SECISBP2

SECISBP2
Identifiers
Aliases	SECISBP2, SBP2, SECIS binding protein 2
External IDs	OMIM: 607693 MGI: 1922670 HomoloGene: 11415 GeneCards: SECISBP2
Gene location (Human) Chr. Chromosome 9 (human) Band 9q22.2 Start 89,318,500 bp End 89,359,663 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A5 Start 51,805,733 bp End 51,838,080 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte sperm body of pancreas right uterine tube sural nerve ganglionic eminence left lobe of thyroid gland right lung Achilles tendon right lobe of thyroid gland Top expressed in hand otolith organ utricle primitive streak hair follicle bone marrow secondary oocyte seminal vesicula foot spleen More reference expression data BioGPS More reference expression data
Gene ontology Molecular function mRNA 3'-UTR binding protein binding RNA binding selenocysteine insertion sequence binding ribonucleoprotein complex binding Cellular component nucleus mitochondrion ribonucleoprotein complex Biological process protein biosynthesis striatum development neuron development negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay selenocysteine incorporation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 79048 75420 Ensembl ENSG00000187742 ENSMUSG00000035139 UniProt Q96T21 n/a RefSeq (mRNA) NM_001282688 NM_001282689 NM_001282690 NM_024077 NM_001354696 NM_001354697 NM_001354698 NM_001354702 NM_029279 NM_001308448 RefSeq (protein) NP_001269617 NP_001269618 NP_001269619 NP_076982 NP_001341625 NP_001341626 NP_001341627 NP_001341631 n/a Location (UCSC) Chr 9: 89.32 – 89.36 Mb Chr 13: 51.81 – 51.84 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

SECIS-binding protein 2 (commonly referred to as SBP2) is a protein that in humans is encoded by the SECISBP2 gene.

Function

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. SBP2 is a nuclear protein that functions as a SECIS binding protein, but experimental evidence indicates that SBP2 is cytoplasmic.

Clinical significance

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.

See also

• Thyroid hormone resistance

Further reading

• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Copeland PR, Fletcher JE, Carlson BA, Hatfield DL, Driscoll DM (January 2000). "A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs". The EMBO Journal. 19 (2): 306–14. doi:10.1093/emboj/19.2.306. PMC 305564. PMID 10637234.
• Hartley JL, Temple GF, Brasch MA (November 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Low SC, Grundner-Culemann E, Harney JW, Berry MJ (December 2000). "SECIS-SBP2 interactions dictate selenocysteine incorporation efficiency and selenoprotein hierarchy". The EMBO Journal. 19 (24): 6882–90. doi:10.1093/emboj/19.24.6882. PMC 305907. PMID 11118223.
• Lescure A, Allmang C, Yamada K, Carbon P, Krol A (May 2002). "cDNA cloning, expression pattern and RNA binding analysis of human selenocysteine insertion sequence (SECIS) binding protein 2". Gene. 291 (1–2): 279–85. doi:10.1016/S0378-1119(02)00629-7. PMID 12095701.
• Allmang C, Carbon P, Krol A (October 2002). "The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding". RNA. 8 (10): 1308–18. doi:10.1017/S1355838202020034. PMC 1370339. PMID 12403468.
• Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (October 2004). "From ORFeome to biology: a functional genomics pipeline". Genome Research. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Dumitrescu AM, Liao XH, Abdullah MS, Lado-Abeal J, Majed FA, Moeller LC, Boran G, Schomburg L, Weiss RE, Refetoff S (November 2005). "Mutations in SECISBP2 result in abnormal thyroid hormone metabolism". Nature Genetics. 37 (11): 1247–52. doi:10.1038/ng1654. PMID 16228000. S2CID 35631638.
• Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S (January 2006). "The LIFEdb database in 2006". Nucleic Acids Research. 34 (Database issue): D415-8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
• Papp LV, Lu J, Striebel F, Kennedy D, Holmgren A, Khanna KK (July 2006). "The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function". Molecular and Cellular Biology. 26 (13): 4895–910. doi:10.1128/MCB.02284-05. PMC 1489162. PMID 16782878.