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Q16881

- TRXR1_HUMAN

UniProt

Q16881 - TRXR1_HUMAN

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Protein
Thioredoxin reductase 1, cytoplasmic
Gene
TXNRD1, GRIM12, KDRF
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 FAD per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei622 – 6221Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 20918FAD By similarity
Add
BLAST

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: InterPro
  4. protein binding Source: IntAct
  5. protein disulfide oxidoreductase activity Source: InterPro
  6. thioredoxin-disulfide reductase activity Source: Reactome

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. cell redox homeostasis Source: InterPro
  3. cellular lipid metabolic process Source: Reactome
  4. mesoderm formation Source: Ensembl
  5. nucleobase-containing small molecule interconversion Source: Reactome
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. signal transduction Source: ProtInc
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12437. TXNRD1.

Subcellular locationi

Cytoplasm By similarity 1 Publication
Isoform 4 : Cytoplasm. Nucleus 1 Publication
Isoform 5 : Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: Ensembl
  3. nucleolus Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37093.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 649649Thioredoxin reductase 1, cytoplasmic
PRO_0000030286Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi209 ↔ 214Redox-active By similarity
Modified residuei218 – 2181N6-succinyllysine By similarity
Modified residuei281 – 2811Phosphotyrosine1 Publication
Cross-linki647 ↔ 648Cysteinyl-selenocysteine (Cys-Sec) By similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16881.
PaxDbiQ16881.
PRIDEiQ16881.

2D gel databases

REPRODUCTION-2DPAGEIPI00554786.

PTM databases

PhosphoSiteiQ16881.

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.3 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.2 Publications

Gene expression databases

ArrayExpressiQ16881.
BgeeiQ16881.
GenevestigatoriQ16881.

Organism-specific databases

HPAiCAB004607.
CAB015834.
HPA001395.
HPA043871.

Interactioni

Subunit structurei

Homodimer. Isoform 4 interacts with ESR1 and ESR2. Interacts with HERC5.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113147. 31 interactions.
IntActiQ16881. 9 interactions.
MINTiMINT-1525880.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi162 – 1687
Helixi172 – 18312
Beta strandi188 – 1914
Helixi208 – 2125
Helixi214 – 23320
Turni234 – 2374
Helixi248 – 27225
Beta strandi276 – 2783
Beta strandi280 – 2867
Beta strandi289 – 2935
Beta strandi295 – 2973
Beta strandi301 – 3099
Beta strandi313 – 3153
Helixi323 – 3264
Helixi330 – 3334
Beta strandi342 – 3465
Helixi350 – 36112
Beta strandi366 – 3727
Turni374 – 3774
Helixi380 – 39213
Beta strandi396 – 41015
Beta strandi412 – 4143
Beta strandi416 – 42712
Beta strandi429 – 43911
Beta strandi443 – 4464
Beta strandi448 – 4503
Turni453 – 4564
Turni461 – 4633
Beta strandi479 – 4813
Helixi483 – 4853
Beta strandi486 – 4894
Helixi493 – 50816
Beta strandi522 – 5243
Beta strandi526 – 5283
Beta strandi530 – 5345
Helixi537 – 5448
Helixi546 – 5483
Beta strandi549 – 5568
Helixi559 – 5624
Turni563 – 5653
Turni568 – 5703
Beta strandi571 – 5788
Turni579 – 5824
Beta strandi584 – 5929
Helixi595 – 60713
Helixi612 – 6176
Helixi625 – 6317
Turni636 – 6394

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 59-644.

Miscellaneous databases

EvolutionaryTraceiQ16881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 156101Glutaredoxin
Add
BLAST

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

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOVERGENiHBG004959.
InParanoidiQ16881.
KOiK00384.
OMAiILQAGCX.
OrthoDBiEOG779NXG.
PhylomeDBiQ16881.
TreeFamiTF314782.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF52833. 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. Align

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

MGCAEGKAVA AAAPTELQTK GKNGDGRRRS AKDHHPGKTL PENPAGFTST    50
ATADSRALLQ AYIDGHSVVI FSRSTCTRCT EVKKLFKSLC VPYFVLELDQ 100
TEDGRALEGT LSELAAETDL PVVFVKQRKI GGHGPTLKAY QEGRLQKLLK 150
MNGPEDLPKS YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG 200
TRWGLGGTCV NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR 250
MIEAVQNHIG SLNWGYRVAL REKKVVYENA YGQFIGPHRI KATNNKGKEK 300
IYSAERFLIA TGERPRYLGI PGDKEYCISS DDLFSLPYCP GKTLVVGASY 350
VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM EEHGIKFIRQ 400
FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVMLA IGRDACTRKI 450
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG 500
RLLAQRLYAG STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE 550
VYHSYFWPLE WTIPSRDNNK CYAKIICNTK DNERVVGFHV LGPNAGEVTQ 600
GFAAALKCGL TKKQLDSTIG IHPVCAEVFT TLSVTKRSGA SILQAGCUG 649

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.

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 AAB35418.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence AAC69621.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence AAF15900.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence AAV38446.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence AAZ67916.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence BAA13674.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence BAH11490.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence BAH12374.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence BAH14140.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence CAA04503.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence CAA62629.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence CAG38744.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.
The sequence EAW97745.1 differs from that shown. Reason: Erroneous termination at position 648. Translated as Sec.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti365 – 3651D → G.2 Publications
Corresponds to variant rs1127954 [ dbSNP | Ensembl ].
VAR_051776

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 188188Missing in isoform 7.
VSP_053819Add
BLAST
Alternative sequencei1 – 150150Missing in isoform 5.
VSP_031558Add
BLAST
Alternative sequencei1 – 139139MGCAE…PTLKA → MPVDDYWLCLPASCARPFVQ TVRVVQSCPHCCWFPGVLPS VPEPLRMPAMLPTGSHSAVL PPSHCSTAPPSTSQEPSSSA DPKLCLSPPTSDSRQERNVQ FGLA in isoform 6.
VSP_031559Add
BLAST
Alternative sequencei1 – 106106Missing in isoform 2.
VSP_031560Add
BLAST
Alternative sequencei1 – 9898Missing in isoform 4.
VSP_031561Add
BLAST
Alternative sequencei1 – 5151Missing in isoform 3.
VSP_031562Add
BLAST
Alternative sequencei52 – 10049TADSR…LELDQ → MQQVMLTCKGVNRGHAVPAG PGRKPRPRRSSRLLAGEKHL TRSALLLCH in isoform 3.
VSP_031563Add
BLAST
Alternative sequencei99 – 1013DQT → MSC in isoform 4.
VSP_031564
Alternative sequencei107 – 13832LEGTL…GPTLK → MLSRLVLNSWAQAIIRPRPP KVLGLQVTTFSE in isoform 2.
VSP_031565Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti153 – 1531G → S in AAQ62473. 1 Publication
Sequence conflicti181 – 1811A → P in AAF15900. 1 Publication
Sequence conflicti194 – 1941V → G in AAF15900. 1 Publication
Sequence conflicti200 – 2001G → E in AAQ62469. 1 Publication
Sequence conflicti202 – 2021R → K in AAQ62463. 1 Publication
Sequence conflicti215 – 2151I → N in AAQ62463. 1 Publication
Sequence conflicti297 – 2971G → D in BAH11490. 1 Publication
Sequence conflicti306 – 3061R → S in AAB35418. 1 Publication
Sequence conflicti306 – 3061R → S in CAA62629. 1 Publication
Sequence conflicti306 – 3061R → S in AAL15432. 1 Publication
Sequence conflicti365 – 3651D → N in AAC69621. 1 Publication
Sequence conflicti437 – 4371V → A in BAH12374. 1 Publication
Sequence conflicti441 – 4411I → M in BAH12374. 1 Publication
Sequence conflicti449 – 4491K → R in CAG38744. 1 Publication
Sequence conflicti641 – 6411S → R in AAC69621. 1 Publication

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei648 – 6481Selenocysteine1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Genome annotation databases

EnsembliENST00000388854; ENSP00000373506; ENSG00000198431.
ENST00000429002; ENSP00000412045; ENSG00000198431.
ENST00000503506; ENSP00000421934; ENSG00000198431. [Q16881-5]
ENST00000524698; ENSP00000433425; ENSG00000198431. [Q16881-5]
ENST00000525566; ENSP00000434516; ENSG00000198431. [Q16881-1]
ENST00000526390; ENSP00000435123; ENSG00000198431. [Q16881-2]
ENST00000526580; ENSP00000433887; ENSG00000198431.
ENST00000526691; ENSP00000435929; ENSG00000198431. [Q16881-4]
ENST00000529546; ENSP00000434919; ENSG00000198431.
ENST00000540716; ENSP00000442709; ENSG00000198431.
GeneIDi7296.
KEGGihsa:7296.
UCSCiuc010swp.3. human. [Q16881-1]
uc021rcy.2. human. [Q16881-4]

Polymorphism databases

DMDMi172046253.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53820.1. [Q16881-1 ]
CCDS53821.1. [Q16881-4 ]
CCDS53823.1. [Q16881-5 ]
CCDS58274.1. [Q16881-7 ]
PIRi S66677.
RefSeqi NP_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 ]
UniGenei Hs.654922.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W1C model - A/B 161-649 [» ]
2CFY X-ray 2.70 A/B/C/D/E/F 151-647 [» ]
2J3N X-ray 2.80 A/B/C/D/E/F 151-647 [» ]
2ZZ0 X-ray 2.80 A/B/C/D 150-647 [» ]
2ZZB X-ray 3.20 A/B/C/D 150-647 [» ]
2ZZC X-ray 2.60 A/B/C/D 150-647 [» ]
3QFA X-ray 2.20 A/B 151-649 [» ]
3QFB X-ray 2.60 A/B 151-649 [» ]
ProteinModelPortali Q16881.
SMRi Q16881. Positions 59-644.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113147. 31 interactions.
IntActi Q16881. 9 interactions.
MINTi MINT-1525880.

Chemistry

BindingDBi Q16881.
ChEMBLi CHEMBL2096978.

PTM databases

PhosphoSitei Q16881.

Polymorphism databases

DMDMi 172046253.

2D gel databases

REPRODUCTION-2DPAGE IPI00554786.

Proteomic databases

MaxQBi Q16881.
PaxDbi Q16881.
PRIDEi Q16881.

Protocols and materials databases

DNASUi 7296.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000388854 ; ENSP00000373506 ; ENSG00000198431 .
ENST00000429002 ; ENSP00000412045 ; ENSG00000198431 .
ENST00000503506 ; ENSP00000421934 ; ENSG00000198431 . [Q16881-5 ]
ENST00000524698 ; ENSP00000433425 ; ENSG00000198431 . [Q16881-5 ]
ENST00000525566 ; ENSP00000434516 ; ENSG00000198431 . [Q16881-1 ]
ENST00000526390 ; ENSP00000435123 ; ENSG00000198431 . [Q16881-2 ]
ENST00000526580 ; ENSP00000433887 ; ENSG00000198431 .
ENST00000526691 ; ENSP00000435929 ; ENSG00000198431 . [Q16881-4 ]
ENST00000529546 ; ENSP00000434919 ; ENSG00000198431 .
ENST00000540716 ; ENSP00000442709 ; ENSG00000198431 .
GeneIDi 7296.
KEGGi hsa:7296.
UCSCi uc010swp.3. human. [Q16881-1 ]
uc021rcy.2. human. [Q16881-4 ]

Organism-specific databases

CTDi 7296.
GeneCardsi GC12P104609.
H-InvDB HIX0010939.
HGNCi HGNC:12437. TXNRD1.
HPAi CAB004607.
CAB015834.
HPA001395.
HPA043871.
MIMi 601112. gene.
neXtProti NX_Q16881.
PharmGKBi PA37093.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1249.
HOVERGENi HBG004959.
InParanoidi Q16881.
KOi K00384.
OMAi ILQAGCX.
OrthoDBi EOG779NXG.
PhylomeDBi Q16881.
TreeFami TF314782.

Enzyme and pathway databases

Reactomei REACT_116145. PPARA activates gene expression.
REACT_172715. Detoxification of Reactive Oxygen Species.
REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

ChiTaRSi TXNRD1. human.
EvolutionaryTracei Q16881.
GeneWikii TXNRD1.
GenomeRNAii 7296.
NextBioi 28527.
PROi Q16881.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q16881.
Bgeei Q16881.
Genevestigatori Q16881.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view ]
Pfami PF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR01438. TGR. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a human thioredoxin reductase."
    Gasdaska P.Y., Gasdaska J.R., Cochran S., Powis G.
    FEBS Lett. 373:5-9(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF 153-161; 307-315 AND 585-607, VARIANT GLY-365.
    Tissue: Placenta.
  2. "Cloning and characterization of a novel oxidoreductase KDRF from a human bone marrow-derived stromal cell line KM-102."
    Koishi R., Kawashima I., Yoshimura C., Sugawara M., Serizawa N.
    J. Biol. Chem. 272:2570-2577(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 122-127 AND 147-151, TISSUE SPECIFICITY.
    Tissue: Bone marrow stroma.
  3. "Thioredoxin reductase mediates cell death effects of the combination of beta interferon and retinoic acid."
    Hofman E.R., Boyanapalli M., Lindner D.J., Weihua X., Hassel B.A., Jagus R., Gutierrez P.L., Kalvakolanu D.V.
    Mol. Cell. Biol. 18:6493-6504(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INDUCTION.
    Tissue: Mammary carcinoma.
  4. "Evidence for intriguingly complex transcription of human thioredoxin reductase 1."
    Rundloef A.-K., Janard M., Miranda-Vizuete A., Arner E.S.
    Free Radic. Biol. Med. 36:641-656(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), VARIANT GLY-365.
    Tissue: Mammary gland, Ovary, Testis and Thymus.
  5. "Identification by ddPCR of thioredoxin reductase as a vitamin D regulated gene in human osteoblasts."
    Schuetze N., Bachthaler M., Lechner A., Koehrle J., Jakob F.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  6. "Cloning and sequencing of thioredoxin reductase gene from human brain."
    Xu L., Dai R., Xu J.Y.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Brain.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
    Tissue: Astrocyte, Thalamus and Trachea.
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  10. NIEHS SNPs program
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION.
    Tissue: Trachea.
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Lung.
  14. "Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene."
    Gladyshev V.N., Jeang K.-T., Stadtman T.C.
    Proc. Natl. Acad. Sci. U.S.A. 93:6146-6151(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 307-316; 449-456; 466-476 AND 638-649, BLOCKAGE OF N-TERMINUS, SELENOCYSTEINE AT SEC-648, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity."
    Tamura T., Stadtman T.C.
    Proc. Natl. Acad. Sci. U.S.A. 93:1006-1011(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, CHARACTERIZATION, PRESENCE OF SELENOCYSTEINE.
  16. "Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1."
    Su D., Gladyshev V.N.
    Biochemistry 43:12177-12188(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), DOMAIN.
  17. "An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling."
    Damdimopoulos A.E., Miranda-Vizuete A., Treuter E., Gustafsson J.-A., Spyrou G.
    J. Biol. Chem. 279:38721-38729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ESR1 AND ESR2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY (ISOFORM 4).
  18. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-281, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
    Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERC5, ISGYLATION.
  20. "Induction of cell membrane protrusions by the N-terminal glutaredoxin domain of a rare splice variant of human thioredoxin reductase 1."
    Dammeyer P., Damdimopoulos A.E., Nordman T., Jimenez A., Miranda-Vizuete A., Arner E.S.J.
    J. Biol. Chem. 283:2814-2821(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION (ISOFORM 1).
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "The structure of human thioredoxin reductase 1 provides insights into C-terminal rearrangements during catalysis."
    Fritz-Wolf K., Urig S., Becker K.
    J. Mol. Biol. 370:116-127(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) (ISOFORM 5).

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: September 3, 2014
This is version 169 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

External Data

Dasty 3

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