SOSB1_BOVIN
ID SOSB1_BOVIN Reviewed; 211 AA.
AC A6QLK2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; BC147994; AAI47995.1; -; mRNA.
DR RefSeq; NP_001094621.1; NM_001101151.1.
DR RefSeq; XP_005206696.1; XM_005206639.2.
DR RefSeq; XP_005206697.1; XM_005206640.3.
DR RefSeq; XP_005206698.1; XM_005206641.2.
DR AlphaFoldDB; A6QLK2; -.
DR SMR; A6QLK2; -.
DR STRING; 9913.ENSBTAP00000041786; -.
DR PaxDb; A6QLK2; -.
DR PRIDE; A6QLK2; -.
DR Ensembl; ENSBTAT00000044279; ENSBTAP00000041786; ENSBTAG00000002798.
DR GeneID; 533842; -.
DR KEGG; bta:533842; -.
DR CTD; 79035; -.
DR VEuPathDB; HostDB:ENSBTAG00000002798; -.
DR VGNC; VGNC:31860; NABP2.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000161079; -.
DR HOGENOM; CLU_102724_0_1_1; -.
DR InParanoid; A6QLK2; -.
DR OMA; INISLWG; -.
DR OrthoDB; 1512483at2759; -.
DR TreeFam; TF313902; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000002798; Expressed in gluteus medius and 105 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
DR GO; GO:1904355; P:positive regulation of telomere capping; IEA:Ensembl.
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; Reference proteome.
FT CHAIN 1..211
FT /note="SOSS complex subunit B1"
FT /id="PRO_0000333959"
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..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 22275 MW; 9721B80BBF7D8154 CRC64;
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN
LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYSAQQA
PNKTVQNDSG PAAPQPPTGP PATSPASESQ NGNGLSAPPG SGGGPHPPHT PSHPPSTRIT
RSQPNHTAAG PPGPSNNPVS NGKETRRSSK R
