SOSB2_MOUSE
ID SOSB2_MOUSE Reviewed; 198 AA.
AC Q8BGW5; Q8C154; Q8C164;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=SOSS complex subunit B2;
DE AltName: Full=Nucleic acid-binding protein 1;
DE AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 2A;
DE AltName: Full=Sensor of single-strand DNA complex subunit B2;
DE AltName: Full=Sensor of ssDNA subunit B2;
DE Short=SOSS-B2;
DE AltName: Full=Single-stranded DNA-binding protein 2;
GN Name=Nabp1; Synonyms=Obfc2a, Ssb2;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP 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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Amnion, Embryo, Mammary gland, Skin,
RC Spinal ganglion, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Brain, and 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).
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 ECO:0000269|PubMed:16533169}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16533169}.
CC Note=Localizes to nuclear foci following DNA damage. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGW5-2; Sequence=VSP_033603;
CC -!- TISSUE SPECIFICITY: Ubiquitous with high expression in the thymus.
CC {ECO:0000269|PubMed:16533169}.
CC -!- SIMILARITY: Belongs to the SOSS-B family. SOSS-B2 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; AY880264; AAX68444.1; -; mRNA.
DR EMBL; AK015312; BAE43243.1; -; mRNA.
DR EMBL; AK028886; BAC26173.1; -; mRNA.
DR EMBL; AK028936; BAC26201.1; -; mRNA.
DR EMBL; AK049396; BAC33732.1; -; mRNA.
DR EMBL; AK083915; BAC39059.1; -; mRNA.
DR EMBL; AK163613; BAE37421.1; -; mRNA.
DR EMBL; AK166300; BAE38689.1; -; mRNA.
DR EMBL; AK167652; BAE39703.1; -; mRNA.
DR EMBL; BC095967; AAH95967.1; -; mRNA.
DR EMBL; BC131923; AAI31924.1; -; mRNA.
DR EMBL; BC132532; AAI32533.1; -; mRNA.
DR CCDS; CCDS35559.1; -. [Q8BGW5-1]
DR CCDS; CCDS78580.1; -. [Q8BGW5-2]
DR RefSeq; NP_001297477.1; NM_001310548.1. [Q8BGW5-2]
DR RefSeq; NP_001297478.1; NM_001310549.1. [Q8BGW5-2]
DR RefSeq; NP_082972.2; NM_028696.3. [Q8BGW5-1]
DR AlphaFoldDB; Q8BGW5; -.
DR SMR; Q8BGW5; -.
DR ComplexPortal; CPX-615; SOSS2 complex.
DR STRING; 10090.ENSMUSP00000027279; -.
DR PhosphoSitePlus; Q8BGW5; -.
DR EPD; Q8BGW5; -.
DR MaxQB; Q8BGW5; -.
DR PaxDb; Q8BGW5; -.
DR PeptideAtlas; Q8BGW5; -.
DR PRIDE; Q8BGW5; -.
DR ProteomicsDB; 261553; -. [Q8BGW5-1]
DR ProteomicsDB; 261554; -. [Q8BGW5-2]
DR Antibodypedia; 34048; 120 antibodies from 20 providers.
DR DNASU; 109019; -.
DR Ensembl; ENSMUST00000027279; ENSMUSP00000027279; ENSMUSG00000026107. [Q8BGW5-1]
DR Ensembl; ENSMUST00000185534; ENSMUSP00000140557; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000186003; ENSMUSP00000140126; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000186684; ENSMUSP00000140179; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000188051; ENSMUSP00000139853; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000188204; ENSMUSP00000140469; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000189542; ENSMUSP00000140059; ENSMUSG00000026107. [Q8BGW5-2]
DR Ensembl; ENSMUST00000190103; ENSMUSP00000140556; ENSMUSG00000026107. [Q8BGW5-1]
DR GeneID; 109019; -.
DR KEGG; mmu:109019; -.
DR UCSC; uc007axn.1; mouse. [Q8BGW5-1]
DR CTD; 64859; -.
DR MGI; MGI:1923258; Nabp1.
DR VEuPathDB; HostDB:ENSMUSG00000026107; -.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000155812; -.
DR HOGENOM; CLU_102724_2_0_1; -.
DR InParanoid; Q8BGW5; -.
DR OMA; HTVMTTI; -.
DR OrthoDB; 1512483at2759; -.
DR PhylomeDB; Q8BGW5; -.
DR TreeFam; TF313902; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 109019; 3 hits in 108 CRISPR screens.
DR ChiTaRS; Nabp1; mouse.
DR PRO; PR:Q8BGW5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BGW5; protein.
DR Bgee; ENSMUSG00000026107; Expressed in urinary bladder urothelium and 246 other tissues.
DR Genevisible; Q8BGW5; 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; IDA:MGI.
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:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
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:0044818; P:mitotic G2/M transition checkpoint; ISS:UniProtKB.
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 SUPFAM; SSF50249; SSF50249; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..198
FT /note="SOSS complex subunit B2"
FT /id="PRO_0000333955"
FT DNA_BIND 26..89
FT /note="OB"
FT REGION 114..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033603"
FT CONFLICT 182
FT /note="V -> F (in Ref. 2; BAC26173)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21749 MW; 68B2F33CD51D28BE CRC64;
MHGVNDPPLF IKDIKAGLKN LNVVFIVLEI GRVTKTKDGH EVRSCKVADR TGSITISVWD
EIGGLIQTGD IIRLTRGYAS MWKGCLTLYT GRGGELQKIG EFCMVYSEVP NFSEPNPDYR
GQQNRGVQNE QKDKLSTNTF GPVGNGDQTG PESRGYHLPY GRSNGPGPIS PQLPGTPSSQ
TVRTTISNAR DPRRAFKR
