GENTAUR Molecular Products.

 NRIP1_HUMAN             Reviewed;        1158 AA.
 P48552; Q8IWE8;
 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2000, sequence version 2.
 28-MAR-2018, entry version 161.
 RecName: Full=Nuclear receptor-interacting protein 1;
 AltName: Full=Nuclear factor RIP140;
 AltName: Full=Receptor-interacting protein 140;
 Name=NRIP1;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1,
 SUBCELLULAR LOCATION, AND VARIANT GLY-448.
 TISSUE=Mammary gland;
 PubMed=7641693;
 Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S.,
 Kushner P.J., Parker M.G.;
 "Nuclear factor RIP140 modulates transcriptional activation by the
 estrogen receptor.";
 EMBO J. 14:3741-3751(1995).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=10830953; DOI=10.1038/35012518;
 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.;
 "The DNA sequence of human chromosome 21.";
 Nature 405:311-319(2000).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Skin;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 INTERACTION WITH NR2C2.
 PubMed=9556573; DOI=10.1074/jbc.273.18.10948;
 Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I.,
 Jetten A.M.;
 "Regulation of peroxisome proliferator-activated receptor alpha-
 induced transactivation by the nuclear orphan receptor TAK1/TR4.";
 J. Biol. Chem. 273:10948-10957(1998).
 [5]
 FUNCTION, AND INTERACTION WITH NR3C1.
 PubMed=10364267; DOI=10.1074/jbc.274.25.18121;
 Subramaniam N., Treuter E., Okret S.;
 "Receptor interacting protein RIP140 inhibits both positive and
 negative gene regulation by glucocorticoids.";
 J. Biol. Chem. 274:18121-18127(1999).
 [6]
 FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND
 LYS-446, AND ACETYLATION AT LYS-446.
 PubMed=11509661; DOI=10.1128/MCB.21.18.6181-6188.2001;
 Vo N., Fjeld C., Goodman R.H.;
 "Acetylation of nuclear hormone receptor-interacting protein RIP140
 regulates binding of the transcriptional corepressor CtBP.";
 Mol. Cell. Biol. 21:6181-6188(2001).
 [7]
 INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH
 NR3C1 AND YWHAH, AND SUBCELLULAR LOCATION.
 PubMed=11266503; DOI=10.1210/mend.15.4.0624;
 Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
 Gustafsson J.-A.;
 "Regulation of glucocorticoid receptor activity by 14-3-3-dependent
 intracellular relocalization of the corepressor RIP140.";
 Mol. Endocrinol. 15:501-511(2001).
 [8]
 FUNCTION, AND INTERACTION WITH NR3C2.
 PubMed=11518808; DOI=10.1210/mend.15.9.0689;
 Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.;
 "A new human MR splice variant is a ligand-independent transactivator
 modulating corticosteroid action.";
 Mol. Endocrinol. 15:1586-1598(2001).
 [9]
 INTERACTION WITH NR3C1, AND SUBCELLULAR LOCATION.
 PubMed=12773562; DOI=10.1128/MCB.23.12.4187-4198.2003;
 Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A.,
 Zilliacus J.;
 "Regulation of subnuclear localization is associated with a mechanism
 for nuclear receptor corepression by RIP140.";
 Mol. Cell. Biol. 23:4187-4198(2003).
 [10]
 FUNCTION, AND INTERACTION WITH ESR1; FOS AND JUN.
 PubMed=12554755; DOI=10.1210/me.2002-0324;
 Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.;
 "Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-
 induced activator protein-1 activity by reversing glucocorticoid
 receptor-interacting protein 1 effect.";
 Mol. Endocrinol. 17:287-299(2003).
 [11]
 INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443;
 567-ASN--LEU-568 AND 948-ASP--LEU-949, AND IDENTIFICATION OF
 REPRESSION DOMAINS.
 PubMed=14736873; DOI=10.1074/jbc.M313906200;
 Christian M., Tullet J.M.A., Parker M.G.;
 "Characterization of four autonomous repression domains in the
 corepressor receptor interacting protein 140.";
 J. Biol. Chem. 279:15645-15651(2004).
 [12]
 FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND
 HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, AND
 SUBCELLULAR LOCATION.
 PubMed=15060175; DOI=10.1093/nar/gkh524;
 Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
 Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
 "Multiple domains of the receptor-interacting protein 140 contribute
 to transcription inhibition.";
 Nucleic Acids Res. 32:1957-1966(2004).
 [13]
 INTERACTION WITH NR2C2.
 PubMed=16887930; DOI=10.1074/mcp.M600180-MCP200;
 Huq M.D., Gupta P., Tsai N.P., Wei L.N.;
 "Modulation of testicular receptor 4 activity by mitogen-activated
 protein kinase-mediated phosphorylation.";
 Mol. Cell. Proteomics 5:2072-2082(2006).
 [14]
 INTERACTION WITH ZNF366.
 PubMed=17085477; DOI=10.1093/nar/gkl875;
 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.;
 "ZNF366 is an estrogen receptor corepressor that acts through CtBP and
 histone deacetylases.";
 Nucleic Acids Res. 34:6126-6136(2006).
 [15]
 FUNCTION, INTERACTION WITH RORA, AND INDUCTION.
 PubMed=21628546; DOI=10.1177/0748730411401579;
 Poliandri A.H., Gamsby J.J., Christian M., Spinella M.J., Loros J.J.,
 Dunlap J.C., Parker M.G.;
 "Modulation of clock gene expression by the transcriptional
 coregulator receptor interacting protein 140 (RIP140).";
 J. Biol. Rhythms 26:187-199(2011).
 [16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-807, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [17]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-671 AND
 SER-807, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
 Wang L., Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human
 liver phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [18]
 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-756 AND LYS-1105, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=25218447; DOI=10.1038/nsmb.2890;
 Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
 Vertegaal A.C.;
 "Uncovering global SUMOylation signaling networks in a site-specific
 manner.";
 Nat. Struct. Mol. Biol. 21:927-936(2014).
 [19]
 SUMOYLATION [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-1154, AND IDENTIFICATION BY MASS
 SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=28112733; DOI=10.1038/nsmb.3366;
 Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
 Nielsen M.L.;
 "Site-specific mapping of the human SUMO proteome reveals co-
 modification with phosphorylation.";
 Nat. Struct. Mol. Biol. 24:325-336(2017).
 [20]
 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH
 ESRRG.
 PubMed=16990259; DOI=10.1074/jbc.M608410200;
 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.;
 "X-ray crystal structures of the estrogen-related receptor-gamma
 ligand binding domain in three functional states reveal the molecular
 basis of small molecule regulation.";
 J. Biol. Chem. 281:37773-37781(2006).
 [21]
 VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.
 PubMed=16131398; DOI=10.1186/1743-1050-2-11;
 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.;
 "Preliminary molecular genetic analysis of the receptor interacting
 protein 140 (RIP140) in women affected by endometriosis.";
 J. Exp. Clin. Assist. Reprod. 2:11-11(2005).
 -!- 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. {ECO:0000269|PubMed:10364267,
     ECO:0000269|PubMed:11509661, ECO:0000269|PubMed:11518808,
     ECO:0000269|PubMed:12554755, ECO:0000269|PubMed:15060175,
     ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693}.
 -!- SUBUNIT: 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.
     {ECO:0000250|UniProtKB:Q8CBD1, ECO:0000269|PubMed:10364267,
     ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11509661,
     ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12554755,
     ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:14736873,
     ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:16887930,
     ECO:0000269|PubMed:16990259, ECO:0000269|PubMed:17085477,
     ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693,
     ECO:0000269|PubMed:9556573}.
 -!- INTERACTION:
     O15145:ARPC3; NbExp=3; IntAct=EBI-746484, EBI-351829;
     Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-746484, EBI-739624;
     P26358:DNMT1; NbExp=3; IntAct=EBI-746484, EBI-719459;
     Q13642:FHL1; NbExp=6; IntAct=EBI-746484, EBI-912547;
     O15379:HDAC3; NbExp=2; IntAct=EBI-746484, EBI-607682;
     O95751:LDOC1; NbExp=3; IntAct=EBI-746484, EBI-740738;
     Q99873:PRMT1; NbExp=4; IntAct=EBI-746484, EBI-78738;
     P10276:RARA; NbExp=4; IntAct=EBI-746484, EBI-413374;
     P10276-2:RARA; NbExp=3; IntAct=EBI-746484, EBI-10197061;
     Q8N895:ZNF366; NbExp=2; IntAct=EBI-746484, EBI-2813661;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11266503,
     ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:15060175,
     ECO:0000269|PubMed:7641693}. Note=Localized to discrete foci and
     redistributes to larger nuclear domains upon binding to ligand-
     bound NR3C1.
 -!- INDUCTION: Expressed in a circadian manner in the liver (at
     protein level). {ECO:0000269|PubMed:21628546}.
 -!- 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 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.
     {ECO:0000250}.
 -!- PTM: Acetylation regulates its nuclear translocation and
     corepressive activity (By similarity). Acetylation abolishes
     interaction with CTBP1. Phosphorylation enhances interaction with
     YWHAH. {ECO:0000250, ECO:0000269|PubMed:11509661}.
 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
     and Haematology;
     URL="http://atlasgeneticsoncology.org/Genes/NRIP1ID44067ch21q11.html";
 -----------------------------------------------------------------------
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 EMBL; X84373; CAA59108.1; -; mRNA.
 EMBL; AF248484; AAF62185.1; -; Genomic_DNA.
 EMBL; AF127577; AAF35255.1; -; Genomic_DNA.
 EMBL; AL163207; CAB90396.1; -; Genomic_DNA.
 EMBL; BC040361; AAH40361.1; -; mRNA.
 CCDS; CCDS13568.1; -.
 PIR; S57348; S57348.
 RefSeq; NP_003480.2; NM_003489.3.
 RefSeq; XP_005261120.1; XM_005261063.3.
 RefSeq; XP_005261122.1; XM_005261065.3.
 RefSeq; XP_011528049.1; XM_011529747.1.
 RefSeq; XP_011528050.1; XM_011529748.2.
 RefSeq; XP_011528051.1; XM_011529749.2.
 RefSeq; XP_011528053.1; XM_011529751.2.
 RefSeq; XP_011528054.1; XM_011529752.1.
 RefSeq; XP_016883962.1; XM_017028473.1.
 RefSeq; XP_016883963.1; XM_017028474.1.
 RefSeq; XP_016883964.1; XM_017028475.1.
 RefSeq; XP_016883965.1; XM_017028476.1.
 UniGene; Hs.155017; -.
 PDB; 2GPO; X-ray; 1.95 A; C=366-390.
 PDB; 2GPP; X-ray; 2.60 A; C/D=366-390.
 PDB; 4S14; X-ray; 3.54 A; C=499-510.
 PDB; 4S15; X-ray; 1.90 A; C/D=499-510.
 PDB; 5NTI; X-ray; 2.40 A; P/Q/R/S=493-512.
 PDB; 5NTN; X-ray; 1.90 A; P/Q/R/S=493-512.
 PDB; 5NTW; X-ray; 1.64 A; P/Q/R/S=493-512.
 PDB; 5NU1; X-ray; 1.85 A; P/Q=493-512.
 PDBsum; 2GPO; -.
 PDBsum; 2GPP; -.
 PDBsum; 4S14; -.
 PDBsum; 4S15; -.
 PDBsum; 5NTI; -.
 PDBsum; 5NTN; -.
 PDBsum; 5NTW; -.
 PDBsum; 5NU1; -.
 ProteinModelPortal; P48552; -.
 SMR; P48552; -.
 BioGrid; 113843; 58.
 DIP; DIP-5964N; -.
 IntAct; P48552; 27.
 MINT; P48552; -.
 STRING; 9606.ENSP00000327213; -.
 DrugBank; DB06884; 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE.
 iPTMnet; P48552; -.
 PhosphoSitePlus; P48552; -.
 BioMuta; NRIP1; -.
 DMDM; 9988061; -.
 EPD; P48552; -.
 MaxQB; P48552; -.
 PaxDb; P48552; -.
 PeptideAtlas; P48552; -.
 PRIDE; P48552; -.
 DNASU; 8204; -.
 Ensembl; ENST00000318948; ENSP00000327213; ENSG00000180530.
 Ensembl; ENST00000400199; ENSP00000383060; ENSG00000180530.
 Ensembl; ENST00000400202; ENSP00000383063; ENSG00000180530.
 GeneID; 8204; -.
 KEGG; hsa:8204; -.
 UCSC; uc002yjx.2; human.
 CTD; 8204; -.
 DisGeNET; 8204; -.
 EuPathDB; HostDB:ENSG00000180530.9; -.
 GeneCards; NRIP1; -.
 H-InvDB; HIX0027827; -.
 HGNC; HGNC:8001; NRIP1.
 HPA; HPA046571; -.
 HPA; HPA060036; -.
 MIM; 602490; gene.
 neXtProt; NX_P48552; -.
 OpenTargets; ENSG00000180530; -.
 PharmGKB; PA31780; -.
 eggNOG; ENOG410IFW7; Eukaryota.
 eggNOG; ENOG410XPVS; LUCA.
 GeneTree; ENSGT00390000007999; -.
 HOGENOM; HOG000236277; -.
 HOVERGEN; HBG052667; -.
 InParanoid; P48552; -.
 KO; K17965; -.
 OMA; YMLQKGG; -.
 OrthoDB; EOG091G07UX; -.
 PhylomeDB; P48552; -.
 TreeFam; TF332210; -.
 Reactome; R-HSA-1368082; RORA activates gene expression.
 Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
 Reactome; R-HSA-400253; Circadian Clock.
 SignaLink; P48552; -.
 SIGNOR; P48552; -.
 ChiTaRS; NRIP1; human.
 EvolutionaryTrace; P48552; -.
 GeneWiki; NRIP1; -.
 GenomeRNAi; 8204; -.
 PRO; PR:P48552; -.
 Proteomes; UP000005640; Chromosome 21.
 Bgee; ENSG00000180530; -.
 CleanEx; HS_NRIP1; -.
 ExpressionAtlas; P48552; baseline and differential.
 Genevisible; P48552; HS.
 GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
 GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
 GO; GO:0005730; C:nucleolus; IDA:HPA.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
 GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
 GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
 GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB.
 GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
 GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
 GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
 GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
 GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
 GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
 GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
 GO; GO:0019915; P:lipid storage; IEA:Ensembl.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
 GO; GO:0001543; P:ovarian follicle rupture; IEA:Ensembl.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
 InterPro; IPR026649; NRIP1.
 InterPro; IPR031405; NRIP1_RD1.
 InterPro; IPR031406; NRIP1_RD2.
 InterPro; IPR031407; NRIP1_RD3.
 InterPro; IPR031408; NRIP1_RD4.
 PANTHER; PTHR15088; PTHR15088; 1.
 Pfam; PF15687; NRIP1_repr_1; 1.
 Pfam; PF15688; NRIP1_repr_2; 1.
 Pfam; PF15689; NRIP1_repr_3; 1.
 Pfam; PF15690; NRIP1_repr_4; 1.
 1: Evidence at protein level;
 3D-structure; Acetylation; Activator; Biological rhythms;
 Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
 Polymorphism; Reference proteome; Repeat; Transcription;
 Transcription regulation; Ubl conjugation.
 CHAIN         1   1158       Nuclear receptor-interacting protein 1.
                              /FTId=PRO_0000057951.
 REGION        1    415       Interaction with ZNF366.
                              {ECO:0000269|PubMed:17085477}.
 REGION       78    333       Repression domain 1.
 REGION      410    700       Repression domain 2.
 REGION      431    472       Required for targeting to small nuclear
                              foci.
 REGION      735    885       Repression domain 3.
 REGION      753   1158       Interaction with ZNF366.
                              {ECO:0000269|PubMed:17085477}.
 REGION     1118   1158       Repression domain 4.
 MOTIF        21     25       LXXLL motif 1.
 MOTIF       133    137       LXXLL motif 2.
 MOTIF       185    189       LXXLL motif 3.
 MOTIF       266    270       LXXLL motif 4.
 MOTIF       380    384       LXXLL motif 5.
 MOTIF       440    446       CTBP-binding; principal site.
 MOTIF       500    504       LXXLL motif 6.
 MOTIF       565    569       CTBP-binding.
 MOTIF       599    603       CTBP-binding. {ECO:0000255}.
 MOTIF       713    717       LXXLL motif 7.
 MOTIF       819    823       LXXLL motif 8.
 MOTIF       936    940       LXXLL motif 9.
 MOTIF       946    950       CTBP-binding.
 MOTIF      1061   1074       Ligand-dependent nuclear receptor
                              binding. {ECO:0000250}.
 MOD_RES     104    104       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     111    111       N6-acetyllysine; alternate.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     158    158       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     207    207       Phosphothreonine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     218    218       Phosphoserine.
                              {ECO:0000244|PubMed:24275569}.
 MOD_RES     286    286       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     310    310       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     356    356       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     378    378       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     446    446       N6-acetyllysine.
                              {ECO:0000269|PubMed:11509661}.
 MOD_RES     481    481       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     487    487       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     518    518       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     528    528       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     542    542       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     564    564       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     606    606       N6-acetyllysine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES     671    671       Phosphoserine.
                              {ECO:0000244|PubMed:24275569}.
 MOD_RES     807    807       Phosphoserine.
                              {ECO:0000244|PubMed:23186163,
                              ECO:0000244|PubMed:24275569}.
 MOD_RES     931    931       N6-acetyllysine; alternate.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 MOD_RES    1001   1001       Phosphoserine.
                              {ECO:0000250|UniProtKB:Q8CBD1}.
 CROSSLNK    111    111       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2);
                              alternate. {ECO:0000244|PubMed:28112733}.
 CROSSLNK    170    170       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    195    195       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    198    198       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    372    372       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    508    508       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    756    756       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:25218447,
                              ECO:0000244|PubMed:28112733}.
 CROSSLNK    802    802       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    850    850       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    901    901       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK    931    931       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2);
                              alternate. {ECO:0000244|PubMed:28112733}.
 CROSSLNK   1105   1105       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:25218447,
                              ECO:0000244|PubMed:28112733}.
 CROSSLNK   1115   1115       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 CROSSLNK   1154   1154       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 VARIANT      37     37       V -> I (in dbSNP:rs9941840).
                              /FTId=VAR_051241.
 VARIANT     221    221       H -> R (in dbSNP:rs139263261).
                              {ECO:0000269|PubMed:16131398}.
                              /FTId=VAR_023706.
 VARIANT     315    315       Y -> F (in dbSNP:rs2228507).
                              /FTId=VAR_034142.
 VARIANT     441    441       I -> V (in dbSNP:rs150468995).
                              {ECO:0000269|PubMed:16131398}.
                              /FTId=VAR_023707.
 VARIANT     448    448       R -> G (common polymorphism;
                              dbSNP:rs2229742).
                              {ECO:0000269|PubMed:16131398,
                              ECO:0000269|PubMed:7641693}.
                              /FTId=VAR_023708.
 VARIANT     567    567       N -> S (in dbSNP:rs9975169).
                              /FTId=VAR_051242.
 VARIANT     803    803       S -> L (in dbSNP:rs61750208).
                              {ECO:0000269|PubMed:16131398}.
                              /FTId=VAR_023709.
 VARIANT    1079   1079       V -> F (in dbSNP:rs140803495).
                              {ECO:0000269|PubMed:16131398}.
                              /FTId=VAR_023710.
 MUTAGEN     440    443       PIDL->AAAA: Abolishes interaction with
                              CTBP1. {ECO:0000269|PubMed:11509661}.
 MUTAGEN     440    442       PID->AIA: Abolishes interaction with
                              CTBP1 and attenuates nuclear hormone
                              receptor-dependent transcription
                              repression.
 MUTAGEN     442    443       DL->AA: Reduces, but does not completely
                              abolish, interaction with CTBP. Reduces
                              transcriptional repression.
                              {ECO:0000269|PubMed:14736873,
                              ECO:0000269|PubMed:15060175}.
 MUTAGEN     442    443       DL->AS: Disrupts interaction with CTBP1,
                              and CTBP2 to a lesser extent. Disrupts
                              transcriptional repression; when
                              associated with 567-AS-568.
                              {ECO:0000269|PubMed:14736873,
                              ECO:0000269|PubMed:15060175}.
 MUTAGEN     446    446       K->Q: Disrupts interaction with CTBP1.
                              Decreases lysine acetylation. Disrupts
                              nuclear hormone receptor-dependent
                              transcription repression.
                              {ECO:0000269|PubMed:11509661}.
 MUTAGEN     446    446       K->R: Does not disrupt nuclear hormone
                              receptor-dependent transcription
                              repression.
                              {ECO:0000269|PubMed:11509661}.
 MUTAGEN     567    568       NL->AA: Disrupts transcriptional
                              repression. {ECO:0000269|PubMed:14736873,
                              ECO:0000269|PubMed:15060175}.
 MUTAGEN     567    568       NL->AS: Disrupts interaction with CTBP1
                              and CTBP2. Disrupts transcriptional
                              repression; when associated with 442-AS-
                              443. {ECO:0000269|PubMed:14736873,
                              ECO:0000269|PubMed:15060175}.
 MUTAGEN     599    603       SMDLT->PIAAS: Does not further disrupt
                              transcriptional repression; when
                              associated with 442-AA-443 and 567-AA-
                              568.
 MUTAGEN     948    949       DL->AA: Abolishes CTBP binding but
                              retains transcriptional repressor
                              activity. {ECO:0000269|PubMed:14736873}.
 CONFLICT    124    124       P -> R (in Ref. 1; CAA59108).
                              {ECO:0000305}.
 CONFLICT    721    726       NKGKSE -> TKGRVK (in Ref. 1; CAA59108).
                              {ECO:0000305}.
 CONFLICT    954    954       S -> I (in Ref. 3; AAH40361).
                              {ECO:0000305}.
 CONFLICT   1080   1080       T -> A (in Ref. 1; CAA59108).
                              {ECO:0000305}.
 HELIX       379    385       {ECO:0000244|PDB:2GPO}.
 HELIX       500    505       {ECO:0000244|PDB:5NTW}.
 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

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