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SECIS binding protein 2

SBP2, SECIS binding protein 2
The incorporation of selenocysteine into a protein requires the concerted action of an mRNA element called a sec insertion sequence (SECIS), a selenocysteine-specific translation elongation factor and a SECIS binding protein. With these elements in place, a UGA codon can be decoded as selenocysteine. The gene described in this record encodes a nuclear protein that functions as a SECIS binding protein. Mutations in this gene have been associated with a reduction in activity of a specific thyroxine deiodinase, a selenocysteine-containing enzyme, and abnormal thyroid hormone metabolism. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ethanolaminephosphotransferase, ACID, AGE, CAN, HAD
Papers on SBP2
Molecular epidemiology of bovine Babesia spp. and Theileria orientalis parasites in beef cattle from northern and northeastern Thailand.
Xuan et al., Obihiro, Japan. In Parasitol Int, Feb 2016
Sequencing analysis revealed that B. bigemina RAP1 gene and B. bovis SBP2 gene were conserved among the parasites from different cattle samples.
Efficient butanol recovery from acetone-butanol-ethanol fermentation cultures grown on sweet sorghum juice by pervaporation using silicalite-1 membrane.
Ohta et al., Fuchū, Japan. In J Biosci Bioeng, Jan 2016
UNASSIGNED: We investigated butanol recovery by pervaporation separation, using a silicalite-1 membrane, from batch cultures of butanol-producing Clostridium beijerinckii SBP2 grown on sweet sorghum juice as a fermentation medium.
The Vaccine Candidate, Substrate Binding Protein SBP2, Plays a Key Role in Arginine Uptake, which is Required for Growth of Moraxella catarrhalis.
Murphy et al., Buffalo, United States. In Infect Immun, Dec 2015
SBP2 mediates uptake of arginine, a strict growth requirement of M. catarrhalis.
Enhancement of lipid peroxidation and its amelioration by vitamin E in a subject with mutations in the SBP2 gene.
Noguchi et al., Kyoto, Japan. In J Lipid Res, Nov 2015
Selenocysteine (Sec) insertion sequence-binding protein 2 (SBP2) is essential for the biosynthesis of Sec-containing proteins, termed selenoproteins.
Orthostatic Blood Pressure Changes and Subclinical Markers of Atherosclerosis.
Arita et al., Wakayama, Japan. In Am J Hypertens, Sep 2015
Stepwise regression analysis adjusted for age, sex, BMI, baseline SBP, triglycerides, high-density lipoprotein cholesterol, low-density lipoprotein cholesterol, fasting glucose, HbA1c, hs-CRP, IMT, late systolic peak of the pressure wave form (SBP2), and baPWV confirmed that baPWV, SBP2, and triglycerides were independently related to orthostatic BP changes.
Arita et al., Wakayama, Japan. In J Hypertens, Jun 2015
Brachial ankle pulse wave velocity (baPWV), late systolic peak of the pressure wave form (SBP2) and carotid mean IMT were measured.
Selective up-regulation of human selenoproteins in response to oxidative stress.
Laurent et al., France. In Free Radic Biol Med, 2014
While a modest change in mRNA levels was noted, we identified a novel translational control mechanism stimulated by oxidative stress that is characterized by upregulation of UGA-selenocysteine recoding efficiency and relocalization of SBP2, EFsec and L30 recoding factors from cytoplasm to nucleus.
Decline of Renal Function and Progression of Left Ventricular Hypertrophy Are Independently Determined in Chronic Kidney Disease Stages 3-5.
Okada et al., Saitama, Japan. In Pulse (basel), 2014
Second systolic aortic blood pressure (SBP2) was employed as an index of CAP.
Inherited defects in thyroid hormone cell-membrane transport and metabolism.
Dumitrescu et al., Chicago, United States. In Best Pract Res Clin Endocrinol Metab, 2014
Recessive mutations in the selenocysteine insertion sequence binding protein 2 (SBP2) gene present a variable clinical phenotype depending on the severity of the defect and its consequences on the selenoprotein hierarchy.
Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.
Driscoll et al., Cleveland, United States. In Rna Biol, 2013
The SECIS is recognized by SECIS-binding protein 2 (SBP2) and this RNA:protein interaction is essential for UGA recoding to occur.
Different causes of reduced sensitivity to thyroid hormone: diagnosis and clinical management.
Peeters et al., Rotterdam, Netherlands. In Clin Endocrinol (oxf), 2013
Mutations in the SBP2 protein, which is required for normal deiodination, give rise to a multisystem disorder including abnormal thyroid function tests.
[Biosyinthesis and mechanism of selenocysteine incorporation into synthesized proteins].
Fecenko et al., In Mol Biol (mosk), 2013
The trans-factors include Sec-tRNA([Ser]Sec) that has a unique system of biosynthesis, Sec-specific elongation factor EFsec and SBP2--Sec binding protein.
Post-transcriptional control of selenoprotein biosynthesis.
Schweizer et al., Berlin, Germany. In Curr Protein Pept Sci, 2012
The SECIS element is bound by several proteins, including SECIS-binding protein 2 (SBP2).
Novel compound heterozygous mutations in the SBP2 gene: characteristic clinical manifestations and the implications of GH and triiodothyronine in longitudinal bone growth and maturation.
Onigata et al., Ōbu, Japan. In Eur J Endocrinol, 2012
The patient showed typical symptoms of SBP2 deficiency, and novel compound heterozygous mutations were identified in SBP2 (p.M515fsX563/p.Q79X).
Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.
Copeland et al., United States. In J Biol Chem, 2012
Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.
Inherited defects of thyroid hormone metabolism.
Refetoff et al., Chicago, United States. In Ann Endocrinol (paris), 2011
Selenium (Se) is an essential trace element required for the biosynthesis of selenoproteins, and selenocysteine insertion sequence (SECIS) binding protein 2 (SBP2) represents a key trans-acting factor for the cotranslational insertion of selenocysteine into selenoproteins.
Mutations in the selenocysteine insertion sequence-binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans.
Chatterjee et al., Cambridge, United Kingdom. In J Clin Invest, 2010
Describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype.
SECIS-binding protein 2 promotes cell survival by protecting against oxidative stress.
Khanna et al., Australia. In Antioxid Redox Signal, 2010
Results demonstrate that SECIS-binding protein 2 is required for protection against reactive oxygen species-induced cellular damage and cell survival.
Eukaryotic initiation factor 4a3 is a selenium-regulated RNA-binding protein that selectively inhibits selenocysteine incorporation.
Driscoll et al., Cleveland, United States. In Mol Cell, 2009
The interaction of eIF4a3 with selenoprotein mRNA prevents the binding of SECIS binding protein 2, which is required for selenocysteine insertion, thereby inhibiting selenoprotein synthesis.
Mutations in SECISBP2 result in abnormal thyroid hormone metabolism.
Refetoff et al., Chicago, United States. In Nat Genet, 2005
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).
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