HSCB
entrez
150274
canonical
uniprot
Q8IWL3
canonical
ensembl
ENSG00000100209
resolver
ensp
ENSP00000216027
resolver
ensp
ENSP00000381914
resolver
ensp
ENSP00000416679
resolver
ensp
ENSP00000649401
resolver
ensp
ENSP00000777935
resolver
enst
ENST00000216027
resolver
enst
ENST00000398941
resolver
enst
ENST00000420442
resolver
genesymbol
HSCB
resolver
genesymbol_syn
DNAJC20
resolver
genesymbol_syn
HSC20
resolver
hgnc
HGNC:28913
resolver
uniprot
A8MYY2
resolver
uniprot
B0QYH2
resolver
uniprot
Q9BWS7
resolver
uniprot_entry
B0QYH2_HUMAN
resolver
uniprot_entry
HSC20_HUMAN
resolver
uniprot_sec
A8MYY2
resolver
uniprot_sec
Q9BWS7
resolver
amino_acid_sequence
MWRGRAGALLRVWGFWPTGVPRRRPLSCDAASQAGSNYPRCWNCGGPWGPGREDRFFCPQCRALQAPDPTRDYFSLMDCNRSFRVDTAKLQHRYQQLQRLVHPDFFSQRSQTEKDFSEKHSTLVNDAYKTLLAPLSRGLYLLKLHGIEIPERTDYEMDRQFLIEIMEINEKLAEAESEAAMKEIESIVKAKQKEFTDNVSSAFEQDDFEEAKEILTKMRYFSNIEEKIKLKKIPL
uniprot
proteins
disease_involvement
DISEASE: Anemia, sideroblastic, 5 (SIDBA5) [MIM:619523]: 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. SIDBA5 inheritance is autosomal recessive. {ECO:0000269|PubMed:32634119}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (PubMed:20668094). Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain (PubMed:26749241). Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241). Plays an essential role in hematopoiesis (By similarity). {ECO:0000250|UniProtKB:Q8K3A0, ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:26749241}.; FUNCTION: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Acts as a co-chaperone in iron-sulfur cluster assembly in the cytoplasm (PubMed:29309586). Also mediates complex formation between components of the cytosolic iron-sulfur biogenesis pathway and the CIA targeting complex composed of CIAO1, DIPK1B/FAM69B and MMS19 by binding directly to the scaffold protein ISCU and to CIAO1 (PubMed:29309586). This facilitates iron-sulfur cluster insertion into a number of cytoplasmic and nuclear proteins including POLD1, ELP3, DPYD and PPAT (PubMed:29309586). {ECO:0000269|PubMed:29309586}.
uniprot
proteins
mass_dalton
27422
uniprot
proteins
mutagenesis
MUTAGEN 41; /note="C->S: Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-44; S-58 and S-61."; /evidence="ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586"; MUTAGEN 44; /note="C->S: Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-58 and S-61."; /evidence="ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586"; MUTAGEN 58; /note="C->S: Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-44 and S-61."; /evidence="ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586"; MUTAGEN 61; /note="C->S: Abolishes self-interaction and interaction with HSPA9 and the CIA complex but does not alter subcellular localization; when associated with S-41; S-44 and S-58."; /evidence="ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586"; MUTAGEN 102..104; /note="HPD->AAA: Does not interact with HSPA9. Does not inhibit interaction with ISCU."; /evidence="ECO:0000269|PubMed:20668094
uniprot
proteins
pathway_participation
PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
uniprot
proteins
protein_family
HscB family
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
12938016
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18713742
uniprot
proteins
pubmed
20668094
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
26749241
uniprot
proteins
pubmed
29309586
uniprot
proteins
pubmed
32634119
uniprot
proteins
sequence_length
235
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:29309586}.; SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB, mitochondrial]: Mitochondrion {ECO:0000269|PubMed:20668094}.
uniprot
proteins