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UniProtKB - P30041 (PRDX6_HUMAN)

Entry version 217 (10 Feb 2021)
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 (PubMed:9497358, PubMed:10893423). Can reduce H2O2 and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10893423). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10893423, PubMed:26830860). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed:10893423). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed:10893423). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (PubMed:26830860).3 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%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 <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

MJ33 or lithium;[(2R)-1-hexadecoxy-3-(2,2,2-trifluoroethoxy)propan-2-yl] methyl phosphate inhibits its phospholipase A2 activity (PubMed:26830860). CI-976 or 2,2-Dimethyl-N-(2,4,6-trimethoxyphenyl)dodecanamide inhibits its lysophosphatidylcholine acyltransferase activity (PubMed:26830860).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=18 µM for palmitoyl-CoA (lysophosphatidylcholine acyltransferase activity at pH 4.0)1 Publication
  2. KM=15 µM for palmitoyl-CoA (lysophosphatidylcholine acyltransferase activity for the phosphorylated form at pH 7.0)1 Publication
  1. Vmax=30 nmol/min/mg enzyme with palmitoyl-CoA as substrate for lysophosphatidylcholine acyltransferase activity (at pH 4.0)1 Publication
  2. Vmax=770 nmol/min/mg enzyme with palmitoyl-CoA as substrate for lysophosphatidylcholine acyltransferase activity (phosphorylated form at pH 7.0)1 Publication

pH dependencei

Shows a 3-fold greater lysophosphatidylcholine acyltransferase activity at pH 4.0 than at pH 7.0.1 Publication

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%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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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, Transferase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS04152-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.11.1.15, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P30041

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%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:
Peroxiredoxin-6 (EC:1.11.1.272 Publications)
Alternative name(s):
1-Cys peroxiredoxin
Short name:
1-Cys PRX
24 kDa protein
Acidic calcium-independent phospholipase A2 (EC:3.1.1.42 Publications)
Short name:
aiPLA2
Antioxidant protein 2
Glutathione-dependent peroxiredoxinCurated
Liver 2D page spot 40
Lysophosphatidylcholine acyltransferase 51 Publication (EC:2.3.1.231 Publication)
Short name:
LPC acyltransferase 5
Short name:
LPCAT-5
Short name:
Lyso-PC acyltransferase 5
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%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:PRDX6
Synonyms:AOP2, KIAA0106
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000117592.8

<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%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>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

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P30041, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4295741

Drug and drug target database

More...DrugBanki		DB03814, 2-(N-morpholino)ethanesulfonic acid
DB09130, Copper

Genetic variation 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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). The phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860).By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-117
CPTAC-118

Encyclopedia of Proteome Dynamics

More...EPDi		P30041

jPOST - Japan Proteome Standard Repository/Database

More...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

More...PRIDEi		P30041

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		54620

Consortium for Top Down Proteomics

More...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

MetOSite database of methionine sulfoxide sites

More...MetOSitei		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 amniotic fluid and 251 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P30041, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P30041, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000117592, Low tissue specificity

<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

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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114956, 161 interactors

Protein interaction database and analysis system

More...IntActi		P30041, 39 interactors

Molecular INTeraction database

More...MINTi		P30041

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000342026

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P30041, protein

<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

Biological Magnetic Resonance Data Bank

More...BMRBi		P30041

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

More...SMRi		P30041

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		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%5Fand%5Fdomains%5Fsection">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

More...eggNOGi		KOG0854, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074794

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_042529_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30041

Identification of Orthologs from Complete Genome Data

More...OMAi		IPLTCRA

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

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.30.10, 1 hit

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%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.

<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 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

More...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%5Freferences%5Fsection">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[»]
BMRBiP30041
SMRiP30041
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114956, 161 interactors
IntActiP30041, 39 interactors
MINTiP30041
STRINGi9606.ENSP00000342026

Chemistry databases

ChEMBLiCHEMBL4295741
DrugBankiDB03814, 2-(N-morpholino)ethanesulfonic acid
DB09130, Copper
SwissLipidsiSLP:000001691

Protein family/group databases

MoonDBiP30041, Curated
MoonProtiP30041
PeroxiBasei4426, Hs1CysPrx01

PTM databases

CarbonylDBiP30041
iPTMnetiP30041
MetOSiteiP30041
PhosphoSitePlusiP30041
SwissPalmiP30041

Genetic variation 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

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1681, 591 antibodies

The DNASU plasmid repository

More...DNASUi		9588

Genome annotation databases

EnsembliENST00000340385; ENSP00000342026; ENSG00000117592
GeneIDi9588
KEGGihsa:9588

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9588
DisGeNETi9588

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRDX6
HGNCiHGNC:16753, PRDX6
HPAiENSG00000117592, Low tissue specificity
MIMi602316, gene
neXtProtiNX_P30041
OpenTargetsiENSG00000117592
PharmGKBiPA134992760
VEuPathDBiHostDB:ENSG00000117592.8

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0854, Eukaryota
GeneTreeiENSGT00550000074794
HOGENOMiCLU_042529_4_1_1
InParanoidiP30041
OMAiIPLTCRA
OrthoDBi1129256at2759
PhylomeDBiP30041
TreeFamiTF105183

Enzyme and pathway databases

BioCyciMetaCyc:HS04152-MONOMER
BRENDAi1.11.1.15, 2681
PathwayCommonsiP30041
ReactomeiR-HSA-3299685, Detoxification of Reactive Oxygen Species
R-HSA-6798695, Neutrophil degranulation
SIGNORiP30041

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		9588, 9 hits in 875 CRISPR screens

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

More...ChiTaRSi		PRDX6, human
EvolutionaryTraceiP30041

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PRDX6

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

More...GenomeRNAii		9588
PharosiP30041, Tbio

Protein Ontology

More...PROi		PR:P30041
RNActiP30041, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000117592, Expressed in amniotic fluid and 251 other tissues
ExpressionAtlasiP30041, baseline and differential
GenevisibleiP30041, HS

Family and domain databases

Gene3Di3.40.30.10, 1 hit
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

More...ProtoNeti		Search...

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 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%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: April 1, 1993
Last sequence update: January 23, 2007
Last modified: February 10, 2021
This is version 217 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, Direct protein sequencing, Reference proteome

Documents

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