SOSB1_RAT
ID SOSB1_RAT Reviewed; 211 AA.
AC Q3SWT1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
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}.
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DR EMBL; BC104710; AAI04711.1; -; mRNA.
DR RefSeq; NP_001030111.2; NM_001034939.1.
DR RefSeq; NP_001231748.1; NM_001244819.1.
DR RefSeq; XP_006240831.1; XM_006240769.3.
DR RefSeq; XP_006240832.1; XM_006240770.3.
DR RefSeq; XP_006240833.1; XM_006240771.3.
DR RefSeq; XP_008763251.1; XM_008765029.2.
DR AlphaFoldDB; Q3SWT1; -.
DR SMR; Q3SWT1; -.
DR STRING; 10116.ENSRNOP00000036341; -.
DR iPTMnet; Q3SWT1; -.
DR PhosphoSitePlus; Q3SWT1; -.
DR PaxDb; Q3SWT1; -.
DR PRIDE; Q3SWT1; -.
DR Ensembl; ENSRNOT00000111806; ENSRNOP00000090943; ENSRNOG00000023480.
DR GeneID; 362813; -.
DR KEGG; rno:362813; -.
DR UCSC; RGD:1308158; rat.
DR CTD; 79035; -.
DR RGD; 1308158; Nabp2.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000161079; -.
DR HOGENOM; CLU_102724_0_1_1; -.
DR InParanoid; Q3SWT1; -.
DR OrthoDB; 1512483at2759; -.
DR PhylomeDB; Q3SWT1; -.
DR TreeFam; TF313902; -.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q3SWT1; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000023480; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q3SWT1; baseline and differential.
DR Genevisible; Q3SWT1; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISO:RGD.
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:RGD.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:RGD.
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; ISS:UniProtKB.
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:RGD.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD.
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 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..211
FT /note="SOSS complex subunit B1"
FT /id="PRO_0000333961"
FT DNA_BIND 22..92
FT /note="OB"
FT REGION 110..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..158
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 211 AA; 22377 MW; F3532C0DB7B24F96 CRC64;
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN
LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYNTQQA
SNKSVQNDSS PTAPQATTGP PAASPASESQ NGNGLSTQPG PVGGPHPSHA PSHPPSTRIT
RSQPNHTPSG PPGPSSSPVS NGKETRRSSK R
