Ring Finger Protein, LIM Domain Interacting (RLIM) Antibody – Rabbit Polyclonal

The protein encoded by this gene is a RING-H2 zinc finger protein. It has been shown to be an E3 ubiquitin protein ligase that targets LIM domain binding 1 (LDB1/CLIM), and causes proteasome-dependent degradation of LDB1. This protein and LDB1 are co-repressors of LHX1/LIM-1, a homeodomain transcription factor. Multiple alternatively spliced variants, encoding the same protein, have been identified. [provided by RefSeq, Feb 2009]

RNF12: E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex- related dosage differences of X-encoded genes in somatic cells of female placental mammals. Belongs to the RNF12 family.

Protein type: Transcription, coactivator/corepressor; Ligase; Ubiquitin conjugating system; EC 6.3.2.-; Ubiquitin ligase

Chromosomal Location of Human Ortholog: Xq13-q21

Cellular Component: nucleoplasm; transcriptional repressor complex; cytoplasm; nucleus

Molecular Function: zinc ion binding; ubiquitin-protein ligase activity; transcription corepressor activity; ligase activity

Biological Process: ubiquitin-dependent protein catabolic process; transcription, DNA-dependent; negative regulation of transcription factor activity; protein ubiquitination; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent