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SOSS complex subunit B1 (Nucleic acid-binding protein 2) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2B) (Sensor of single-strand DNA complex subunit B1) (Sensor of ssDNA subunit B1) (SOSS-B1) (Single-stranded DNA-binding protein 1) (hSSB1)

 SOSB1_HUMAN             Reviewed;         211 AA.
Q9BQ15; A6NDF8; Q6XYC8;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
05-DEC-2018, entry version 142.
RecName: Full=SOSS complex subunit B1;
AltName: Full=Nucleic acid-binding protein 2;
AltName: Full=Oligonucleotide/oligosaccharide-binding fold-containing protein 2B;
AltName: Full=Sensor of single-strand DNA complex subunit B1;
AltName: Full=Sensor of ssDNA subunit B1;
Short=SOSS-B1;
AltName: Full=Single-stranded DNA-binding protein 1;
Short=hSSB1;
Name=NABP2; Synonyms=OBFC2B, SSB1; ORFNames=LP3587;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH ATM AND
RAD51, PHOSPHORYLATION AT THR-117, AND MUTAGENESIS OF THR-117.
PubMed=18449195; DOI=10.1038/nature06883;
Richard D.J., Bolderson E., Cubeddu L., Wadsworth R.I.M., Savage K.,
Sharma G.G., Nicolette M.L., Tsvetanov S., McIlwraith M.J.,
Pandita R.K., Takeda S., Hay R.T., Gautier J., West S.C., Paull T.T.,
Pandita T.K., White M.F., Khanna K.K.;
"Single-stranded DNA-binding protein hSSB1 is critical for genomic
stability.";
Nature 453:677-681(2008).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SOSS
COMPLEX.
PubMed=19605351; DOI=10.1074/jbc.C109.039586;
Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J.,
Seidman M., Pandita T.K., Khanna K.K., Wang W.;
"hSSB1 and hSSB2 form similar multiprotein complexes that participate
in DNA damage response.";
J. Biol. Chem. 284:23525-23531(2009).
[7]
FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, DNA-BINDING,
IDENTIFICATION IN THE SOSS COMPLEX, AND INTERACTION WITH INTS3.
PubMed=19683501; DOI=10.1016/j.molcel.2009.06.011;
Huang J., Gong Z., Ghosal G., Chen J.;
"SOSS complexes participate in the maintenance of genomic stability.";
Mol. Cell 35:384-393(2009).
[8]
INTERACTION WITH INTS7.
PubMed=21659603; DOI=10.1126/science.1203430;
Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E.,
Harper J.W., Elledge S.J.;
"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1
interacting protein required for ATR signaling.";
Science 332:1313-1317(2011).
-!- FUNCTION: Component of the SOSS complex, a multiprotein complex
that functions downstream of the MRN complex to promote DNA repair
and G2/M checkpoint. In the SOSS complex, acts as a sensor of
single-stranded DNA that binds to single-stranded DNA, in
particular to polypyrimidines. The SOSS complex associates with
DNA lesions and influences diverse endpoints in the cellular DNA
damage response including cell-cycle checkpoint activation,
recombinational repair and maintenance of genomic stability.
Required for efficient homologous recombination-dependent repair
of double-strand breaks (DSBs) and ATM-dependent signaling
pathways. {ECO:0000269|PubMed:18449195,
ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
-!- SUBUNIT: Component of the SOSS complex, composed of SOSS-B (SOSS-
B1/NABP2 or SOSS-B2/NABP1), SOSS-A/INTS3 and SOSS-C/INIP. SOSS
complexes containing SOSS-B1/NABP2 are more abundant than
complexes containing SOSS-B2/NABP1. Directly interacts with ATM,
SOSS-A/INTS3 and RAD51. Interacts with INTS7.
{ECO:0000269|PubMed:18449195, ECO:0000269|PubMed:19605351,
ECO:0000269|PubMed:19683501, ECO:0000269|PubMed:21659603}.
-!- INTERACTION:
Q13315:ATM; NbExp=4; IntAct=EBI-2120336, EBI-495465;
P38936:CDKN1A; NbExp=7; IntAct=EBI-2120336, EBI-375077;
Q68E01:INTS3; NbExp=7; IntAct=EBI-2120336, EBI-2680854;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18449195,
ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}.
Note=Localizes to nuclear foci following DNA damage. Foci
formation is not cell-cycle dependent. Partial colocalization with
RAD51 after ionizing radiation treatment.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BQ15-1; Sequence=Displayed;
Name=2;
IsoId=Q9BQ15-2; Sequence=VSP_033604;
-!- PTM: Phosphorylated by ATM in response to DNA damage.
Phosphorylation prevents degradation by the proteasome, hence
stabilization of the protein and accumulation within cells.
{ECO:0000269|PubMed:18449195}.
-!- SIMILARITY: Belongs to the SOSS-B family. SOSS-B1 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAP34465.1; Type=Frameshift; Positions=169; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY203942; AAP34465.1; ALT_FRAME; mRNA.
EMBL; CH471054; EAW96913.1; -; Genomic_DNA.
EMBL; AC073896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001079; AAH01079.1; -; mRNA.
EMBL; BC006171; AAH06171.1; -; mRNA.
CCDS; CCDS8911.1; -. [Q9BQ15-1]
RefSeq; NP_076973.1; NM_024068.3. [Q9BQ15-1]
RefSeq; XP_005269205.1; XM_005269148.4.
RefSeq; XP_005269206.1; XM_005269149.4. [Q9BQ15-1]
UniGene; Hs.240170; -.
PDB; 4OWT; X-ray; 2.00 A; B=1-211.
PDB; 4OWW; X-ray; 2.30 A; B=1-211.
PDB; 4OWX; X-ray; 2.30 A; B=1-211.
PDB; 5D8E; X-ray; 3.00 A; A/B/C/D=1-109.
PDB; 5D8F; X-ray; 2.35 A; A/B=1-109.
PDBsum; 4OWT; -.
PDBsum; 4OWW; -.
PDBsum; 4OWX; -.
PDBsum; 5D8E; -.
PDBsum; 5D8F; -.
DisProt; DP00864; -.
ProteinModelPortal; Q9BQ15; -.
SMR; Q9BQ15; -.
BioGrid; 122500; 51.
ComplexPortal; CPX-482; SOSS1 complex.
IntAct; Q9BQ15; 20.
STRING; 9606.ENSP00000267023; -.
iPTMnet; Q9BQ15; -.
PhosphoSitePlus; Q9BQ15; -.
BioMuta; NABP2; -.
DMDM; 74761196; -.
EPD; Q9BQ15; -.
MaxQB; Q9BQ15; -.
PaxDb; Q9BQ15; -.
PeptideAtlas; Q9BQ15; -.
PRIDE; Q9BQ15; -.
ProteomicsDB; 78609; -.
ProteomicsDB; 78610; -. [Q9BQ15-2]
DNASU; 79035; -.
Ensembl; ENST00000267023; ENSP00000267023; ENSG00000139579. [Q9BQ15-1]
Ensembl; ENST00000341463; ENSP00000368862; ENSG00000139579. [Q9BQ15-1]
Ensembl; ENST00000380198; ENSP00000369545; ENSG00000139579. [Q9BQ15-1]
GeneID; 79035; -.
KEGG; hsa:79035; -.
UCSC; uc001ski.4; human. [Q9BQ15-1]
CTD; 79035; -.
DisGeNET; 79035; -.
EuPathDB; HostDB:ENSG00000139579.12; -.
GeneCards; NABP2; -.
HGNC; HGNC:28412; NABP2.
HPA; HPA044615; -.
HPA; HPA057213; -.
MIM; 612104; gene.
neXtProt; NX_Q9BQ15; -.
OpenTargets; ENSG00000139579; -.
PharmGKB; PA143485567; -.
eggNOG; KOG3416; Eukaryota.
eggNOG; ENOG4111MBP; LUCA.
GeneTree; ENSGT00940000161079; -.
HOGENOM; HOG000006622; -.
InParanoid; Q9BQ15; -.
OMA; MASENGT; -.
OrthoDB; EOG091G0YHH; -.
PhylomeDB; Q9BQ15; -.
TreeFam; TF313902; -.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
ChiTaRS; NABP2; human.
GenomeRNAi; 79035; -.
PRO; PR:Q9BQ15; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139579; Expressed in 209 organ(s), highest expression level in anterior cingulate cortex.
CleanEx; HS_OBFC2B; -.
ExpressionAtlas; Q9BQ15; baseline and differential.
Genevisible; Q9BQ15; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070876; C:SOSS complex; IDA:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
GO; GO:0070200; P:establishment of protein localization to telomere; IMP:BHF-UCL.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:UniProtKB.
GO; GO:1904355; P:positive regulation of telomere capping; IMP:BHF-UCL.
GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004365; NA-bd_OB_tRNA.
Pfam; PF01336; tRNA_anti-codon; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 211 SOSS complex subunit B1.
/FTId=PRO_0000333958.
DNA_BIND 22 92 OB.
COMPBIAS 158 198 Pro-rich.
MOD_RES 117 117 Phosphothreonine; by ATM.
{ECO:0000269|PubMed:18449195}.
VAR_SEQ 1 99 Missing (in isoform 2).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_033604.
MUTAGEN 117 117 T->A: Loss of phosphorylation by ATM.
{ECO:0000269|PubMed:18449195}.
MUTAGEN 117 117 T->E: Enhances ATM-dependent signaling.
{ECO:0000269|PubMed:18449195}.
HELIX 7 9 {ECO:0000244|PDB:4OWT}.
STRAND 20 26 {ECO:0000244|PDB:4OWT}.
STRAND 33 35 {ECO:0000244|PDB:4OWW}.
STRAND 40 45 {ECO:0000244|PDB:4OWT}.
STRAND 48 53 {ECO:0000244|PDB:4OWT}.
HELIX 56 61 {ECO:0000244|PDB:4OWT}.
STRAND 66 69 {ECO:0000244|PDB:4OWT}.
STRAND 93 98 {ECO:0000244|PDB:4OWT}.
STRAND 100 104 {ECO:0000244|PDB:5D8E}.
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


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