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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Tonsoku-like protein

UniprotKB/SwissProt ID: Q96HA7 (Q96HA7)

Gene Name: TONSL

Organism: Homo sapiens (Human)

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 (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:21113133, PubMed:26527279, PubMed:27338793, PubMed:27797818, PubMed:29478807, PubMed:30773278). The MMS22L-TONSL complex is required to maintain genome integrity during DNA replication (PubMed:21055983, PubMed:21055984, PubMed:21055985). 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 (PubMed:21055983, PubMed:21055984, PubMed:21055985, PubMed:27797818, PubMed:29478807). Following recruitment to DSBs, the TONSL-MMS22L complex promotes recruitment of RAD51 filaments and subsequent homologous recombination (PubMed:27797818, PubMed:29478807). Within the complex, TONSL acts as a histone reader, which recognizes and binds newly synthesized histones following their replacement by histone chaperones (PubMed:27338793, PubMed:29478807). Specifically binds histone H4 lacking methylation at 'Lys-20' (H4K20me0) and histone H3.1 (PubMed:27338793)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Chromosome. Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002110 Ankyrin_rpt
IPR036770 Ankyrin_rpt-contain_sf
IPR001611 Leu-rich_rpt
IPR032675 LRR_dom_sf
IPR052311 MMS22L-TONSL_complex_comp
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_rpt

The S-nitrosylation sites of Q96HA7

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 537 DMGETLLHRA C IEGQLRRVQD