SOSB2_HUMAN
ID SOSB2_HUMAN Reviewed; 204 AA.
AC Q96AH0; Q658Y8; Q9H5X6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
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;
DE Short=hSSB2;
GN Name=NABP1; Synonyms=OBFC2A, SSB2;
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 3).
RC TISSUE=Ileal mucosa;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
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 [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, AND IDENTIFICATION IN
RP THE SOSS COMPLEX.
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).
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:19605351,
CC 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. {ECO:0000269|PubMed:19605351,
CC ECO:0000269|PubMed:19683501}.
CC -!- INTERACTION:
CC Q96AH0; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-2889252, EBI-350590;
CC Q96AH0; Q68E01: INTS3; NbExp=5; IntAct=EBI-2889252, EBI-2680854;
CC Q96AH0; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-2889252, EBI-742808;
CC Q96AH0; Q13064: MKRN3; NbExp=3; IntAct=EBI-2889252, EBI-2340269;
CC Q96AH0; Q96QR8: PURB; NbExp=3; IntAct=EBI-2889252, EBI-2880222;
CC Q96AH0; Q96PU8: QKI; NbExp=3; IntAct=EBI-2889252, EBI-945792;
CC Q96AH0; P38159: RBMX; NbExp=6; IntAct=EBI-2889252, EBI-743526;
CC Q96AH0; Q04864-2: REL; NbExp=3; IntAct=EBI-2889252, EBI-10829018;
CC Q96AH0; Q12800: TFCP2; NbExp=3; IntAct=EBI-2889252, EBI-717422;
CC Q96AH0; Q9C029: TRIM7; NbExp=3; IntAct=EBI-2889252, EBI-2813981;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19605351,
CC ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following
CC DNA damage.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96AH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AH0-2; Sequence=VSP_033600;
CC Name=3;
CC IsoId=Q96AH0-3; Sequence=VSP_033601, VSP_033602;
CC -!- SIMILARITY: Belongs to the SOSS-B family. SOSS-B2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK026486; BAB15491.1; -; mRNA.
DR EMBL; AL832659; CAH56209.1; -; mRNA.
DR EMBL; AC114778; AAY24348.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10836.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10837.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX10838.1; -; Genomic_DNA.
DR EMBL; BC017114; AAH17114.1; -; mRNA.
DR EMBL; BC107723; AAI07724.1; -; mRNA.
DR CCDS; CCDS33352.1; -. [Q96AH0-1]
DR CCDS; CCDS58745.1; -. [Q96AH0-2]
DR RefSeq; NP_001026886.1; NM_001031716.2. [Q96AH0-1]
DR RefSeq; NP_001241665.1; NM_001254736.1. [Q96AH0-2]
DR RefSeq; XP_016860211.1; XM_017004722.1.
DR AlphaFoldDB; Q96AH0; -.
DR SMR; Q96AH0; -.
DR BioGRID; 122332; 24.
DR ComplexPortal; CPX-614; SOSS2 complex.
DR IntAct; Q96AH0; 21.
DR STRING; 9606.ENSP00000403683; -.
DR GlyGen; Q96AH0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96AH0; -.
DR PhosphoSitePlus; Q96AH0; -.
DR BioMuta; NABP1; -.
DR DMDM; 74760705; -.
DR EPD; Q96AH0; -.
DR jPOST; Q96AH0; -.
DR MassIVE; Q96AH0; -.
DR MaxQB; Q96AH0; -.
DR PaxDb; Q96AH0; -.
DR PeptideAtlas; Q96AH0; -.
DR PRIDE; Q96AH0; -.
DR ProteomicsDB; 75963; -. [Q96AH0-1]
DR ProteomicsDB; 75964; -. [Q96AH0-2]
DR ProteomicsDB; 75965; -. [Q96AH0-3]
DR Antibodypedia; 34048; 120 antibodies from 20 providers.
DR DNASU; 64859; -.
DR Ensembl; ENST00000307849.7; ENSP00000307968.3; ENSG00000173559.15. [Q96AH0-3]
DR Ensembl; ENST00000409510.5; ENSP00000386605.1; ENSG00000173559.15. [Q96AH0-2]
DR Ensembl; ENST00000410026.7; ENSP00000387243.1; ENSG00000173559.15. [Q96AH0-2]
DR Ensembl; ENST00000425611.9; ENSP00000403683.2; ENSG00000173559.15. [Q96AH0-1]
DR Ensembl; ENST00000451500.5; ENSP00000390901.1; ENSG00000173559.15. [Q96AH0-3]
DR Ensembl; ENST00000674172.1; ENSP00000501340.1; ENSG00000173559.15. [Q96AH0-1]
DR Ensembl; ENST00000674187.1; ENSP00000501440.1; ENSG00000173559.15. [Q96AH0-2]
DR Ensembl; ENST00000674262.1; ENSP00000501487.1; ENSG00000173559.15. [Q96AH0-1]
DR Ensembl; ENST00000674360.1; ENSP00000501480.1; ENSG00000173559.15. [Q96AH0-2]
DR Ensembl; ENST00000674406.1; ENSP00000501496.1; ENSG00000173559.15. [Q96AH0-2]
DR Ensembl; ENST00000674414.1; ENSP00000501415.1; ENSG00000173559.15. [Q96AH0-1]
DR GeneID; 64859; -.
DR KEGG; hsa:64859; -.
DR MANE-Select; ENST00000425611.9; ENSP00000403683.2; NM_001031716.5; NP_001026886.1.
DR UCSC; uc002usw.4; human. [Q96AH0-1]
DR CTD; 64859; -.
DR DisGeNET; 64859; -.
DR GeneCards; NABP1; -.
DR HGNC; HGNC:26232; NABP1.
DR HPA; ENSG00000173559; Tissue enhanced (lymphoid).
DR MalaCards; NABP1; -.
DR MIM; 612103; gene.
DR neXtProt; NX_Q96AH0; -.
DR OpenTargets; ENSG00000173559; -.
DR Orphanet; 520; Acute promyelocytic leukemia.
DR PharmGKB; PA143485566; -.
DR VEuPathDB; HostDB:ENSG00000173559; -.
DR eggNOG; KOG3416; Eukaryota.
DR GeneTree; ENSGT00940000155812; -.
DR HOGENOM; CLU_102724_2_0_1; -.
DR InParanoid; Q96AH0; -.
DR OMA; HTVMTTI; -.
DR OrthoDB; 1512483at2759; -.
DR PhylomeDB; Q96AH0; -.
DR TreeFam; TF313902; -.
DR PathwayCommons; Q96AH0; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q96AH0; -.
DR BioGRID-ORCS; 64859; 12 hits in 1086 CRISPR screens.
DR ChiTaRS; NABP1; human.
DR GenomeRNAi; 64859; -.
DR Pharos; Q96AH0; Tbio.
DR PRO; PR:Q96AH0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q96AH0; protein.
DR Bgee; ENSG00000173559; Expressed in secondary oocyte and 160 other tissues.
DR ExpressionAtlas; Q96AH0; baseline and differential.
DR Genevisible; Q96AH0; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS: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:0003723; F:RNA 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; 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:0044818; P:mitotic G2/M transition checkpoint; IDA:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..204
FT /note="SOSS complex subunit B2"
FT /id="PRO_0000333954"
FT DNA_BIND 26..99
FT /note="OB"
FT REGION 114..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
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:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_033600"
FT VAR_SEQ 101..134
FT /note="EFCMVYSEVPNFSEPNPDYRGQQNKGAQSEQKNN -> DLGAVQAAAMRDSI
FT HYYPGNDLHPDLEEPSSLGV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033601"
FT VAR_SEQ 135..204
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033602"
FT VARIANT 154
FT /note="T -> S (in dbSNP:rs12612256)"
FT /id="VAR_043340"
SQ SEQUENCE 204 AA; 22423 MW; EF7579A452381E47 CRC64;
MNRVNDPLIF IRDIKPGLKN LNVVFIVLEI GRVTKTKDGH EVRSCKVADK TGSITISVWD
EIGGLIQPGD IIRLTRGYAS MWKGCLTLYT GRGGELQKIG EFCMVYSEVP NFSEPNPDYR
GQQNKGAQSE QKNNSMNSNM GTGTFGPVGN GVHTGPESRE HQFSHAGRSN GRGLINPQLQ
GTASNQTVMT TISNGRDPRR AFKR
