TONSL report

I. Expression across cell types

Insufficient scRNA-seq data for expression of TONSL at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of TONSL at tissue level.

III. Associated gene sets

GO_0006325Biological processchromatin organization
GO_0000724Biological processdouble-strand break repair via homologous recombination
GO_0031297Biological processreplication fork processing
GO_0071168Biological processprotein localization to chromatin
GO_0043596Cellular componentnuclear replication fork
GO_0042555Cellular componentMCM complex
GO_0035101Cellular componentFACT complex
GO_0005662Cellular componentDNA replication factor A complex
GO_0005654Cellular componentnucleoplasm
GO_0016604Cellular componentnuclear body
GO_0035861Cellular componentsite of double-strand break
GO_0005737Cellular componentcytoplasm
GO_0005515Molecular functionprotein binding
GO_0042393Molecular functionhistone binding
GO_0140566Molecular functionhistone reader activity

IV. Literature review

[source]
Gene nameTONSL
Protein nameTonsoku-like protein (Inhibitor of kappa B-related protein) (I-kappa-B-related protein) (IkappaBR) (NF-kappa-B inhibitor-like protein 2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 2)
SynonymsIKBR
NFKBIL2
DescriptionFUNCTION: Component of the MMS22L-TONSL complex, a complex that promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks . The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication . It mediates the assembly of RAD51 filaments on single-stranded DNA (ssDNA): the MMS22L-TONSL complex is recruited to DSBs following histone replacement by histone chaperones and eviction of the replication protein A complex (RPA/RP-A) from DSBs . Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination . Within the complex, TONSL acts as a histone reader, which recognizes and binds newly synthesized histones following their replacement by histone chaperones . Specifically binds histone H4 lacking methylation at 'Lys-20' (H4K20me0) and histone H3.1 . .

AccessionsQ96HA7
ENST00000409379.8 [Q96HA7-1]