TXN
entrez
7295
canonical
uniprot
P10599
canonical
ensembl
ENSG00000136810
resolver
ensp
ENSP00000363639
resolver
ensp
ENSP00000363641
resolver
genesymbol
TXN
resolver
genesymbol_syn
TRDX
resolver
genesymbol_syn
TRX
resolver
genesymbol_syn
TRX1
resolver
hgnc
HGNC:12435
resolver
uniprot
B1ALW1
resolver
uniprot
H9ZYJ2
resolver
uniprot
O60744
resolver
uniprot
Q53X69
resolver
uniprot
Q96KI3
resolver
uniprot
Q9UDG5
resolver
uniprot_entry
H9ZYJ2_HUMAN
resolver
uniprot_entry
THIO_HUMAN
resolver
uniprot_sec
B1ALW1
resolver
uniprot_sec
O60744
resolver
uniprot_sec
Q53X69
resolver
uniprot_sec
Q96KI3
resolver
uniprot_sec
Q9UDG5
resolver
amino_acid_sequence
MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
uniprot
proteins
function
FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). 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 (PubMed:16408020, PubMed:17606900). 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 (PubMed:11118054, PubMed:9108029). {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17182577, ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:19032234, ECO:0000269|PubMed:2176490, ECO:0000269|PubMed:9108029}.; FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).
uniprot
proteins
mass_dalton
11737
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="C->S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35."; /evidence="ECO:0000269|PubMed:9108029"; MUTAGEN 35; /note="C->S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32."; /evidence="ECO:0000269|PubMed:9108029"; MUTAGEN 60; /note="D->N: Loss of pH-dependence of dimerization."; MUTAGEN 62; /note="C->S: Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73."; /evidence="ECO:0000269|PubMed:9108029"; MUTAGEN 69; /note="C->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."; /evidence="ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"; MUTAGEN 70; /note="E->A: Strongly reduced interaction with CASP3; when associated with A-72."; /evidence="ECO:0000269|PubMed:17606900"; MUTAGEN 72; /note="K->A: Strongly reduced interaction with CASP3; when associated with A-70."; /evidence="ECO:0000269|PubMed:17606900"; MUTAGEN 73; /note="C->D: Strongly reduced S-nitrosylation of CASP3."; /evidence="ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"; MUTAGEN 73; /note="C->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."; /evidence="ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029"; MUTAGEN 73; /note="C->S: Retains its reducing activity."; /evidence="ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17606900, ECO:0000269|PubMed:9108029
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:15246877, ECO:0000269|PubMed:16408020, ECO:0000269|PubMed:17260951, ECO:0000269|PubMed:17606900}.; PTM: In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation. {ECO:0000269|PubMed:19690162}.
uniprot
proteins
protein_family
Thioredoxin family
uniprot
proteins
pubmed
11118054
uniprot
proteins
pubmed
1332947
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15246877
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16408020
uniprot
proteins
pubmed
17182577
uniprot
proteins
pubmed
17260951
uniprot
proteins
pubmed
17606900
uniprot
proteins
pubmed
1874447
uniprot
proteins
pubmed
19032234
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690162
uniprot
proteins
pubmed
1998498
uniprot
proteins
pubmed
2001356
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21489611
uniprot
proteins
pubmed
2176490
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2684271
uniprot
proteins
pubmed
2785919
uniprot
proteins
pubmed
3170595
uniprot
proteins
pubmed
7788295
uniprot
proteins
pubmed
7818492
uniprot
proteins
pubmed
7922028
uniprot
proteins
pubmed
8736558
uniprot
proteins
pubmed
8805557
uniprot
proteins
pubmed
9108029
uniprot
proteins
pubmed
9369469
uniprot
proteins
sequence_length
105
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Cytoplasm {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:9108029}. Secreted {ECO:0000269|PubMed:1332947}. Note=Translocates from the cytoplasm into the nucleus after phorbol 12-myristate 13-acetate induction (PMA) (PubMed:9108029). Predominantly in the cytoplasm in non irradiated cells (PubMed:11118054). Radiation induces translocation of TRX from the cytoplasm to the nucleus (PubMed:11118054). Secreted by a leaderless secretory pathway (PubMed:1332947). {ECO:0000269|PubMed:11118054, ECO:0000269|PubMed:1332947, ECO:0000269|PubMed:9108029}.
uniprot
proteins