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Q9BQ15

- SOSB1_HUMAN

UniProt

Q9BQ15 - SOSB1_HUMAN

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Protein

SOSS complex subunit B1

Gene

NABP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9BQ15.
CleanExiHS_OBFC2B.
ExpressionAtlasiQ9BQ15. baseline and differential.
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 – 93Combined sources
Beta strandi20 – 267Combined sources
Beta strandi33 – 353Combined sources
Beta strandi40 – 456Combined sources
Beta strandi48 – 536Combined sources
Helixi56 – 616Combined sources
Beta strandi66 – 694Combined sources
Beta strandi93 – 986Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4OWTX-ray2.00B1-211[»]
4OWWX-ray2.30B1-211[»]
4OWXX-ray2.30B1-211[»]
ProteinModelPortaliQ9BQ15.
SMRiQ9BQ15. Positions 5-111.
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.
GeneTreeiENSGT00390000001913.
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

        10         20         30         40         50
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI
60 70 80 90 100
NISVWDDVGN LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM
110 120 130 140 150
VYSEVPNFSE PNPEYSTQQA PNKAVQNDSN PSASQPTTGP SAASPASENQ
160 170 180 190 200
NGNGLSAPPG PGGGPHPPHT PSHPPSTRIT RSQPNHTPAG PPGPSSNPVS
210
NGKETRRSSK R
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. Curated

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 5-111.
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.
GeneTreei ENSGT00390000001913.
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

Bgeei Q9BQ15.
CleanExi HS_OBFC2B.
ExpressionAtlasi Q9BQ15. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 111 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