|Institutional Source||Beutler Lab|
|Gene Name||HscB iron-sulfur cluster co-chaperone|
|Is this an essential gene?||Probably essential (E-score: 0.960)|
|Stock #||R5294 (G1)|
|Chromosomal Location||110829070-110839777 bp(-) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||A to G at 110834792 bp (GRCm38)|
|Amino Acid Change||Leucine to Proline at position 143 (L143P)|
|Ref Sequence||ENSEMBL: ENSMUSP00000062811 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000056937] [ENSMUST00000145318]|
|AlphaFold||no structure available at present|
AA Change: L143P
PolyPhen 2 Score 1.000 (Sensitivity: 0.00; Specificity: 1.00)
AA Change: L143P
|Meta Mutation Damage Score||0.9668|
|Coding Region Coverage||
|Validation Efficiency||97% (70/72)|
|MGI Phenotype||FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] 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]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Hscb||
(F):5'- TGTCCTCCTTGGGGAAATTAAGC -3'
(R):5'- ATACCAGCACTCACTGTTACTAGG -3'
(F):5'- CGTCTGCGAGTCTTTCAT -3'
(R):5'- TCACTGTTACTAGGACAGCTCAAG -3'