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Protein

Thioredoxin

Gene

TXN

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

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

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>Sitei26Deprotonates C-terminal active site Cys1
<p>This subsection of the ‘Function’ 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 sitei32Nucleophile1
Sitei33Contributes to redox potential value1
Sitei34Contributes to redox potential value1
Active sitei35Nucleophile1

<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 functionActivator
Biological processElectron transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-499943 Interconversion of nucleotide di- and triphosphates
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-5676934 Protein repair
R-HSA-844456 The NLRP3 inflammasome

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P10599

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P10599

<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:
Thioredoxin
Short name:
Trx
Alternative name(s):
ATL-derived factor
Short name:
ADF
Surface-associated sulphydryl protein
Short name:
SASP
<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:TXN
Synonyms:TRDX, TRX, TRX1
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000136810.12

Human Gene Nomenclature Database

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HGNCi
HGNC:12435 TXN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
187700 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P10599

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

<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>Mutagenesisi32C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35. 1 Publication1
Mutagenesisi35C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32. 1 Publication1
Mutagenesisi60D → N: Loss of pH-dependence of dimerization. 1
Mutagenesisi62C → S: Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73. 1 Publication1
Mutagenesisi69C → S: No effect on reducing activity, interaction with APEX1 and on S-nitrosylation of C-73. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-73. 2 Publications1
Mutagenesisi70E → A: Strongly reduced interaction with CASP3; when associated with A-72. 1 Publication1
Mutagenesisi72K → A: Strongly reduced interaction with CASP3; when associated with A-70. 1 Publication1
Mutagenesisi73C → D: Strongly reduced S-nitrosylation of CASP3. 3 Publications1
Mutagenesisi73C → S: Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-69. 3 Publications1
Mutagenesisi73C → S: Retains its reducing activity. 3 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
7295

Open Targets

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OpenTargetsi
ENSG00000136810

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37091

Protein family/group databases

Allergome; a platform for allergen knowledge

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Allergomei
3543 Hom s Trx

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2010624

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TXN

Domain mapping of disease mutations (DMDM)

More...
DMDMi
135773

<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 methionineiRemoved2 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_00001200052 – 105ThioredoxinAdd BLAST104

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 residuei3N6-acetyllysineCombined sources1
Modified residuei8N6-succinyllysineBy 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 bondi32 ↔ 35Redox-activePROSITE-ProRule annotation2 Publications
Modified residuei39N6-acetyllysineCombined sources1
Modified residuei62S-nitrosocysteine1 Publication1
Modified residuei69S-nitrosocysteine1 Publication1
Modified residuei73S-nitrosocysteine; alternate2 Publications1
Disulfide bondi73Interchain; alternate1 Publication
Modified residuei94N6-acetyllysine; alternateBy similarity1
Modified residuei94N6-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

In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins.4 Publications
In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, S-nitrosylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P10599

MaxQB - The MaxQuant DataBase

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MaxQBi
P10599

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

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PaxDbi
P10599

PeptideAtlas

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PeptideAtlasi
P10599

PRoteomics IDEntifications database

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PRIDEi
P10599

ProteomicsDB human proteome resource

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ProteomicsDBi
12706
52616

Consortium for Top Down Proteomics

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TopDownProteomicsi
P10599-1 [P10599-1]
P10599-2 [P10599-2]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P10599

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00216298

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

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SWISS-2DPAGEi
P10599

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P10599

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P10599

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

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PhosphoSitePlusi
P10599

SwissPalm database of S-palmitoylation events

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SwissPalmi
P10599

<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

Up-regulated by ionizing radiation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136810 Expressed in 233 organ(s), highest expression level in mouth mucosa

CleanEx database of gene expression profiles

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CleanExi
HS_TXN

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P10599 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P10599 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008678
HPA047478
HPA055752

<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; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner.5 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113146, 130 interactors

Database of interacting proteins

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DIPi
DIP-6129N

Protein interaction database and analysis system

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IntActi
P10599, 67 interactors

Molecular INTeraction database

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MINTi
P10599

STRING: functional protein association networks

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STRINGi
9606.ENSP00000363641

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P10599

<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

1105
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P10599

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

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SMRi
P10599

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P10599

<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>Domaini2 – 105ThioredoxinPROSITE-ProRule annotationAdd BLAST104

<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 thioredoxin family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0907 Eukaryota
COG0526 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154259

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000292977

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009243

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P10599

KEGG Orthology (KO)

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KOi
K03671

Identification of Orthologs from Complete Genome Data

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OMAi
SKYAFQE

Database of Orthologous Groups

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OrthoDBi
EOG091G01FG

Database for complete collections of gene phylogenies

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PhylomeDBi
P10599

TreeFam database of animal gene trees

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TreeFami
TF318932

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR005746 Thioredoxin
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain

The PANTHER Classification System

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PANTHERi
PTHR10438 PTHR10438, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00085 Thioredoxin, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000077 Thioredoxin, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52833 SSF52833, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00194 THIOREDOXIN_1, 1 hit
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P10599-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS
60 70 80 90 100
NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT

INELV
Length:105
Mass (Da):11,737
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:i256F4E3C8A187693
GO
Isoform 2 (identifier: P10599-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-63: Missing.

Show »
Length:85
Mass (Da):9,452
Checksum:i3CC6254BD6A1D66F
GO

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 conflicti39K → N in AAA74596 (PubMed:3170595).Curated1
Sequence conflicti39K → N in AAF86466 (Ref. 4) Curated1
Sequence conflicti74M → T in AAA74596 (PubMed:3170595).Curated1
Sequence conflicti74M → T in AAF86466 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04560744 – 63Missing in isoform 2. 1 PublicationAdd BLAST20

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

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DDBJi
Links Updated
J04026 mRNA Translation: AAA74596.1
X77584 mRNA Translation: CAA54687.1
X54539, X54540, X54541 Genomic DNA Translation: CAA38410.1
AF276919 mRNA Translation: AAF86466.1
AY004872 mRNA Translation: AAF87085.1
AF313911 mRNA Translation: AAG34699.1
AK289508 mRNA Translation: BAF82197.1
CR407665 mRNA Translation: CAG28593.1
AF548001 Genomic DNA Translation: AAN33187.1
AL158158 Genomic DNA No translation available.
CH471105 Genomic DNA Translation: EAW59059.1
CH471105 Genomic DNA Translation: EAW59060.1
BC003377 mRNA Translation: AAH03377.1
BC054866 mRNA Translation: AAH54866.1
AF065241 mRNA Translation: AAC17430.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS35103.1 [P10599-1]
CCDS59139.1 [P10599-2]

Protein sequence database of the Protein Information Resource

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PIRi
JH0568

NCBI Reference Sequences

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RefSeqi
NP_001231867.1, NM_001244938.1 [P10599-2]
NP_003320.2, NM_003329.3 [P10599-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.435136

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000374515; ENSP00000363639; ENSG00000136810 [P10599-2]
ENST00000374517; ENSP00000363641; ENSG00000136810 [P10599-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
7295

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:7295

UCSC genome browser

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UCSCi
uc004bep.3 human [P10599-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04026 mRNA Translation: AAA74596.1
X77584 mRNA Translation: CAA54687.1
X54539, X54540, X54541 Genomic DNA Translation: CAA38410.1
AF276919 mRNA Translation: AAF86466.1
AY004872 mRNA Translation: AAF87085.1
AF313911 mRNA Translation: AAG34699.1
AK289508 mRNA Translation: BAF82197.1
CR407665 mRNA Translation: CAG28593.1
AF548001 Genomic DNA Translation: AAN33187.1
AL158158 Genomic DNA No translation available.
CH471105 Genomic DNA Translation: EAW59059.1
CH471105 Genomic DNA Translation: EAW59060.1
BC003377 mRNA Translation: AAH03377.1
BC054866 mRNA Translation: AAH54866.1
AF065241 mRNA Translation: AAC17430.1
CCDSiCCDS35103.1 [P10599-1]
CCDS59139.1 [P10599-2]
PIRiJH0568
RefSeqiNP_001231867.1, NM_001244938.1 [P10599-2]
NP_003320.2, NM_003329.3 [P10599-1]
UniGeneiHs.435136

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIUX-ray2.00A1-105[»]
1AUCX-ray2.10A1-105[»]
1CQGNMR-A1-105[»]
1CQHNMR-A1-105[»]
1ERTX-ray1.70A1-105[»]
1ERUX-ray2.10A1-105[»]
1ERVX-ray1.65A1-105[»]
1ERWX-ray1.80A1-105[»]
1M7TNMR-A1-66[»]
1MDINMR-A1-105[»]
1MDJNMR-A1-105[»]
1MDKNMR-A1-105[»]
1TRSNMR-A1-105[»]
1TRUNMR-A1-105[»]
1TRVNMR-A1-105[»]
1TRWNMR-A1-105[»]
1W1Cmodel-C1-105[»]
1W1Emodel-C1-105[»]
2HSHX-ray1.35A1-105[»]
2HXKX-ray1.65A/B/C1-105[»]
2IFQX-ray1.20A/B/C1-105[»]
2IIYX-ray1.70A1-105[»]
3E3EX-ray2.01A/B1-105[»]
3KD0X-ray1.70A1-105[»]
3M9JX-ray1.10A/B1-105[»]
3M9KX-ray1.50A/B1-105[»]
3QFAX-ray2.20C/D2-105[»]
3QFBX-ray2.60C/D2-105[»]
3TRXNMR-A1-105[»]
4LL1X-ray2.00B/D1-105[»]
4LL4X-ray2.70B/D1-105[»]
4OO4X-ray0.97A/B1-105[»]
4OO5X-ray1.54A1-105[»]
4POKX-ray2.52A/B/C/D1-105[»]
4POLX-ray2.80A/B/C/D1-105[»]
4POMX-ray1.85A/B/C/D1-105[»]
4PUFX-ray3.30C/D1-105[»]
4TRXNMR-A1-105[»]
5DQYX-ray1.40A1-105[»]
ProteinModelPortaliP10599
SMRiP10599
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113146, 130 interactors
DIPiDIP-6129N
IntActiP10599, 67 interactors
MINTiP10599
STRINGi9606.ENSP00000363641

Chemistry databases

BindingDBiP10599
ChEMBLiCHEMBL2010624

Protein family/group databases

Allergomei3543 Hom s Trx

PTM databases

CarbonylDBiP10599
iPTMnetiP10599
PhosphoSitePlusiP10599
SwissPalmiP10599

Polymorphism and mutation databases

BioMutaiTXN
DMDMi135773

2D gel databases

DOSAC-COBS-2DPAGEiP10599
REPRODUCTION-2DPAGEiIPI00216298
SWISS-2DPAGEiP10599

Proteomic databases

EPDiP10599
MaxQBiP10599
PaxDbiP10599
PeptideAtlasiP10599
PRIDEiP10599
ProteomicsDBi12706
52616
TopDownProteomicsiP10599-1 [P10599-1]
P10599-2 [P10599-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
7295
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374515; ENSP00000363639; ENSG00000136810 [P10599-2]
ENST00000374517; ENSP00000363641; ENSG00000136810 [P10599-1]
GeneIDi7295
KEGGihsa:7295
UCSCiuc004bep.3 human [P10599-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7295
DisGeNETi7295
EuPathDBiHostDB:ENSG00000136810.12

GeneCards: human genes, protein and diseases

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GeneCardsi
TXN
HGNCiHGNC:12435 TXN
HPAiCAB008678
HPA047478
HPA055752
MIMi187700 gene
neXtProtiNX_P10599
OpenTargetsiENSG00000136810
PharmGKBiPA37091

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0907 Eukaryota
COG0526 LUCA
GeneTreeiENSGT00940000154259
HOGENOMiHOG000292977
HOVERGENiHBG009243
InParanoidiP10599
KOiK03671
OMAiSKYAFQE
OrthoDBiEOG091G01FG
PhylomeDBiP10599
TreeFamiTF318932

Enzyme and pathway databases

ReactomeiR-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-3299685 Detoxification of Reactive Oxygen Species
R-HSA-499943 Interconversion of nucleotide di- and triphosphates
R-HSA-5628897 TP53 Regulates Metabolic Genes
R-HSA-5676934 Protein repair
R-HSA-844456 The NLRP3 inflammasome
SignaLinkiP10599
SIGNORiP10599

Miscellaneous databases

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

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ChiTaRSi
TXN human
EvolutionaryTraceiP10599

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Thioredoxin

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

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GenomeRNAii
7295

Protein Ontology

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PROi
PR:P10599

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136810 Expressed in 233 organ(s), highest expression level in mouth mucosa
CleanExiHS_TXN
ExpressionAtlasiP10599 baseline and differential
GenevisibleiP10599 HS

Family and domain databases

InterProiView protein in InterPro
IPR005746 Thioredoxin
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain
PANTHERiPTHR10438 PTHR10438, 1 hit
PfamiView protein in Pfam
PF00085 Thioredoxin, 1 hit
PIRSFiPIRSF000077 Thioredoxin, 1 hit
SUPFAMiSSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS00194 THIOREDOXIN_1, 1 hit
PS51352 THIOREDOXIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiTHIO_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: P10599
Secondary accession number(s): B1ALW1
, O60744, Q53X69, Q96KI3, Q9UDG5
<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: July 1, 1989
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 220 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. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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