NRIP1

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.

Full Name

Nuclear Receptor Interacting Protein 1

Function

Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors. Positive regulator of the circadian clock gene expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a coactivator for RORA and RORC. Involved in the regulation of ovarian function (By similarity).
Plays a role in renal development (PubMed:28381549).

Biological Process

Cellular response to estradiol stimulusManual Assertion Based On ExperimentIDA:BHF-UCL
Circadian regulation of gene expressionManual Assertion Based On ExperimentIMP:UniProtKB
Circadian rhythmManual Assertion Based On ExperimentIEP:UniProtKB
Lipid storageIEA:Ensembl
Negative regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:UniProtKB
Ovarian follicle ruptureIEA:Ensembl
Positive regulation of transcription by RNA polymerase IIManual Assertion Based On ExperimentIDA:UniProtKB

Cellular Location

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

Involvement in disease

Congenital anomalies of kidney and urinary tract 3 (CAKUT3):
A disorder encompassing a broad spectrum of renal and urinary tract malformations that include renal agenesis, kidney hypodysplasia, multicystic kidney dysplasia, duplex collecting system, posterior urethral valves and ureter abnormalities. Congenital anomalies of kidney and urinary tract are the commonest cause of chronic kidney disease in children. CAKUT3 inheritance is autosomal dominant.

PTM

Acetylation regulates its nuclear translocation and corepressive activity (By similarity).
Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH.