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Protein

Myeloperoxidase

Gene

MPO

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

Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide
LigandCalcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00140-MONOMER
BRENDAi1.11.2.2 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
SIGNORiP05164

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

EuPathDBiHostDB:ENSG00000005381.7
HGNCiHGNC:7218 MPO
MIMi606989 gene
neXtProtiNX_P05164

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Myeloperoxidase deficiency (MPOD)5 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 dbSNP:rs78950939EnsemblClinVar.1
Natural variantiVAR_015378251M → T in MPOD. 1 PublicationCorresponds to variant dbSNP:rs56378716EnsemblClinVar.1
Natural variantiVAR_015379569R → W in MPOD; suppress post-translational processing. 3 PublicationsCorresponds to variant dbSNP:rs119468010EnsemblClinVar.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
DB05161 Elafin
DB01225 Enoxaparin
DB04827 Ethyl carbamate
DB00062 Human Serum Albumin
DB00583 L-Carnitine
DB01065 Melatonin
DB00244 Mesalazine
DB00461 Nabumetone
DB04821 Nomifensine
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...) asparagine1 Publication1
Disulfide bondi167 ↔ 180
Disulfide bondi281 ↔ 291
Disulfide bondi285 ↔ 309
Modified residuei316Cysteine sulfenic acid (-SOH)1 Publication1
Disulfide bondi319Interchain
Glycosylationi323N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi355N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi387 ↔ 398
Glycosylationi391N-linked (GlcNAc...) asparagine2 Publications1
GlycosylationiCAR_000220483N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi606 ↔ 663
Disulfide bondi704 ↔ 730
Glycosylationi729N-linked (GlcNAc...) asparagine1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Oxidation

Proteomic databases

EPDiP05164
PaxDbiP05164
PeptideAtlasiP05164
PRIDEiP05164
ProteomicsDBi51811
51812 [P05164-2]
51813 [P05164-3]

PTM databases

GlyConnecti428
iPTMnetiP05164
PhosphoSitePlusiP05164
SwissPalmiP05164
UniCarbKBiP05164

Miscellaneous databases

PMAP-CutDBiP05164

Expressioni

Gene expression databases

BgeeiENSG00000005381 Expressed in 99 organ(s), highest expression level in bone marrow cell
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
CORUMiP05164
IntActiP05164, 3 interactors
MINTiP05164
STRINGi9606.ENSP00000225275

Chemistry databases

BindingDBiP05164

Structurei

Secondary structure

1745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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, 1 hit
InterProiView protein in InterPro
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf
IPR029609 MPO
PANTHERiPTHR11475:SF108 PTHR11475:SF108, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit

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

This entry has 3 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QSF7J3QSF7_HUMAN
Myeloperoxidase
MPO
86Annotation score:

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 → F1 PublicationCorresponds to variant dbSNP:rs7208693Ensembl.1
Natural variantiVAR_015377173Y → C in MPOD; affects proteolytic processing and secretion. 1 PublicationCorresponds to variant dbSNP:rs78950939EnsemblClinVar.1
Natural variantiVAR_015378251M → T in MPOD. 1 PublicationCorresponds to variant dbSNP:rs56378716EnsemblClinVar.1
Natural variantiVAR_036517447R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs762688992Ensembl.1
Natural variantiVAR_015379569R → W in MPOD; suppress post-translational processing. 3 PublicationsCorresponds to variant dbSNP:rs119468010EnsemblClinVar.1
Natural variantiVAR_023996604R → C1 PublicationCorresponds to variant dbSNP:rs35670089Ensembl.1
Natural variantiVAR_023997683E → Q1 PublicationCorresponds to variant dbSNP:rs35702888Ensembl.1
Natural variantiVAR_012066717I → V1 PublicationCorresponds to variant dbSNP:rs2759Ensembl.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

Similar proteinsi

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[»]
5MFAX-ray1.20A49-745[»]
5UZUX-ray2.40A167-744[»]
6AZPX-ray2.29A167-743[»]
6BMTX-ray2.40A1-745[»]
ProteinModelPortaliP05164
SMRiP05164
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110493, 6 interactors
CORUMiP05164
IntActiP05164, 3 interactors
MINTiP05164
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
DB05161 Elafin
DB01225 Enoxaparin
DB04827 Ethyl carbamate
DB00062 Human Serum Albumin
DB00583 L-Carnitine
DB01065 Melatonin
DB00244 Mesalazine
DB00461 Nabumetone
DB04821 Nomifensine
DB00104 Octreotide
DB00526 Oxaliplatin
DB00550 Propylthiouracil
DB00208 Ticlopidine
DB06823 Tiopronin
DB00500 Tolmetin
GuidetoPHARMACOLOGYi2789

Protein family/group databases

PeroxiBasei3315 HsMPO

PTM databases

GlyConnecti428
iPTMnetiP05164
PhosphoSitePlusiP05164
SwissPalmiP05164
UniCarbKBiP05164

Polymorphism and mutation databases

BioMutaiMPO
DMDMi129825

Proteomic databases

EPDiP05164
PaxDbiP05164
PeptideAtlasiP05164
PRIDEiP05164
ProteomicsDBi51811
51812 [P05164-2]
51813 [P05164-3]

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
EuPathDBiHostDB:ENSG00000005381.7
GeneCardsiMPO
H-InvDBiHIX0039242
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
BRENDAi1.11.2.2 2681
ReactomeiR-HSA-6798695 Neutrophil degranulation
SIGNORiP05164

Miscellaneous databases

ChiTaRSiMPO human
EvolutionaryTraceiP05164
GeneWikiiMyeloperoxidase
GenomeRNAii4353
PMAP-CutDBiP05164
PROiPR:P05164
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000005381 Expressed in 99 organ(s), highest expression level in bone marrow cell
CleanExiHS_MPO
ExpressionAtlasiP05164 baseline and differential
GenevisibleiP05164 HS

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR010255 Haem_peroxidase
IPR019791 Haem_peroxidase_animal
IPR037120 Haem_peroxidase_sf
IPR029609 MPO
PANTHERiPTHR11475:SF108 PTHR11475:SF108, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPERM_HUMAN
AccessioniPrimary (citable) accession number: P05164
Secondary accession number(s): A1L4B8
, Q14862, Q4PJH5, Q9UCL7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 7, 2018
This is version 214 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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