SOSB1_HUMAN
ID SOSB1_HUMAN Reviewed; 211 AA.
AC Q9BQ15; A6NDF8; Q6XYC8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
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;
DE Short=hSSB1;
GN Name=NABP2; Synonyms=OBFC2B, SSB1; ORFNames=LP3587;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Skin;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH ATM AND
RP RAD51, PHOSPHORYLATION AT THR-117, AND MUTAGENESIS OF THR-117.
RX PubMed=18449195; DOI=10.1038/nature06883;
RA Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K.,
RA Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J., Pandita R.K.,
RA Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T., Pandita T.K.,
RA White M.F., Khanna K.K.;
RT "Single-stranded DNA-binding protein hSSB1 is critical for genomic
RT stability.";
RL Nature 453:677-681(2008).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SOSS COMPLEX.
RX PubMed=19605351; DOI=10.1074/jbc.c109.039586;
RA Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J.,
RA Seidman M., Pandita T.K., Khanna K.K., Wang W.;
RT "hSSB1 and hSSB2 form similar multiprotein complexes that participate in
RT DNA damage response.";
RL J. Biol. Chem. 284:23525-23531(2009).
RN [7]
RP FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, DNA-BINDING,
RP IDENTIFICATION IN THE SOSS COMPLEX, AND INTERACTION WITH INTS3.
RX PubMed=19683501; DOI=10.1016/j.molcel.2009.06.011;
RA Huang J., Gong Z., Ghosal G., Chen J.;
RT "SOSS complexes participate in the maintenance of genomic stability.";
RL Mol. Cell 35:384-393(2009).
RN [8]
RP INTERACTION WITH INTS7.
RX PubMed=21659603; DOI=10.1126/science.1203430;
RA Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W.,
RA Elledge S.J.;
RT "A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
RT interacting protein required for ATR signaling.";
RL Science 332:1313-1317(2011).
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. {ECO:0000269|PubMed:18449195,
CC ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
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. {ECO:0000269|PubMed:18449195,
CC ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501,
CC ECO:0000269|PubMed:21659603}.
CC -!- INTERACTION:
CC Q9BQ15; Q13315: ATM; NbExp=4; IntAct=EBI-2120336, EBI-495465;
CC Q9BQ15; P54132: BLM; NbExp=6; IntAct=EBI-2120336, EBI-621372;
CC Q9BQ15; P38936: CDKN1A; NbExp=7; IntAct=EBI-2120336, EBI-375077;
CC Q9BQ15; Q68E01: INTS3; NbExp=9; IntAct=EBI-2120336, EBI-2680854;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18449195,
CC ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
CC Note=Localizes to nuclear foci following DNA damage. Foci formation is
CC not cell-cycle dependent. Partial colocalization with RAD51 after
CC ionizing radiation treatment.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQ15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQ15-2; Sequence=VSP_033604;
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. {ECO:0000269|PubMed:18449195}.
CC -!- SIMILARITY: Belongs to the SOSS-B family. SOSS-B1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP34465.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY203942; AAP34465.1; ALT_FRAME; mRNA.
DR EMBL; CH471054; EAW96913.1; -; Genomic_DNA.
DR EMBL; AC073896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001079; AAH01079.1; -; mRNA.
DR EMBL; BC006171; AAH06171.1; -; mRNA.
DR CCDS; CCDS8911.1; -. [Q9BQ15-1]
DR RefSeq; NP_076973.1; NM_024068.3. [Q9BQ15-1]
DR RefSeq; XP_005269205.1; XM_005269148.4.
DR RefSeq; XP_005269206.1; XM_005269149.4. [Q9BQ15-1]
DR PDB; 4OWT; X-ray; 2.00 A; B=1-211.
DR PDB; 4OWW; X-ray; 2.30 A; B=1-211.
DR PDB; 4OWX; X-ray; 2.30 A; B=1-211.
DR PDB; 5D8E; X-ray; 3.00 A; A/B/C/D=1-109.
DR PDB; 5D8F; X-ray; 2.35 A; A/B=1-109.
DR PDBsum; 4OWT; -.
DR PDBsum; 4OWW; -.
DR PDBsum; 4OWX; -.
DR PDBsum; 5D8E; -.
DR PDBsum; 5D8F; -.
DR AlphaFoldDB; Q9BQ15; -.
DR SMR; Q9BQ15; -.
DR BioGRID; 122500; 59.
DR ComplexPortal; CPX-482; SOSS1 complex.
DR IntAct; Q9BQ15; 21.
DR STRING; 9606.ENSP00000369545; -.
DR GlyGen; Q9BQ15; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ15; -.
DR PhosphoSitePlus; Q9BQ15; -.
DR BioMuta; NABP2; -.
DR DMDM; 74761196; -.
DR EPD; Q9BQ15; -.
DR jPOST; Q9BQ15; -.
DR MassIVE; Q9BQ15; -.
DR MaxQB; Q9BQ15; -.
DR PaxDb; Q9BQ15; -.
DR PeptideAtlas; Q9BQ15; -.
DR PRIDE; Q9BQ15; -.
DR ProteomicsDB; 78609; -. [Q9BQ15-1]
DR ProteomicsDB; 78610; -. [Q9BQ15-2]
DR Antibodypedia; 28054; 137 antibodies from 23 providers.
DR DNASU; 79035; -.
DR Ensembl; ENST00000267023.9; ENSP00000267023.4; ENSG00000139579.13. [Q9BQ15-1]
DR Ensembl; ENST00000341463.5; ENSP00000368862.3; ENSG00000139579.13. [Q9BQ15-1]
DR Ensembl; ENST00000380198.6; ENSP00000369545.2; ENSG00000139579.13. [Q9BQ15-1]
DR GeneID; 79035; -.
DR KEGG; hsa:79035; -.
DR MANE-Select; ENST00000267023.9; ENSP00000267023.4; NM_024068.4; NP_076973.1.
DR UCSC; uc001ski.4; human. [Q9BQ15-1]
DR CTD; 79035; -.
DR DisGeNET; 79035; -.
DR GeneCards; NABP2; -.
DR HGNC; HGNC:28412; NABP2.
DR HPA; ENSG00000139579; Low tissue specificity.
DR MIM; 612104; gene.
DR neXtProt; NX_Q9BQ15; -.
DR OpenTargets; ENSG00000139579; -.
DR PharmGKB; PA143485567; -.
DR VEuPathDB; HostDB:ENSG00000139579; -.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000161079; -.
DR HOGENOM; CLU_102724_0_1_1; -.
DR InParanoid; Q9BQ15; -.
DR OMA; INISLWG; -.
DR OrthoDB; 1512483at2759; -.
DR PhylomeDB; Q9BQ15; -.
DR TreeFam; TF313902; -.
DR PathwayCommons; Q9BQ15; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q9BQ15; -.
DR SIGNOR; Q9BQ15; -.
DR BioGRID-ORCS; 79035; 23 hits in 1085 CRISPR screens.
DR ChiTaRS; NABP2; human.
DR GenomeRNAi; 79035; -.
DR Pharos; Q9BQ15; Tbio.
DR PRO; PR:Q9BQ15; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BQ15; protein.
DR Bgee; ENSG00000139579; Expressed in prefrontal cortex and 183 other tissues.
DR ExpressionAtlas; Q9BQ15; baseline and differential.
DR Genevisible; Q9BQ15; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0070876; C:SOSS complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0070200; P:establishment of protein localization to telomere; IMP:BHF-UCL.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IDA:ComplexPortal.
DR GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR DisProt; DP00864; -.
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 3D-structure; Alternative splicing; DNA damage; DNA repair; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..211
FT /note="SOSS complex subunit B1"
FT /id="PRO_0000333958"
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..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 117
FT /note="Phosphothreonine; by ATM"
FT /evidence="ECO:0000269|PubMed:18449195"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_033604"
FT MUTAGEN 117
FT /note="T->A: Loss of phosphorylation by ATM."
FT /evidence="ECO:0000269|PubMed:18449195"
FT MUTAGEN 117
FT /note="T->E: Enhances ATM-dependent signaling."
FT /evidence="ECO:0000269|PubMed:18449195"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4OWW"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4OWT"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4OWT"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5D8E"
SQ SEQUENCE 211 AA; 22338 MW; B72014397B7947E2 CRC64;
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN
LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYSTQQA
PNKAVQNDSN PSASQPTTGP SAASPASENQ NGNGLSAPPG PGGGPHPPHT PSHPPSTRIT
RSQPNHTPAG PPGPSSNPVS NGKETRRSSK R
