Entry - *615756 - SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2-LIKE; SECISBP2L - OMIM

 
 
* 615756

SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2-LIKE; SECISBP2L


Alternative titles; symbols

SECIS-BINDING PROTEIN 2-LIKE; SBP2L
KIAA0256


HGNC Approved Gene Symbol: SECISBP2L

Cytogenetic location: 15q21.1     Genomic coordinates (GRCh38): 15:48,988,638-49,046,446 (from NCBI)


TEXT

▼ Description

Selenoproteins contain the amino acid selenocysteine (sec), which is encoded by UGA, normally a termination codon. SECISBP2 (607693) binds a sec insertion sequence (SECIS) in the 3-prime UTRs of selenoprotein mRNAs, permitting decoding of UGA as sec. SECISBP2L shares significant similarity with SECISBP2 and binds SECIS-containing sequences, but it lacks the ability to catalyze incorporation of sec into proteins (Donovan and Copeland, 2012).


▼ Cloning and Expression

By sequencing clones obtained from a size-fractionated human KG-1 immature myeloid leukemia cell line cDNA library, Nagase et al. (1996) obtained a partial SECISBP2L clone, which they designated KIAA0256. Northern blot analysis detected variable SECISBP2L expression in all human tissues and cell lines examined.

Donovan and Copeland (2012) stated that the deduced 1,101-amino acid SBP2L protein contains an N-terminal motif conserved with SECISBP2, a central sec-incorporation domain (SID), and a C-terminal RNA-binding domain (RBD). Database analysis revealed that vertebrates express both SBP2 and SBP2L, whereas some invertebrates express only Sbp2l.


▼ Gene Function

Donovan and Copeland (2012) had previously found that in vitro-translated human SBP2L lacked sec-incorporation activity. They found that the isolated catalytic region of SBP2L, encompassing the SID and RBD, bound synthetic SECIS-containing sequences but was similarly inactive in sec incorporation. Immunoprecipitation of human U87MG glioblastoma cells revealed that SBP2L bound several endogenous selenoprotein mRNAs. However, unlike the SID and RBD of SBP2, the SID and RBD in SBP2L did not form a stable interaction. Neither overexpression nor knockdown of SBP2L altered the content of selenoproteins in transfected HEK293 cells. Donovan and Copeland (2012) concluded that SBP2L may have a regulatory role in the expression of selenoproteins.


▼ Mapping

By radiation hybrid analysis, Nagase et al. (1996) mapped the SECISBP2L gene to chromosome 15.

Hartz (2014) mapped the SECISBP2L gene to chromosome 15q21.1 based on an alignment of the SECISBP2L sequence (GenBank D87445) with the genomic sequence (GRCh37).

▼ REFERENCES

  1. Donovan, J., Copeland, P. R. Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression. PLoS One 7: e35581, 2012. Note: Electronic Article. [PubMed: 22530054, images, related citations] [Full Text]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 4/23/2014.

  3. Nagase, T., Seki, N., Ishikawa, K., Ohira, M., Kawarabayasi, Y., Ohara, O., Tanaka, A., Kotani, H., Miyajima, N., Nomura, N. Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329, 1996. [PubMed: 9039502, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 4/23/2014
Edit History:
mgross : 04/23/2014
mcolton : 4/23/2014

* 615756

SELENOCYSTEINE INSERTION SEQUENCE-BINDING PROTEIN 2-LIKE; SECISBP2L


Alternative titles; symbols

SECIS-BINDING PROTEIN 2-LIKE; SBP2L
KIAA0256


HGNC Approved Gene Symbol: SECISBP2L

Cytogenetic location: 15q21.1     Genomic coordinates (GRCh38): 15:48,988,638-49,046,446 (from NCBI)


TEXT

Description

Selenoproteins contain the amino acid selenocysteine (sec), which is encoded by UGA, normally a termination codon. SECISBP2 (607693) binds a sec insertion sequence (SECIS) in the 3-prime UTRs of selenoprotein mRNAs, permitting decoding of UGA as sec. SECISBP2L shares significant similarity with SECISBP2 and binds SECIS-containing sequences, but it lacks the ability to catalyze incorporation of sec into proteins (Donovan and Copeland, 2012).


Cloning and Expression

By sequencing clones obtained from a size-fractionated human KG-1 immature myeloid leukemia cell line cDNA library, Nagase et al. (1996) obtained a partial SECISBP2L clone, which they designated KIAA0256. Northern blot analysis detected variable SECISBP2L expression in all human tissues and cell lines examined.

Donovan and Copeland (2012) stated that the deduced 1,101-amino acid SBP2L protein contains an N-terminal motif conserved with SECISBP2, a central sec-incorporation domain (SID), and a C-terminal RNA-binding domain (RBD). Database analysis revealed that vertebrates express both SBP2 and SBP2L, whereas some invertebrates express only Sbp2l.


Gene Function

Donovan and Copeland (2012) had previously found that in vitro-translated human SBP2L lacked sec-incorporation activity. They found that the isolated catalytic region of SBP2L, encompassing the SID and RBD, bound synthetic SECIS-containing sequences but was similarly inactive in sec incorporation. Immunoprecipitation of human U87MG glioblastoma cells revealed that SBP2L bound several endogenous selenoprotein mRNAs. However, unlike the SID and RBD of SBP2, the SID and RBD in SBP2L did not form a stable interaction. Neither overexpression nor knockdown of SBP2L altered the content of selenoproteins in transfected HEK293 cells. Donovan and Copeland (2012) concluded that SBP2L may have a regulatory role in the expression of selenoproteins.


Mapping

By radiation hybrid analysis, Nagase et al. (1996) mapped the SECISBP2L gene to chromosome 15.

Hartz (2014) mapped the SECISBP2L gene to chromosome 15q21.1 based on an alignment of the SECISBP2L sequence (GenBank D87445) with the genomic sequence (GRCh37).

REFERENCES

  1. Donovan, J., Copeland, P. R. Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression. PLoS One 7: e35581, 2012. Note: Electronic Article. [PubMed: 22530054] [Full Text: https://doi.org/10.1371/journal.pone.0035581]

  2. Hartz, P. A. Personal Communication. Baltimore, Md. 4/23/2014.

  3. Nagase, T., Seki, N., Ishikawa, K., Ohira, M., Kawarabayasi, Y., Ohara, O., Tanaka, A., Kotani, H., Miyajima, N., Nomura, N. Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 3: 321-329, 1996. [PubMed: 9039502] [Full Text: https://doi.org/10.1093/dnares/3.5.321]


Creation Date:
Patricia A. Hartz : 4/23/2014

Edit History:
mgross : 04/23/2014
mcolton : 4/23/2014



NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: April 24, 2024