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Gene Review

SECISBP2  -  SECIS binding protein 2

Homo sapiens

Synonyms: SBP2, SECIS-binding protein 2, Selenocysteine insertion sequence-binding protein 2
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Disease relevance of SECISBP2

  • Ascites improved after TIPSS in 36 patients (87.8%), but reaccumulated in seven (17.5%), associated with shunt dysfunction in five (SBP 2, IH 3, HVS 2) [1].
  • Purified recombinant S64/SBP2 protein, expressed as a histidine-tagged protein in Escherichia coli, exhibited nucleotide-binding specificity to guanine nucleotides [2].
  • The only novel protein with regard to liver fibrosis depicting a unidirectional expression pattern in both animal models was Sbp2 [3].

High impact information on SECISBP2

  • An unrelated child with a similar phenotype was compound heterozygous with respect to mutations in SECISBP2 [4].
  • Mutations in SECISBP2 result in abnormal thyroid hormone metabolism [4].
  • Systematic linkage analysis of genes involved in DIO2 synthesis and degradation led to the identification of an inherited Sec incorporation defect, caused by a homozygous missense mutation in SECISBP2 (also called SBP2) [4].
  • The predicted amino acid sequence of the LG1 protein is largely novel but contains an internal domain of 77 amino acids with significant similarity to a domain present in two recently identified SQUAMOSA PROMOTER-BINDING proteins 1 and 2 (SBP1 and SBP2) in Antirhinum majus [5].
  • We purified a SECIS binding protein, SBP2, and obtained a cDNA clone that encodes this activity [6].

Biological context of SECISBP2

  • Furthermore, Sec incorporation is reduced substantially after treatment of cells with agents that cause oxidative stress, suggesting that nuclear sequestration of SBP2 under such conditions may represent a mechanism to regulate the expression of selenoproteins [7].
  • We show that SBP2 shuttles between the nucleus and the cytoplasm via intrinsic, functional nuclear localization signal and nuclear export signal motifs and that its nuclear export is dependent on the CRM1 pathway [7].
  • The SBP2 promoter directed expression of both GUS and GFP reporter genes with high specificity to the phloem of leaves, stems and roots [8].

Anatomical context of SECISBP2

  • Examination of the expression pattern revealed that the human SBP2 protein is encoded by a 4 kb long mRNA that is over-expressed in testis [9].
  • SBP2 may, therefore, have a distinct function in selecting the ribosomes to be used for Sec insertion [10].
  • Depletion of SBP2 in cell lines using small interfering RNA results in a decrease in Sec incorporation, providing direct evidence for its requirement for selenoprotein synthesis [7].
  • When transiently expressed in mammalian cells, Fep15 incorporated Sec in an SECIS- and SBP2 (SECIS-binding protein 2)-dependent manner and was targeted to the endoplasmic reticulum by its N-terminal signal peptide [11].

Associations of SECISBP2 with chemical compounds

  • Finally, we show that SBP2 preferentially stimulates incorporation directed by the seleno protein P and phospholipid hydroperoxide glutathione peroxidase SECIS elements over those of other selenoproteins [12].
  • Alanine substitution of these amino acids followed by gel shift assays of the SBP2 mutant proteins identified four residues whose mutation severely diminished or abolished SECIS RNA binding, the other eight provoking intermediate down effects [13].
  • Using glycerol gradient sedimentation, we found that SBP2 was stably associated with the ribosomal fraction of cell lysates and that this interaction was not dependent on its SECIS binding activity [10].
  • Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain [7].
  • The soybean sucrose binding protein gene family: genomic organization, gene copy number and tissue-specific expression of the SBP2 promoter [8].

Physical interactions of SECISBP2


Other interactions of SECISBP2

  • We report that co-expression of SBP2 overcomes the limitation produced by selenoprotein mRNA overexpression, whereas selenocysteyl-tRNA and the selenocysteine-specific elongation factor do not [12].
  • The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding [13].

Analytical, diagnostic and therapeutic context of SECISBP2

  • Here we report a detailed analysis of SBP2 structure and function using truncation and site-directed mutagenesis [10].
  • Contrary to previous findings, a combination of gel filtration chromatography and co-purification studies demonstrates that SBP2 does not self-associate [14].


  1. Transjugular intrahepatic portosystemic stent-shunt (TIPSS): long-term follow-up. Jalan, R., Redhead, D.N., Simpson, K.J., Elton, R.A., Hayes, P.C. QJM : monthly journal of the Association of Physicians. (1994) [Pubmed]
  2. A sucrose-binding protein homologue from soybean exhibits GTP-binding activity that functions independently of sucrose transport activity. Pirovani, C.P., Macêdo, J.N., Contim, L.A., Matrangolo, F.S., Loureiro, M.E., Fontes, E.P. Eur. J. Biochem. (2002) [Pubmed]
  3. Changes of the hepatic proteome in murine models for toxically induced fibrogenesis and sclerosing cholangitis. Henkel, C., Roderfeld, M., Weiskirchen, R., Berres, M.L., Hillebrandt, S., Lammert, F., Meyer, H.E., St??hler, K., Graf, J., Roeb, E. Proteomics (2006) [Pubmed]
  4. Mutations in SECISBP2 result in abnormal thyroid hormone metabolism. Dumitrescu, A.M., Liao, X.H., Abdullah, M.S., Lado-Abeal, J., Majed, F.A., Moeller, L.C., Boran, G., Schomburg, L., Weiss, R.E., Refetoff, S. Nat. Genet. (2005) [Pubmed]
  5. liguleless1 encodes a nuclear-localized protein required for induction of ligules and auricles during maize leaf organogenesis. Moreno, M.A., Harper, L.C., Krueger, R.W., Dellaporta, S.L., Freeling, M. Genes Dev. (1997) [Pubmed]
  6. A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs. Copeland, P.R., Fletcher, J.E., Carlson, B.A., Hatfield, D.L., Driscoll, D.M. EMBO J. (2000) [Pubmed]
  7. The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function. Papp, L.V., Lu, J., Striebel, F., Kennedy, D., Holmgren, A., Khanna, K.K. Mol. Cell. Biol. (2006) [Pubmed]
  8. The soybean sucrose binding protein gene family: genomic organization, gene copy number and tissue-specific expression of the SBP2 promoter. Contim, L.A., Waclawovsky, A.J., Delú-Filho, N., Pirovani, C.P., Clarindo, W.R., Loureiro, M.E., Carvalho, C.R., Fontes, E.P. J. Exp. Bot. (2003) [Pubmed]
  9. cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2. Lescure, A., Allmang, C., Yamada, K., Carbon, P., Krol, A. Gene (2002) [Pubmed]
  10. Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of Sec insertion sequence binding protein 2. Copeland, P.R., Stepanik, V.A., Driscoll, D.M. Mol. Cell. Biol. (2001) [Pubmed]
  11. Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family. Novoselov, S.V., Hua, D., Lobanov, A.V., Gladyshev, V.N. Biochem. J. (2006) [Pubmed]
  12. SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy. Low, S.C., Grundner-Culemann, E., Harney, J.W., Berry, M.J. EMBO J. (2000) [Pubmed]
  13. The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding. Allmang, C., Carbon, P., Krol, A. RNA (2002) [Pubmed]
  14. Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals. Kinzy, S.A., Caban, K., Copeland, P.R. Nucleic Acids Res. (2005) [Pubmed]
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