a core component of the BAF (hSWI/SNF) complex. This family of complexes remodels chromatin structures, enabling transcription factors to gain access to DNA. They play important roles in cell proliferation and differentiation, in cellular antiviral activities and inhibition of tumor formation. The BAF complex is able to create a stable, altered form of chromatin that constrains fewer negative supercoils than normal. This change in supercoiling is due to the conversion of up to one-half of the nucleosomes on polynucleosomal arrays into asymmetric structures, termed altosomes, each composed of 2 histones octamers. Stimulates in vitro the remodeling activity of SMARCA4. Involved in activation of CSF1 promoter. Belongs to the neural progenitors- specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain BAF53A and PHF10, are exchanged for homologous alternative BAF53B and BAF45B or BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Plays a key role in cell-cycle control and causes cell cycle arrest in G0/G1. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand- bound VDR-mediated transrepression of the CYP27B1 gene. Component of the BAF (hSWI/SNF) complex, which includes at least actin (ACTB), ARID1A, ARID1B, SMARCA2, SMARCA4, BAF53A, BAF53B, SMARCE1 SMARCC1, SMARCC2, SMARCB1, and one or more of SMARCD1, SMARCD2, or SMARCD3. In muscle cells, the BAF complex also contains DPF3. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Binds to double-stranded DNA. Interacts with EphB4 and MAEL. Interacts with GADD34. Binds tightly to the human immunodeficiency virus-type 1 (HIV-1) integrase in vitro and stimulates its DNA-joining activity. Interacts with human papillomavirus 18 E1 protein to stimulates its viral replication. Belongs to the SNF5 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation; Transcription, coactivator/corepressor; Tumor suppressor
Molecular Function: DNA binding; nucleosomal DNA binding; p53 binding; protein binding; Tat protein binding; transcription coactivator activity
Biological Process: ATP-dependent chromatin remodeling; cell differentiation; chromatin remodeling; DNA integration; DNA repair; negative regulation of cell proliferation; nucleosome disassembly; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.