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Protein

Thioredoxin reductase 1, cytoplasmic

Gene

TXNRD1

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

Functioni

Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.4 Publications

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADNote: Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei622Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi192 – 209FADBy similarityAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciZFISH:HS06102-MONOMER.
BRENDAi1.8.1.9. 2681.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2408550. Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-HSA-5263617. Metabolism of ingested MeSeO2H into MeSeH.
R-HSA-5336415. Uptake and function of diphtheria toxin.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 1, cytoplasmic (EC:1.8.1.9)
Short name:
TR
Alternative name(s):
Gene associated with retinoic and interferon-induced mortality 12 protein
Short name:
GRIM-12
Short name:
Gene associated with retinoic and IFN-induced mortality 12 protein
KM-102-derived reductase-like factor
Thioredoxin reductase TR1
Gene namesi
Name:TXNRD1
Synonyms:GRIM12, KDRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12437. TXNRD1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi7296.
OpenTargetsiENSG00000198431.
PharmGKBiPA37093.

Chemistry databases

ChEMBLiCHEMBL1927.
DrugBankiDB01169. Arsenic trioxide.
DB03147. Flavin adenine dinucleotide.

Polymorphism and mutation databases

BioMutaiTXNRD1.
DMDMi172046253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000302861 – 649Thioredoxin reductase 1, cytoplasmicAdd BLAST649

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi209 ↔ 214Redox-activeBy similarity
Modified residuei218N6-succinyllysineBy similarity1
Modified residuei281PhosphotyrosineCombined sources1
Cross-linki647 ↔ 648Cysteinyl-selenocysteine (Cys-Sec)By similarity
Isoform 5 (identifier: Q16881-5)
Modified residuei1N-acetylmethionineCombined sources1

Post-translational modificationi

The N-terminus of isoform 5 is blocked.
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16881.
MaxQBiQ16881.
PaxDbiQ16881.
PeptideAtlasiQ16881.
PRIDEiQ16881.

2D gel databases

REPRODUCTION-2DPAGEIPI00554786.

PTM databases

iPTMnetiQ16881.
PhosphoSitePlusiQ16881.
SwissPalmiQ16881.

Expressioni

Tissue specificityi

Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver.2 Publications

Inductioni

Isoform 5 is induced by a combination of interferon-beta and retinoic acid (at protein level). Isoform 1 is induced by estradiol or testosterone in HeLa cells.1 Publication

Gene expression databases

BgeeiENSG00000198431.
ExpressionAtlasiQ16881. baseline and differential.
GenevisibleiQ16881. HS.

Organism-specific databases

HPAiHPA001395.
HPA043871.

Interactioni

Subunit structurei

Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAV1Q031354EBI-716617,EBI-603614
ESR1P033724EBI-9080335,EBI-78473
ESR2Q927313EBI-9080335,EBI-78505

Protein-protein interaction databases

BioGridi113147. 39 interactors.
IntActiQ16881. 9 interactors.
MINTiMINT-1525880.
STRINGi9606.ENSP00000434516.

Chemistry databases

BindingDBiQ16881.

Structurei

Secondary structure

1649
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi162 – 168Combined sources7
Helixi172 – 183Combined sources12
Beta strandi188 – 191Combined sources4
Helixi208 – 212Combined sources5
Helixi214 – 233Combined sources20
Turni234 – 237Combined sources4
Helixi248 – 272Combined sources25
Beta strandi276 – 278Combined sources3
Beta strandi280 – 286Combined sources7
Beta strandi289 – 293Combined sources5
Beta strandi295 – 297Combined sources3
Beta strandi301 – 309Combined sources9
Beta strandi313 – 315Combined sources3
Helixi323 – 326Combined sources4
Helixi330 – 333Combined sources4
Beta strandi342 – 346Combined sources5
Helixi350 – 361Combined sources12
Beta strandi366 – 372Combined sources7
Turni374 – 377Combined sources4
Helixi380 – 392Combined sources13
Beta strandi396 – 410Combined sources15
Beta strandi412 – 414Combined sources3
Beta strandi416 – 427Combined sources12
Beta strandi429 – 439Combined sources11
Beta strandi443 – 446Combined sources4
Beta strandi448 – 450Combined sources3
Turni453 – 456Combined sources4
Turni461 – 463Combined sources3
Beta strandi479 – 481Combined sources3
Helixi483 – 485Combined sources3
Beta strandi486 – 489Combined sources4
Helixi493 – 508Combined sources16
Beta strandi522 – 524Combined sources3
Beta strandi526 – 528Combined sources3
Beta strandi530 – 534Combined sources5
Helixi537 – 544Combined sources8
Helixi546 – 548Combined sources3
Beta strandi549 – 556Combined sources8
Helixi559 – 562Combined sources4
Turni563 – 565Combined sources3
Turni568 – 570Combined sources3
Beta strandi571 – 578Combined sources8
Turni579 – 582Combined sources4
Beta strandi584 – 592Combined sources9
Helixi595 – 607Combined sources13
Helixi612 – 617Combined sources6
Helixi625 – 631Combined sources7
Turni636 – 639Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1Cmodel-A/B161-649[»]
2CFYX-ray2.70A/B/C/D/E/F151-647[»]
2J3NX-ray2.80A/B/C/D/E/F151-647[»]
2ZZ0X-ray2.80A/B/C/D150-647[»]
2ZZBX-ray3.20A/B/C/D150-647[»]
2ZZCX-ray2.60A/B/C/D150-647[»]
3QFAX-ray2.20A/B151-649[»]
3QFBX-ray2.60A/B151-649[»]
ProteinModelPortaliQ16881.
SMRiQ16881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 156GlutaredoxinPROSITE-ProRule annotationAdd BLAST101

Domaini

The N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays.1 Publication

Sequence similaritiesi

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
KOG4716. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
HOVERGENiHBG004959.
InParanoidiQ16881.
KOiK00384.
OrthoDBiEOG091G03IU.
PhylomeDBiQ16881.
TreeFamiTF314782.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR002109. Glutaredoxin.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16881-1) [UniParc]FASTAAdd to basket
Also known as: V, TXNRD1_v3

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
MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST
60 70 80 90 100
ATADSRALLQ AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ
110 120 130 140 150
TEDGRALEGT LSELAAETDL PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK
160 170 180 190 200
MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG
210 220 230 240 250
TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR
260 270 280 290 300
MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK
310 320 330 340 350
IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY
360 370 380 390 400
VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ
410 420 430 440 450
FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA IGRDACTRKI
460 470 480 490 500
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG
510 520 530 540 550
RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE
560 570 580 590 600
VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ
610 620 630 640
GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG
Note: Minor isoform.
Length:649
Mass (Da):70,906
Last modified:February 26, 2008 - v3
Checksum:i5A51C3F77EB03EFE
GO
Isoform 2 (identifier: Q16881-2) [UniParc]FASTAAdd to basket
Also known as: II, TXNRD1_v4

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.
     107-138: LEGTLSELAAETDLPVVFVKQRKIGGHGPTLK → MLSRLVLNSWAQAIIRPRPPKVLGLQVTTFSE

Show »
Length:543
Mass (Da):59,787
Checksum:i990DB8D334659B4D
GO
Isoform 3 (identifier: Q16881-3) [UniParc]FASTAAdd to basket
Also known as: III, TXNRD1_v5

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: Missing.
     52-100: TADSRALLQA...VPYFVLELDQ → MQQVMLTCKG...LTRSALLLCH

Show »
Length:598
Mass (Da):65,567
Checksum:i81F496F5BB85A49E
GO
Isoform 4 (identifier: Q16881-4) [UniParc]FASTAAdd to basket
Also known as: IV, TXNRD1_v2, TrxR1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     99-101: DQT → MSC

Show »
Length:551
Mass (Da):60,419
Checksum:iF54B034AADF51E5B
GO
Isoform 5 (identifier: Q16881-5) [UniParc]FASTAAdd to basket
Also known as: I, TXNRD1_v1, TrxR1a

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: Missing.

Note: Major isoform. The N-terminus of the sequence is processed into a mature form that lacks residues Met-151 and Asn-152 at the N-terminus.Combined sources
Show »
Length:499
Mass (Da):54,754
Checksum:iC24BAEB4A573EABE
GO
Isoform 6 (identifier: Q16881-6) [UniParc]FASTAAdd to basket
Also known as: VI

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: MGCAEGKAVA...IGGHGPTLKA → MPVDDYWLCL...QERNVQFGLA

Show »
Length:614
Mass (Da):67,266
Checksum:i9C635E1C6EA94934
GO
Isoform 7 (identifier: Q16881-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-188: Missing.

Note: No experimental confirmation.
Show »
Length:461
Mass (Da):50,873
Checksum:i07D3A620A6BD82EA
GO

Sequence cautioni

The sequence AAB35418 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence AAC69621 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence AAF15900 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence AAV38446 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence AAZ67916 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence BAA13674 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence BAH11490 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence BAH12374 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence BAH14140 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence CAA04503 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence CAA62629 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence CAG38744 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated
The sequence EAW97745 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153G → S in AAQ62473 (PubMed:14980707).Curated1
Sequence conflicti181A → P in AAF15900 (Ref. 6) Curated1
Sequence conflicti194V → G in AAF15900 (Ref. 6) Curated1
Sequence conflicti200G → E in AAQ62469 (PubMed:14980707).Curated1
Sequence conflicti202R → K in AAQ62463 (PubMed:14980707).Curated1
Sequence conflicti215I → N in AAQ62463 (PubMed:14980707).Curated1
Sequence conflicti297G → D in BAH11490 (PubMed:14702039).Curated1
Sequence conflicti306R → S in AAB35418 (PubMed:7589432).Curated1
Sequence conflicti306R → S in CAA62629 (PubMed:7589432).Curated1
Sequence conflicti306R → S in AAL15432 (PubMed:14980707).Curated1
Sequence conflicti365D → N in AAC69621 (PubMed:9774665).Curated1
Sequence conflicti437V → A in BAH12374 (PubMed:14702039).Curated1
Sequence conflicti441I → M in BAH12374 (PubMed:14702039).Curated1
Sequence conflicti449K → R in CAG38744 (Ref. 8) Curated1
Sequence conflicti641S → R in AAC69621 (PubMed:9774665).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051776365D → G.2 PublicationsCorresponds to variant rs1127954dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0538191 – 188Missing in isoform 7. 1 PublicationAdd BLAST188
Alternative sequenceiVSP_0315581 – 150Missing in isoform 5. 7 PublicationsAdd BLAST150
Alternative sequenceiVSP_0315591 – 139MGCAE…PTLKA → MPVDDYWLCLPASCARPFVQ TVRVVQSCPHCCWFPGVLPS VPEPLRMPAMLPTGSHSAVL PPSHCSTAPPSTSQEPSSSA DPKLCLSPPTSDSRQERNVQ FGLA in isoform 6. CuratedAdd BLAST139
Alternative sequenceiVSP_0315601 – 106Missing in isoform 2. CuratedAdd BLAST106
Alternative sequenceiVSP_0315611 – 98Missing in isoform 4. 1 PublicationAdd BLAST98
Alternative sequenceiVSP_0315621 – 51Missing in isoform 3. CuratedAdd BLAST51
Alternative sequenceiVSP_03156352 – 100TADSR…LELDQ → MQQVMLTCKGVNRGHAVPAG PGRKPRPRRSSRLLAGEKHL TRSALLLCH in isoform 3. CuratedAdd BLAST49
Alternative sequenceiVSP_03156499 – 101DQT → MSC in isoform 4. 1 Publication3
Alternative sequenceiVSP_031565107 – 138LEGTL…GPTLK → MLSRLVLNSWAQAIIRPRPP KVLGLQVTTFSE in isoform 2. CuratedAdd BLAST32

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei648Selenocysteine1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91247 mRNA. Translation: CAA62629.1. Sequence problems.
S79851 mRNA. Translation: AAB35418.1. Sequence problems.
D88687 mRNA. Translation: BAA13674.1. Sequence problems.
AF077367 mRNA. Translation: AAC69621.1. Sequence problems.
AY057105 mRNA. Translation: AAL15432.1.
AY344081 mRNA. Translation: AAQ62461.1.
AY344083 mRNA. Translation: AAQ62462.1.
AY344084 mRNA. Translation: AAQ62463.1.
AY344086 mRNA. Translation: AAQ62464.1.
AY344087 mRNA. Translation: AAQ62465.1.
AY344089 mRNA. Translation: AAQ62466.1.
AY344092 mRNA. Translation: AAQ62467.1.
AY344093 mRNA. Translation: AAQ62468.1.
AY344095 mRNA. Translation: AAQ62469.1.
AY344096 mRNA. Translation: AAQ62470.1.
AY344670 mRNA. Translation: AAQ62471.1.
AY344673 mRNA. Translation: AAQ62472.1.
AY344679 mRNA. Translation: AAQ62473.1.
AJ001050 mRNA. Translation: CAA04503.1. Sequence problems.
AF208018 mRNA. Translation: AAF15900.1. Sequence problems.
AK293322 mRNA. Translation: BAH11490.1. Sequence problems.
AK296495 mRNA. Translation: BAH12374.1. Sequence problems.
AK304241 mRNA. Translation: BAH14140.1. Sequence problems.
CR536506 mRNA. Translation: CAG38744.1. Sequence problems.
BT019640 mRNA. Translation: AAV38446.1. Sequence problems.
DQ157758 Genomic DNA. Translation: AAZ67916.1. Sequence problems.
AC089983 Genomic DNA. No translation available.
AC090107 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97745.1. Sequence problems.
BC018122 mRNA. Translation: AAH18122.2.
CCDSiCCDS53820.1. [Q16881-1]
CCDS53821.1. [Q16881-4]
CCDS53823.1. [Q16881-5]
CCDS58274.1. [Q16881-7]
PIRiS66677.
RefSeqiNP_001087240.1. NM_001093771.2. [Q16881-1]
NP_001248374.1. NM_001261445.1.
NP_001248375.1. NM_001261446.1. [Q16881-7]
NP_003321.3. NM_003330.3. [Q16881-4]
NP_877393.1. NM_182729.2. [Q16881-5]
NP_877419.1. NM_182742.2. [Q16881-5]
NP_877420.1. NM_182743.2. [Q16881-5]
UniGeneiHs.654922.
Hs.690011.

Genome annotation databases

EnsembliENST00000503506; ENSP00000421934; ENSG00000198431. [Q16881-5]
ENST00000524698; ENSP00000433425; ENSG00000198431. [Q16881-5]
ENST00000525566; ENSP00000434516; ENSG00000198431. [Q16881-1]
ENST00000526390; ENSP00000435123; ENSG00000198431. [Q16881-2]
ENST00000526691; ENSP00000435929; ENSG00000198431. [Q16881-4]
ENST00000529546; ENSP00000434919; ENSG00000198431. [Q16881-7]
GeneIDi7296.
KEGGihsa:7296.
UCSCiuc010swp.4. human. [Q16881-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91247 mRNA. Translation: CAA62629.1. Sequence problems.
S79851 mRNA. Translation: AAB35418.1. Sequence problems.
D88687 mRNA. Translation: BAA13674.1. Sequence problems.
AF077367 mRNA. Translation: AAC69621.1. Sequence problems.
AY057105 mRNA. Translation: AAL15432.1.
AY344081 mRNA. Translation: AAQ62461.1.
AY344083 mRNA. Translation: AAQ62462.1.
AY344084 mRNA. Translation: AAQ62463.1.
AY344086 mRNA. Translation: AAQ62464.1.
AY344087 mRNA. Translation: AAQ62465.1.
AY344089 mRNA. Translation: AAQ62466.1.
AY344092 mRNA. Translation: AAQ62467.1.
AY344093 mRNA. Translation: AAQ62468.1.
AY344095 mRNA. Translation: AAQ62469.1.
AY344096 mRNA. Translation: AAQ62470.1.
AY344670 mRNA. Translation: AAQ62471.1.
AY344673 mRNA. Translation: AAQ62472.1.
AY344679 mRNA. Translation: AAQ62473.1.
AJ001050 mRNA. Translation: CAA04503.1. Sequence problems.
AF208018 mRNA. Translation: AAF15900.1. Sequence problems.
AK293322 mRNA. Translation: BAH11490.1. Sequence problems.
AK296495 mRNA. Translation: BAH12374.1. Sequence problems.
AK304241 mRNA. Translation: BAH14140.1. Sequence problems.
CR536506 mRNA. Translation: CAG38744.1. Sequence problems.
BT019640 mRNA. Translation: AAV38446.1. Sequence problems.
DQ157758 Genomic DNA. Translation: AAZ67916.1. Sequence problems.
AC089983 Genomic DNA. No translation available.
AC090107 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97745.1. Sequence problems.
BC018122 mRNA. Translation: AAH18122.2.
CCDSiCCDS53820.1. [Q16881-1]
CCDS53821.1. [Q16881-4]
CCDS53823.1. [Q16881-5]
CCDS58274.1. [Q16881-7]
PIRiS66677.
RefSeqiNP_001087240.1. NM_001093771.2. [Q16881-1]
NP_001248374.1. NM_001261445.1.
NP_001248375.1. NM_001261446.1. [Q16881-7]
NP_003321.3. NM_003330.3. [Q16881-4]
NP_877393.1. NM_182729.2. [Q16881-5]
NP_877419.1. NM_182742.2. [Q16881-5]
NP_877420.1. NM_182743.2. [Q16881-5]
UniGeneiHs.654922.
Hs.690011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W1Cmodel-A/B161-649[»]
2CFYX-ray2.70A/B/C/D/E/F151-647[»]
2J3NX-ray2.80A/B/C/D/E/F151-647[»]
2ZZ0X-ray2.80A/B/C/D150-647[»]
2ZZBX-ray3.20A/B/C/D150-647[»]
2ZZCX-ray2.60A/B/C/D150-647[»]
3QFAX-ray2.20A/B151-649[»]
3QFBX-ray2.60A/B151-649[»]
ProteinModelPortaliQ16881.
SMRiQ16881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113147. 39 interactors.
IntActiQ16881. 9 interactors.
MINTiMINT-1525880.
STRINGi9606.ENSP00000434516.

Chemistry databases

BindingDBiQ16881.
ChEMBLiCHEMBL1927.
DrugBankiDB01169. Arsenic trioxide.
DB03147. Flavin adenine dinucleotide.

PTM databases

iPTMnetiQ16881.
PhosphoSitePlusiQ16881.
SwissPalmiQ16881.

Polymorphism and mutation databases

BioMutaiTXNRD1.
DMDMi172046253.

2D gel databases

REPRODUCTION-2DPAGEIPI00554786.

Proteomic databases

EPDiQ16881.
MaxQBiQ16881.
PaxDbiQ16881.
PeptideAtlasiQ16881.
PRIDEiQ16881.

Protocols and materials databases

DNASUi7296.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000503506; ENSP00000421934; ENSG00000198431. [Q16881-5]
ENST00000524698; ENSP00000433425; ENSG00000198431. [Q16881-5]
ENST00000525566; ENSP00000434516; ENSG00000198431. [Q16881-1]
ENST00000526390; ENSP00000435123; ENSG00000198431. [Q16881-2]
ENST00000526691; ENSP00000435929; ENSG00000198431. [Q16881-4]
ENST00000529546; ENSP00000434919; ENSG00000198431. [Q16881-7]
GeneIDi7296.
KEGGihsa:7296.
UCSCiuc010swp.4. human. [Q16881-1]

Organism-specific databases

CTDi7296.
DisGeNETi7296.
GeneCardsiTXNRD1.
H-InvDBHIX0010939.
HGNCiHGNC:12437. TXNRD1.
HPAiHPA001395.
HPA043871.
MIMi601112. gene.
neXtProtiNX_Q16881.
OpenTargetsiENSG00000198431.
PharmGKBiPA37093.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
KOG4716. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
HOVERGENiHBG004959.
InParanoidiQ16881.
KOiK00384.
OrthoDBiEOG091G03IU.
PhylomeDBiQ16881.
TreeFamiTF314782.

Enzyme and pathway databases

BioCyciZFISH:HS06102-MONOMER.
BRENDAi1.8.1.9. 2681.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-2408550. Metabolism of ingested H2SeO4 and H2SeO3 into H2Se.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-HSA-5263617. Metabolism of ingested MeSeO2H into MeSeH.
R-HSA-5336415. Uptake and function of diphtheria toxin.
R-HSA-5628897. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiTXNRD1. human.
EvolutionaryTraceiQ16881.
GeneWikiiTXNRD1.
GenomeRNAii7296.
PROiQ16881.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198431.
ExpressionAtlasiQ16881. baseline and differential.
GenevisibleiQ16881. HS.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR002109. Glutaredoxin.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXR1_HUMAN
AccessioniPrimary (citable) accession number: Q16881
Secondary accession number(s): B7Z1F4
, B7Z3Y8, B7Z904, E9PMY9, F5H780, Q6FI31, Q6VB40, Q6VB41, Q6VB42, Q6VBP2, Q6VBP3, Q6VBP4, Q6VBP5, Q6VBP9, Q6VBQ0, Q6YNQ1, Q76P53, Q7LA96, Q8WVC8, Q99475, Q9UES8, Q9UH79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 192 of the entry and version 3 of the sequence. [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

Miscellaneous

The thioredoxin reductase active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.