RAP140 Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2. Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed. Belongs to the TASOR family. 4 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Unknown function
Chromosomal Location of human Ortholog: 3p14.3
Cellular Component:  heterochromatin; nucleoplasm
Molecular Function:  chromatin binding; protein binding
Biological Process:  negative regulation of gene expression, epigenetic; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; positive regulation of methylation-dependent chromatin silencing; protein localization to heterochromatin
Reference #:  Q9UK61 (UniProtKB)
Alt. Names/Synonyms: C3orf63; CTCL tumor antigen se89-1; DKFZp686C2456; FAM208A; family with sequence similarity 208 member A; KIAA1105; protein FAM208A; Protein TASOR; RAP140; retinoblastoma-associated protein 140; Retinoblastoma-associated protein RAP140; se89-1; TASOR; TASOR1; transcription activation suppressor; Transgene activation suppressor protein; Uncharacterized protein C3orf63
Gene Symbols: TASOR
Molecular weight: 189,032 Da
Basal Isoelectric point: 5.55  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene