true1996-02-012024-03-27199NRIP1_HUMANNuclear factor RIP140 modulates transcriptional activation by the estrogen receptor.Cavailles V.Dauvois S.L'Horset F.Lopez G.Hoare S.Kushner P.J.Parker M.G.doi:10.1002/j.1460-2075.1995.tb00044.x1995EMBO J.143741-3751NUCLEOTIDE SEQUENCE [MRNA]FUNCTIONINTERACTION WITH ESR1SUBCELLULAR LOCATIONVARIANT GLY-448Mammary glandThe DNA sequence of human chromosome 21.Hattori M.Fujiyama A.Taylor T.D.Watanabe H.Yada T.Park H.-S.Toyoda A.Ishii K.Totoki Y.Choi D.-K.Groner Y.Soeda E.Ohki M.Takagi T.Sakaki Y.Taudien S.Blechschmidt K.Polley A.Menzel U.Delabar J.Kumpf K.Lehmann R.Patterson D.Reichwald K.Rump A.Schillhabel M.Schudy A.Zimmermann W.Rosenthal A.Kudoh J.Shibuya K.Kawasaki K.Asakawa S.Shintani A.Sasaki T.Nagamine K.Mitsuyama S.Antonarakis S.E.Minoshima S.Shimizu N.Nordsiek G.Hornischer K.Brandt P.Scharfe M.Schoen O.Desario A.Reichelt J.Kauer G.Bloecker H.Ramser J.Beck A.Klages S.Hennig S.Riesselmann L.Dagand E.Wehrmeyer S.Borzym K.Gardiner K.Nizetic D.Francis F.Lehrach H.Reinhardt R.Yaspo M.-L.doi:10.1038/350125182000Nature405311-319NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]SkinRegulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4.Yan Z.H.Karam W.G.Staudinger J.L.Medvedev A.Ghanayem B.I.Jetten A.M.doi:10.1074/jbc.273.18.109481998J. Biol. Chem.27310948-10957INTERACTION WITH NR2C2Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids.Subramaniam N.Treuter E.Okret S.doi:10.1074/jbc.274.25.181211999J. Biol. Chem.27418121-18127FUNCTIONINTERACTION WITH NR3C1Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP.Vo N.Fjeld C.Goodman R.H.doi:10.1128/mcb.21.18.6181-6188.20012001Mol. Cell. Biol.216181-6188FUNCTIONINTERACTION WITH CTBP1MUTAGENESIS OF 440-PRO--LEU-443 AND LYS-446ACETYLATION AT LYS-446Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140.Zilliacus J.Holter E.Wakui H.Tazawa H.Treuter E.Gustafsson J.-A.doi:10.1210/mend.15.4.06242001Mol. Endocrinol.15501-511INTERACTION WITH NR3C1 AND YWHAHIDENTIFICATION IN A COMPLEX WITH NR3C1 AND YWHAHSUBCELLULAR LOCATIONA new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action.Zennaro M.-C.Souque A.Viengchareun S.Poisson E.Lombes M.doi:10.1210/mend.15.9.06892001Mol. Endocrinol.151586-1598FUNCTIONINTERACTION WITH NR3C2Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140.Tazawa H.Osman W.Shoji Y.Treuter E.Gustafsson J.-A.Zilliacus J.doi:10.1128/mcb.23.12.4187-4198.20032003Mol. Cell. Biol.234187-4198INTERACTION WITH NR3C1SUBCELLULAR LOCATIONReceptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect.Teyssier C.Belguise K.Galtier F.Cavailles V.Chalbos D.doi:10.1210/me.2002-03242003Mol. Endocrinol.17287-299FUNCTIONINTERACTION WITH ESR1; FOS AND JUNCharacterization of four autonomous repression domains in the corepressor receptor interacting protein 140.Christian M.Tullet J.M.A.Parker M.G.doi:10.1074/jbc.m3139062002004J. Biol. Chem.27915645-15651INTERACTION WITH CTBP1 AND CTBP2MUTAGENESIS OF 442-ASP--LEU-443; 567-ASN--LEU-568 AND 948-ASP--LEU-949IDENTIFICATION OF REPRESSION DOMAINSMultiple domains of the receptor-interacting protein 140 contribute to transcription inhibition.Castet A.Boulahtouf A.Versini G.Bonnet S.Augereau P.Vignon F.Khochbin S.Jalaguier S.Cavailles V.doi:10.1093/nar/gkh5242004Nucleic Acids Res.321957-1966FUNCTIONINTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND HDAC6MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568SUBCELLULAR LOCATIONModulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation.Huq M.D.Gupta P.Tsai N.P.Wei L.N.doi:10.1074/mcp.m600180-mcp2002006Mol. Cell. Proteomics52072-2082INTERACTION WITH NR2C2ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases.Lopez-Garcia J.Periyasamy M.Thomas R.S.Christian M.Leao M.Jat P.Kindle K.B.Heery D.M.Parker M.G.Buluwela L.Kamalati T.Ali S.doi:10.1093/nar/gkl8752006Nucleic Acids Res.346126-6136INTERACTION WITH ZNF366Modulation of clock gene expression by the transcriptional coregulator receptor interacting protein 140 (RIP140).Poliandri A.H.Gamsby J.J.Christian M.Spinella M.J.Loros J.J.Dunlap J.C.Parker M.G.doi:10.1177/07487304114015792011J. Biol. Rhythms26187-199FUNCTIONINTERACTION WITH RORAINDUCTIONToward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-807IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y.Song C.Cheng K.Dong M.Wang F.Huang J.Sun D.Wang L.Ye M.Zou H.doi:10.1016/j.jprot.2013.11.0142014J. Proteomics96253-262PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-671 AND SER-807IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverUncovering global SUMOylation signaling networks in a site-specific manner.Hendriks I.A.D'Souza R.C.Yang B.Verlaan-de Vries M.Mann M.Vertegaal A.C.doi:10.1038/nsmb.28902014Nat. Struct. Mol. Biol.21927-936SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-756 AND LYS-1105IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]A dominant mutation in nuclear receptor interacting protein 1 causes urinary tract malformations via dysregulation of retinoic acid signaling.Vivante A.Mann N.Yonath H.Weiss A.C.Getwan M.Kaminski M.M.Bohnenpoll T.Teyssier C.Chen J.Shril S.van der Ven A.T.Ityel H.Schmidt J.M.Widmeier E.Bauer S.B.Sanna-Cherchi S.Gharavi A.G.Lu W.Magen D.Shukrun R.Lifton R.P.Tasic V.Stanescu H.C.Cavailles V.Kleta R.Anikster Y.Dekel B.Kispert A.Lienkamp S.S.Hildebrandt F.doi:10.1681/asn.20160606942017J. Am. Soc. Nephrol.282364-2376FUNCTIONINVOLVEMENT IN CAKUT3Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.Hendriks I.A.Lyon D.Young C.Jensen L.J.Vertegaal A.C.Nielsen M.L.doi:10.1038/nsmb.33662017Nat. Struct. Mol. Biol.24325-336SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-170; LYS-195; LYS-198; LYS-372; LYS-508; LYS-756; LYS-802; LYS-850; LYS-901; LYS-931; LYS-1105; LYS-1115 AND LYS-1154IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Whole-exome sequencing identifies causative mutations in families with congenital anomalies of the kidney and urinary tract.van der Ven A.T.Connaughton D.M.Ityel H.Mann N.Nakayama M.Chen J.Vivante A.Hwang D.Y.Schulz J.Braun D.A.Schmidt J.M.Schapiro D.Schneider R.Warejko J.K.Daga A.Majmundar A.J.Tan W.Jobst-Schwan T.Hermle T.Widmeier E.Ashraf S.Amar A.Hoogstraaten C.A.Hugo H.Kitzler T.M.Kause F.Kolvenbach C.M.Dai R.Spaneas L.Amann K.Stein D.R.Baum M.A.Somers M.J.G.Rodig N.M.Ferguson M.A.Traum A.Z.Daouk G.H.Bogdanovic R.Stajic N.Soliman N.A.Kari J.A.El Desoky S.Fathy H.M.Milosevic D.Al-Saffar M.Awad H.S.Eid L.A.Selvin A.Senguttuvan P.Sanna-Cherchi S.Rehm H.L.MacArthur D.G.Lek M.Laricchia K.M.Wilson M.W.Mane S.M.Lifton R.P.Lee R.S.Bauer S.B.Lu W.Reutter H.M.Tasic V.Shril S.Hildebrandt F.doi:10.1681/asn.20171212652018J. Am. Soc. Nephrol.292348-2361INVOLVEMENT IN CAKUT3X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation.Wang L.Zuercher W.J.Consler T.G.Lambert M.H.Miller A.B.Orband-Miller L.A.McKee D.D.Willson T.M.Nolte R.T.doi:10.1074/jbc.m6084102002006J. Biol. Chem.28137773-37781X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH ESRRGPreliminary molecular genetic analysis of the receptor interacting protein 140 (RIP140) in women affected by endometriosis.Caballero V.Ruiz R.Sainz J.A.Cruz M.Lopez-Nevot M.A.Galan J.J.Real L.M.de Castro F.Lopez-Villaverde V.Ruiz A.doi:10.1186/1743-1050-2-112005J. Exp. Clin. Assist. Reprod.211VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079Atlas of Genetics and Cytogenetics in Oncology and Haematology1.95C=366-3902.60C/D=366-3903.54C=499-5101.90C/D=499-5102.40P/Q/R/S=493-5121.90P/Q/R/S=493-5121.64P/Q/R/S=493-5121.85P/Q=493-5121.80P/Q=493-5121.90P/Q=493-5121.66P/Q/R/S=493-512891014-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE2 sites, 1 O-linked glycan (2 sites)272 antibodies from 34 providershumanNRIP1Low tissue specificitygenephenotypeEukaryotaSUMOylation of transcription cofactorsCircadian ClockEstrogen-dependent gene expressionNR1H2 & NR1H3 regulate gene expression linked to lipogenesisNR1H2 & NR1H3 regulate gene expression linked to gluconeogenesisHeme signaling17 hits in 1162 CRISPR screenshumanTbioProteinExpressed in corpus epididymis and 212 other cell types or tissuesbaseline and differentialNRIP1NRIP1_RD1NRIP1_RD2NRIP1_RD3NRIP1_RD4NUCLEAR FACTOR RIP140NUCLEAR RECEPTOR-INTERACTING PROTEIN 1NRIP1_repr_1NRIP1_repr_2NRIP1_repr_3NRIP1_repr_4HSNuclear receptor-interacting protein 1Nuclear factor RIP140Receptor-interacting protein 140NRIP1Modulates 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 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).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. Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1 (By similarity). Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH. Interacts with ZNF366. Interacts with RORA.Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.Expressed in a circadian manner in the liver (at protein level).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 homodimers 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.Acetylation regulates its nuclear translocation and corepressive activity (By similarity). Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH.The disease is caused by variants affecting the gene represented in this entry.Nuclear receptor-interacting protein 112694211158Interaction with ZNF366415Disordered3356Repression domain 178333Disordered393435Repression domain 2410700Required for targeting to small nuclear foci431472Disordered540563Disordered592622Disordered641663Disordered716745Repression domain 3735885Interaction with ZNF366753Disordered950974Repression domain 41118LXXLL motif 12125LXXLL motif 2133137LXXLL motif 3185189LXXLL motif 4266270LXXLL motif 5380384CTBP-binding; principal site440446LXXLL motif 6500504CTBP-binding565569CTBP-binding599603LXXLL motif 7713717LXXLL motif 8819823LXXLL motif 9936940CTBP-binding946Ligand-dependent nuclear receptor binding10611074Polar residues404Polar residues658Basic and acidic residues722743Basic and acidic residues954969Phosphoserine104N6-acetyllysine; alternate111N6-acetyllysine158Phosphothreonine207Phosphoserine218N6-acetyllysine286N6-acetyllysine310Phosphoserine356Phosphoserine378N6-acetyllysineN6-acetyllysine481Phosphoserine487Phosphoserine518N6-acetyllysine528Phosphoserine542Phosphoserine564N6-acetyllysine606Phosphoserine671Phosphoserine807N6-acetyllysine; alternate931Phosphoserine1001Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)170Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)198Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)508Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)802Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)850Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)901Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)1105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)1115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)1154I37R221F315V441G448S567L803F1079Abolishes interaction with CTBP1.AAAA443Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression.AIA442Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression.AADisrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568.ASDisrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression.QDoes not disrupt nuclear hormone receptor-dependent transcription repression.RDisrupts transcriptional repression.AA568Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443.ASDoes not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568.PIAASAbolishes CTBP binding but retains transcriptional repressor activity.AA948949R124TKGRVK721726IA1080379385505false3false4false3false3false3false6false3false3false2false3false3false4false4false3false2ARPC3CEP70CTBP1DNMT1ESRRGFHL1GOLGA2GPRASP3HDAC3LDOC1PKNOX2PRMT1RARARARAZNF3662000-12-0121269420102132689fc3f3faf541cab2e6969b6MTHGEELGSDVHQDSIVLTYLEGLLMHQAAGGSGTAVDKKSAGHNEEDQNFNISGSAFPTCQSNGPVLNTHTYQGSGMLHLKKARLLQSSEDWNAAKRKRLSDSIMNLNVKKEALLAGMVDSVPKGKQDSTLLASLLQSFSSRLQTVALSQQIRQSLKEQGYALSHDSLKVEKDLRCYGVASSHLKTLLKKSKVKDQKPDTNLPDVTKNLIRDRFAESPHHVGQSGTKVMSEPLSCAARLQAVASMVEKRASPATSPKPSVACSQLALLLSSEAHLQQYSREHALKTQNANQAASERLAAMARLQENGQKDVGSYQLPKGMSSHLNGQARTSSSKLMASKSSATVFQNPMGIIPSSPKNAGYKNSLERNNIKQAANNSLLLHLLKSQTIPKPMNGHSHSERGSIFEESSTPTTIDEYSDNNPSFTDDSSGDESSYSNCVPIDLSCKHRTEKSESDQPVSLDNFTQSLLNTWDPKVPDVDIKEDQDTSKNSKLNSHQKVTLLQLLLGHKNEENVEKNTSPQGVHNDVSKFNTQNYARTSVIESPSTNRTTPVSTPPLLTSSKAGSPINLSQHSLVIKWNSPPYVCSTQSEKLTNTASNHSMDLTKSKDPPGEKPAQNEGAQNSATFSASKLLQNLAQCGMQSSMSVEEQRPSKQLLTGNTDKPIGMIDRLNSPLLSNKTNAVEENKAFSSQPTGPEPGLSGSEIENLLERRTVLQLLLGNPNKGKSEKKEKTPLRDESTQEHSERALSEQILMVKIKSEPCDDLQIPNTNVHLSHDAKSAPFLGMAPAVQRSAPALPVSEDFKSEPVSPQDFSFSKNGLLSRLLRQNQDSYLADDSDRSHRNNEMALLESKNLCMVPKKRKLYTEPLENPFKKMKNNIVDAANNHSAPEVLYGSLLNQEELKFSRNDLEFKYPAGHGSASESEHRSWARESKSFNVLKQLLLSENCVRDLSPHRSNSVADSKKKGHKNNVTNSKPEFSISSLNGLMYSSTQPSSCMDNRTFSYPGVVKTPVSPTFPEHLGCAGSRPESGLLNGCSMPSEKGPIKWVITDAEKNEYEKDSPRLTKTNPILYYMLQKGGNSVTSRETQDKDIWREASSAESVSQVTAKEELLPTAETKASFFNLRSPYNSHMGNNASRPHSANGEVYGLLGSVLTIKKESEtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue