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Protein

Thioredoxin, mitochondrial

Gene

TXN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84Deprotonates C-terminal active site CysBy similarity1
Active sitei90NucleophileBy similarity1
Sitei91Contributes to redox potential valueBy similarity1
Sitei92Contributes to redox potential valueBy similarity1
Active sitei93NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processElectron transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin, mitochondrial
Short name:
MTRX
Short name:
Mt-Trx
Alternative name(s):
Thioredoxin-2
Gene namesi
Name:TXN2
Synonyms:TRX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

EuPathDBiHostDB:ENSG00000100348.9.
HGNCiHGNC:17772. TXN2.

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

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 29 (COXPD29)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, infantile-onset, neurodegenerative disorder characterized by decreased activities of mitochondrial respiratory complexes I and III, severe cerebellar atrophy, epilepsy, dystonia, optic atrophy, and peripheral neuropathy.
See also OMIM:616811

Keywords - Diseasei

Neurodegeneration, Primary mitochondrial disease

Organism-specific databases

DisGeNETi25828.
MalaCardsiTXN2.
MIMi616811. phenotype.
OpenTargetsiENSG00000100348.
PharmGKBiPA38245.

Chemistry databases

ChEMBLiCHEMBL2189153.

Polymorphism and mutation databases

BioMutaiTXN2.
DMDMi20455529.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 59MitochondrionCombined sources1 PublicationAdd BLAST59
ChainiPRO_000003415060 – 166Thioredoxin, mitochondrialAdd BLAST107

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi90 ↔ 93Redox-active
Modified residuei152N6-acetyllysine; alternateCombined sources1
Modified residuei152N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiQ99757.
MaxQBiQ99757.
PaxDbiQ99757.
PeptideAtlasiQ99757.
PRIDEiQ99757.
TopDownProteomicsiQ99757.

PTM databases

iPTMnetiQ99757.
PhosphoSitePlusiQ99757.

Expressioni

Tissue specificityi

Widely expressed in adult (at protein level) and fetal tissues.2 Publications

Gene expression databases

BgeeiENSG00000100348.
CleanExiHS_TXN2.
ExpressionAtlasiQ99757. baseline and differential.
GenevisibleiQ99757. HS.

Organism-specific databases

HPAiCAB008681.
HPA000994.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi117356. 59 interactors.
IntActiQ99757. 67 interactors.
STRINGi9606.ENSP00000216185.

Chemistry databases

BindingDBiQ99757.

Structurei

Secondary structure

1166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi60 – 63Combined sources4
Helixi67 – 73Combined sources7
Turni74 – 76Combined sources3
Beta strandi81 – 86Combined sources6
Helixi91 – 106Combined sources16
Turni107 – 109Combined sources3
Beta strandi110 – 117Combined sources8
Turni118 – 121Combined sources4
Helixi122 – 127Combined sources6
Beta strandi132 – 140Combined sources9
Beta strandi143 – 150Combined sources8
Helixi154 – 165Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UVZX-ray2.01A/B/C/D/E/F60-166[»]
1W4VX-ray1.80A/B/C/D/E/F60-166[»]
1W89X-ray2.00A/B/C/D/E/F60-166[»]
ProteinModelPortaliQ99757.
SMRiQ99757.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99757.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 166ThioredoxinPROSITE-ProRule annotationAdd BLAST106

Sequence similaritiesi

Belongs to the thioredoxin family.Curated

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0910. Eukaryota.
COG0526. LUCA.
GeneTreeiENSGT00530000064086.
HOVERGENiHBG009243.
InParanoidiQ99757.
KOiK03671.
OMAiCRMLTPR.
OrthoDBiEOG091G0UDG.
PhylomeDBiQ99757.
TreeFamiTF314517.

Family and domain databases

InterProiView protein in InterPro
IPR005746. Thioredoxin.
IPR036249. Thioredoxin-like_sf.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF00085. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiView protein in PROSITE
PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQRLLLRRF LASVISRKPS QGQWPPLTSR ALQTPQCSPG GLTVTPNPAR
60 70 80 90 100
TIYTTRISLT TFNIQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL
110 120 130 140 150
EKMVAKQHGK VVMAKVDIDD HTDLAIEYEV SAVPTVLAMK NGDVVDKFVG
160
IKDEDQLEAF LKKLIG
Length:166
Mass (Da):18,383
Last modified:May 2, 2002 - v2
Checksum:iC4CA8CDAD485D499
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30R → K in AAB41631 (PubMed:12080052).Curated1
Sequence conflicti30R → K in AAF86467 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF480262 mRNA. Translation: AAN05576.1.
U78678 mRNA. Translation: AAB41631.1.
AF276920 mRNA. Translation: AAF86467.1.
CR456601 mRNA. Translation: CAG30487.1.
CR541896 mRNA. Translation: CAG46694.1.
CR541917 mRNA. Translation: CAG46715.1.
AL022313 Genomic DNA. No translation available.
CH471095 Genomic DNA. Translation: EAW60103.1.
BC013726 mRNA. Translation: AAH13726.1.
BC050610 mRNA. Translation: AAH50610.1.
CCDSiCCDS13928.1.
RefSeqiNP_036605.2. NM_012473.3.
XP_006724289.1. XM_006724226.1.
UniGeneiHs.211929.

Genome annotation databases

EnsembliENST00000216185; ENSP00000216185; ENSG00000100348.
ENST00000403313; ENSP00000385393; ENSG00000100348.
GeneIDi25828.
KEGGihsa:25828.
UCSCiuc003apk.2. human.

Similar proteinsi

Entry informationi

Entry nameiTHIOM_HUMAN
AccessioniPrimary (citable) accession number: Q99757
Secondary accession number(s): Q5JZA0, Q6FH60, Q9UH29
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 2, 2002
Last modified: October 25, 2017
This is version 174 of the entry and version 2 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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