NRIP1_MOUSE
ID NRIP1_MOUSE Reviewed; 1161 AA.
AC Q8CBD1; Q3U166; Q8C3Y8; Q9Z2K2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nuclear receptor-interacting protein 1;
DE AltName: Full=Nuclear factor RIP140;
DE AltName: Full=Receptor-interacting protein 140;
GN Name=Nrip1 {ECO:0000312|MGI:MGI:1315213};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC69611.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH NR2C1 AND RARA.
RC STRAIN=ICR {ECO:0000312|EMBL:AAC69611.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:9774688};
RX PubMed=9774688; DOI=10.1128/mcb.18.11.6745;
RA Lee C.-H., Chinpaisal C., Wei L.-N.;
RT "Cloning and characterization of mouse RIP140, a corepressor for nuclear
RT orphan receptor TR2.";
RL Mol. Cell. Biol. 18:6745-6755(1998).
RN [2] {ECO:0000312|EMBL:BAC29368.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29368.1}, and NOD;
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC29368.1},
RC Heart {ECO:0000312|EMBL:BAC39197.1}, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH60232.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH60232.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH60232.1};
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] {ECO:0000305}
RP PROTEIN SEQUENCE OF 101-112; 155-170; 283-298; 305-320; 476-492; 517-537;
RP 606-630 AND 930-938, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND ACETYLATION AT LYS-111; LYS-158; LYS-287; LYS-311; LYS-482;
RP LYS-529; LYS-607 AND LYS-932.
RX PubMed=15879431; DOI=10.1074/mcp.m500015-mcp200;
RA Huq M.D.M., Wei L.-N.;
RT "Post-translational modification of nuclear co-repressor receptor-
RT interacting protein 140 by acetylation.";
RL Mol. Cell. Proteomics 4:975-983(2005).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 101-112; 199-212; 343-360; 375-387; 476-492; 517-548;
RP 670-678 AND 1001-1009, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT SER-104; THR-207; SER-358; SER-380; SER-488; SER-519;
RP SER-531; SER-543; SER-672 AND SER-1003.
RX PubMed=15846843; DOI=10.1002/pmic.200401090;
RA Huq M.D.M., Khan S.A., Park S.W., Wei L.-N.;
RT "Mapping of phosphorylation sites of nuclear corepressor receptor
RT interacting protein 140 by liquid chromatography-tandem mass
RT spectroscopy.";
RL Proteomics 5:2157-2166(2005).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RARA AND RXRB.
RX PubMed=10531331; DOI=10.1074/jbc.274.44.31320;
RA Lee C.-H., Wei L.-N.;
RT "Characterization of receptor-interacting protein 140 in retinoid receptor
RT activities.";
RL J. Biol. Chem. 274:31320-31326(1999).
RN [7] {ECO:0000305}
RP INTERACTION WITH HDAC1 AND HDAC3.
RX PubMed=11006275; DOI=10.1074/jbc.m004821200;
RA Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.;
RT "Receptor-interacting protein 140 directly recruits histone deacetylases
RT for gene silencing.";
RL J. Biol. Chem. 275:40782-40787(2000).
RN [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11100122; DOI=10.1038/82183;
RA White R., Leonardsson G., Rosewell I., Jacobs M.A., Milligan S.,
RA Parker M.G.;
RT "The nuclear receptor co-repressor Nrip1 (RIP140) is essential for female
RT fertility.";
RL Nat. Med. 6:1368-1374(2000).
RN [9] {ECO:0000305}
RP INTERACTION WITH RARA AND RXRB, AND IDENTIFICATION IN A COMPLEX WITH HDAC3.
RX PubMed=11278635; DOI=10.1074/jbc.m010185200;
RA Wei L.-N., Farooqui M., Hu X.;
RT "Ligand-dependent formation of retinoid receptors, receptor-interacting
RT protein 140 (RIP140), and histone deacetylase complex is mediated by a
RT novel receptor-interacting motif of RIP140.";
RL J. Biol. Chem. 276:16107-16112(2001).
RN [10] {ECO:0000305}
RP INTERACTION WITH RARA AND RXRB, AND MUTAGENESIS OF ASN-1067; PRO-1068 AND
RP MET-1073.
RX PubMed=12549917; DOI=10.1021/bi020497k;
RA Farooqui M., Franco P.J., Thompson J., Kagechika H., Chandraratna R.A.S.,
RA Banaszak L., Wei L.-N.;
RT "Effects of retinoid ligands on RIP140: molecular interaction with retinoid
RT receptors and biological activity.";
RL Biochemistry 42:971-979(2003).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=15130509; DOI=10.1016/j.mce.2003.12.010;
RA Wei L.-N., Hu X.;
RT "Receptor interacting protein 140 as a thyroid hormone-dependent, negative
RT co-regulator for the induction of cellular retinoic acid binding protein I
RT gene.";
RL Mol. Cell. Endocrinol. 218:39-48(2004).
RN [12] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15155905; DOI=10.1073/pnas.0401013101;
RA Leonardsson G., Steel J.H., Christian M., Pocock V., Milligan S., Bell J.,
RA So P.-W., Medina-Gomez G., Vidal-Puig A., White R., Parker M.G.;
RT "Nuclear receptor corepressor RIP140 regulates fat accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8437-8442(2004).
RN [13] {ECO:0000305}
RP FUNCTION.
RX PubMed=15919748; DOI=10.1210/en.2005-0348;
RA Tullet J.M.A., Pocock V., Steel J.H., White R., Milligan S., Parker M.G.;
RT "Multiple signaling defects in the absence of RIP140 impair both cumulus
RT expansion and follicle rupture.";
RL Endocrinology 146:4127-4137(2005).
RN [14]
RP INTERACTION WITH NR2C1.
RX PubMed=17187077; DOI=10.1038/nsmb1185;
RA Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT expression in stem cells.";
RL Nat. Struct. Mol. Biol. 14:68-75(2007).
RN [15]
RP INTERACTION WITH NR2C1.
RX PubMed=18682553; DOI=10.1073/pnas.0710561105;
RA Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P.,
RA Wei L.N.;
RT "Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and
RT SUMOylation of nuclear receptor TR2 to suppress Oct4 expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH RORA.
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 [17]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Modulates transcriptional repression by nuclear hormone
CC receptors such as NR2C1, thyroid hormone receptor and retinoic acid
CC receptor/RARA. Essential for cumulus expansion and follicle rupture
CC during ovulation. Also controls the balance between fat accumulation
CC and energy expenditure. Positive regulator of the circadian clock gene
CC expression: stimulates transcription of ARNTL/BMAL1, CLOCK and CRY1 by
CC acting as a coactivator for RORA and RORC. Involved in the regulation
CC of ovarian function (PubMed:11100122). Plays a role in renal
CC development (PubMed:28381549). {ECO:0000269|PubMed:10531331,
CC ECO:0000269|PubMed:11100122, ECO:0000269|PubMed:15130509,
CC ECO:0000269|PubMed:15155905, ECO:0000269|PubMed:15919748,
CC ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:28381549,
CC ECO:0000269|PubMed:9774688}.
CC -!- SUBUNIT: Interacts with CTBP1, CTBP2, ERS1, HDAC1, HDAC2, HDAC5, HDAC6,
CC NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both
CC NR3C1 and YWHAH (By similarity). Interacts with NR2C1 (sumoylated form
CC and via the ligand-binding domain); the interaction results in
CC promoting the repressor activity of NR2C1. Interacts with RARA and RXRB
CC homodimers and RARA/RXRB heterodimers in the presence of ligand.
CC Interacts with HDAC1 and HDAC3 via its N-terminal domain. Interacts
CC with ZNF366 (By similarity). Interacts with RORA.
CC {ECO:0000250|UniProtKB:P48552, ECO:0000269|PubMed:21628546}.
CC -!- INTERACTION:
CC Q8CBD1; Q505F1: Nr2c1; NbExp=3; IntAct=EBI-1771626, EBI-15617004;
CC Q8CBD1; O15379: HDAC3; Xeno; NbExp=2; IntAct=EBI-1771626, EBI-607682;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15879431}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryonic placenta. In the adult,
CC expression is strong in the testis and brain. Also expressed at a high
CC level in the white adipose tissue. Expressed constantly but at a weaker
CC level in the adult heart, lung, stomach and kidney. Expressed
CC moderately in the skeletal muscle. Expressed at a low level in the
CC adult spleen, liver and brown adipose tissue. Expressed in the ovary at
CC a high level in granulosa cells and at a lower level in the thecal and
CC interstitial compartments. {ECO:0000269|PubMed:11100122,
CC ECO:0000269|PubMed:15155905, ECO:0000269|PubMed:9774688}.
CC -!- DOMAIN: Contains at least 4 autonomous repression domains (RD1-4).
CC {ECO:0000250}.
CC -!- DOMAIN: Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have
CC different affinities for nuclear receptors.
CC -!- DOMAIN: The Ligand-dependent nuclear receptor binding region is
CC required for ligand-dependent interaction with RAAR and RXRB homo- and
CC heterodimers, for the corepressor activity, and for the formation of an
CC HDAC3 complex with RARA/RXRB.
CC -!- PTM: Acetylation abolishes interaction with CTBP1. Phosphorylation
CC enhances interaction with YWHAH (By similarity). Acetylation regulates
CC its nuclear translocation and corepressive activity.
CC {ECO:0000250|UniProtKB:P48552, ECO:0000269|PubMed:15846843,
CC ECO:0000269|PubMed:15879431}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and morphologically normal, but
CC smaller than wild-type and heterozygous littermates. Homozygous NRIP1-
CC null mature female are defective in ovulation and completely infertile
CC (PubMed:11100122). Embryos with heterozygous NRIP1 loss show anomalies
CC of the urinary tract including dysplastic kidneys with cystic
CC dilations, severe hydoureter with hydronephrosis and ureterocele
CC (PubMed:28381549). {ECO:0000269|PubMed:11100122,
CC ECO:0000269|PubMed:28381549}.
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DR EMBL; AF053062; AAC69611.1; -; mRNA.
DR EMBL; AK036273; BAC29368.1; -; mRNA.
DR EMBL; AK084498; BAC39197.1; -; mRNA.
DR EMBL; AK156233; BAE33634.1; -; mRNA.
DR EMBL; BC060232; AAH60232.1; -; mRNA.
DR CCDS; CCDS28274.1; -.
DR RefSeq; NP_775616.1; NM_173440.2.
DR RefSeq; XP_006523113.1; XM_006523050.2.
DR RefSeq; XP_006523114.1; XM_006523051.3.
DR RefSeq; XP_006523117.1; XM_006523054.2.
DR RefSeq; XP_017172509.1; XM_017317020.1.
DR AlphaFoldDB; Q8CBD1; -.
DR BioGRID; 234576; 16.
DR DIP; DIP-29280N; -.
DR IntAct; Q8CBD1; 6.
DR MINT; Q8CBD1; -.
DR STRING; 10090.ENSMUSP00000051726; -.
DR iPTMnet; Q8CBD1; -.
DR PhosphoSitePlus; Q8CBD1; -.
DR MaxQB; Q8CBD1; -.
DR PaxDb; Q8CBD1; -.
DR PeptideAtlas; Q8CBD1; -.
DR PRIDE; Q8CBD1; -.
DR ProteomicsDB; 253016; -.
DR Antibodypedia; 5789; 238 antibodies from 34 providers.
DR DNASU; 268903; -.
DR Ensembl; ENSMUST00000054178; ENSMUSP00000051726; ENSMUSG00000048490.
DR Ensembl; ENSMUST00000121927; ENSMUSP00000112959; ENSMUSG00000048490.
DR GeneID; 268903; -.
DR KEGG; mmu:268903; -.
DR UCSC; uc007zrx.1; mouse.
DR CTD; 8204; -.
DR MGI; MGI:1315213; Nrip1.
DR VEuPathDB; HostDB:ENSMUSG00000048490; -.
DR eggNOG; ENOG502QS1C; Eukaryota.
DR GeneTree; ENSGT00390000007999; -.
DR HOGENOM; CLU_008553_0_0_1; -.
DR InParanoid; Q8CBD1; -.
DR OMA; RSGAWND; -.
DR OrthoDB; 345693at2759; -.
DR PhylomeDB; Q8CBD1; -.
DR TreeFam; TF332210; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR BioGRID-ORCS; 268903; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Nrip1; mouse.
DR PRO; PR:Q8CBD1; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CBD1; protein.
DR Bgee; ENSMUSG00000048490; Expressed in metanephric cortical collecting duct and 280 other tissues.
DR ExpressionAtlas; Q8CBD1; baseline and differential.
DR Genevisible; Q8CBD1; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IPI:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
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; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001543; P:ovarian follicle rupture; IMP:UniProtKB.
DR GO; GO:0030728; P:ovulation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
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; PTHR15088; 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.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Biological rhythms; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1161
FT /note="Nuclear receptor-interacting protein 1"
FT /id="PRO_0000057952"
FT REGION 1..416
FT /note="Interaction with ZNF366"
FT /evidence="ECO:0000250"
FT REGION 34..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..335
FT /note="Repression domain 1"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT REGION 393..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..701
FT /note="Repression domain 2"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT REGION 432..473
FT /note="Required for targeting to small nuclear foci"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT REGION 517..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..886
FT /note="Repression domain 3"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT REGION 754..1161
FT /note="Interaction with ZNF366"
FT /evidence="ECO:0000250"
FT REGION 829..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1076
FT /note="Ligand-dependent nuclear receptor binding"
FT REGION 1121..1161
FT /note="Repression domain 4"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOTIF 21..25
FT /note="LXXLL motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 133..137
FT /note="LXXLL motif 2"
FT /evidence="ECO:0000255"
FT MOTIF 185..189
FT /note="LXXLL motif 3"
FT /evidence="ECO:0000255"
FT MOTIF 267..271
FT /note="LXXLL motif 4"
FT /evidence="ECO:0000255"
FT MOTIF 382..386
FT /note="LXXLL motif 5"
FT /evidence="ECO:0000255"
FT MOTIF 441..447
FT /note="CTBP-binding; principal site"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOTIF 501..505
FT /note="LXXLL motif 6"
FT /evidence="ECO:0000255"
FT MOTIF 566..570
FT /note="CTBP-binding"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOTIF 714..718
FT /note="LXXLL motif 7"
FT /evidence="ECO:0000255"
FT MOTIF 820..824
FT /note="LXXLL motif 8"
FT /evidence="ECO:0000255"
FT MOTIF 937..941
FT /note="LXXLL motif 9"
FT /evidence="ECO:0000255"
FT MOTIF 947..951
FT /note="CTBP-binding"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT COMPBIAS 48..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 158
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 311
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 447
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOD_RES 482
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 529
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MOD_RES 932
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15879431"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15846843"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 374
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 757
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 803
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 851
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 902
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 932
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 1108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 1118
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT CROSSLNK 1157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P48552"
FT MUTAGEN 1067
FT /note="N->G: Reduces binding to RAR, RXR and RAR/RXR."
FT /evidence="ECO:0000269|PubMed:12549917"
FT MUTAGEN 1068
FT /note="P->A: Abolishes binding to RAR, RXR and RAR/RXR."
FT /evidence="ECO:0000269|PubMed:12549917"
FT MUTAGEN 1073
FT /note="M->I: Reduces binding to RAR, RXR and RAR/RXR."
FT /evidence="ECO:0000269|PubMed:12549917"
FT MUTAGEN 1073
FT /note="M->K: Abolishes binding to RAR, RXR and RAR/RXR."
FT /evidence="ECO:0000269|PubMed:12549917"
FT MUTAGEN 1073
FT /note="M->L: Reduces binding to RAR, RXR and RAR/RXR."
FT /evidence="ECO:0000269|PubMed:12549917"
FT CONFLICT 106
FT /note="V -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> NN (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 119..120
FT /note="MV -> IL (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="K -> R (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="Q -> E (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> D (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="D -> V (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="A -> V (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="S -> N (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="S -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="L -> Q (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="G -> F (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 855
FT /note="M -> I (in Ref. 2; BAE33634)"
FT /evidence="ECO:0000305"
FT CONFLICT 886
FT /note="S -> R (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
FT CONFLICT 1049
FT /note="A -> T (in Ref. 1; AAC69611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1161 AA; 126337 MW; 56ABD0C2A5AAC0A1 CRC64;
MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAINKK SAGHKEEDQN FNLSGSAFPS
CQSNGPTVST QTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIVNLNV KKEALLAGMV
DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHESLK VEKDLRCYGV
ASSHLKTLLK KSKTKDQKSG PTLPDVTPNL IRDSFVESSH PAVGQSGTKV MSEPLSCAAR
LQAVASMVEK RASPAASPKP SVACSQLALL LSSEAHLQQY SREHALKTQN AHQVASERLA
AMARLQENGQ KDVGSSQLSK GVSGHLNGQA RALPASKLVA NKNNAATFQS PMGVVPSSPK
NTSYKNSLER NNLKQAANNS LLLHLLKSQT IPTPMNGHSQ NERASSFESS TPTTIDEYSD
NNPSFTDDSS GDESSYSNCV PIDLSCKHRI EKPEAERPVS LENLTQSLLN TWDPKIPGVD
IKEDQDTSTN SKLNSHQKVT LLQLLLGHKS EETVERNASP QDIHSDGTKF SPQNYTRTSV
IESPSTNRTT PVSTPPLYTA SQAESPINLS QHSLVIKWNS PPYACSTPAS KLTNTAPSHL
MDLTKGKESQ AEKPAPSEGA QNSATFSASK LLQNLAQCGL QSSGPGEEQR PCKQLLSGNP
DKPLGLIDRL NSPLLSNKTN AAEESKAFSS QPAGPEPGLP GCEIENLLER RTVLQLLLGN
SSKGKNEKKE KTPARDEAPQ EHSERAANEQ ILMVKIKSEP CDDFQTHNTN LPLNHDAKSA
PFLGVTPAIH RSTAALPVSE DFKSEPASPQ DFSFSKNGLL SRLLRQNQES YPADEQDKSH
RNSELPTLES KNICMVPKKR KLYTEPLENP FKKMKNTAVD TANHHSGPEV LYGSLLHQEE
LKFSRNELDY KYPAGHSSAS DGDHRSWARE SKSFNVLKQL LLSENCVRDL SPHRSDSVPD
TKKKGHKNNA PGSKPEFGIS SLNGLMYSSP QPGSCVTDHR TFSYPGMVKT PLSPPFPEHL
GCVGSRPEPG LLNGCSVPGE KGPIKWVIAD MDKNEYEKDS PRLTKTNPIL YYMLQKGGGN
SVTTQETQDK DIWREPASAE SLSQVTVKEE LLPAAETKAS FFNLRSPYNS HMGNNASRPH
STNGEVYGLL GNALTIKKES E
