SMARCA2

From Wikipedia, the free encyclopedia

SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2

PDB rendering based on 2dat.

Available structures: 2dat

Identifiers

Symbol(s)

SMARCA2; SWI2; BAF190; BRM; FLJ36757; MGC74511; SNF2; SNF2L2; SNF2LA; Sth1p; hBRM; hSNF2a

External IDs

OMIM: 600014 MGI: 99603 HomoloGene: 2308

Gene ontology
Molecular Function:	• nucleotide binding • DNA binding • transcription coactivator activity • helicase activity • protein binding • ATP binding • hydrolase activity
Cellular Component:	• nucleus • nucleoplasm
Biological Process:	• transcription • regulation of transcription from RNA polymerase II promoter • negative regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_003070 (mRNA)
NP_003061 (protein)

NM_011416 (mRNA)
NP_035546 (protein)

Location

Chr 9: 2.01 - 2.18 Mb

Chr 19: 26.67 - 26.85 Mb

Pubmed search

[1]

[2]

SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2, also known as SMARCA2, is a human gene.^[1]

The protein encoded by this gene is a member of the SWI/SNF family of proteins and is highly similar to the brahma protein of Drosophila. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The encoded protein is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is required for transcriptional activation of genes normally repressed by chromatin. Two transcript variants encoding different isoforms have been found for this gene, which contains a trinucleotide repeat (CAG) length polymorphism.^[1]

[edit] References

^ ^a ^b Entrez Gene: SMARCA2 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2.

[edit] Further reading

Aves SJ, Hindley J, Phear GA, Tongue N (1995). "A fission yeast gene mapping close to suc1 encodes a protein containing two bromodomains.". Mol. Gen. Genet. 248 (4): 491–8. PMID 7565614.
Muchardt C, Yaniv M, Mattei MG (1994). "Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2 and Drosophila brm genes, to chromosome region 9p23-p24, by in situ hybridization.". Mamm. Genome 5 (4): 241–3. PMID 8012116.
Chiba H, Muramatsu M, Nomoto A, Kato H (1994). "Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor.". Nucleic Acids Res. 22 (10): 1815–20. PMID 8208605.
Muchardt C, Yaniv M (1993). "A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor.". EMBO J. 12 (11): 4279–90. PMID 8223438.
Muchardt C, Reyes JC, Bourachot B, et al. (1996). "The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis.". EMBO J. 15 (13): 3394–402. PMID 8670841.
Wang W, Xue Y, Zhou S, et al. (1996). "Diversity and specialization of mammalian SWI/SNF complexes.". Genes Dev. 10 (17): 2117–30. PMID 8804307.
Wang W, Côté J, Xue Y, et al. (1996). "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex.". EMBO J. 15 (19): 5370–82. PMID 8895581.
Ichinose H, Garnier JM, Chambon P, Losson R (1997). "Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2.". Gene 188 (1): 95–100. PMID 9099865.
Cho H, Orphanides G, Sun X, et al. (1998). "A human RNA polymerase II complex containing factors that modify chromatin structure.". Mol. Cell. Biol. 18 (9): 5355–63. PMID 9710619.
Thaete C, Brett D, Monaghan P, et al. (1999). "Functional domains of the SYT and SYT-SSX synovial sarcoma translocation proteins and co-localization with the SNF protein BRM in the nucleus.". Hum. Mol. Genet. 8 (4): 585–91. PMID 10072425.
Phelan ML, Sif S, Narlikar GJ, Kingston RE (1999). "Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits.". Mol. Cell 3 (2): 247–53. PMID 10078207.
Lee DW, Zhang K, Ning ZQ, et al. (2000). "Proliferation-associated SNF2-like gene (PASG): a SNF2 family member altered in leukemia.". Cancer Res. 60 (13): 3612–22. PMID 10910076.
Phelan ML, Schnitzler GR, Kingston RE (2000). "Octamer transfer and creation of stably remodeled nucleosomes by human SWI-SNF and its isolated ATPases.". Mol. Cell. Biol. 20 (17): 6380–9. PMID 10938115.
Xue Y, Canman JC, Lee CS, et al. (2001). "The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes.". Proc. Natl. Acad. Sci. U.S.A. 97 (24): 13015–20. doi:10.1073/pnas.240208597. PMID 11078522.
Machida Y, Murai K, Miyake K, Iijima S (2001). "Expression of chromatin remodeling factors during neural differentiation.". J. Biochem. 129 (1): 43–9. PMID 11134956.
de la Serna IL, Carlson KA, Imbalzano AN (2001). "Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation.". Nat. Genet. 27 (2): 187–90. doi:10.1038/84826. PMID 11175787.
Ruhf ML, Braun A, Papoulas O, et al. (2001). "The domino gene of Drosophila encodes novel members of the SWI2/SNF2 family of DNA-dependent ATPases, which contribute to the silencing of homeotic genes.". Development 128 (8): 1429–41. PMID 11262242.
Strobeck MW, Reisman DN, Gunawardena RW, et al. (2002). "Compensation of BRG-1 function by Brm: insight into the role of the core SWI-SNF subunits in retinoblastoma tumor suppressor signaling.". J. Biol. Chem. 277 (7): 4782–9. doi:10.1074/jbc.M109532200. PMID 11719516.
Kato H, Tjernberg A, Zhang W, et al. (2002). "SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones.". J. Biol. Chem. 277 (7): 5498–505. doi:10.1074/jbc.M108702200. PMID 11734557.
Mizutani T, Ito T, Nishina M, et al. (2002). "Maintenance of integrated proviral gene expression requires Brm, a catalytic subunit of SWI/SNF complex.". J. Biol. Chem. 277 (18): 15859–64. doi:10.1074/jbc.M112421200. PMID 11850427.