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Q9BQ15

- SOSB1_HUMAN

UniProt

Q9BQ15 - SOSB1_HUMAN

Protein

SOSS complex subunit B1

Gene

NABP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi22 – 9271OBAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB
    3. double-strand break repair via homologous recombination Source: UniProtKB
    4. mitotic cell cycle checkpoint Source: UniProtKB
    5. response to ionizing radiation Source: UniProtKB

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:NABP2
    Synonyms:OBFC2B, SSB1
    ORF Names:LP3587
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:28412. NABP2.

    Subcellular locationi

    Nucleus 3 Publications
    Note: Localizes to nuclear foci following DNA damage. Foci formation is not cell-cycle dependent. Partial colocalization with RAD51 after ionizing radiation treatment.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. SOSS complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi117 – 1171T → A: Loss of phosphorylation by ATM. 1 Publication
    Mutagenesisi117 – 1171T → E: Enhances ATM-dependent signaling. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485567.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211SOSS complex subunit B1PRO_0000333958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei117 – 1171Phosphothreonine; by ATM1 Publication

    Post-translational modificationi

    Phosphorylated by ATM in response to DNA damage. Phosphorylation prevents degradation by the proteasome, hence stabilization of the protein and accumulation within cells.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BQ15.
    PaxDbiQ9BQ15.
    PRIDEiQ9BQ15.

    PTM databases

    PhosphoSiteiQ9BQ15.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BQ15.
    BgeeiQ9BQ15.
    CleanExiHS_OBFC2B.
    GenevestigatoriQ9BQ15.

    Organism-specific databases

    HPAiHPA044615.

    Interactioni

    Subunit structurei

    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 INTS7.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATMQ133154EBI-2120336,EBI-495465
    CDKN1AP389367EBI-2120336,EBI-375077

    Protein-protein interaction databases

    BioGridi122500. 23 interactions.
    IntActiQ9BQ15. 5 interactions.
    STRINGi9606.ENSP00000267023.

    Structurei

    Secondary structure

    1
    211
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 93
    Beta strandi20 – 267
    Beta strandi33 – 353
    Beta strandi40 – 456
    Beta strandi48 – 536
    Helixi56 – 616
    Beta strandi66 – 694
    Beta strandi93 – 986

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4OWTX-ray2.00B1-211[»]
    4OWWX-ray2.30B1-211[»]
    4OWXX-ray2.30B1-211[»]
    ProteinModelPortaliQ9BQ15.
    SMRiQ9BQ15. Positions 3-101.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi158 – 19841Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SOSS-B family. SOSS-B1 subfamily.Curated
    Contains 1 OB DNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiNOG285523.
    HOGENOMiHOG000006622.
    InParanoidiQ9BQ15.
    OMAiNHTAAGP.
    OrthoDBiEOG793B8S.
    PhylomeDBiQ9BQ15.
    TreeFamiTF313902.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view]
    PfamiPF01336. tRNA_anti-codon. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQ15-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI    50
    NISVWDDVGN LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM 100
    VYSEVPNFSE PNPEYSTQQA PNKAVQNDSN PSASQPTTGP SAASPASENQ 150
    NGNGLSAPPG PGGGPHPPHT PSHPPSTRIT RSQPNHTPAG PPGPSSNPVS 200
    NGKETRRSSK R 211
    Length:211
    Mass (Da):22,338
    Last modified:June 1, 2001 - v1
    Checksum:iB72014397B7947E2
    GO
    Isoform 2 (identifier: Q9BQ15-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:112
    Mass (Da):11,493
    Checksum:iB066AA52BECFDC94
    GO

    Sequence cautioni

    The sequence AAP34465.1 differs from that shown. Reason: Frameshift at position 169.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9999Missing in isoform 2. 1 PublicationVSP_033604Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS8911.1. [Q9BQ15-1]
    RefSeqiNP_076973.1. NM_024068.3. [Q9BQ15-1]
    XP_005269205.1. XM_005269148.2. [Q9BQ15-1]
    XP_005269206.1. XM_005269149.2. [Q9BQ15-1]
    UniGeneiHs.240170.

    Genome annotation databases

    EnsembliENST00000267023; ENSP00000267023; ENSG00000139579. [Q9BQ15-1]
    ENST00000341463; ENSP00000368862; ENSG00000139579. [Q9BQ15-1]
    ENST00000380198; ENSP00000369545; ENSG00000139579. [Q9BQ15-1]
    GeneIDi79035.
    KEGGihsa:79035.
    UCSCiuc001ski.3. human. [Q9BQ15-1]

    Polymorphism databases

    DMDMi74761196.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS8911.1. [Q9BQ15-1 ]
    RefSeqi NP_076973.1. NM_024068.3. [Q9BQ15-1 ]
    XP_005269205.1. XM_005269148.2. [Q9BQ15-1 ]
    XP_005269206.1. XM_005269149.2. [Q9BQ15-1 ]
    UniGenei Hs.240170.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4OWT X-ray 2.00 B 1-211 [» ]
    4OWW X-ray 2.30 B 1-211 [» ]
    4OWX X-ray 2.30 B 1-211 [» ]
    ProteinModelPortali Q9BQ15.
    SMRi Q9BQ15. Positions 3-101.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122500. 23 interactions.
    IntActi Q9BQ15. 5 interactions.
    STRINGi 9606.ENSP00000267023.

    PTM databases

    PhosphoSitei Q9BQ15.

    Polymorphism databases

    DMDMi 74761196.

    Proteomic databases

    MaxQBi Q9BQ15.
    PaxDbi Q9BQ15.
    PRIDEi Q9BQ15.

    Protocols and materials databases

    DNASUi 79035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267023 ; ENSP00000267023 ; ENSG00000139579 . [Q9BQ15-1 ]
    ENST00000341463 ; ENSP00000368862 ; ENSG00000139579 . [Q9BQ15-1 ]
    ENST00000380198 ; ENSP00000369545 ; ENSG00000139579 . [Q9BQ15-1 ]
    GeneIDi 79035.
    KEGGi hsa:79035.
    UCSCi uc001ski.3. human. [Q9BQ15-1 ]

    Organism-specific databases

    CTDi 79035.
    GeneCardsi GC12P056616.
    HGNCi HGNC:28412. NABP2.
    HPAi HPA044615.
    MIMi 612104. gene.
    neXtProti NX_Q9BQ15.
    PharmGKBi PA143485567.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285523.
    HOGENOMi HOG000006622.
    InParanoidi Q9BQ15.
    OMAi NHTAAGP.
    OrthoDBi EOG793B8S.
    PhylomeDBi Q9BQ15.
    TreeFami TF313902.

    Miscellaneous databases

    GenomeRNAii 79035.
    NextBioi 67757.
    PROi Q9BQ15.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BQ15.
    Bgeei Q9BQ15.
    CleanExi HS_OBFC2B.
    Genevestigatori Q9BQ15.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    Pfami PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiSOSB1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQ15
    Secondary accession number(s): A6NDF8, Q6XYC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3