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General description of the gene and the encoded protein(s) using information from HGNC and Ensembl, as well as predictions made by the Human Protein Atlas project.
Gene namei
Official gene symbol, which is typically a short form of the gene name, according to HGNC.
Assigned HPA protein class(es) for the encoded protein(s).
Disease related genes Human disease related genes
Predicted locationi
All transcripts of all genes have been analyzed regarding the location(s) of corresponding protein based on prediction methods for signal peptides and transmembrane regions.
Genes with at least one transcript predicted to encode a secreted protein, according to prediction methods or to UniProt location data, have been further annotated and classified with the aim to determine if the corresponding protein(s) are secreted or actually retained in intracellular locations or membrane-attached.
Remaining genes, with no transcript predicted to encode a secreted protein, will be assigned the prediction-based location(s).
The annotated location overrules the predicted location, so that a gene encoding a predicted secreted protein that has been annotated as intracellular will have intracellular as the final location.
Gene information from Ensembl and Entrez, as well as links to available gene identifiers are displayed here. Information was retrieved from Ensembl if not indicated otherwise.
Chromosome
9
Cytoband
q22.2
Chromosome location (bp)
89318500 - 89359663
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
mRNA-binding protein that binds to the SECIS (selenocysteine insertion sequence) element present in the 3'-UTR of mRNAs encoding selenoproteins and facilitates the incorporation of the rare amino acid selenocysteine 1. Insertion of selenocysteine at UGA codons is mediated by SECISBP2 and EEFSEC: SECISBP2 (1) specifically binds the SECIS sequence once the 80S ribosome encounters an in-frame UGA codon and (2) contacts the RPS27A/eS31 of the 40S ribosome before ribosome stalling 2. (3) GTP-bound EEFSEC then delivers selenocysteinyl-tRNA(Sec) to the 80S ribosome and adopts a preaccommodated state conformation 3. (4) After GTP hydrolysis, EEFSEC dissociates from the assembly, selenocysteinyl-tRNA(Sec) accommodates, and peptide bond synthesis and selenoprotein elongation occur 4....show less
Molecular function (UniProt)i
Keywords assigned by UniProt to proteins due to their particular molecular function.
RNA-binding
Biological process (UniProt)i
Keywords assigned by UniProt to proteins because they are involved in a particular biological process.
Protein biosynthesis
Gene summary (Entrez)i
Useful information about the gene from Entrez
The protein encoded by this gene is one of the essential components of the machinery involved in co-translational insertion of selenocysteine (Sec) into selenoproteins. Sec is encoded by the UGA codon, which normally signals translation termination. The recoding of UGA as Sec codon requires a Sec insertion sequence (SECIS) element; present in the 3' untranslated regions of eukaryotic selenoprotein mRNAs. This protein specifically binds to the SECIS element, which is stimulated by a Sec-specific translation elongation factor. Mutations in this gene have been associated with reduction in enzymatic activity of type II iodothyronine deiodinase (a selenoprotein) and abnormal thyroid hormone metabolism. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Aug 2017]...show less
PROTEIN INFORMATIONi
The protein information section displays alternative protein-coding transcripts (splice variants) encoded by this gene according to the Ensembl database.
The Splice variant identifier links to the Ensembl website protein summary for the selected splice variant. The data in the Swissprot and TrEMBL columns links to corresponding pages in the UniProt database.
The protein classes assigned to this protein are shown if expanding the data in the protein class column. Parent protein classes are in bold font and subclasses are listed under the parent class.
The length of the protein (amino acid residues according to Ensembl), molecular mass (kDalton), predicted signal peptide and number of predicted transmembrane region(s) according to in-house majority decision methods based on sets of predictors are also reported.
Q96T21 [Direct mapping] Selenocysteine insertion sequence-binding protein 2
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Phobius predicted secreted proteins SPOCTOPUS predicted secreted proteins Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Disease related genes Human disease related genes Endocrine and metabolic diseases Thyroid gland diseases Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Ezkurdia et al 2014)
Q96T21 [Direct mapping] Selenocysteine insertion sequence-binding protein 2
Show all
Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Disease related genes Human disease related genes Endocrine and metabolic diseases Thyroid gland diseases Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
Q5HYY5 [Direct mapping] Selenocysteine insertion sequence-binding protein 2
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Human disease related genes Endocrine and metabolic diseases Thyroid gland diseases Protein evidence (Ezkurdia et al 2014)
Q4V370 [Direct mapping] Selenocysteine insertion sequence-binding protein 2
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Human disease related genes Endocrine and metabolic diseases Thyroid gland diseases Protein evidence (Ezkurdia et al 2014)
Q96T21 [Direct mapping] Selenocysteine insertion sequence-binding protein 2
Show all
Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Disease related genes Human disease related genes Endocrine and metabolic diseases Thyroid gland diseases Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Ezkurdia et al 2014)
The Human Protein Atlas project is funded
