05164-1 ]
    UniGenei Hs.458272.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CXP X-ray 1.80 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1D2V X-ray 1.75 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1D5L X-ray 1.90 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1D7W X-ray 1.90 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1DNU X-ray 1.85 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1DNW X-ray 1.90 A/B 167-270 [» ]
    C/D 279-744 [» ]
    1MHL X-ray 2.25 A/B 165-272 [» ]
    C/D 279-744 [» ]
    1MYP X-ray 3.00 A/B 165-272 [» ]
    C/D 279-744 [» ]
    3F9P X-ray 2.93 A/B 165-278 [» ]
    C/D 279-745 [» ]
    3ZS0 X-ray 2.30 A/B 165-272 [» ]
    C/D 279-745 [» ]
    3ZS1 X-ray 2.60 A/B 165-278 [» ]
    C/D 279-745 [» ]
    4C1M X-ray 2.00 A/B 165-272 [» ]
    C/D 279-745 [» ]
    4DL1 X-ray 2.00 A/B/E/F/I/J/M/N 167-270 [» ]
    C/D/G/H/K/L/O/P 279-744 [» ]
    4EJX X-ray 4.69 B 165-278 [» ]
    D 279-745 [» ]
    ProteinModelPortali P05164.
    SMRi P05164. Positions 157-744.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110493. 2 interactions.
    IntActi P05164. 3 interactions.
    MINTi MINT-1522833.
    STRINGi 9606.ENSP00000225275.

    Chemistry

    BindingDBi P05164.
    ChEMBLi CHEMBL2439.
    DrugBanki DB00535. Cefdinir.

    Protein family/group databases

    PeroxiBasei 3315. HsMPO.

    PTM databases

    PhosphoSitei P05164.
    UniCarbKBi P05164.

    Polymorphism databases

    DMDMi 129825.

    Proteomic databases

    PaxDbi P05164.
    PRIDEi P05164.

    Protocols and materials databases

    DNASUi 4353.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225275 ; ENSP00000225275 ; ENSG00000005381 . [P05164-1 ]
    GeneIDi 4353.
    KEGGi hsa:4353.
    UCSCi uc002ivu.1. human. [P05164-1 ]

    Organism-specific databases

    CTDi 4353.
    GeneCardsi GC17M056347.
    H-InvDB HIX0039242.
    HGNCi HGNC:7218. MPO.
    HPAi CAB000059.
    HPA021147.
    MIMi 254600. phenotype.
    606989. gene.
    neXtProti NX_P05164.
    Orphaneti 2587. Myeloperoxidase deficiency.
    PharmGKBi PA243.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262194.
    HOGENOMi HOG000016084.
    HOVERGENi HBG000071.
    KOi K10789.
    OMAi QDKYRTI.
    OrthoDBi EOG7M0NQW.
    PhylomeDBi P05164.
    TreeFami TF314316.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00140-MONOMER.

    Miscellaneous databases

    ChiTaRSi MPO. human.
    EvolutionaryTracei P05164.
    GeneWikii Myeloperoxidase.
    GenomeRNAii 4353.
    NextBioi 17126.
    PMAP-CutDB P05164.
    PROi P05164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05164.
    Bgeei P05164.
    CleanExi HS_MPO.
    Genevestigatori P05164.

    Family and domain databases

    Gene3Di 1.10.640.10. 2 hits.
    InterProi IPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR029609. MPO.
    [Graphical view ]
    PANTHERi PTHR11475:SF46. PTHR11475:SF46. 1 hit.
    Pfami PF03098. An_peroxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00457. ANPEROXIDASE.
    SUPFAMi SSF48113. SSF48113. 1 hit.
    PROSITEi PS00435. PEROXIDASE_1. 1 hit.
    PS50292. PEROXIDASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of cDNA for human myeloperoxidase."
      Morishita K., Kubota N., Asano S., Kaziro Y., Nagata S.
      J. Biol. Chem. 262:3844-3851(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
    2. "Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor."
      Morishita K., Tsuchiya M., Asano S., Kaziro Y., Nagata S.
      J. Biol. Chem. 262:15208-15213(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase."
      Seto P., Hirayu H., Magnusson R.P., Gestautas J., Portmann L., Degroot L.J., Rapoport B.
      J. Clin. Invest. 80:1205-1208(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
    4. "Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species."
      Johnson K.R., Nauseef W.M., Care A., Wheelock M.J., Shane S., Hudson S., Koeffler H.P., Selsted M., Miller C., Rovera G.
      Nucleic Acids Res. 15:2013-2028(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
    5. "Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation."
      Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.
      Biochemistry 27:5906-5914(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS H7; H14 AND H17), PROTEIN SEQUENCE OF 165-183; 216-222; 295-304; 311-331; 464-479; 662-676 AND 766-776.
      Tissue: Leukemia.
    6. Erratum
      Hashinaka K., Nishio C., Hur S.-J., Sakiyama F., Tsunasawa S., Yamada M.
      Biochemistry 27:9226-9226(1988)
    7. "Complete nucleotide sequence of the human myeloperoxidase gene."
      Johnson K.R., Gemperlein I., Hudson S., Shane S., Rovera G.
      Nucleic Acids Res. 17:7985-7986(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. "Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1."
      Hosokawa Y., Kawaguchi R., Hikiji K., Yamada M., Suzuki K., Nakagawa T., Yoshihara T., Yamaguchi K.
      Leukemia 7:441-445(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM H17).
    9. NIEHS SNPs program
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PHE-53; CYS-604; GLN-683 AND VAL-717.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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 H17).
    12. "Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures."
      Yamada M., Hur S.-J., Toda H.
      Biochem. Biophys. Res. Commun. 166:852-859(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-66.
    13. "Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity."
      Van Antwerpen P., Slomianny M.C., Boudjeltia K.Z., Delporte C., Faid V., Calay D., Rousseau A., Moguilevsky N., Raes M., Vanhamme L., Furtmueller P.G., Obinger C., Vanhaeverbeek M., Neve J., Michalski J.C.
      J. Biol. Chem. 285:16351-16359(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-53, SUBUNIT, GLYCOSYLATION AT ASN-323; ASN-355; ASN-391; ASN-483 AND ASN-729, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409."
      Taylor K.L., Pohl J., Kinkade J.M. Jr.
      J. Biol. Chem. 267:25282-25288(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 279-424.
      Tissue: Leukocyte.
    15. "Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene."
      Yamada M., Yoshida M., Hashinaka K.
      J. Biol. Chem. 268:13479-13485(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-629.
    16. "Isolation and characterization of a cDNA coding for human myeloperoxidase."
      Yamada M., Hur S.-J., Hashinaka K., Tsuneoka K., Saeki T., Nishio C., Sakiyama F., Tsunasawa S.
      Arch. Biochem. Biophys. 255:147-155(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 588-745.
    17. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-483.
      Tissue: Plasma.
    18. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323 AND ASN-483.
      Tissue: Saliva.
    19. "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-355 AND ASN-391.
      Tissue: Liver.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8-A resolution."
      Fiedler T.J., Davey C.A., Fenna R.E.
      J. Biol. Chem. 275:11964-11971(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 167-744, SUBUNIT.
    22. "Structure of the green heme in myeloperoxidase."
      Fenna R.E., Zeng J., Davey C.
      Arch. Biochem. Biophys. 316:653-656(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 167-744, OXIDATION AT CYS-316.
    23. "Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution."
      Blair-Johnson M., Fiedler T., Fenna R.
      Biochemistry 40:13990-13997(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-744.
    24. "Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency."
      Kizaki M., Miller C.W., Selsted M.E., Koeffler H.P.
      Blood 83:1935-1940(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPOD TRP-569.
    25. "Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan."
      Nauseef W.M., Brigham S., Cogley M.
      J. Biol. Chem. 269:1212-1216(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPOD TRP-569.
    26. "Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase."
      Nauseef W., Cogley M., McCormick S.
      J. Biol. Chem. 271:9546-9549(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT MPOD TRP-569.
    27. "A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation."
      DeLeo F.R., Goedken M., McCormick S.J., Nauseef W.M.
      J. Clin. Invest. 101:2900-2909(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPOD CYS-173, CHARACTERIZATION OF VARIANT MPOD CYS-173.
    28. "Biochemical and molecular characterization of hereditary myeloperoxidase deficiency."
      Romano M., Dri P., Dadalt L., Patriarca P., Baralle F.E.
      Blood 90:4126-4134(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPOD THR-251.
    29. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-447.

    Entry informationi

    Entry nameiPERM_HUMAN
    AccessioniPrimary (citable) accession number: P05164
    Secondary accession number(s): A1L4B8
    , Q14862, Q4PJH5, Q9UCL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 175 of the entry and version 1 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 17
      Human chromosome 17: 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