GLRX5
entrez
51218
canonical
uniprot
Q86SX6
canonical
ensembl
ENSG00000182512
resolver
ensp
ENSP00000328570
resolver
enst
ENST00000331334
resolver
genesymbol
GLRX5
resolver
genesymbol_syn
C14orf87
resolver
hgnc
HGNC:20134
resolver
uniprot
A0A384MDT9
resolver
uniprot
Q0X088
resolver
uniprot
Q3YML0
resolver
uniprot
Q86WY3
resolver
uniprot
Q8IZ54
resolver
uniprot_entry
A0A384MDT9_HUMAN
resolver
uniprot_entry
GLRX5_HUMAN
resolver
uniprot_sec
Q0X088
resolver
uniprot_sec
Q3YML0
resolver
uniprot_sec
Q86WY3
resolver
uniprot_sec
Q8IZ54
resolver
amino_acid_sequence
MSGSLGRAAAALLRWGRGAGGGGLWGPGVRAAGSGAGGGGSAEQLDALVKKDKVVVFLKGTPEQPQCGFSNAVVQILRLHGVRDYAAYNVLDDPELRQGIKDYSNWPTIPQVYLNGEFVGGCDILLQMHQNGDLVEELKKLGIHSALLDEKKDQDSK
uniprot
proteins
disease_involvement
DISEASE: Anemia, sideroblastic, 3, pyridoxine-refractory (SIDBA3) [MIM:616860]: A form of sideroblastic anemia, a bone marrow disorder defined by the presence of pathologic iron deposits in erythroblast mitochondria. Sideroblastic anemia is characterized by anemia of varying severity, hypochromic peripheral erythrocytes, systemic iron overload secondary to chronic ineffective erythropoiesis, and the presence of bone marrow ringed sideroblasts. Sideroblasts are characterized by iron-loaded mitochondria clustered around the nucleus. SIDBA3 is refractory to treatment with vitamin B6, while iron chelation therapy may result in clinical improvement. SIDBA3 inheritance is autosomal recessive. {ECO:0000269|PubMed:17485548, ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:25342667, ECO:0000269|PubMed:26100117}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spasticity, childhood-onset, with hyperglycinemia (SPAHGC) [MIM:616859]: An autosomal recessive disorder characterized by childhood-onset of spasticity, spinal lesions, leukodystrophy, optic atrophy in some patients, non-ketotic hyperglycinemia, and defective enzymatic glycine cleavage. Glycine levels in the cerebrospinal fluid are mildly increased in some but not all patients. The increase is less pronounced than in patients with classic non-ketotic hyperglycinemia. {ECO:0000269|PubMed:24334290}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Monothiol glutaredoxin involved in mitochondrial iron-sulfur (Fe/S) cluster transfer (PubMed:20364084, PubMed:23615440). Receives 2Fe/2S clusters from scaffold protein ISCU and mediates their transfer to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export from mitochondrion (PubMed:20364084, PubMed:23615440, PubMed:24334290). Required for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1 (PubMed:20364084). {ECO:0000269|PubMed:20364084, ECO:0000269|PubMed:23615440, ECO:0000269|PubMed:24334290}.
uniprot
proteins
mass_dalton
16628
uniprot
proteins
protein_family
Glutaredoxin family
uniprot
proteins
protein_family
Monothiol subfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16110529
uniprot
proteins
pubmed
17485548
uniprot
proteins
pubmed
20364084
uniprot
proteins
pubmed
21029046
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23615440
uniprot
proteins
pubmed
24334290
uniprot
proteins
pubmed
25342667
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26100117
uniprot
proteins
pubmed
27532772
uniprot
proteins
pubmed
27532773
uniprot
proteins
sequence_length
157
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:20364084}.
uniprot
proteins