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P05164

- PERM_HUMAN

UniProt

P05164 - PERM_HUMAN

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Protein
Myeloperoxidase
Gene
MPO
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
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. 3 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 Publications
Add
BLAST
Chaini49 – 74569789 kDa myeloperoxidase
PRO_0000023651Add
BLAST
Chaini155 – 74559184 kDa myeloperoxidase
PRO_0000023653Add
BLAST
Chaini165 – 745581Myeloperoxidase
PRO_0000023654Add
BLAST
Chaini165 – 278114Myeloperoxidase light chain
PRO_0000023655Add
BLAST
Chaini279 – 745467Myeloperoxidase heavy chain
PRO_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)
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 Publications
CAR_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

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.

Miscellaneous databases

EvolutionaryTraceiP05164.

Family & Domainsi

Sequence similaritiesi

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

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. 3 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.
VSP_007206Add
BLAST
Alternative sequencei182 – 1821N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7.
VSP_007207

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361L → V in CAA28565. 1 Publication
Sequence conflicti36 – 361L → V in CAA33438. 1 Publication

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]
ENST00000340482; ENSP00000344419; ENSG00000005381. [P05164-3]
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 ]
ENST00000340482 ; ENSP00000344419 ; ENSG00000005381 . [P05164-3 ]
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

« Hide 'large scale' publications
  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.
  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: September 3, 2014
This is version 174 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

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