HSCB

Protein identityUniProt · HPA

UniProt accession

Q8IWL3

Gene

HSCB

Ensembl

ENSG00000100209

Chromosome

22

Canonical length

235 aa

Protein class

Disease related genes, Human disease related genes, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Mitochondria,Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes a DnaJ-type co-chaperone and member of the heat shock cognate B (HscB) family of proteins. The encoded protein plays a role in the synthesis of iron-sulfur clusters, protein cofactors that are involved in the redox reactions of mitochondrial electron transport and other processes. Cells in which this gene is knocked down exhibit reduced activity of iron-sulfur cluster-dependent enzymes including succinate dehydrogenase and aconitase. The encoded protein may stimulate the ATPase activity of the mitochondrial stress-70 protein. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2015]

Canonical amino-acid sequenceUniProt

235 residues, UniProt reviewed canonical sequence.

>Q8IWL3|HSCB
     1  MWRGRAGALL RVWGFWPTGV PRRRPLSCDA ASQAGSNYPR CWNCGGPWGP GREDRFFCPQ
    61  CRALQAPDPT RDYFSLMDCN RSFRVDTAKL QHRYQQLQRL VHPDFFSQRS QTEKDFSEKH
   121  STLVNDAYKT LLAPLSRGLY LLKLHGIEIP ERTDYEMDRQ FLIEIMEINE KLAEAESEAA
   181  MKEIESIVKA KQKEFTDNVS SAFEQDDFEE AKEILTKMRY FSNIEEKIKL KKIPL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against HSCB can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.39

Highest tissue expression

21 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about HSCB.

Disease | AllUniProt

Conditions HSCB is implicated in, by any mechanism.

• Anemia, sideroblastic, 5 (SIDBA5) MIM:619523

Disease | GeneticClinVar

2 pathogenic / likely-pathogenic of 53 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Anemia, sideroblastic, 5

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.91

gnomAD pLI

0

gnomAD missense Z

0.19

DepMap mean gene effect

-0.63

DepMap dependency class

common

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• [2Fe-2S] cluster assembly
• iron-sulfur cluster assembly
• primitive erythrocyte differentiation
• primitive hemopoiesis
• protein complex oligomerization

Molecular functions

• ATPase activator activity
• identical protein binding
• metal ion binding
• protein-folding chaperone binding

Cellular components

• cytoplasm
• cytosol
• mitochondrion
• nucleoplasm

Protein domainsUniProt · Pfam · InterPro

• Chaperone J-domain superfamily
• Co-chaperone Hsc20
• Co-chaperone HscB, C-terminal oligomerisation domain
• HscB, C-terminal domain superfamily
• HscB, tetracysteine metal binding motif
• HSCB C-terminal oligomerisation domain
• Co-chaperone HscB tetracysteine metal binding motif

KeywordsUniProt

• Chaperone
• Cytoplasm
• Metal-binding
• Mitochondrion

InteractionsUniProt · HPA

Protein binding partners of HSCB in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• HSC20
• HSPA9
• ISCU
• SDHAF1
• ETFA
• LYRM7
• NDUFV2
• PDHX
• PNPT1