SOSB1_MOUSE
ID SOSB1_MOUSE Reviewed; 212 AA.
AC Q8R2Y9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=SOSS complex subunit B1;
DE AltName: Full=Nucleic acid-binding protein 2;
DE AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 2B;
DE AltName: Full=Sensor of single-strand DNA complex subunit B1;
DE AltName: Full=Sensor of ssDNA subunit B1;
DE Short=SOSS-B1;
DE AltName: Full=Single-stranded DNA-binding protein 1;
GN Name=Nabp2; Synonyms=Obfc2b, Ssb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16533169; DOI=10.1042/bj20051781;
RA Kang H.S., Beak J.Y., Kim Y.-S., Petrovich R.M., Collins J.B.,
RA Grissom S.F., Jetten A.M.;
RT "NABP1, a novel RORgamma-regulated gene encoding a single-stranded nucleic-
RT acid-binding protein.";
RL Biochem. J. 397:89-99(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the SOSS complex, a multiprotein complex that
CC functions downstream of the MRN complex to promote DNA repair and G2/M
CC checkpoint. In the SOSS complex, acts as a sensor of single-stranded
CC DNA that binds to single-stranded DNA, in particular to
CC polypyrimidines. The SOSS complex associates with DNA lesions and
CC influences diverse endpoints in the cellular DNA damage response
CC including cell-cycle checkpoint activation, recombinational repair and
CC maintenance of genomic stability. Required for efficient homologous
CC recombination-dependent repair of double-strand breaks (DSBs) and ATM-
CC dependent signaling pathways (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-
CC B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS
CC complexes containing SOSS-B1/NABP2 are more abundant than complexes
CC containing SOSS-B2/NABP1. Directly interacts with ATM, SOSS-A/INTS3 and
CC RAD51. Interacts with INTS7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear
CC foci following DNA damage. Foci formation is not cell-cycle dependent.
CC Partial colocalization with RAD51 after ionizing radiation treatment
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by ATM in response to DNA damage. Phosphorylation
CC prevents degradation by the proteasome, hence stabilization of the
CC protein and accumulation within cells (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SOSS-B family. SOSS-B1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ158906; AAZ85395.1; -; mRNA.
DR EMBL; BC026942; AAH26942.1; -; mRNA.
DR CCDS; CCDS24276.1; -.
DR RefSeq; NP_081533.1; NM_027257.1.
DR RefSeq; XP_006514129.1; XM_006514066.3.
DR RefSeq; XP_006514130.1; XM_006514067.2.
DR RefSeq; XP_006514131.1; XM_006514068.1.
DR AlphaFoldDB; Q8R2Y9; -.
DR SMR; Q8R2Y9; -.
DR BioGRID; 213754; 1.
DR ComplexPortal; CPX-613; SOSS1 complex.
DR STRING; 10090.ENSMUSP00000026439; -.
DR PhosphoSitePlus; Q8R2Y9; -.
DR EPD; Q8R2Y9; -.
DR MaxQB; Q8R2Y9; -.
DR PaxDb; Q8R2Y9; -.
DR PRIDE; Q8R2Y9; -.
DR ProteomicsDB; 261552; -.
DR Antibodypedia; 28054; 137 antibodies from 23 providers.
DR Ensembl; ENSMUST00000026439; ENSMUSP00000026439; ENSMUSG00000025374.
DR Ensembl; ENSMUST00000164199; ENSMUSP00000128634; ENSMUSG00000025374.
DR GeneID; 69917; -.
DR KEGG; mmu:69917; -.
DR UCSC; uc007hmq.1; mouse.
DR CTD; 79035; -.
DR MGI; MGI:1917167; Nabp2.
DR VEuPathDB; HostDB:ENSMUSG00000025374; -.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000161079; -.
DR HOGENOM; CLU_102724_0_1_1; -.
DR InParanoid; Q8R2Y9; -.
DR OMA; INISLWG; -.
DR OrthoDB; 1512483at2759; -.
DR PhylomeDB; Q8R2Y9; -.
DR TreeFam; TF313902; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 69917; 3 hits in 108 CRISPR screens.
DR ChiTaRS; Nabp2; mouse.
DR PRO; PR:Q8R2Y9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8R2Y9; protein.
DR Bgee; ENSMUSG00000025374; Expressed in embryonic post-anal tail and 73 other tissues.
DR ExpressionAtlas; Q8R2Y9; baseline and differential.
DR Genevisible; Q8R2Y9; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISO:MGI.
DR GO; GO:0070876; C:SOSS complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:BHF-UCL.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..212
FT /note="SOSS complex subunit B1"
FT /id="PRO_0000333960"
FT DNA_BIND 22..92
FT /note="OB"
FT REGION 110..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphothreonine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ15"
SQ SEQUENCE 212 AA; 22628 MW; C9DFB0B6AB3323CE CRC64;
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN
LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYNTQQA
PNKSVQNNDN SPTAPQATTG PPAASPASEN QNGNGLSTQL GPVGGPHPSH TPSHPPSTRI
TRSQPNHTPS GPPGPSSNPV SNGKETRRSS KR
