Synthesized acetyl-peptide derived from human RIP140 around the acetylation site of K158.

Acetyl-RIP140 (K158) Polyclonal Antibody detects endogenous levels of RIP140 around the acetylation site of K158 protein.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):SLkEQ

NRIP1

Nuclear receptor-interacting protein 1

NRIP1 ;
Nuclear receptor-interacting protein 1 ;
Nuclear factor RIP140 ;
Receptor-interacting protein 140

Nuclear receptor interacting protein 1 (NRIP1) is a nuclear protein that specifically interacts with the hormone-dependent activation domain AF2 of nuclear receptors. Also known as RIP140, this protein modulates transcriptional activity of the estrogen receptor. [provided by RefSeq, Jul 2008],

Disease:Genetic variation in NRIP1 may act as predisposing factor for endometriosis.,Domain:Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have different affinities for nuclear receptors. The C-terminal LTKTNPILYYMLQK motif is required for ligand-dependent interaction with RAAR and RXRB homo- and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB (By similarity). Contains at least four autonomous repression domains (RD1-4). RD1 functions via a histone deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4 can function by HDAC-dependent or independent mechanisms, depending on cell type. RD2 is dependent on CTBP binding.,Function:Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors.,PTM:Acetylation regulates its nuclear translocation and corepressive activity (By similarity). Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH.,subcellular location:Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.,subunit:Interacts with the ligand binding domain (LBD) of NR2C1 in the absence of ligand. Interacts with RARA and RXRB homodimers and RARA/RXRB heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 via its N-terminal domain (By similarity). Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH.,

Nucleus . Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.

Brain,Epithelium,Mammary gland,Skin,