ID:SOSB1_HUMAN DESCRIPTION: RecName: Full=SOSS complex subunit B1; AltName: Full=Nucleic acid-binding protein 2; AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 2B; AltName: Full=Sensor of single-strand DNA complex subunit B1; AltName: Full=Sensor of ssDNA subunit B1; Short=SOSS-B1; AltName: Full=Single-stranded DNA-binding protein 1; Short=hSSB1; FUNCTION: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways. SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS- B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS complexes containing SOSS-B1/NABP2 are more abundant than complexes containing SOSS-B2/NABP1. Directly interacts with ATM, SOSS-A/INTS3 and RAD51. Interacts with INTS7. INTERACTION: Q13315:ATM; NbExp=4; IntAct=EBI-2120336, EBI-495465; P38936:CDKN1A; NbExp=7; IntAct=EBI-2120336, EBI-375077; SUBCELLULAR LOCATION: Nucleus. Note=Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment. PTM: Phosphorylated by ATM in response to DNA damage. Phosphorylation prevents degradation by the proteasome, hence stabilization of the protein and accumulation within cells. SIMILARITY: Belongs to the SOSS-B family. SOSS-B1 subfamily. SIMILARITY: Contains 1 OB DNA-binding domain. SEQUENCE CAUTION: Sequence=AAP34465.1; Type=Frameshift; Positions=169;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9BQ15
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0000724 double-strand break repair via homologous recombination GO:0006281 DNA repair GO:0006974 cellular response to DNA damage stimulus GO:0007093 mitotic cell cycle checkpoint GO:0010212 response to ionizing radiation GO:0042795 snRNA transcription from RNA polymerase II promoter GO:0070200 establishment of protein localization to telomere GO:1904355 positive regulation of telomere capping GO:0051972 regulation of telomerase activity
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Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
