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P05164 (PERM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cl- + H2O2 = HOCl + 2 H2O.

Cofactor

Binds 1 calcium ion per monomer.

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

Subunit structure

Homodimer; disulfide-linked. Each monomer consists of a light and a heavy chain. Ref.13 Ref.21

Subcellular location

Lysosome.

Involvement in disease

Myeloperoxidase deficiency (MPOD) [MIM:254600]: A disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24 Ref.25 Ref.26 Ref.27 Ref.28

Sequence similarities

Belongs to the peroxidase family. XPO subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentLysosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainSignal
   LigandCalcium
Heme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   PTMDisulfide bond
Glycoprotein
Oxidation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

defense response

Traceable author statement Ref.26. Source: ProtInc

defense response to fungus

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 10772654. Source: BHF-UCL

hypochlorous acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle remodeling

Inferred from direct assay PubMed 10772654. Source: BHF-UCL

negative regulation of apoptotic process

Traceable author statement PubMed 10801811. Source: ProtInc

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay PubMed 10772654. Source: BHF-UCL

removal of superoxide radicals

Inferred from electronic annotation. Source: Ensembl

respiratory burst involved in defense response

Inferred from electronic annotation. Source: Ensembl

response to food

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Traceable author statement Ref.5. Source: UniProtKB

response to yeast

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentazurophil granule

Inferred from direct assay PubMed 2981589. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 10772654. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

lysosome

Traceable author statement Ref.26. Source: ProtInc

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Traceable author statement PubMed 2829220. Source: ProtInc

secretory granule

Inferred from direct assay PubMed 11907569. Source: MGI

   Molecular_functionchromatin binding

Traceable author statement PubMed 2829220. Source: ProtInc

heme binding

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from direct assay PubMed 11907569. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from direct assay PubMed 10772654. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform H17 (identifier: P05164-1)

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.
Isoform H14 (identifier: P05164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.
Isoform H7 (identifier: P05164-3)

Also known as: A;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4848 Ref.12 Ref.13
Chain49 – 74569789 kDa myeloperoxidase
PRO_0000023651
Chain155 – 74559184 kDa myeloperoxidase
PRO_0000023653
Chain165 – 745581Myeloperoxidase
PRO_0000023654
Chain165 – 278114Myeloperoxidase light chain
PRO_0000023655
Chain279 – 745467Myeloperoxidase heavy chain
PRO_0000023656

Sites

Active site2611Proton acceptor
Metal binding2621Calcium
Metal binding3341Calcium
Metal binding3361Calcium; via carbonyl oxygen
Metal binding3381Calcium
Metal binding3401Calcium
Metal binding5021Iron (heme axial ligand)
Binding site2601Heme (covalent; via 3 links)
Binding site4081Heme (covalent; via 3 links)
Binding site4091Heme (covalent; via 3 links)
Site4051Transition state stabilizer

Amino acid modifications

Modified residue3161Cysteine sulfenic acid (-SOH)
Glycosylation1391N-linked (GlcNAc...) Ref.17
Glycosylation3231N-linked (GlcNAc...) Ref.13 Ref.18
Glycosylation3551N-linked (GlcNAc...) Ref.13 Ref.19
Glycosylation3911N-linked (GlcNAc...) Ref.13 Ref.19
Glycosylation4831N-linked (GlcNAc...) Ref.13 Ref.17 Ref.18
CAR_000220
Glycosylation7291N-linked (GlcNAc...) Ref.13
Disulfide bond167 ↔ 180
Disulfide bond281 ↔ 291
Disulfide bond285 ↔ 309
Disulfide bond319Interchain
Disulfide bond387 ↔ 398
Disulfide bond606 ↔ 663
Disulfide bond704 ↔ 730

Natural variations

Alternative sequence1 – 9595Missing in isoform H14.
VSP_007206
Alternative sequence1821N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7.
VSP_007207
Natural variant531V → F. Ref.9
Corresponds to variant rs7208693 [ dbSNP | Ensembl ].
VAR_023995
Natural variant1731Y → C in MPOD; affects proteolytic processing and secretion. Ref.27
Corresponds to variant rs78950939 [ dbSNP | Ensembl ].
VAR_015377
Natural variant2511M → T in MPOD. Ref.28
Corresponds to variant rs56378716 [ dbSNP | Ensembl ].
VAR_015378
Natural variant4471R → Q in a colorectal cancer sample; somatic mutation. Ref.29
VAR_036517
Natural variant5691R → W in MPOD; suppress post-translational processing. Ref.24 Ref.25 Ref.26
VAR_015379
Natural variant6041R → C. Ref.9
Corresponds to variant rs35670089 [ dbSNP | Ensembl ].
VAR_023996
Natural variant6831E → Q. Ref.9
Corresponds to variant rs35702888 [ dbSNP | Ensembl ].
VAR_023997
Natural variant7171I → V. Ref.9
Corresponds to variant rs2759 [ dbSNP | Ensembl ].
VAR_012066

Experimental info

Sequence conflict361L → V in CAA28565. Ref.4
Sequence conflict361L → V in CAA33438. Ref.7

Secondary structure

..................................................................................................... 745
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform H17 (B) [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 348B1CE0A11038B4

FASTA74583,869
        10         20         30         40         50         60 
MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA PAVLGEVDTS 

        70         80         90        100        110        120 
LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS YFKQPVAATR TAVRAADYLH 

       130        140        150        160        170        180 
VALDLLERKL RSLWRRPFNV TDVLTPAQLN VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC 

       190        200        210        220        230        240 
NNRRSPTLGA SNRAFVRWLP AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD 

       250        260        270        280        290        300 
QLTPDQERSL MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND 

       310        320        330        340        350        360 
PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA RNLRNMSNQL 

       370        380        390        400        410        420 
GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL AGDTRSSEMP ELTSMHTLLL 

       430        440        450        460        470        480 
REHNRLATEL KSLNPRWDGE RLYQEARKIV GAMVQIITYR DYLPLVLGPT AMRKYLPTYR 

       490        500        510        520        530        540 
SYNDSVDPRI ANVFTNAFRY GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE 

       550        560        570        580        590        600 
GGIDPILRGL MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN 

       610        620        630        640        650        660 
AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP LKRKGRVGPL 

       670        680        690        700        710        720 
LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP RIICDNTGIT TVSKNNIFMS 

       730        740 
NSYPRDFVNC STLPALNLAS WREAS 

« Hide

Isoform H14 [UniParc].

Checksum: 7A29F89DFE6B4916
Show »

FASTA65073,854
Isoform H7 (A) [UniParc].

Checksum: F15BC771A9C6F6A6
Show »

FASTA77787,248

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
[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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-447.
+Additional computationally mapped references.

Web resources

MPObase

MPO mutation db

NIEHS-SNPs
Wikipedia

Myeloperoxidase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02694 mRNA. Translation: AAA59896.1.
M17176 expand/collapse EMBL AC list , 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.
PIROPHUM. A29467.
B28894.
D28894.
RefSeqNP_000241.1. NM_000250.1.
UniGeneHs.458272.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP05164.
SMRP05164. Positions 157-744.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110493. 2 interactions.
IntActP05164. 3 interactions.
MINTMINT-1522833.
STRING9606.ENSP00000225275.

Chemistry

BindingDBP05164.
ChEMBLCHEMBL2439.
DrugBankDB00535. Cefdinir.

Protein family/group databases

PeroxiBase3315. HsMPO.

PTM databases

PhosphoSiteP05164.
UniCarbKBP05164.

Polymorphism databases

DMDM129825.

Proteomic databases

PaxDbP05164.
PRIDEP05164.

Protocols and materials databases

DNASU4353.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225275; ENSP00000225275; ENSG00000005381. [P05164-1]
ENST00000340482; ENSP00000344419; ENSG00000005381. [P05164-3]
GeneID4353.
KEGGhsa:4353.
UCSCuc002ivu.1. human. [P05164-1]

Organism-specific databases

CTD4353.
GeneCardsGC17M056347.
H-InvDBHIX0039242.
HGNCHGNC:7218. MPO.
HPACAB000059.
HPA021147.
MIM254600. phenotype.
606989. gene.
neXtProtNX_P05164.
Orphanet2587. Myeloperoxidase deficiency.
PharmGKBPA243.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262194.
HOGENOMHOG000016084.
HOVERGENHBG000071.
KOK10789.
OMAQDKYRTI.
OrthoDBEOG7M0NQW.
PhylomeDBP05164.
TreeFamTF314316.

Enzyme and pathway databases

BioCycMetaCyc:HS00140-MONOMER.

Gene expression databases

ArrayExpressP05164.
BgeeP05164.
CleanExHS_MPO.
GenevestigatorP05164.

Family and domain databases

Gene3D1.10.640.10. 2 hits.
InterProIPR010255. Haem_peroxidase.
IPR002007. Haem_peroxidase_animal.
IPR019791. Haem_peroxidase_animal_subgr.
[Graphical view]
PfamPF03098. An_peroxidase. 1 hit.
[Graphical view]
PRINTSPR00457. ANPEROXIDASE.
SUPFAMSSF48113. SSF48113. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS50292. PEROXIDASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMPO. human.
EvolutionaryTraceP05164.
GeneWikiMyeloperoxidase.
GenomeRNAi4353.
NextBio17126.
PMAP-CutDBP05164.
PROP05164.
SOURCESearch...

Entry information

Entry namePERM_HUMAN
AccessionPrimary (citable) accession number: P05164
Secondary accession number(s): A1L4B8 expand/collapse secondary AC list , Q14862, Q4PJH5, Q9UCL7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM