Alternative titles; symbols
HGNC Approved Gene Symbol: CECR2
Cytogenetic location: 22q11.1-q11.21 Genomic coordinates (GRCh38): 22:17,359,949-17,558,151 (from NCBI)
By sequencing clones obtained from a size-fractionated adult hippocampus cDNA library, Nagase et al. (2000) cloned CECR2, which they designated KIAA1740. The deduced protein contains 1,119 amino acids. RT-PCR followed by ELISA detected moderate expression in all tissues tested except spleen. In brain, KIAA1740 expression was high in cerebellum, elevated in hippocampus, and moderate in all other regions tested.
Footz et al. (2001) cloned CECR2 by genomic sequencing of the cat eye syndrome (115470) critical region of chromosome 22, followed by 5-prime and 3-prime RACE. The deduced 1,464-amino acid protein contains a bromodomain.
Using the SEC1 homology domain of LRPPRC (607544) as bait in a yeast 2-hybrid screen, Liu and McKeehan (2002) cloned CECR2 from a liver cDNA library. Northern blot analysis of 12 tissues detected distinct CECR2 banding only in placenta, with transcripts of about 2, 4, 6.5, and 9 kb. Other tissues showed a smear beginning at about 10 kb, with variable intensities between tissues. Liu and McKeehan (2002) concluded that the smearing may indicate particular lability of CECR2 mRNA.
Footz et al. (2001) determined that the CECR2 gene contains 19 exons and spans about 186 kb. Intron 1 extends about 106 kb. The mouse Cecr2 gene has a similar structure.
By genomic sequence analysis, Footz et al. (2001) mapped the CECR2 gene within the cat eye syndrome critical region on chromosome 22q11.2.
Banting et al. (2005) generated a mutant mouse line containing a gene trap insertion within Cecr2. Cecr2 expression was predominantly neural in the embryo, and mice homozygous for the Cecr2 gene trap insertion showed a high penetrance of exencephaly, which is the human equivalent of anencephaly, in a strain-dependent fashion. In HEK293 cells, they isolated CECR2 and SMARCA1 (300012) as components of a complex, which they termed CECR2-containing remodeling factor (CERF). CERF was capable of remodeling chromatin in vitro and displayed an ATP-hydrolyzing activity that was stimulated by nucleosomes. Banting et al. (2005) suggested that CERF plays a critical role in neurulation.
Banting, G. S., Barak, O., Ames, T. M., Burnham, A. C., Kardel, M. D., Cooch, N. S., Davidson, C. E., Godbout, R., McDermid, H. E., Shiekhattar, R. CECR2, a protein involved in neurulation, forms a novel chromatin remodeling complex with SNF2L. Hum. Molec. Genet. 14: 513-524, 2005. [PubMed: 15640247] [Full Text: https://doi.org/10.1093/hmg/ddi048]
Footz, T. K., Brinkman-Mills, P., Banting, G. S., Maier, S. A., Riazi, M. A., Bridgland, L., Hu, S., Birren, B., Minoshima, S., Shimizu, N., Pan, H., Nguyen, T., and 15 others. Analysis of the cat eye syndrome critical region in humans and the region of conserved synteny in mice: a search for candidate genes at or near the human chromosome 22 pericentromere. Genome Res. 11: 1053-1070, 2001. [PubMed: 11381032] [Full Text: https://doi.org/10.1101/gr.154901]
Liu, L., McKeehan, W. L. Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggest roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity. Genomics 79: 124-136, 2002. [PubMed: 11827465] [Full Text: https://doi.org/10.1006/geno.2001.6679]
Nagase, T., Kikuno, R., Hattori, A., Kondo, Y., Okumura, K., Ohara, O. Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 7: 347-355, 2000. [PubMed: 11214970] [Full Text: https://doi.org/10.1093/dnares/7.6.347]