Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myeloperoxidase

Gene

MPO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

Cl- + H2O2 + H+ = HClO + H2O.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 1 Ca2+ ion per monomer.
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei260Heme (covalent; via 3 links)1
Active sitei261Proton acceptor1
Metal bindingi262Calcium1
Metal bindingi334Calcium1
Metal bindingi336Calcium; via carbonyl oxygen1
Metal bindingi338Calcium1
Metal bindingi340Calcium1
Sitei405Transition state stabilizer1
Binding sitei408Heme (covalent; via 3 links)1
Binding sitei409Heme (covalent; via 3 links)1
Metal bindingi502Iron (heme axial ligand)1

GO - Molecular functioni

  • chromatin binding Source: ProtInc
  • heme binding Source: InterPro
  • heparin binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • peroxidase activity Source: BHF-UCL

GO - Biological processi

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.
ZFISH:HS00140-MONOMER.
BRENDAi1.11.2.2. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Protein family/group databases

PeroxiBasei3315. HsMPO.

Names & Taxonomyi

Protein namesi
Recommended name:
Myeloperoxidase (EC:1.11.2.21 Publication)
Short name:
MPO
Cleaved into the following 5 chains:
Gene namesi
Name:MPO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:7218. MPO.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • lysosome Source: ProtInc
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
  • secretory granule Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Myeloperoxidase deficiency (MPOD)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by decreased myeloperoxidase activity in neutrophils and monocytes that results in disseminated candidiasis.
See also OMIM:254600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015377173Y → C in MPOD; affects proteolytic processing and secretion. 1 PublicationCorresponds to variant rs78950939dbSNPEnsembl.1
Natural variantiVAR_015378251M → T in MPOD. 1 PublicationCorresponds to variant rs56378716dbSNPEnsembl.1
Natural variantiVAR_015379569R → W in MPOD; suppress post-translational processing. 3 PublicationsCorresponds to variant rs119468010dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4353.
MalaCardsiMPO.
MIMi254600. phenotype.
OpenTargetsiENSG00000005381.
Orphaneti2587. Myeloperoxidase deficiency.
PharmGKBiPA243.

Chemistry databases

ChEMBLiCHEMBL2439.
DrugBankiDB00233. Aminosalicylic Acid.
DB00006. Bivalirudin.
DB02300. Calcipotriol.
DB06774. Capsaicin.
DB00958. Carboplatin.
DB00833. Cefaclor.
DB00535. Cefdinir.
DB00515. Cisplatin.
DB00847. Cysteamine.
DB00250. Dapsone.
DB01225. Enoxaparin.
DB00062. Human Serum Albumin.
DB00583. L-Carnitine.
DB01065. Melatonin.
DB00244. Mesalazine.
DB00461. Nabumetone.
DB00104. Octreotide.
DB00526. Oxaliplatin.
DB00550. Propylthiouracil.
DB00208. Ticlopidine.
DB06823. Tiopronin.
DB00500. Tolmetin.
GuidetoPHARMACOLOGYi2789.

Polymorphism and mutation databases

BioMutaiMPO.
DMDMi129825.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 482 PublicationsAdd BLAST48
ChainiPRO_000002365149 – 74589 kDa myeloperoxidaseAdd BLAST697
ChainiPRO_0000023653155 – 74584 kDa myeloperoxidaseAdd BLAST591
ChainiPRO_0000023654165 – 745MyeloperoxidaseAdd BLAST581
ChainiPRO_0000023655165 – 278Myeloperoxidase light chainAdd BLAST114
ChainiPRO_0000023656279 – 745Myeloperoxidase heavy chainAdd BLAST467

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi139N-linked (GlcNAc...)1 Publication1
Disulfide bondi167 ↔ 180
Disulfide bondi281 ↔ 291
Disulfide bondi285 ↔ 309
Modified residuei316Cysteine sulfenic acid (-SOH)1 Publication1
Disulfide bondi319Interchain
Glycosylationi323N-linked (GlcNAc...)2 Publications1
Glycosylationi355N-linked (GlcNAc...)2 Publications1
Disulfide bondi387 ↔ 398
Glycosylationi391N-linked (GlcNAc...)2 Publications1
GlycosylationiCAR_000220483N-linked (GlcNAc...)3 Publications1
Modified residuei516Nitrated tyrosineBy similarity1
Disulfide bondi606 ↔ 663
Disulfide bondi704 ↔ 730
Glycosylationi729N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration, Oxidation

Proteomic databases

EPDiP05164.
PaxDbiP05164.
PeptideAtlasiP05164.
PRIDEiP05164.

PTM databases

iPTMnetiP05164.
PhosphoSitePlusiP05164.
SwissPalmiP05164.
UniCarbKBiP05164.

Miscellaneous databases

PMAP-CutDBP05164.

Expressioni

Gene expression databases

BgeeiENSG00000005381.
CleanExiHS_MPO.
ExpressionAtlasiP05164. baseline and differential.
GenevisibleiP05164. HS.

Organism-specific databases

HPAiCAB000059.
HPA021147.
HPA061464.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110493. 6 interactors.
IntActiP05164. 3 interactors.
MINTiMINT-1522833.
STRINGi9606.ENSP00000225275.

Chemistry databases

BindingDBiP05164.

Structurei

Secondary structure

1745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi181 – 185Combined sources5
Turni186 – 189Combined sources4
Beta strandi191 – 194Combined sources4
Beta strandi206 – 208Combined sources3
Beta strandi218 – 223Combined sources6
Helixi227 – 234Combined sources8
Helixi239 – 241Combined sources3
Beta strandi244 – 249Combined sources6
Helixi250 – 263Combined sources14
Turni281 – 283Combined sources3
Beta strandi317 – 319Combined sources3
Beta strandi323 – 325Combined sources3
Beta strandi329 – 331Combined sources3
Beta strandi335 – 338Combined sources4
Helixi340 – 343Combined sources4
Helixi347 – 352Combined sources6
Beta strandi357 – 360Combined sources4
Beta strandi371 – 374Combined sources4
Helixi386 – 389Combined sources4
Turni392 – 394Combined sources3
Beta strandi401 – 403Combined sources3
Turni404 – 407Combined sources4
Helixi410 – 433Combined sources24
Helixi439 – 460Combined sources22
Helixi463 – 467Combined sources5
Helixi469 – 475Combined sources7
Helixi494 – 497Combined sources4
Helixi498 – 504Combined sources7
Beta strandi507 – 510Combined sources4
Beta strandi516 – 518Combined sources3
Beta strandi523 – 526Combined sources4
Helixi527 – 529Combined sources3
Turni530 – 532Combined sources3
Helixi534 – 539Combined sources6
Helixi544 – 551Combined sources8
Beta strandi552 – 556Combined sources5
Helixi566 – 569Combined sources4
Turni573 – 576Combined sources4
Beta strandi577 – 579Combined sources3
Helixi583 – 593Combined sources11
Helixi599 – 605Combined sources7
Helixi614 – 621Combined sources8
Helixi624 – 634Combined sources11
Helixi637 – 639Combined sources3
Helixi642 – 648Combined sources7
Beta strandi655 – 657Combined sources3
Helixi659 – 674Combined sources16
Turni683 – 685Combined sources3
Helixi688 – 694Combined sources7
Helixi699 – 706Combined sources8
Beta strandi711 – 713Combined sources3
Turni717 – 719Combined sources3
Turni723 – 726Combined sources4
Beta strandi727 – 729Combined sources3
Helixi730 – 732Combined sources3
Helixi739 – 741Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FIWX-ray1.70A/B167-271[»]
C/D279-744[»]
ProteinModelPortaliP05164.
SMRiP05164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05164.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP05164.
KOiK10789.
OMAiKSSGCAY.
OrthoDBiEOG091G02JC.
PhylomeDBiP05164.
TreeFamiTF314316.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029609. MPO.
[Graphical view]
PANTHERiPTHR11475:SF49. PTHR11475:SF49. 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. AlignAdd to basket

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

        10         20         30         40         50
MGVPFFSSLR CMVDLGPCWA GGLTAEMKLL LALAGLLAIL ATPQPSEGAA
60 70 80 90 100
PAVLGEVDTS LVLSSMEEAK QLVDKAYKER RESIKQRLRS GSASPMELLS
110 120 130 140 150
YFKQPVAATR TAVRAADYLH VALDLLERKL RSLWRRPFNV TDVLTPAQLN
160 170 180 190 200
VLSKSSGCAY QDVGVTCPEQ DKYRTITGMC NNRRSPTLGA SNRAFVRWLP
210 220 230 240 250
AEYEDGFSLP YGWTPGVKRN GFPVALARAV SNEIVRFPTD QLTPDQERSL
260 270 280 290 300
MFMQWGQLLD HDLDFTPEPA ARASFVTGVN CETSCVQQPP CFPLKIPPND
310 320 330 340 350
PRIKNQADCI PFFRSCPACP GSNITIRNQI NALTSFVDAS MVYGSEEPLA
360 370 380 390 400
RNLRNMSNQL GLLAVNQRFQ DNGRALLPFD NLHDDPCLLT NRSARIPCFL
410 420 430 440 450
AGDTRSSEMP ELTSMHTLLL REHNRLATEL KSLNPRWDGE RLYQEARKIV
460 470 480 490 500
GAMVQIITYR DYLPLVLGPT AMRKYLPTYR SYNDSVDPRI ANVFTNAFRY
510 520 530 540 550
GHTLIQPFMF RLDNRYQPME PNPRVPLSRV FFASWRVVLE GGIDPILRGL
560 570 580 590 600
MATPAKLNRQ NQIAVDEIRE RLFEQVMRIG LDLPALNMQR SRDHGLPGYN
610 620 630 640 650
AWRRFCGLPQ PETVGQLGTV LRNLKLARKL MEQYGTPNNI DIWMGGVSEP
660 670 680 690 700
LKRKGRVGPL LACIIGTQFR KLRDGDRFWW ENEGVFSMQQ RQALAQISLP
710 720 730 740
RIICDNTGIT TVSKNNIFMS NSYPRDFVNC STLPALNLAS WREAS
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)DescriptionActionsGraphical viewLength
Sequence conflicti36L → V in CAA28565 (PubMed:3031585).Curated1
Sequence conflicti36L → V in CAA33438 (PubMed:2552418).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02399553V → F.1 PublicationCorresponds to variant rs7208693dbSNPEnsembl.1
Natural variantiVAR_015377173Y → C in MPOD; affects proteolytic processing and secretion. 1 PublicationCorresponds to variant rs78950939dbSNPEnsembl.1
Natural variantiVAR_015378251M → T in MPOD. 1 PublicationCorresponds to variant rs56378716dbSNPEnsembl.1
Natural variantiVAR_036517447R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs762688992dbSNPEnsembl.1
Natural variantiVAR_015379569R → W in MPOD; suppress post-translational processing. 3 PublicationsCorresponds to variant rs119468010dbSNPEnsembl.1
Natural variantiVAR_023996604R → C.1 PublicationCorresponds to variant rs35670089dbSNPEnsembl.1
Natural variantiVAR_023997683E → Q.1 PublicationCorresponds to variant rs35702888dbSNPEnsembl.1
Natural variantiVAR_012066717I → V.1 PublicationCorresponds to variant rs2759dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0072061 – 95Missing in isoform H14. 1 PublicationAdd BLAST95
Alternative sequenceiVSP_007207182N → NRCGWLGVAAGTGLREASRT PQASRCQRPVLPC in isoform H7. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FIWX-ray1.70A/B167-271[»]
C/D279-744[»]
ProteinModelPortaliP05164.
SMRiP05164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110493. 6 interactors.
IntActiP05164. 3 interactors.
MINTiMINT-1522833.
STRINGi9606.ENSP00000225275.

Chemistry databases

BindingDBiP05164.
ChEMBLiCHEMBL2439.
DrugBankiDB00233. Aminosalicylic Acid.
DB00006. Bivalirudin.
DB02300. Calcipotriol.
DB06774. Capsaicin.
DB00958. Carboplatin.
DB00833. Cefaclor.
DB00535. Cefdinir.
DB00515. Cisplatin.
DB00847. Cysteamine.
DB00250. Dapsone.
DB01225. Enoxaparin.
DB00062. Human Serum Albumin.
DB00583. L-Carnitine.
DB01065. Melatonin.
DB00244. Mesalazine.
DB00461. Nabumetone.
DB00104. Octreotide.
DB00526. Oxaliplatin.
DB00550. Propylthiouracil.
DB00208. Ticlopidine.
DB06823. Tiopronin.
DB00500. Tolmetin.
GuidetoPHARMACOLOGYi2789.

Protein family/group databases

PeroxiBasei3315. HsMPO.

PTM databases

iPTMnetiP05164.
PhosphoSitePlusiP05164.
SwissPalmiP05164.
UniCarbKBiP05164.

Polymorphism and mutation databases

BioMutaiMPO.
DMDMi129825.

Proteomic databases

EPDiP05164.
PaxDbiP05164.
PeptideAtlasiP05164.
PRIDEiP05164.

Protocols and materials databases

DNASUi4353.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4353.
DisGeNETi4353.
GeneCardsiMPO.
H-InvDBHIX0039242.
HGNCiHGNC:7218. MPO.
HPAiCAB000059.
HPA021147.
HPA061464.
MalaCardsiMPO.
MIMi254600. phenotype.
606989. gene.
neXtProtiNX_P05164.
OpenTargetsiENSG00000005381.
Orphaneti2587. Myeloperoxidase deficiency.
PharmGKBiPA243.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2408. Eukaryota.
ENOG410XPZ3. LUCA.
GeneTreeiENSGT00550000074325.
HOGENOMiHOG000016084.
HOVERGENiHBG000071.
InParanoidiP05164.
KOiK10789.
OMAiKSSGCAY.
OrthoDBiEOG091G02JC.
PhylomeDBiP05164.
TreeFamiTF314316.

Enzyme and pathway databases

BioCyciMetaCyc:HS00140-MONOMER.
ZFISH:HS00140-MONOMER.
BRENDAi1.11.2.2. 2681.
ReactomeiR-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiMPO. human.
EvolutionaryTraceiP05164.
GeneWikiiMyeloperoxidase.
GenomeRNAii4353.
PMAP-CutDBP05164.
PROiP05164.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005381.
CleanExiHS_MPO.
ExpressionAtlasiP05164. baseline and differential.
GenevisibleiP05164. HS.

Family and domain databases

Gene3Di1.10.640.10. 2 hits.
InterProiIPR010255. Haem_peroxidase.
IPR019791. Haem_peroxidase_animal.
IPR029609. MPO.
[Graphical view]
PANTHERiPTHR11475:SF49. PTHR11475:SF49. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 199 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.