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UniProtKB - Q06830 (PRDX1_HUMAN)

Entry version 226 (10 Feb 2021)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
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Protein

Peroxiredoxin-1

Gene

PRDX1

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. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2 (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity).By similarity1 Publication

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 typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication

<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

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 sitei52Cysteine sulfenic acid (-SOH) intermediate2 Publications1

<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, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS04134-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.11.1.15, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q06830

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3299685, Detoxification of Reactive Oxygen Species
R-HSA-5628897, TP53 Regulates Metabolic Genes
R-HSA-8862803, Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q06830

Protein family/group databases

PeroxiBase, a peroxidase database

More...PeroxiBasei		4501, Hs2CysPrx01

<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-1 (EC:1.11.1.242 Publications)
Alternative name(s):
Natural killer cell-enhancing factor A
Short name:
NKEF-A
Proliferation-associated gene protein
Short name:
PAG
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Thioredoxin-dependent peroxiredoxin 1Curated
<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:PRDX1
Synonyms:PAGA, PAGB, TDPX2
<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:9352, PRDX1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		176763, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q06830

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000117450.13

<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

<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>Mutagenesisi90T → A: Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity. 1 Publication1
Mutagenesisi90T → D: 87% reduction in enzymatic activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5052

MalaCards human disease database

More...MalaCardsi		PRDX1

Open Targets

More...OpenTargetsi		ENSG00000117450

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33722

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q06830, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5315

Drug and drug target database

More...DrugBanki		DB11638, Artenimol
DB09130, Copper
DB09221, Polaprezinc
DB01593, Zinc
DB14487, Zinc acetate
DB14533, Zinc chloride
DB14548, Zinc sulfate, unspecified form

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PRDX1

Domain mapping of disease mutations (DMDM)

More...DMDMi		548453

<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 sources
<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_00001350762 – 199Peroxiredoxin-1Add BLAST198

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 residuei2N-acetylserineCombined sources1
Modified residuei7N6-acetyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei16N6-acetyllysineCombined sources1
Modified residuei27N6-acetyllysineCombined sources1
Modified residuei32PhosphoserineCombined sources1
Modified residuei35N6-acetyllysine; alternateCombined sources1
Modified residuei35N6-succinyllysine; alternateBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi52Interchain (with C-173); in linked formCombined sources1 Publication
Modified residuei90Phosphothreonine; by CDK11 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei136N6-acetyllysineBy similarity1
Disulfide bondi173Interchain (with C-52); in linked formCombined sources1 Publication
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources

<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

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity.1 Publication
The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.6 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q06830

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q06830

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q06830

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q06830

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

More...PaxDbi		Q06830

PeptideAtlas

More...PeptideAtlasi		Q06830

PRoteomics IDEntifications database

More...PRIDEi		Q06830

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		12697
58486

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q06830

2D gel databases

DOSAC-COBS 2D-PAGE database

More...DOSAC-COBS-2DPAGEi		Q06830

USC-OGP 2-DE database

More...OGPi		Q06830

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

More...SWISS-2DPAGEi		Q06830

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		Q06830

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06830

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q06830

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

More...PhosphoSitePlusi		Q06830

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q06830

<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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000117450, Expressed in thyroid gland and 241 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q06830, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q06830, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000117450, 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; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (PubMed:18172504).

Interacts with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).

Interacts with SESN1 and SESN2 (PubMed:15105503).

Interacts with FAM107A (PubMed:21969592).

By similarity3 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		111089, 218 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q06830

Database of interacting proteins

More...DIPi		DIP-33152N

Protein interaction database and analysis system

More...IntActi		Q06830, 100 interactors

Molecular INTeraction database

More...MINTi		Q06830

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000262746

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q06830, 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

1199
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

More...SMRi		Q06830

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		Q06830

<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>Domaini6 – 165ThioredoxinPROSITE-ProRule annotationAdd BLAST160

<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. AhpC/Prx1 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0852, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154277

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06830

Identification of Orthologs from Complete Genome Data

More...OMAi		FWYPKDF

Database of Orthologous Groups

More...OrthoDBi		1326484at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q06830

TreeFam database of animal gene trees

More...TreeFami		TF105181

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>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q06830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF 
        60         70         80         90        100
VCPTEIIAFS DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM 
       110        120        130        140        150
NIPLVSDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITVNDLPVG 
       160        170        180        190 
RSVDETLRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVQK SKEYFSKQK
Length:199
Mass (Da):22,110
Last modified:June 1, 1994 - 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:i8F68E56D75BF5304
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MSI0A0A0A0MSI0_HUMAN
Peroxiredoxin-1
PRDX1
171Annotation score:

Annotation score:2 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>
A0A0A0MRQ5A0A0A0MRQ5_HUMAN
Peroxiredoxin-1
PRDX1
97Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti147L → P (PubMed:8026862).Curated1
Sequence conflicti149 – 150VG → CC (PubMed:8026862).Curated2
Sequence conflicti189Q → P (PubMed:8026862).Curated1
Sequence conflicti191S → T (PubMed:8026862).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02505062R → G1 PublicationCorresponds to variant dbSNP:rs34034070Ensembl.1

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
X67951 mRNA Translation: CAA48137.1
L19184 mRNA Translation: AAA50464.1
BT019740 mRNA Translation: AAV38545.1
CR407652 mRNA Translation: CAG28580.1
DQ297142 Genomic DNA Translation: ABB84465.1
AB451262 mRNA Translation: BAG70076.1
AB451388 mRNA Translation: BAG70202.1
AL451136 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX06975.1
CH471059 Genomic DNA Translation: EAX06976.1
CH471059 Genomic DNA Translation: EAX06978.1
CH471059 Genomic DNA Translation: EAX06979.1
CH471059 Genomic DNA Translation: EAX06980.1
CH471059 Genomic DNA Translation: EAX06981.1
CH471059 Genomic DNA Translation: EAX06982.1
BC007063 mRNA Translation: AAH07063.1
BC021683 mRNA Translation: AAH21683.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS522.1

Protein sequence database of the Protein Information Resource

More...PIRi		A46711

NCBI Reference Sequences

More...RefSeqi		NP_001189360.1, NM_001202431.1
NP_002565.1, NM_002574.3
NP_859047.1, NM_181696.2
NP_859048.1, NM_181697.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000262746; ENSP00000262746; ENSG00000117450
ENST00000319248; ENSP00000361152; ENSG00000117450

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5052

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5052

UCSC genome browser

More...UCSCi		uc001coa.4, human

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67951 mRNA Translation: CAA48137.1
L19184 mRNA Translation: AAA50464.1
BT019740 mRNA Translation: AAV38545.1
CR407652 mRNA Translation: CAG28580.1
DQ297142 Genomic DNA Translation: ABB84465.1
AB451262 mRNA Translation: BAG70076.1
AB451388 mRNA Translation: BAG70202.1
AL451136 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX06975.1
CH471059 Genomic DNA Translation: EAX06976.1
CH471059 Genomic DNA Translation: EAX06978.1
CH471059 Genomic DNA Translation: EAX06979.1
CH471059 Genomic DNA Translation: EAX06980.1
CH471059 Genomic DNA Translation: EAX06981.1
CH471059 Genomic DNA Translation: EAX06982.1
BC007063 mRNA Translation: AAH07063.1
BC021683 mRNA Translation: AAH21683.1
CCDSiCCDS522.1
PIRiA46711
RefSeqiNP_001189360.1, NM_001202431.1
NP_002565.1, NM_002574.3
NP_859047.1, NM_181696.2
NP_859048.1, NM_181697.2

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
2RIIX-ray2.60A/B1-199[»]
3HY2X-ray2.10A/B1-199[»]
4XCSX-ray2.10A/B/C/D/E/F1-199[»]
SMRiQ06830
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111089, 218 interactors
CORUMiQ06830
DIPiDIP-33152N
IntActiQ06830, 100 interactors
MINTiQ06830
STRINGi9606.ENSP00000262746

Chemistry databases

ChEMBLiCHEMBL5315
DrugBankiDB11638, Artenimol
DB09130, Copper
DB09221, Polaprezinc
DB01593, Zinc
DB14487, Zinc acetate
DB14533, Zinc chloride
DB14548, Zinc sulfate, unspecified form

Protein family/group databases

PeroxiBasei4501, Hs2CysPrx01

PTM databases

iPTMnetiQ06830
MetOSiteiQ06830
PhosphoSitePlusiQ06830
SwissPalmiQ06830

Genetic variation databases

BioMutaiPRDX1
DMDMi548453

2D gel databases

DOSAC-COBS-2DPAGEiQ06830
OGPiQ06830
SWISS-2DPAGEiQ06830
UCD-2DPAGEiQ06830

Proteomic databases

EPDiQ06830
jPOSTiQ06830
MassIVEiQ06830
MaxQBiQ06830
PaxDbiQ06830
PeptideAtlasiQ06830
PRIDEiQ06830
ProteomicsDBi12697
58486
TopDownProteomicsiQ06830

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1574, 666 antibodies

The DNASU plasmid repository

More...DNASUi		5052

Genome annotation databases

EnsembliENST00000262746; ENSP00000262746; ENSG00000117450
ENST00000319248; ENSP00000361152; ENSG00000117450
GeneIDi5052
KEGGihsa:5052
UCSCiuc001coa.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5052
DisGeNETi5052

GeneCards: human genes, protein and diseases

More...GeneCardsi		PRDX1
HGNCiHGNC:9352, PRDX1
HPAiENSG00000117450, Low tissue specificity
MalaCardsiPRDX1
MIMi176763, gene
neXtProtiNX_Q06830
OpenTargetsiENSG00000117450
PharmGKBiPA33722
VEuPathDBiHostDB:ENSG00000117450.13

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0852, Eukaryota
GeneTreeiENSGT00940000154277
InParanoidiQ06830
OMAiFWYPKDF
OrthoDBi1326484at2759
PhylomeDBiQ06830
TreeFamiTF105181

Enzyme and pathway databases

BioCyciMetaCyc:HS04134-MONOMER
BRENDAi1.11.1.15, 2681
PathwayCommonsiQ06830
ReactomeiR-HSA-3299685, Detoxification of Reactive Oxygen Species
R-HSA-5628897, TP53 Regulates Metabolic Genes
R-HSA-8862803, Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models
SIGNORiQ06830

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5052, 50 hits in 890 CRISPR screens

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

More...ChiTaRSi		PRDX1, human
EvolutionaryTraceiQ06830

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Peroxiredoxin_1

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

More...GenomeRNAii		5052
PharosiQ06830, Tbio

Protein Ontology

More...PROi		PR:Q06830
RNActiQ06830, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000117450, Expressed in thyroid gland and 241 other tissues
ExpressionAtlasiQ06830, baseline and differential
GenevisibleiQ06830, 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 nameiPRDX1_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: Q06830
Secondary accession number(s): B5BU26
, D3DPZ8, P35703, Q2V576, Q5T154, Q5T155
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 10, 2021
This is version 226 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 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. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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