Tonsl
entrez
72749
canonical
uniprot
Q6NZL6
canonical
ensembl
ENSMUSG00000059323
resolver
ensp
ENSMUSP00000129597
resolver
enst
ENSMUST00000168185
resolver
genesymbol
Tonsl
resolver
genesymbol_syn
Ikbr
resolver
genesymbol_syn
Nfkbil2
resolver
uniprot
G3UW83
resolver
uniprot
Q8BT74
resolver
uniprot
Q9ER45
resolver
uniprot_entry
G3UW83_MOUSE
resolver
uniprot_entry
TONSL_MOUSE
resolver
uniprot_sec
Q8BT74
resolver
uniprot_sec
Q9ER45
resolver
amino_acid_sequence
MTLEQELRQLSKAKTRAQRNGQLREEAAYCHQLGELLASHGRFKDALEEHQQELHLLESVQDTLGCAVAHRKIGERLAEMENYSAALKHQHLYLDLAGSLSNHTELQRAWATIGRTHLDIYDHCQSRDSLLQAQAAFEKSLAIVDEKLEGMLTQRELSEMRTRLYLNLGLTCESLQQTALCNNYFKKSIFLAEQNHLYEDLFRARYNLGAIHWRGGQHSQAMRCLEGARECARAMKMRFMESECCVLVSQVLQDLGDFLAAKRALKKAYRLGSQKPNQRVTVCQSLKYVLAVIQLQQQLEEAEGNDLQGAMAICEQLGDLFSKAGDFPKAAEAYQKQLHLAELLNRPDLELAVIHVSLATTLGDMKDHRKAVHHYEEELRLRKGNALEEAKTWFNIALSREEAGDAYELLAPCFQKAFCCAQQAQRFQLQRQILQHLYTVQLKLQPQEARDTEIRLQELSMAKDTEEEEEEEEEEEEEASEAPETSELELSESEDDADGLSQQLEEDEELQGCVGRRKVNKWNRRNDMGETLLHRACIEGQLRRVQDLVKQGHPLNPRDYCGWTPLHEACNYGHLEIVRFLLDHGAAVDDPGGQGCDGITPLHDALNCGHFEVAELLIERGASVTLRTRKGLSPLETLQQWVKLYFRDLDLETRQKAATMEERLQMASSGQASRSSPALQTIPSNHLFDPETSPPSSPCPEPSSYTPRPPEASPAPAKVFLEETVSAVSRPRKTRHRPTSSSSSSEDEDNPSPCRPSQKRLRHTTQQGEVKIPDPPKSRETATSSACRAAYQAAIRGVGSAQSRRLVPSLPRGSEEVPAPKTALIPEEEYLAGEWLEVDTPLTRSGRPSTSVSDYERCPARPRTRVKQSRLTSLDGWCARTQAGDGSLNAEPAENPSVPRTSGPNKENYAAGQPLLLVQPPPIRVRVQIQDNLFLIPVPQSDIRPVAWLTEQAAQRYFQTCGLLPRLTLRKDGALLAPQDPIPDVLQSNDEVLAEVTSWDLPPLKDRYRRACLSLGQGEHQQVLHAMDHQSSSPSFSACSLALCQAQLTPLLRALKLHTALRELRLAGNRLGDACATELLATLGTTPNLVLLDLSSNHLGQEGLRQLVEGSSGQAALQNLEELDLSMNPLGDGCGQALASLLRACPMLSTLRLQACGFSSSFFLSHQAALGGAFQDAVHLKTLSLSYNLLGAPALARVLQTLPACTLKRLDLSSVAASKSNSGIIEPVIKYLTKEGCALAHLTLSANCLGDKAVRELSRCLPCCPSLTSLDLSANPEVSCASLEELLSALQERSQGLSFLGLSGCSIQGPLNSDLWDKIFVQLQELQLCTKDLSTKDRDSVCQRLPEGACTMDQSSKLFFKCL
uniprot
proteins
function
FUNCTION: 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. {ECO:0000250|UniProtKB:Q96HA7}.
uniprot
proteins
mass_dalton
151108
uniprot
proteins
mutagenesis
MUTAGEN 924; /note="R->W: Homozygous mice are not viable. Embryos show early lethality along with fetal growth restriction and lack of visible blood vessels in yolk sacs."; /evidence="ECO:0000269|PubMed:30773278
uniprot
proteins
protein_family
Tonsoku family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
30773278
uniprot
proteins
pubmed
35298257
uniprot
proteins
sequence_length
1363
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96HA7}. Chromosome {ECO:0000250|UniProtKB:Q96HA7}. Cytoplasm {ECO:0000250|UniProtKB:Q96HA7}. Note=Mainly nuclear. Localizes to DNA damage sites, accumulates at stressed replication forks. Recruited to stalled or collapsed replication forks following histone replacement by histone chaperones ASF1A and the CAF-1 complex: TONSL acts as a histone reader that recognizes and binds newly synthesized histones. {ECO:0000250|UniProtKB:Q96HA7}.
uniprot
proteins