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Entry version 207 (18 Sep 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Peroxiredoxin-6

Gene

PRDX6

Organism
Homo sapiens (Human)
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

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis.2 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this 1-Cys peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide with a cysteine from another protein or with a small thiol molecule. C(P) is reactivated by glutathionylation mediated by glutathione S-transferase Pi, followed by spontaneous reduction of the enzyme with glutathione.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei32Important for phospholipase activity1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei47Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity3 Publications1
Active sitei140For phospholipase activityBy similarity1

<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 functionAntioxidant, Hydrolase, Multifunctional enzyme, Oxidoreductase, Peroxidase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.11.1.15 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-6798695 Neutrophil degranulation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P30041

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
P30041 Curated

MoonProt database of moonlighting proteins

More...
MoonProti
P30041

PeroxiBase, a peroxidase database

More...
PeroxiBasei
4426 Hs1CysPrx01

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001691

<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_and_taxonomy_section">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:
Peroxiredoxin-6 (EC:1.11.1.152 Publications)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
24 kDa protein
Acidic calcium-independent phospholipase A2 (EC:3.1.1.41 Publication)
Short name:
aiPLA2
Antioxidant protein 2
Liver 2D page spot 40
Non-selenium glutathione peroxidase
Short name:
NSGPx
Red blood cells page spot 12
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:PRDX6
Synonyms:AOP2, KIAA0106
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:16753 PRDX6

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602316 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P30041

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lysosome

<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_and_biotech_section">'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>Mutagenesisi32S → A: Loss of phospholipase activity, but no effect on peroxidase activity. 1 Publication1
Mutagenesisi47C → S: Loss of peroxidase activity, but no effect on phospholipase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
9588

Open Targets

More...
OpenTargetsi
ENSG00000117592

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134992760

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03814 2-(N-Morpholino)-Ethanesulfonic Acid
DB09130 Copper
DB02325 Isopropyl alcohol

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PRDX6

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1718024

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources4 Publications
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001351022 – 224Peroxiredoxin-6Add BLAST223

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei44PhosphothreonineCombined sources1
Modified residuei63N6-acetyllysineCombined sources1
Modified residuei89PhosphotyrosineCombined sources1
Modified residuei177Phosphothreonine; by MAPKBy similarity1
Modified residuei209N6-acetyllysine; alternateCombined sources1
Modified residuei209N6-succinyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO2H) and sulfonic acid (Cys-SO3H) forms upon oxidative stress.2 Publications
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-117
CPTAC-118

Encyclopedia of Proteome Dynamics

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EPDi
P30041

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P30041

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P30041

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P30041

PeptideAtlas

More...
PeptideAtlasi
P30041

PRoteomics IDEntifications database

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PRIDEi
P30041

ProteomicsDB human proteome resource

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ProteomicsDBi
54620

Consortium for Top Down Proteomics

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TopDownProteomicsi
P30041

2D gel databases

DOSAC-COBS 2D-PAGE database

More...
DOSAC-COBS-2DPAGEi
P30041

USC-OGP 2-DE database

More...
OGPi
P30041

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00220301
P30041

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P30041

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P30041

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P30041

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P30041

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P30041

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000117592 Expressed in 241 organ(s), highest expression level in amniotic fluid

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P30041 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P30041 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008663
HPA006983

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:9587003, PubMed:27353378).

Interacts with GSTP1; mediates PRDX6 glutathionylation and regeneration (By similarity).

Interacts with APEX1 (PubMed:19188445).

Interacts with STH (PubMed:16186110). May interact with FAM168B (PubMed:20716133). May interact with HTR2A (By similarity).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
114956, 110 interactors

Protein interaction database and analysis system

More...
IntActi
P30041, 35 interactors

Molecular INTeraction database

More...
MINTi
P30041

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000342026

<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

1224
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P30041

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P30041

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 169ThioredoxinPROSITE-ProRule annotationAdd BLAST165

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>Regioni31 – 40Required and sufficient for targeting to lysosomes and lamellar bodiesBy similarity10

<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 peroxiredoxin family. Prx6 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0854 Eukaryota
COG0450 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074794

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000022346

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P30041

KEGG Orthology (KO)

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KOi
K11188

Identification of Orthologs from Complete Genome Data

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OMAi
YPIIADD

Database of Orthologous Groups

More...
OrthoDBi
1129256at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P30041

TreeFam database of animal gene trees

More...
TreeFami
TF105183

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000866 AhpC/TSA
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
IPR013766 Thioredoxin_domain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF10417 1-cysPrx_C, 1 hit
PF00578 AhpC-TSA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000239 AHPC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52833 SSF52833, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51352 THIOREDOXIN_2, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P30041-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE
60 70 80 90 100
LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF
110 120 130 140 150
PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP
160 170 180 190 200
ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK
210 220
LFPKGVFTKE LPSGKKYLRY TPQP
Length:224
Mass (Da):25,035
Last modified:January 23, 2007 - v3
<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:i017D955F0FEEDFBC
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
D14662 mRNA Translation: BAA03496.1
DQ230990 Genomic DNA Translation: ABB02185.1
AL139142 Genomic DNA No translation available.
AK289352 mRNA Translation: BAF82041.1
CH471067 Genomic DNA Translation: EAW90944.1
BC035857 mRNA Translation: AAH35857.1
BC053550 mRNA Translation: AAH53550.1
AJ844621 mRNA Translation: CAH59743.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1307.1

NCBI Reference Sequences

More...
RefSeqi
NP_004896.1, NM_004905.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000340385; ENSP00000342026; ENSG00000117592

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9588

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9588

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14662 mRNA Translation: BAA03496.1
DQ230990 Genomic DNA Translation: ABB02185.1
AL139142 Genomic DNA No translation available.
AK289352 mRNA Translation: BAF82041.1
CH471067 Genomic DNA Translation: EAW90944.1
BC035857 mRNA Translation: AAH35857.1
BC053550 mRNA Translation: AAH53550.1
AJ844621 mRNA Translation: CAH59743.1
CCDSiCCDS1307.1
RefSeqiNP_004896.1, NM_004905.2

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
1PRXX-ray2.00A/B1-224[»]
5B6MX-ray2.50A/B/C/D/E/F1-224[»]
5B6NX-ray2.90A/B/C/D/E/F1-224[»]
SMRiP30041
ModBaseiSearch...

Protein-protein interaction databases

BioGridi114956, 110 interactors
IntActiP30041, 35 interactors
MINTiP30041
STRINGi9606.ENSP00000342026

Chemistry databases

DrugBankiDB03814 2-(N-Morpholino)-Ethanesulfonic Acid
DB09130 Copper
DB02325 Isopropyl alcohol
SwissLipidsiSLP:000001691

Protein family/group databases

MoonDBiP30041 Curated
MoonProtiP30041
PeroxiBasei4426 Hs1CysPrx01

PTM databases

CarbonylDBiP30041
iPTMnetiP30041
PhosphoSitePlusiP30041
SwissPalmiP30041

Polymorphism and mutation databases

BioMutaiPRDX6
DMDMi1718024

2D gel databases

DOSAC-COBS-2DPAGEiP30041
OGPiP30041
REPRODUCTION-2DPAGEiIPI00220301
P30041
SWISS-2DPAGEiP30041

Proteomic databases

CPTACiCPTAC-117
CPTAC-118
EPDiP30041
jPOSTiP30041
MassIVEiP30041
PaxDbiP30041
PeptideAtlasiP30041
PRIDEiP30041
ProteomicsDBi54620
TopDownProteomicsiP30041

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
9588
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340385; ENSP00000342026; ENSG00000117592
GeneIDi9588
KEGGihsa:9588

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
9588
DisGeNETi9588

GeneCards: human genes, protein and diseases

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GeneCardsi
PRDX6
HGNCiHGNC:16753 PRDX6
HPAiCAB008663
HPA006983
MIMi602316 gene
neXtProtiNX_P30041
OpenTargetsiENSG00000117592
PharmGKBiPA134992760

Human Unidentified Gene-Encoded large proteins database

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HUGEi
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GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0854 Eukaryota
COG0450 LUCA
GeneTreeiENSGT00550000074794
HOGENOMiHOG000022346
InParanoidiP30041
KOiK11188
OMAiYPIIADD
OrthoDBi1129256at2759
PhylomeDBiP30041
TreeFamiTF105183

Enzyme and pathway databases

BRENDAi1.11.1.15 2681
ReactomeiR-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-6798695 Neutrophil degranulation
SIGNORiP30041

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
PRDX6 human
EvolutionaryTraceiP30041

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
PRDX6

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
9588

Pharos

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Pharosi
P30041

Protein Ontology

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PROi
PR:P30041

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000117592 Expressed in 241 organ(s), highest expression level in amniotic fluid
ExpressionAtlasiP30041 baseline and differential
GenevisibleiP30041 HS

Family and domain databases

InterProiView protein in InterPro
IPR000866 AhpC/TSA
IPR024706 Peroxiredoxin_AhpC-typ
IPR019479 Peroxiredoxin_C
IPR036249 Thioredoxin-like_sf
IPR013766 Thioredoxin_domain
PfamiView protein in Pfam
PF10417 1-cysPrx_C, 1 hit
PF00578 AhpC-TSA, 1 hit
PIRSFiPIRSF000239 AHPC, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS51352 THIOREDOXIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPRDX6_HUMAN
<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: P30041
Secondary accession number(s): A8JZY7
, P32077, Q5TAH4, Q5ZEZ8
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: September 18, 2019
This is version 207 of the entry and version 3 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 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.

<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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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