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Entry version 136 (25 May 2022)
Sequence version 1 (01 Feb 1997)
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Protein

HPr kinase/phosphorylase

Gene

hprK

Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Is a metabolite-sensitive enzyme that catalyzes the ATP-as well as probably the pyrophosphate-dependent phosphorylation of Ser-47 in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The regulatory role of HPrK/P in the physiology of M.pneumoniae is not known yet.

Miscellaneous

Both phosphorylation and phosphorolysis are carried out by the same active site and suggest a common mechanism for both reactions.
Contrary to HPrK/P of other bacteria, that of M.pneumoniae has a very high affinity for ATP (Kd=5.3 microM), explaining kinase activity even at low ATP concentrations.

Caution

Was originally (PubMed:12368461 and PubMed:12589763) called HPr kinase/phosphatase, but P-Ser-HPr dephosphorylation was shown in several bacteria to follow a quite unique mechanism, in which Pi instead of H2O is used for the nucleophilic attack on the phosphoryl group. P-Ser-HPr dephosphorylation is therefore not a phosphohydrolysis but a phospho-phosphorolysis reaction, and the bifunctional enzyme was dubbed HPr kinase/phosphorylase.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Contrary to HPrK/P of B.subtilis and other bacteria, that of M.pneumoniae is active as a kinase at very low ATP concentrations in the absence of fructose 1,6-bisphosphate (FBP). Kinase activity is slightly activated by FBP, and inhibited by inorganic phosphate (Pi), but FBP prevents kinase inhibition by Pi. Dephosphorylation of P-Ser-HPr by M.pneumoniae HPrK/P is strictly dependent on the presence of Pi, and is inhibited by FBP. This unique mode of control of HPrK/P activity is proposed to reflect the parasitic lifestyle of M.pneumoniae, that is strictly adapted to its ecological niche on nutrient-rich human mucous membranes.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei139By similarity1
Active sitei160By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi161MagnesiumCurated1
Active sitei178Proton acceptor; for phosphorylation activity. Proton donor; for dephosphorylation activityBy similarity1
Metal bindingi202MagnesiumSequence analysis1
Active sitei245By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi154 – 161ATPCurated8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
HPr kinase/phosphorylase (EC:2.7.11.-, EC:2.7.4.-)
Short name:
HPrK/P
Alternative name(s):
HPr kinase/phosphatase
HPr(Ser) kinase/phosphorylase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:hprK
Synonyms:ptsK
Ordered Locus Names:MPN_223
ORF Names:MP608
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycoplasma pneumoniae (strain ATCC 29342 / M129)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri272634 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000808 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi140G → A: Kinase activity not affected and 6-fold increase in phosphorylase activity. 1 Publication1
Mutagenesisi154G → A: 4-fold reduction in kinase activity and loss of phosphorylase activity; 8-fold reduction in ATP affinity. 1 Publication1
Mutagenesisi156S → A: Kinase activity not affected and 4-fold increase in phosphorylase activity. 1 Publication1
Mutagenesisi156S → T: 4-fold reduction in kinase activity and loss of phosphorylase activity. 1 Publication1
Mutagenesisi157G → A: 4-fold reduction in kinase activity and strongly reduced phosphorylase activity. 1 Publication1
Mutagenesisi159G → A: Loss of both kinase and phosphorylase activities; no ATP binding. 1 Publication1
Mutagenesisi160K → A: Loss of both kinase and phosphorylase activities; no ATP binding. 1 Publication1
Mutagenesisi160K → R: Loss of both kinase and phosphorylase activities. 1 Publication1
Mutagenesisi161S → A: 10-fold reduction in kinase activity and loss of phosphorylase activity; affinity for ATP is only slightly affected. 1 Publication1
Mutagenesisi161S → T: 2-fold reduction in kinase activity and strongly reduced phosphorylase activity; binds ATP with high affinity. 1 Publication1
Mutagenesisi162E → D: Kinase activity not affected and loss of phosphorylase activity. 1 Publication1
Mutagenesisi204R → K: Kinase activity not affected and strongly reduced phosphorylase activity; ATP binding not affected. 1 Publication1
Mutagenesisi207G → A: Loss of both kinase and phosphorylase activities; ATP binding not affected. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000589731 – 312HPr kinase/phosphorylaseAdd BLAST312

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homohexamer, arranged as bilayered trimers.

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
P75548, 4 interactors

STRING: functional protein association networks

More...
STRINGi
272634.MPN_223

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P75548

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P75548

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P75548

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni201 – 210Important for the catalytic mechanism of both phosphorylation and dephosphorylation10
Regioni266 – 271Important for the catalytic mechanism of dephosphorylationBy similarity6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Walker A ATP-binding motif also binds Pi and PPi.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HPrK/P family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_052030_0_1_14

Identification of Orthologs from Complete Genome Data

More...
OMAi
AMNNRQK

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01918, HprK_C, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1390.20, 1 hit
3.40.50.300, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01249, HPr_kinase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003755, HPr(Ser)_kin/Pase
IPR011104, Hpr_kin/Pase_C
IPR011126, Hpr_kin/Pase_Hpr_N
IPR027417, P-loop_NTPase
IPR028979, Ser_kin/Pase_Hpr-like_N_sf

The PANTHER Classification System

More...
PANTHERi
PTHR30305:SF1, PTHR30305:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07475, Hpr_kinase_C, 1 hit
PF02603, Hpr_kinase_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF75138, SSF75138, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00679, hpr-ser, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P75548-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKLLVKELI EQFQDCVNLI DGHTNTSNVI RVPGLKRVVF EMLGLFSSQI
60 70 80 90 100
GSVAILGKRE FGFLSQKTLV EQQQILHNLL KLNPPAIILT KSFTDPTVLL
110 120 130 140 150
QVNQTYQVPI LKTDFFSTEL SFTVETYINE QFATVAQIHG VLLEVFGVGV
160 170 180 190 200
LLTGRSGIGK SECALDLINK NHLFVGDDAI EIYRLGNRLF GRAQEVAKKF
210 220 230 240 250
MEIRGLGIIN VERFYGLQIT KQRTEIQLMV NLLSLEKQTT VTFERLGTEL
260 270 280 290 300
KKQRLLGVDL SFYEIPISPG RKTSEIIESA VIDFKLKHSG YNSALDFIEN
310
QKAILKRKKD ES
Length:312
Mass (Da):35,234
Last modified:February 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i475F6B73587517C1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U00089 Genomic DNA Translation: AAB96256.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S73934

NCBI Reference Sequences

More...
RefSeqi
NP_109911.1, NC_000912.1
WP_010874580.1, NC_000912.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAB96256; AAB96256; MPN_223

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
66609131

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mpn:MPN_223

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|272634.6.peg.242

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00089 Genomic DNA Translation: AAB96256.1
PIRiS73934
RefSeqiNP_109911.1, NC_000912.1
WP_010874580.1, NC_000912.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KNXX-ray2.50A/B/C/D/E/F1-312[»]
AlphaFoldDBiP75548
SMRiP75548
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiP75548, 4 interactors
STRINGi272634.MPN_223

Genome annotation databases

EnsemblBacteriaiAAB96256; AAB96256; MPN_223
GeneIDi66609131
KEGGimpn:MPN_223
PATRICifig|272634.6.peg.242

Phylogenomic databases

HOGENOMiCLU_052030_0_1_14
OMAiAMNNRQK

Miscellaneous databases

EvolutionaryTraceiP75548

Family and domain databases

CDDicd01918, HprK_C, 1 hit
Gene3Di3.40.1390.20, 1 hit
3.40.50.300, 1 hit
HAMAPiMF_01249, HPr_kinase, 1 hit
InterProiView protein in InterPro
IPR003755, HPr(Ser)_kin/Pase
IPR011104, Hpr_kin/Pase_C
IPR011126, Hpr_kin/Pase_Hpr_N
IPR027417, P-loop_NTPase
IPR028979, Ser_kin/Pase_Hpr-like_N_sf
PANTHERiPTHR30305:SF1, PTHR30305:SF1, 1 hit
PfamiView protein in Pfam
PF07475, Hpr_kinase_C, 1 hit
PF02603, Hpr_kinase_N, 1 hit
SUPFAMiSSF75138, SSF75138, 1 hit
TIGRFAMsiTIGR00679, hpr-ser, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHPRK_MYCPN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P75548
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: May 25, 2022
This is version 136 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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