Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BQ15 (SOSB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211SOSS complex subunit B1
PRO_0000333958

Regions

DNA binding22 – 9271OB Ref.5 Ref.7
Compositional bias158 – 19841Pro-rich

Amino acid modifications

Modified residue1171Phosphothreonine; by ATM Ref.5

Natural variations

Alternative sequence1 – 9999Missing in isoform 2.
VSP_033604

Experimental info

Mutagenesis1171T → A: Loss of phosphorylation by ATM. Ref.5
Mutagenesis1171T → E: Enhances ATM-dependent signaling. Ref.5

Secondary structure

................. 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B72014397B7947E2

FASTA21122,338
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B066AA52BECFDC94
Show »

FASTA11211,493

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS8911.1. [Q9BQ15-1]
RefSeqNP_076973.1. NM_024068.3. [Q9BQ15-1]
XP_005269205.1. XM_005269148.2. [Q9BQ15-1]
XP_005269206.1. XM_005269149.2. [Q9BQ15-1]
UniGeneHs.240170.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00B1-211[»]
4OWWX-ray2.30B1-211[»]
4OWXX-ray2.30B1-211[»]
ProteinModelPortalQ9BQ15.
SMRQ9BQ15. Positions 3-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122500. 22 interactions.
IntActQ9BQ15. 5 interactions.
STRING9606.ENSP00000267023.

PTM databases

PhosphoSiteQ9BQ15.

Polymorphism databases

DMDM74761196.

Proteomic databases

MaxQBQ9BQ15.
PaxDbQ9BQ15.
PRIDEQ9BQ15.

Protocols and materials databases

DNASU79035.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267023; ENSP00000267023; ENSG00000139579. [Q9BQ15-1]
ENST00000341463; ENSP00000368862; ENSG00000139579. [Q9BQ15-1]
ENST00000380198; ENSP00000369545; ENSG00000139579. [Q9BQ15-1]
GeneID79035.
KEGGhsa:79035.
UCSCuc001ski.3. human. [Q9BQ15-1]

Organism-specific databases

CTD79035.
GeneCardsGC12P056616.
HGNCHGNC:28412. NABP2.
HPAHPA044615.
MIM612104. gene.
neXtProtNX_Q9BQ15.
PharmGKBPA143485567.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG285523.
HOGENOMHOG000006622.
InParanoidQ9BQ15.
OMANHTAAGP.
OrthoDBEOG793B8S.
PhylomeDBQ9BQ15.
TreeFamTF313902.

Gene expression databases

ArrayExpressQ9BQ15.
BgeeQ9BQ15.
CleanExHS_OBFC2B.
GenevestigatorQ9BQ15.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PfamPF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi79035.
NextBio67757.
PROQ9BQ15.
SOURCESearch...

Entry information

Entry nameSOSB1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM