Entry - *607451 - GLUCOCORTICOID MODULATORY ELEMENT-BINDING PROTEIN 2; GMEB2 - OMIM
 
* 607451

GLUCOCORTICOID MODULATORY ELEMENT-BINDING PROTEIN 2; GMEB2


Alternative titles; symbols

PARVOVIRUS INITIATION FACTOR, p79 SUBUNIT
KIAA1269


HGNC Approved Gene Symbol: GMEB2

Cytogenetic location: 20q13.33   Genomic coordinates (GRCh38) : 20:63,587,605-63,627,101 (from NCBI)


TEXT

Cloning and Expression

By sequencing clones obtained from a size-fractionated brain cDNA library, Nagase et al. (1999) cloned GMEB2, which they designated KIAA1269. The deduced 531-amino acid protein shares 94% amino acid identity with rat Gmeb2. RT-PCR followed by ELISA analysis revealed moderate expression of GMEB2 in testis and ovary, and low expression in heart, brain, lung, liver, kidney, and pancreas. Expression was undetectable in skeletal muscle, spleen, and fetal brain. Christensen et al. (1999) copurified GMEB2 in a complex with GMEB1 (604409) from HeLa cell nuclear extracts. Using degenerate primers designed from the amino acid sequence followed by 5-prime and 3-prime RACE, they cloned the full-length cDNAs. The deduced GMEB2 protein, which they called p79, contains 530 amino acids and has a calculated molecular mass of 56.4 kD. By SDS/PAGE, the apparent molecular mass was 79 kD. GMEB2 contains an N-terminal KDWK domain, and a highly acidic C terminus that likely forms a coiled-coil structure. Recombinant and endogenous GMEB2 share identical mobilities when analyzed by SDS/PAGE, indicating a lack of posttranslational modification. Within the N-terminal KDWK domain, GMEB2 shares about 80% identity with GMEB1; overall, they share about 40% identity.


Gene Function

Christensen et al. (1999) noted that the complex of GMEB1 and GMEB2, which they designated parvovirus initiation factor (PIF) subunits p96 and p79, respectively, was originally recognized as a site-specific DNA-binding complex essential for parvovirus DNA replication. The authors found that GMEB2 and GMEB1 self-associate when expressed alone, and that they form heterodimers when expressed together. Cross-linking experiments indicated that no higher-order multimers were formed. Each protein was active in promoter activation assays, and the complex bound regulatory elements within the promoter regions of tyrosine animotransferase (613018) and the transferrin receptor gene (190010). Within its recognition site, PIF coordinately bound 2 copies of the tetranucleotide PuCGPy, and these could be spaced from 1 to 15 nucleotides apart.


Mapping

By radiation hybrid analysis, Nagase et al. (1999) mapped the GMEB2 gene to chromosome 20.


REFERENCES

  1. Christensen, J., Cotmore, S. F., Tattersall, P. Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half sites. Molec. Cell. Biol. 19: 7741-7750, 1999. [PubMed: 10523663, images, related citations] [Full Text]

  2. Nagase, T., Ishikawa, K., Kikuno, R., Hirosawa, M., Nomura, N., Ohara, O. Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 6: 337-345, 1999. [PubMed: 10574462, related citations] [Full Text]


Creation Date:
Patricia A. Hartz : 12/27/2002
carol : 09/17/2009
wwang : 5/27/2005
cwells : 12/27/2002

* 607451

GLUCOCORTICOID MODULATORY ELEMENT-BINDING PROTEIN 2; GMEB2


Alternative titles; symbols

PARVOVIRUS INITIATION FACTOR, p79 SUBUNIT
KIAA1269


HGNC Approved Gene Symbol: GMEB2

Cytogenetic location: 20q13.33   Genomic coordinates (GRCh38) : 20:63,587,605-63,627,101 (from NCBI)


TEXT

Cloning and Expression

By sequencing clones obtained from a size-fractionated brain cDNA library, Nagase et al. (1999) cloned GMEB2, which they designated KIAA1269. The deduced 531-amino acid protein shares 94% amino acid identity with rat Gmeb2. RT-PCR followed by ELISA analysis revealed moderate expression of GMEB2 in testis and ovary, and low expression in heart, brain, lung, liver, kidney, and pancreas. Expression was undetectable in skeletal muscle, spleen, and fetal brain. Christensen et al. (1999) copurified GMEB2 in a complex with GMEB1 (604409) from HeLa cell nuclear extracts. Using degenerate primers designed from the amino acid sequence followed by 5-prime and 3-prime RACE, they cloned the full-length cDNAs. The deduced GMEB2 protein, which they called p79, contains 530 amino acids and has a calculated molecular mass of 56.4 kD. By SDS/PAGE, the apparent molecular mass was 79 kD. GMEB2 contains an N-terminal KDWK domain, and a highly acidic C terminus that likely forms a coiled-coil structure. Recombinant and endogenous GMEB2 share identical mobilities when analyzed by SDS/PAGE, indicating a lack of posttranslational modification. Within the N-terminal KDWK domain, GMEB2 shares about 80% identity with GMEB1; overall, they share about 40% identity.


Gene Function

Christensen et al. (1999) noted that the complex of GMEB1 and GMEB2, which they designated parvovirus initiation factor (PIF) subunits p96 and p79, respectively, was originally recognized as a site-specific DNA-binding complex essential for parvovirus DNA replication. The authors found that GMEB2 and GMEB1 self-associate when expressed alone, and that they form heterodimers when expressed together. Cross-linking experiments indicated that no higher-order multimers were formed. Each protein was active in promoter activation assays, and the complex bound regulatory elements within the promoter regions of tyrosine animotransferase (613018) and the transferrin receptor gene (190010). Within its recognition site, PIF coordinately bound 2 copies of the tetranucleotide PuCGPy, and these could be spaced from 1 to 15 nucleotides apart.


Mapping

By radiation hybrid analysis, Nagase et al. (1999) mapped the GMEB2 gene to chromosome 20.


REFERENCES

  1. Christensen, J., Cotmore, S. F., Tattersall, P. Two new members of the emerging KDWK family of combinatorial transcription modulators bind as a heterodimer to flexibly spaced PuCGPy half sites. Molec. Cell. Biol. 19: 7741-7750, 1999. [PubMed: 10523663] [Full Text: https://doi.org/10.1128/MCB.19.11.7741]

  2. Nagase, T., Ishikawa, K., Kikuno, R., Hirosawa, M., Nomura, N., Ohara, O. Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 6: 337-345, 1999. [PubMed: 10574462] [Full Text: https://doi.org/10.1093/dnares/6.5.337]


Creation Date:
Patricia A. Hartz : 12/27/2002

Edit History:
carol : 09/17/2009
wwang : 5/27/2005
cwells : 12/27/2002