ID NRIP1_HUMAN Reviewed; 1158 AA. AC P48552; Q8IWE8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 199. DE RecName: Full=Nuclear receptor-interacting protein 1; DE AltName: Full=Nuclear factor RIP140; DE AltName: Full=Receptor-interacting protein 140; GN Name=NRIP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR RP LOCATION, AND VARIANT GLY-448. RC TISSUE=Mammary gland; RX PubMed=7641693; DOI=10.1002/j.1460-2075.1995.tb00044.x; RA Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J., RA Parker M.G.; RT "Nuclear factor RIP140 modulates transcriptional activation by the estrogen RT receptor."; RL EMBO J. 14:3741-3751(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH NR2C2. RX PubMed=9556573; DOI=10.1074/jbc.273.18.10948; RA Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., RA Jetten A.M.; RT "Regulation of peroxisome proliferator-activated receptor alpha-induced RT transactivation by the nuclear orphan receptor TAK1/TR4."; RL J. Biol. Chem. 273:10948-10957(1998). RN [5] RP FUNCTION, AND INTERACTION WITH NR3C1. RX PubMed=10364267; DOI=10.1074/jbc.274.25.18121; RA Subramaniam N., Treuter E., Okret S.; RT "Receptor interacting protein RIP140 inhibits both positive and negative RT gene regulation by glucocorticoids."; RL J. Biol. Chem. 274:18121-18127(1999). RN [6] RP FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND RP LYS-446, AND ACETYLATION AT LYS-446. RX PubMed=11509661; DOI=10.1128/mcb.21.18.6181-6188.2001; RA Vo N., Fjeld C., Goodman R.H.; RT "Acetylation of nuclear hormone receptor-interacting protein RIP140 RT regulates binding of the transcriptional corepressor CtBP."; RL Mol. Cell. Biol. 21:6181-6188(2001). RN [7] RP INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH NR3C1 RP AND YWHAH, AND SUBCELLULAR LOCATION. RX PubMed=11266503; DOI=10.1210/mend.15.4.0624; RA Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.; RT "Regulation of glucocorticoid receptor activity by 14-3-3-dependent RT intracellular relocalization of the corepressor RIP140."; RL Mol. Endocrinol. 15:501-511(2001). RN [8] RP FUNCTION, AND INTERACTION WITH NR3C2. RX PubMed=11518808; DOI=10.1210/mend.15.9.0689; RA Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.; RT "A new human MR splice variant is a ligand-independent transactivator RT modulating corticosteroid action."; RL Mol. Endocrinol. 15:1586-1598(2001). RN [9] RP INTERACTION WITH NR3C1, AND SUBCELLULAR LOCATION. RX PubMed=12773562; DOI=10.1128/mcb.23.12.4187-4198.2003; RA Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A., Zilliacus J.; RT "Regulation of subnuclear localization is associated with a mechanism for RT nuclear receptor corepression by RIP140."; RL Mol. Cell. Biol. 23:4187-4198(2003). RN [10] RP FUNCTION, AND INTERACTION WITH ESR1; FOS AND JUN. RX PubMed=12554755; DOI=10.1210/me.2002-0324; RA Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.; RT "Receptor-interacting protein 140 binds c-Jun and inhibits estradiol- RT induced activator protein-1 activity by reversing glucocorticoid receptor- RT interacting protein 1 effect."; RL Mol. Endocrinol. 17:287-299(2003). RN [11] RP INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443; RP 567-ASN--LEU-568 AND 948-ASP--LEU-949, AND IDENTIFICATION OF REPRESSION RP DOMAINS. RX PubMed=14736873; DOI=10.1074/jbc.m313906200; RA Christian M., Tullet J.M.A., Parker M.G.; RT "Characterization of four autonomous repression domains in the corepressor RT receptor interacting protein 140."; RL J. Biol. Chem. 279:15645-15651(2004). RN [12] RP FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND HDAC6, RP MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, AND SUBCELLULAR RP LOCATION. RX PubMed=15060175; DOI=10.1093/nar/gkh524; RA Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., RA Khochbin S., Jalaguier S., Cavailles V.; RT "Multiple domains of the receptor-interacting protein 140 contribute to RT transcription inhibition."; RL Nucleic Acids Res. 32:1957-1966(2004). RN [13] RP INTERACTION WITH NR2C2. RX PubMed=16887930; DOI=10.1074/mcp.m600180-mcp200; RA Huq M.D., Gupta P., Tsai N.P., Wei L.N.; RT "Modulation of testicular receptor 4 activity by mitogen-activated protein RT kinase-mediated phosphorylation."; RL Mol. Cell. Proteomics 5:2072-2082(2006). RN [14] RP INTERACTION WITH ZNF366. RX PubMed=17085477; DOI=10.1093/nar/gkl875; RA Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., RA Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.; RT "ZNF366 is an estrogen receptor corepressor that acts through CtBP and RT histone deacetylases."; RL Nucleic Acids Res. 34:6126-6136(2006). RN [15] RP FUNCTION, INTERACTION WITH RORA, AND INDUCTION. RX PubMed=21628546; DOI=10.1177/0748730411401579; RA Poliandri A.H., Gamsby J.J., Christian M., Spinella M.J., Loros J.J., RA Dunlap J.C., Parker M.G.; RT "Modulation of clock gene expression by the transcriptional coregulator RT receptor interacting protein 140 (RIP140)."; RL J. Biol. Rhythms 26:187-199(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-807, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-671 AND SER-807, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-756 AND LYS-1105, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [19] RP FUNCTION, AND INVOLVEMENT IN CAKUT3. RX PubMed=28381549; DOI=10.1681/asn.2016060694; RA Vivante A., Mann N., Yonath H., Weiss A.C., Getwan M., Kaminski M.M., RA Bohnenpoll T., Teyssier C., Chen J., Shril S., van der Ven A.T., Ityel H., RA Schmidt J.M., Widmeier E., Bauer S.B., Sanna-Cherchi S., Gharavi A.G., RA Lu W., Magen D., Shukrun R., Lifton R.P., Tasic V., Stanescu H.C., RA Cavailles V., Kleta R., Anikster Y., Dekel B., Kispert A., Lienkamp S.S., RA Hildebrandt F.; RT "A dominant mutation in nuclear receptor interacting protein 1 causes RT urinary tract malformations via dysregulation of retinoic acid signaling."; RL J. Am. Soc. Nephrol. 28:2364-2376(2017). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-170; LYS-195; LYS-198; RP LYS-372; LYS-508; LYS-756; LYS-802; LYS-850; LYS-901; LYS-931; LYS-1105; RP LYS-1115 AND LYS-1154, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [21] RP INVOLVEMENT IN CAKUT3. RX PubMed=30143558; DOI=10.1681/asn.2017121265; RA van der Ven A.T., Connaughton D.M., Ityel H., Mann N., Nakayama M., RA Chen J., Vivante A., Hwang D.Y., Schulz J., Braun D.A., Schmidt J.M., RA Schapiro D., Schneider R., Warejko J.K., Daga A., Majmundar A.J., Tan W., RA Jobst-Schwan T., Hermle T., Widmeier E., Ashraf S., Amar A., RA Hoogstraaten C.A., Hugo H., Kitzler T.M., Kause F., Kolvenbach C.M., RA Dai R., Spaneas L., Amann K., Stein D.R., Baum M.A., Somers M.J.G., RA Rodig N.M., Ferguson M.A., Traum A.Z., Daouk G.H., Bogdanovic R., RA Stajic N., Soliman N.A., Kari J.A., El Desoky S., Fathy H.M., Milosevic D., RA Al-Saffar M., Awad H.S., Eid L.A., Selvin A., Senguttuvan P., RA Sanna-Cherchi S., Rehm H.L., MacArthur D.G., Lek M., Laricchia K.M., RA Wilson M.W., Mane S.M., Lifton R.P., Lee R.S., Bauer S.B., Lu W., RA Reutter H.M., Tasic V., Shril S., Hildebrandt F.; RT "Whole-exome sequencing identifies causative mutations in families with RT congenital anomalies of the kidney and urinary tract."; RL J. Am. Soc. Nephrol. 29:2348-2361(2018). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH ESRRG. RX PubMed=16990259; DOI=10.1074/jbc.m608410200; RA Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B., RA Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.; RT "X-ray crystal structures of the estrogen-related receptor-gamma ligand RT binding domain in three functional states reveal the molecular basis of RT small molecule regulation."; RL J. Biol. Chem. 281:37773-37781(2006). RN [23] RP VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079. RX PubMed=16131398; DOI=10.1186/1743-1050-2-11; RA Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A., Galan J.J., RA Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A.; RT "Preliminary molecular genetic analysis of the receptor interacting protein RT 140 (RIP140) in women affected by endometriosis."; RL J. Exp. Clin. Assist. Reprod. 2:11-11(2005). CC -!- FUNCTION: Modulates transcriptional activation by steroid receptors CC such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional CC repression by nuclear hormone receptors. Positive regulator of the CC circadian clock gene expression: stimulates transcription of BMAL1, CC CLOCK and CRY1 by acting as a coactivator for RORA and RORC. Involved CC in the regulation of ovarian function (By similarity). Plays a role in CC renal development (PubMed:28381549). {ECO:0000250|UniProtKB:Q8CBD1, CC ECO:0000269|PubMed:10364267, ECO:0000269|PubMed:11509661, CC ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12554755, CC ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:21628546, CC ECO:0000269|PubMed:28381549, ECO:0000269|PubMed:7641693}. CC -!- SUBUNIT: Interacts with RARA and RXRB homodimers and RARA/RXRB CC heterodimers in the presence of ligand. Interacts with HDAC1 and HDAC3 CC via its N-terminal domain. Interacts with NR2C1 (sumoylated form and CC via the ligand-binding domain); the interaction results in promoting CC the repressor activity of NR2C1 (By similarity). Interacts with CTBP1, CC CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, CC JUN and FOS. Found in a complex with both NR3C1 and YWHAH. Interacts CC with ZNF366. Interacts with RORA. {ECO:0000250|UniProtKB:Q8CBD1, CC ECO:0000269|PubMed:10364267, ECO:0000269|PubMed:11266503, CC ECO:0000269|PubMed:11509661, ECO:0000269|PubMed:11518808, CC ECO:0000269|PubMed:12554755, ECO:0000269|PubMed:12773562, CC ECO:0000269|PubMed:14736873, ECO:0000269|PubMed:15060175, CC ECO:0000269|PubMed:16887930, ECO:0000269|PubMed:16990259, CC ECO:0000269|PubMed:17085477, ECO:0000269|PubMed:21628546, CC ECO:0000269|PubMed:7641693, ECO:0000269|PubMed:9556573}. CC -!- INTERACTION: CC P48552; O15145: ARPC3; NbExp=3; IntAct=EBI-746484, EBI-351829; CC P48552; Q8NHQ1: CEP70; NbExp=4; IntAct=EBI-746484, EBI-739624; CC P48552; Q13363: CTBP1; NbExp=3; IntAct=EBI-746484, EBI-908846; CC P48552; P26358: DNMT1; NbExp=3; IntAct=EBI-746484, EBI-719459; CC P48552; P62508-3: ESRRG; NbExp=3; IntAct=EBI-746484, EBI-12001340; CC P48552; Q13642: FHL1; NbExp=6; IntAct=EBI-746484, EBI-912547; CC P48552; Q08379: GOLGA2; NbExp=3; IntAct=EBI-746484, EBI-618309; CC P48552; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-746484, EBI-11519926; CC P48552; O15379: HDAC3; NbExp=2; IntAct=EBI-746484, EBI-607682; CC P48552; O95751: LDOC1; NbExp=3; IntAct=EBI-746484, EBI-740738; CC P48552; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-746484, EBI-2692890; CC P48552; Q99873: PRMT1; NbExp=4; IntAct=EBI-746484, EBI-78738; CC P48552; P10276: RARA; NbExp=4; IntAct=EBI-746484, EBI-413374; CC P48552; P10276-2: RARA; NbExp=3; IntAct=EBI-746484, EBI-10197061; CC P48552; Q8N895: ZNF366; NbExp=2; IntAct=EBI-746484, EBI-2813661; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11266503, CC ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:15060175, CC ECO:0000269|PubMed:7641693}. Note=Localized to discrete foci and CC redistributes to larger nuclear domains upon binding to ligand-bound CC NR3C1. CC -!- INDUCTION: Expressed in a circadian manner in the liver (at protein CC level). {ECO:0000269|PubMed:21628546}. CC -!- DOMAIN: Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have CC different affinities for nuclear receptors. The C-terminal CC LTKTNPILYYMLQK motif is required for ligand-dependent interaction with CC RAAR and RXRB homodimers and heterodimers, for the corepressor CC activity, and for the formation of an HDAC3 complex with RARA/RXRB (By CC similarity). Contains at least four autonomous repression domains (RD1- CC 4). RD1 functions via a histone deacetylase (HDAC)-independent CC mechanism, whereas RD2, RD3 and RD4 can function by HDAC-dependent or CC independent mechanisms, depending on cell type. RD2 is dependent on CC CTBP binding. {ECO:0000250}. CC -!- PTM: Acetylation regulates its nuclear translocation and corepressive CC activity (By similarity). Acetylation abolishes interaction with CTBP1. CC Phosphorylation enhances interaction with YWHAH. {ECO:0000250, CC ECO:0000269|PubMed:11509661}. CC -!- DISEASE: Congenital anomalies of kidney and urinary tract 3 (CAKUT3) CC [MIM:618270]: A disorder encompassing a broad spectrum of renal and CC urinary tract malformations that include renal agenesis, kidney CC hypodysplasia, multicystic kidney dysplasia, duplex collecting system, CC posterior urethral valves and ureter abnormalities. Congenital CC anomalies of kidney and urinary tract are the commonest cause of CC chronic kidney disease in children. CAKUT3 inheritance is autosomal CC dominant. {ECO:0000269|PubMed:28381549, ECO:0000269|PubMed:30143558}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44067/NRIP1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X84373; CAA59108.1; -; mRNA. DR EMBL; AF248484; AAF62185.1; -; Genomic_DNA. DR EMBL; AF127577; AAF35255.1; -; Genomic_DNA. DR EMBL; AL163207; CAB90396.1; -; Genomic_DNA. DR EMBL; BC040361; AAH40361.1; -; mRNA. DR CCDS; CCDS13568.1; -. DR PIR; S57348; S57348. DR RefSeq; NP_003480.2; NM_003489.3. DR RefSeq; XP_005261120.1; XM_005261063.3. DR RefSeq; XP_005261122.1; XM_005261065.3. DR RefSeq; XP_011528049.1; XM_011529747.1. DR RefSeq; XP_011528050.1; XM_011529748.2. DR RefSeq; XP_011528051.1; XM_011529749.2. DR RefSeq; XP_011528053.1; XM_011529751.2. DR RefSeq; XP_011528054.1; XM_011529752.1. DR RefSeq; XP_016883962.1; XM_017028473.1. DR RefSeq; XP_016883963.1; XM_017028474.1. DR RefSeq; XP_016883964.1; XM_017028475.1. DR RefSeq; XP_016883965.1; XM_017028476.1. DR PDB; 2GPO; X-ray; 1.95 A; C=366-390. DR PDB; 2GPP; X-ray; 2.60 A; C/D=366-390. DR PDB; 4S14; X-ray; 3.54 A; C=499-510. DR PDB; 4S15; X-ray; 1.90 A; C/D=499-510. DR PDB; 5NTI; X-ray; 2.40 A; P/Q/R/S=493-512. DR PDB; 5NTN; X-ray; 1.90 A; P/Q/R/S=493-512. DR PDB; 5NTW; X-ray; 1.64 A; P/Q/R/S=493-512. DR PDB; 5NU1; X-ray; 1.85 A; P/Q=493-512. DR PDB; 6FZU; X-ray; 1.80 A; P/Q=493-512. DR PDB; 6G05; X-ray; 1.90 A; P/Q=493-512. DR PDB; 6G07; X-ray; 1.66 A; P/Q/R/S=493-512. DR PDBsum; 2GPO; -. DR PDBsum; 2GPP; -. DR PDBsum; 4S14; -. DR PDBsum; 4S15; -. DR PDBsum; 5NTI; -. DR PDBsum; 5NTN; -. DR PDBsum; 5NTW; -. DR PDBsum; 5NU1; -. DR PDBsum; 6FZU; -. DR PDBsum; 6G05; -. DR PDBsum; 6G07; -. DR AlphaFoldDB; P48552; -. DR SMR; P48552; -. DR BioGRID; 113843; 89. DR DIP; DIP-5964N; -. DR IntAct; P48552; 101. DR MINT; P48552; -. DR STRING; 9606.ENSP00000327213; -. DR DrugBank; DB06884; 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE. DR GlyGen; P48552; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P48552; -. DR PhosphoSitePlus; P48552; -. DR BioMuta; NRIP1; -. DR DMDM; 9988061; -. DR EPD; P48552; -. DR jPOST; P48552; -. DR MassIVE; P48552; -. DR MaxQB; P48552; -. DR PaxDb; 9606-ENSP00000383063; -. DR PeptideAtlas; P48552; -. DR ProteomicsDB; 55908; -. DR Antibodypedia; 5789; 272 antibodies from 34 providers. DR DNASU; 8204; -. DR Ensembl; ENST00000318948.7; ENSP00000327213.4; ENSG00000180530.11. DR Ensembl; ENST00000400199.5; ENSP00000383060.1; ENSG00000180530.11. DR Ensembl; ENST00000400202.5; ENSP00000383063.1; ENSG00000180530.11. DR GeneID; 8204; -. DR KEGG; hsa:8204; -. DR MANE-Select; ENST00000318948.7; ENSP00000327213.4; NM_003489.4; NP_003480.2. DR UCSC; uc002yjx.2; human. DR AGR; HGNC:8001; -. DR CTD; 8204; -. DR DisGeNET; 8204; -. DR GeneCards; NRIP1; -. DR HGNC; HGNC:8001; NRIP1. DR HPA; ENSG00000180530; Low tissue specificity. DR MalaCards; NRIP1; -. DR MIM; 602490; gene. DR MIM; 618270; phenotype. DR neXtProt; NX_P48552; -. DR OpenTargets; ENSG00000180530; -. DR PharmGKB; PA31780; -. DR VEuPathDB; HostDB:ENSG00000180530; -. DR eggNOG; ENOG502QS1C; Eukaryota. DR GeneTree; ENSGT00390000007999; -. DR HOGENOM; CLU_008553_0_0_1; -. DR InParanoid; P48552; -. DR OMA; TQEHTDR; -. DR OrthoDB; 5317343at2759; -. DR PhylomeDB; P48552; -. DR TreeFam; TF332210; -. DR PathwayCommons; P48552; -. DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors. DR Reactome; R-HSA-400253; Circadian Clock. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR Reactome; R-HSA-9029558; NR1H2 & NR1H3 regulate gene expression linked to lipogenesis. DR Reactome; R-HSA-9632974; NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis. DR Reactome; R-HSA-9707616; Heme signaling. DR SignaLink; P48552; -. DR SIGNOR; P48552; -. DR BioGRID-ORCS; 8204; 17 hits in 1162 CRISPR screens. DR ChiTaRS; NRIP1; human. DR EvolutionaryTrace; P48552; -. DR GeneWiki; NRIP1; -. DR GenomeRNAi; 8204; -. DR Pharos; P48552; Tbio. DR PRO; PR:P48552; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P48552; Protein. DR Bgee; ENSG00000180530; Expressed in corpus epididymis and 212 other cell types or tissues. DR ExpressionAtlas; P48552; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:UniProtKB. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; IPI:UniProtKB. DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB. DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL. DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB. DR GO; GO:0019915; P:lipid storage; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0001543; P:ovarian follicle rupture; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR IDEAL; IID00050; -. DR InterPro; IPR026649; NRIP1. DR InterPro; IPR031405; NRIP1_RD1. DR InterPro; IPR031406; NRIP1_RD2. DR InterPro; IPR031407; NRIP1_RD3. DR InterPro; IPR031408; NRIP1_RD4. DR PANTHER; PTHR15088; NUCLEAR FACTOR RIP140; 1. DR PANTHER; PTHR15088:SF0; NUCLEAR RECEPTOR-INTERACTING PROTEIN 1; 1. DR Pfam; PF15687; NRIP1_repr_1; 1. DR Pfam; PF15688; NRIP1_repr_2; 1. DR Pfam; PF15689; NRIP1_repr_3; 1. DR Pfam; PF15690; NRIP1_repr_4; 1. DR Genevisible; P48552; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Biological rhythms; Isopeptide bond; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..1158 FT /note="Nuclear receptor-interacting protein 1" FT /id="PRO_0000057951" FT REGION 1..415 FT /note="Interaction with ZNF366" FT /evidence="ECO:0000269|PubMed:17085477" FT REGION 33..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 78..333 FT /note="Repression domain 1" FT REGION 393..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 410..700 FT /note="Repression domain 2" FT REGION 431..472 FT /note="Required for targeting to small nuclear foci" FT REGION 540..563 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 592..622 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 641..663 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 716..745 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 735..885 FT /note="Repression domain 3" FT REGION 753..1158 FT /note="Interaction with ZNF366" FT /evidence="ECO:0000269|PubMed:17085477" FT REGION 950..974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1118..1158 FT /note="Repression domain 4" FT MOTIF 21..25 FT /note="LXXLL motif 1" FT MOTIF 133..137 FT /note="LXXLL motif 2" FT MOTIF 185..189 FT /note="LXXLL motif 3" FT MOTIF 266..270 FT /note="LXXLL motif 4" FT MOTIF 380..384 FT /note="LXXLL motif 5" FT MOTIF 440..446 FT /note="CTBP-binding; principal site" FT MOTIF 500..504 FT /note="LXXLL motif 6" FT MOTIF 565..569 FT /note="CTBP-binding" FT MOTIF 599..603 FT /note="CTBP-binding" FT /evidence="ECO:0000255" FT MOTIF 713..717 FT /note="LXXLL motif 7" FT MOTIF 819..823 FT /note="LXXLL motif 8" FT MOTIF 936..940 FT /note="LXXLL motif 9" FT MOTIF 946..950 FT /note="CTBP-binding" FT MOTIF 1061..1074 FT /note="Ligand-dependent nuclear receptor binding" FT /evidence="ECO:0000250" FT COMPBIAS 404..435 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 641..658 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..743 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 954..969 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 104 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 111 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 158 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 207 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 218 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 286 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 310 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 446 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:11509661" FT MOD_RES 481 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 487 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 518 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 528 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 542 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 564 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 606 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 671 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 807 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 931 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT MOD_RES 1001 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8CBD1" FT CROSSLNK 111 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 170 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 195 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 198 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 372 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 508 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 756 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 802 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 850 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 901 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 931 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1105 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1154 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 37 FT /note="V -> I (in dbSNP:rs9941840)" FT /id="VAR_051241" FT VARIANT 221 FT /note="H -> R (in dbSNP:rs139263261)" FT /evidence="ECO:0000269|PubMed:16131398" FT /id="VAR_023706" FT VARIANT 315 FT /note="Y -> F (in dbSNP:rs2228507)" FT /id="VAR_034142" FT VARIANT 441 FT /note="I -> V (in dbSNP:rs150468995)" FT /evidence="ECO:0000269|PubMed:16131398" FT /id="VAR_023707" FT VARIANT 448 FT /note="R -> G (in dbSNP:rs2229742)" FT /evidence="ECO:0000269|PubMed:16131398, FT ECO:0000269|PubMed:7641693" FT /id="VAR_023708" FT VARIANT 567 FT /note="N -> S (in dbSNP:rs9975169)" FT /id="VAR_051242" FT VARIANT 803 FT /note="S -> L (in dbSNP:rs61750208)" FT /evidence="ECO:0000269|PubMed:16131398" FT /id="VAR_023709" FT VARIANT 1079 FT /note="V -> F (in dbSNP:rs140803495)" FT /evidence="ECO:0000269|PubMed:16131398" FT /id="VAR_023710" FT MUTAGEN 440..443 FT /note="PIDL->AAAA: Abolishes interaction with CTBP1." FT /evidence="ECO:0000269|PubMed:11509661" FT MUTAGEN 440..442 FT /note="PID->AIA: Abolishes interaction with CTBP1 and FT attenuates nuclear hormone receptor-dependent transcription FT repression." FT MUTAGEN 442..443 FT /note="DL->AA: Reduces, but does not completely abolish, FT interaction with CTBP. Reduces transcriptional repression." FT /evidence="ECO:0000269|PubMed:14736873, FT ECO:0000269|PubMed:15060175" FT MUTAGEN 442..443 FT /note="DL->AS: Disrupts interaction with CTBP1, and CTBP2 FT to a lesser extent. Disrupts transcriptional repression; FT when associated with 567-AS-568." FT /evidence="ECO:0000269|PubMed:14736873, FT ECO:0000269|PubMed:15060175" FT MUTAGEN 446 FT /note="K->Q: Disrupts interaction with CTBP1. Decreases FT lysine acetylation. Disrupts nuclear hormone FT receptor-dependent transcription repression." FT /evidence="ECO:0000269|PubMed:11509661" FT MUTAGEN 446 FT /note="K->R: Does not disrupt nuclear hormone FT receptor-dependent transcription repression." FT /evidence="ECO:0000269|PubMed:11509661" FT MUTAGEN 567..568 FT /note="NL->AA: Disrupts transcriptional repression." FT /evidence="ECO:0000269|PubMed:14736873, FT ECO:0000269|PubMed:15060175" FT MUTAGEN 567..568 FT /note="NL->AS: Disrupts interaction with CTBP1 and CTBP2. FT Disrupts transcriptional repression; when associated with FT 442-AS-443." FT /evidence="ECO:0000269|PubMed:14736873, FT ECO:0000269|PubMed:15060175" FT MUTAGEN 599..603 FT /note="SMDLT->PIAAS: Does not further disrupt FT transcriptional repression; when associated with 442-AA-443 FT and 567-AA-568." FT MUTAGEN 948..949 FT /note="DL->AA: Abolishes CTBP binding but retains FT transcriptional repressor activity." FT /evidence="ECO:0000269|PubMed:14736873" FT CONFLICT 124 FT /note="P -> R (in Ref. 1; CAA59108)" FT /evidence="ECO:0000305" FT CONFLICT 721..726 FT /note="NKGKSE -> TKGRVK (in Ref. 1; CAA59108)" FT /evidence="ECO:0000305" FT CONFLICT 954 FT /note="S -> I (in Ref. 3; AAH40361)" FT /evidence="ECO:0000305" FT CONFLICT 1080 FT /note="T -> A (in Ref. 1; CAA59108)" FT /evidence="ECO:0000305" FT HELIX 379..385 FT /evidence="ECO:0007829|PDB:2GPO" FT HELIX 500..505 FT /evidence="ECO:0007829|PDB:5NTW" SQ SEQUENCE 1158 AA; 126942 MW; 81FC424968E9A5F6 CRC64; MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN GEVYGLLGSV LTIKKESE //