GLRX3
entrez
10539
canonical
uniprot
O76003
canonical
ensembl
ENSG00000108010
resolver
ensp
ENSP00000330836
resolver
ensp
ENSP00000357633
resolver
ensp
ENSP00000435445
resolver
enst
ENST00000331244
resolver
enst
ENST00000368644
resolver
enst
ENST00000481034
resolver
genesymbol
GLRX3
resolver
genesymbol_syn
PICOT
resolver
genesymbol_syn
TXNL2
resolver
hgnc
HGNC:15987
resolver
uniprot
A0A140VJK1
resolver
uniprot
B3KMP7
resolver
uniprot
B3KMQ5
resolver
uniprot
D3DRG2
resolver
uniprot
Q5JV01
resolver
uniprot
Q96CE0
resolver
uniprot
Q9P1B0
resolver
uniprot
Q9P1B1
resolver
uniprot_entry
A0A140VJK1_HUMAN
resolver
uniprot_entry
GLRX3_HUMAN
resolver
uniprot_sec
B3KMP7
resolver
uniprot_sec
B3KMQ5
resolver
uniprot_sec
D3DRG2
resolver
uniprot_sec
Q5JV01
resolver
uniprot_sec
Q96CE0
resolver
uniprot_sec
Q9P1B0
resolver
uniprot_sec
Q9P1B1
resolver
amino_acid_sequence
MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN
uniprot
proteins
function
FUNCTION: Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins (PubMed:26613676, PubMed:27519415). Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator (By similarity). Required for hemoglobin maturation (PubMed:23615448). Does not possess any thioredoxin activity since it lacks the conserved motif that is essential for catalytic activity. {ECO:0000250|UniProtKB:Q9CQM9, ECO:0000269|PubMed:23615448, ECO:0000269|PubMed:26613676, ECO:0000269|PubMed:27519415}.
uniprot
proteins
mass_dalton
37432
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="C->S: Loss of 2Fe-2S-binding; when associated with S-261. Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with 197-D-A-198."; /evidence="ECO:0000269|PubMed:20226171, ECO:0000269|PubMed:27519415"; MUTAGEN 197..198; /note="WP->DA: Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with S-159."; /evidence="ECO:0000269|PubMed:27519415"; MUTAGEN 261; /note="C->S: Loss of 2Fe-2S-binding; when associated with S-159. Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with 299-D-A-300."; /evidence="ECO:0000269|PubMed:20226171, ECO:0000269|PubMed:27519415"; MUTAGEN 299..300; /note="WP->DA: Loss of 2Fe-2S-binding and interaction with BOLA2; when associated with S-261."; /evidence="ECO:0000269|PubMed:27519415
uniprot
proteins
pubmed
10636891
uniprot
proteins
pubmed
11124703
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20226171
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22309771
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23615448
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26613676
uniprot
proteins
pubmed
27519415
uniprot
proteins
sequence_length
335
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:27519415}. Cytoplasm, cell cortex {ECO:0000269|PubMed:10636891}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:Q9CQM9}. Note=Under the plasma membrane (By similarity). After PMA stimulation, GLRX3 and PRKCQ/PKC-theta translocate to a more extended submembrane area (By similarity). In the Z line, found associated with CSRP3 (By similarity). {ECO:0000250|UniProtKB:Q9CQM9}.
uniprot
proteins