Q9BQ15 (SOSB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SOSS complex subunit B1

Alternative name(s):
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
Short name=SOSS-B1
Single-stranded DNA-binding protein 1
Short name=hSSB1

Gene names

Name:	NABP2
Synonyms:	OBFC2B, SSB1
ORF Names:	LP3587

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6 Ref.7
Subunit structure	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. Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus. Note: Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment. Ref.5 Ref.6 Ref.7
Post-translational modification	Phosphorylated by ATM in response to DNA damage. Phosphorylation prevents degradation by the proteasome, hence stabilization of the protein and accumulation within cells. Ref.5
Sequence similarities	Belongs to the SOSS-B family. SOSS-B1 subfamily. Contains 1 OB DNA-binding domain.
Sequence caution	The sequence AAP34465.1 differs from that shown. Reason: Frameshift at position 169.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle checkpoint Inferred from mutant phenotype Ref.7. Source: UniProtKB double-strand break repair via homologous recombination Inferred from mutant phenotype Ref.6. Source: UniProtKB response to ionizing radiation Inferred from mutant phenotype Ref.6Ref.7. Source: UniProtKB
Cellular_component	SOSS complex Inferred from direct assay Ref.5Ref.7. Source: UniProtKB
Molecular_function	single-stranded DNA binding Inferred from direct assay Ref.5Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATM	Q13315	4	EBI-2120336,EBI-495465
CDKN1A	P38936	7	EBI-2120336,EBI-375077

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BQ15-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BQ15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 211	211	SOSS complex subunit B1		PRO_0000333958
Regions
	DNA binding	22 – 92	71	OB Ref.5 Ref.7
	Compositional bias	158 – 198	41	Pro-rich
Amino acid modifications
	Modified residue	117	1	Phosphothreonine; by ATM Ref.5
Natural variations
	Alternative sequence	1 – 99	99	Missing in isoform 2.		VSP_033604
Experimental info
	Mutagenesis	117	1	T → A: Loss of phosphorylation by ATM. Ref.5
	Mutagenesis	117	1	T → E: Enhances ATM-dependent signaling. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: B72014397B7947E2	FASTA	211	22,338
	10 20 30 40 50 60 MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN 70 80 90 100 110 120 LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYSTQQA 130 140 150 160 170 180 PNKAVQNDSN PSASQPTTGP SAASPASENQ NGNGLSAPPG PGGGPHPPHT PSHPPSTRIT 190 200 210 RSQPNHTPAG PPGPSSNPVS NGKETRRSSK R
	Isoform 2 [UniParc]. Checksum: B066AA52BECFDC94	FASTA	112	11,493
	10 20 30 40 50 60 MVYSEVPNFS EPNPEYSTQQ APNKAVQNDS NPSASQPTTG PSAASPASEN QNGNGLSAPP 70 80 90 100 110 GPGGGPHPPH TPSHPPSTRI TRSQPNHTPA GPPGPSSNPV SNGKETRRSS KR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." 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. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The finished DNA sequence of human chromosome 12." 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. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung and Skin.
[5]	"Single-stranded DNA-binding protein hSSB1 is critical for genomic stability." 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. Nature 453:677-681(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, INTERACTION WITH ATM AND RAD51, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117.
[6]	"hSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response." Li Y., Bolderson E., Kumar R., Muniandy P.A., Xue Y., Richard D.J., Seidman M., Pandita T.K., Khanna K.K., Wang W. J. Biol. Chem. 284:23525-23531(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SOSS COMPLEX.
[7]	"SOSS complexes participate in the maintenance of genomic stability." Huang J., Gong Z., Ghosal G., Chen J. Mol. Cell 35:384-393(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN THE SOSS COMPLEX, SUBCELLULAR LOCATION, DNA-BINDING, IDENTIFICATION IN THE SOSS COMPLEX, INTERACTION WITH INTS3.
[8]	"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling." Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J. Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INTS7.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY203942 mRNA. Translation: AAP34465.1. Frameshift. CH471054 Genomic DNA. Translation: EAW96913.1. AC073896 Genomic DNA. No translation available. BC001079 mRNA. Translation: AAH01079.1. BC006171 mRNA. Translation: AAH06171.1.
IPI	IPI00031633. IPI00893801.
RefSeq	NP_076973.1. NM_024068.3.
UniGene	Hs.240170.
3D structure databases
ProteinModelPortal	Q9BQ15.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BQ15. 5 interactions.
STRING	9606.ENSP00000267023.
PTM databases
PhosphoSite	Q9BQ15.
Polymorphism databases
DMDM	74761196.
Proteomic databases
PaxDb	Q9BQ15.
PRIDE	Q9BQ15.
Protocols and materials databases
DNASU	79035.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000267023; ENSP00000267023; ENSG00000139579. ENST00000341463; ENSP00000368862; ENSG00000139579. ENST00000380198; ENSP00000369545; ENSG00000139579.
GeneID	79035.
KEGG	hsa:79035.
UCSC	uc001ski.3. human.
Organism-specific databases
CTD	79035.
GeneCards	GC12P056616.
HGNC	HGNC:28412. NABP2.
HPA	HPA044615.
MIM	612104. gene.
neXtProt	NX_Q9BQ15.
PharmGKB	PA143485567.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG285523.
HOGENOM	HOG000006622.
InParanoid	Q9BQ15.
OMA	NHTAAGP.
OrthoDB	EOG4PC9T3.
PhylomeDB	Q9BQ15.
Gene expression databases
ArrayExpress	Q9BQ15.
Bgee	Q9BQ15.
CleanEx	HS_OBFC2B.
Genevestigator	Q9BQ15.
Family and domain databases
Gene3D	2.40.50.140. 1 hit.
InterPro	IPR012340. NA-bd_OB-fold. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view]
Pfam	PF01336. tRNA_anti. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	79035.
NextBio	67757.
SOURCE	Search...

Entry information

Entry name

SOSB1_HUMAN

Accession

Primary (citable) accession number: Q9BQ15
Secondary accession number(s): A6NDF8, Q6XYC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.