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Q8CBD1

- NRIP1_MOUSE

UniProt

Q8CBD1 - NRIP1_MOUSE

Protein

Nuclear receptor-interacting protein 1

Gene

Nrip1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Modulates transcriptional repression by nuclear hormone receptors such as NR2C1, thyroid hormone receptor and retinoic acid receptor/RARA. Essential for cumulus expansion and follicle rupture during ovulation. Also controls the balance between fat accumulation and energy expenditure.6 Publications

    GO - Molecular functioni

    1. histone deacetylase binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. receptor binding Source: UniProtKB
    4. retinoic acid receptor binding Source: UniProtKB
    5. retinoid X receptor binding Source: UniProtKB
    6. transcription coactivator activity Source: Ensembl
    7. transcription corepressor activity Source: MGI

    GO - Biological processi

    1. lipid storage Source: UniProtKB
    2. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    3. ovarian follicle rupture Source: UniProtKB
    4. ovulation Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of transcription from RNA polymerase II promoter Source: MGI
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Receptor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor-interacting protein 1
    Alternative name(s):
    Nuclear factor RIP140
    Receptor-interacting protein 140
    Gene namesi
    Name:Nrip1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1315213. Nrip1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. histone deacetylase complex Source: UniProtKB
    2. nuclear speck Source: MGI
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1067 – 10671N → G: Reduces binding to RAR, RXR and RAR/RXR. 1 Publication
    Mutagenesisi1068 – 10681P → A: Abolishes binding to RAR, RXR and RAR/RXR. 1 Publication
    Mutagenesisi1073 – 10731M → I: Reduces binding to RAR, RXR and RAR/RXR. 1 Publication
    Mutagenesisi1073 – 10731M → K: Abolishes binding to RAR, RXR and RAR/RXR. 1 Publication
    Mutagenesisi1073 – 10731M → L: Reduces binding to RAR, RXR and RAR/RXR. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11611161Nuclear receptor-interacting protein 1PRO_0000057952Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041Phosphoserine1 Publication
    Modified residuei111 – 1111N6-acetyllysine1 Publication
    Modified residuei158 – 1581N6-acetyllysine1 Publication
    Modified residuei207 – 2071Phosphothreonine1 Publication
    Modified residuei287 – 2871N6-acetyllysine1 Publication
    Modified residuei311 – 3111N6-acetyllysine1 Publication
    Modified residuei358 – 3581Phosphoserine1 Publication
    Modified residuei380 – 3801Phosphoserine1 Publication
    Modified residuei447 – 4471N6-acetyllysineBy similarity
    Modified residuei482 – 4821N6-acetyllysine1 Publication
    Modified residuei488 – 4881Phosphoserine1 Publication
    Modified residuei519 – 5191Phosphoserine1 Publication
    Modified residuei529 – 5291N6-acetyllysine1 Publication
    Modified residuei531 – 5311Phosphoserine1 Publication
    Modified residuei543 – 5431Phosphoserine1 Publication
    Modified residuei607 – 6071N6-acetyllysine1 Publication
    Modified residuei672 – 6721Phosphoserine1 Publication
    Modified residuei932 – 9321N6-acetyllysine1 Publication
    Modified residuei1003 – 10031Phosphoserine1 Publication

    Post-translational modificationi

    Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH By similarity. Acetylation regulates its nuclear translocation and corepressive activity.By similarity2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ8CBD1.

    PTM databases

    PhosphoSiteiQ8CBD1.

    Expressioni

    Tissue specificityi

    Expressed in the embryonic placenta. In the adult, expression is strong in the testis and brain. Also expressed at a high level in the white adipose tissue. Expressed constantly but at a weaker level in the adult heart, lung, stomach and kidney. Expressed moderately in the skeletal muscle. Expressed at a low level in the adult spleen, liver and brown adipose tissue. Expressed in the ovary at a high level in granulosa cells and at a lower level in the thecal and interstitial compartments.3 Publications

    Gene expression databases

    BgeeiQ8CBD1.
    CleanExiMM_NRIP1.
    GenevestigatoriQ8CBD1.

    Interactioni

    Subunit structurei

    Interacts with CTBP1, CTBP2, ERS1, HDAC1, HDAC2, HDAC5, HDAC6, NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with both NR3C1 and YWHAH By similarity. Interacts with NR2C1 (sumoylated form and via the ligand-binding domain); the interaction results in promoting the repressor activity of NR2C1. 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 ZNF366 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HDAC3O153792EBI-1771626,EBI-607682From a different organism.

    Protein-protein interaction databases

    BioGridi234576. 11 interactions.
    DIPiDIP-29280N.
    IntActiQ8CBD1. 4 interactions.
    STRINGi10090.ENSMUSP00000112959.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CBD1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 416416Interaction with ZNF366By similarityAdd
    BLAST
    Regioni78 – 335258Repression domain 1By similarityAdd
    BLAST
    Regioni411 – 701291Repression domain 2By similarityAdd
    BLAST
    Regioni432 – 47342Required for targeting to small nuclear fociBy similarityAdd
    BLAST
    Regioni736 – 886151Repression domain 3By similarityAdd
    BLAST
    Regioni754 – 1161408Interaction with ZNF366By similarityAdd
    BLAST
    Regioni1063 – 107614Ligand-dependent nuclear receptor bindingAdd
    BLAST
    Regioni1121 – 116141Repression domain 4By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi21 – 255LXXLL motif 1Sequence Analysis
    Motifi133 – 1375LXXLL motif 2Sequence Analysis
    Motifi185 – 1895LXXLL motif 3Sequence Analysis
    Motifi267 – 2715LXXLL motif 4Sequence Analysis
    Motifi382 – 3865LXXLL motif 5Sequence Analysis
    Motifi441 – 4477CTBP-binding; principal siteBy similarity
    Motifi501 – 5055LXXLL motif 6Sequence Analysis
    Motifi566 – 5705CTBP-bindingBy similarity
    Motifi714 – 7185LXXLL motif 7Sequence Analysis
    Motifi820 – 8245LXXLL motif 8Sequence Analysis
    Motifi937 – 9415LXXLL motif 9Sequence Analysis
    Motifi947 – 9515CTBP-bindingBy similarity

    Domaini

    Contains at least 4 autonomous repression domains (RD1-4).By similarity
    The Ligand-dependent nuclear receptor binding region is required for ligand-dependent interaction with RAAR and RXRB homo- and heterodimers, for the corepressor activity, and for the formation of an HDAC3 complex with RARA/RXRB.

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG47583.
    GeneTreeiENSGT00390000007999.
    HOGENOMiHOG000236277.
    HOVERGENiHBG052667.
    InParanoidiQ8CBD1.
    KOiK17965.
    OMAiVEKDLRC.
    OrthoDBiEOG7H1JJQ.
    PhylomeDBiQ8CBD1.
    TreeFamiTF332210.

    Family and domain databases

    InterProiIPR026649. NRIP1.
    [Graphical view]
    PANTHERiPTHR15088. PTHR15088. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8CBD1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAINKK SAGHKEEDQN     50
    FNLSGSAFPS CQSNGPTVST QTYQGSGMLH LKKARLLQSS EDWNAAKRKR 100
    LSDSIVNLNV KKEALLAGMV DSVPKGKQDS TLLASLLQSF SSRLQTVALS 150
    QQIRQSLKEQ GYALSHESLK VEKDLRCYGV ASSHLKTLLK KSKTKDQKSG 200
    PTLPDVTPNL IRDSFVESSH PAVGQSGTKV MSEPLSCAAR LQAVASMVEK 250
    RASPAASPKP SVACSQLALL LSSEAHLQQY SREHALKTQN AHQVASERLA 300
    AMARLQENGQ KDVGSSQLSK GVSGHLNGQA RALPASKLVA NKNNAATFQS 350
    PMGVVPSSPK NTSYKNSLER NNLKQAANNS LLLHLLKSQT IPTPMNGHSQ 400
    NERASSFESS TPTTIDEYSD NNPSFTDDSS GDESSYSNCV PIDLSCKHRI 450
    EKPEAERPVS LENLTQSLLN TWDPKIPGVD IKEDQDTSTN SKLNSHQKVT 500
    LLQLLLGHKS EETVERNASP QDIHSDGTKF SPQNYTRTSV IESPSTNRTT 550
    PVSTPPLYTA SQAESPINLS QHSLVIKWNS PPYACSTPAS KLTNTAPSHL 600
    MDLTKGKESQ AEKPAPSEGA QNSATFSASK LLQNLAQCGL QSSGPGEEQR 650
    PCKQLLSGNP DKPLGLIDRL NSPLLSNKTN AAEESKAFSS QPAGPEPGLP 700
    GCEIENLLER RTVLQLLLGN SSKGKNEKKE KTPARDEAPQ EHSERAANEQ 750
    ILMVKIKSEP CDDFQTHNTN LPLNHDAKSA PFLGVTPAIH RSTAALPVSE 800
    DFKSEPASPQ DFSFSKNGLL SRLLRQNQES YPADEQDKSH RNSELPTLES 850
    KNICMVPKKR KLYTEPLENP FKKMKNTAVD TANHHSGPEV LYGSLLHQEE 900
    LKFSRNELDY KYPAGHSSAS DGDHRSWARE SKSFNVLKQL LLSENCVRDL 950
    SPHRSDSVPD TKKKGHKNNA PGSKPEFGIS SLNGLMYSSP QPGSCVTDHR 1000
    TFSYPGMVKT PLSPPFPEHL GCVGSRPEPG LLNGCSVPGE KGPIKWVIAD 1050
    MDKNEYEKDS PRLTKTNPIL YYMLQKGGGN SVTTQETQDK DIWREPASAE 1100
    SLSQVTVKEE LLPAAETKAS FFNLRSPYNS HMGNNASRPH STNGEVYGLL 1150
    GNALTIKKES E 1161
    Length:1,161
    Mass (Da):126,337
    Last modified:March 1, 2003 - v1
    Checksum:i56ABD0C2A5AAC0A1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061V → N AA sequence (PubMed:15879431)Curated
    Sequence conflicti107 – 1071N → NN AA sequence (PubMed:15846843)Curated
    Sequence conflicti119 – 1202MV → IL in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti190 – 1901K → R in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti197 – 1971Q → E in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti200 – 2001G → D in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti522 – 5221D → V in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti596 – 5961A → V in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti617 – 6171S → N in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti629 – 6291S → K AA sequence (PubMed:15879431)Curated
    Sequence conflicti674 – 6741L → Q in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti818 – 8181G → F in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti855 – 8551M → I in BAE33634. (PubMed:16141072)Curated
    Sequence conflicti886 – 8861S → R in AAC69611. (PubMed:9774688)Curated
    Sequence conflicti1049 – 10491A → T in AAC69611. (PubMed:9774688)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053062 mRNA. Translation: AAC69611.1.
    AK036273 mRNA. Translation: BAC29368.1.
    AK084498 mRNA. Translation: BAC39197.1.
    AK156233 mRNA. Translation: BAE33634.1.
    BC060232 mRNA. Translation: AAH60232.1.
    CCDSiCCDS28274.1.
    RefSeqiNP_775616.1. NM_173440.2.
    XP_006523113.1. XM_006523050.1.
    XP_006523114.1. XM_006523051.1.
    XP_006523115.1. XM_006523052.1.
    XP_006523116.1. XM_006523053.1.
    XP_006523117.1. XM_006523054.1.
    UniGeneiMm.455873.
    Mm.74711.

    Genome annotation databases

    EnsembliENSMUST00000054178; ENSMUSP00000051726; ENSMUSG00000048490.
    ENSMUST00000121927; ENSMUSP00000112959; ENSMUSG00000048490.
    GeneIDi268903.
    KEGGimmu:268903.
    UCSCiuc007zrx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF053062 mRNA. Translation: AAC69611.1 .
    AK036273 mRNA. Translation: BAC29368.1 .
    AK084498 mRNA. Translation: BAC39197.1 .
    AK156233 mRNA. Translation: BAE33634.1 .
    BC060232 mRNA. Translation: AAH60232.1 .
    CCDSi CCDS28274.1.
    RefSeqi NP_775616.1. NM_173440.2.
    XP_006523113.1. XM_006523050.1.
    XP_006523114.1. XM_006523051.1.
    XP_006523115.1. XM_006523052.1.
    XP_006523116.1. XM_006523053.1.
    XP_006523117.1. XM_006523054.1.
    UniGenei Mm.455873.
    Mm.74711.

    3D structure databases

    ProteinModelPortali Q8CBD1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 234576. 11 interactions.
    DIPi DIP-29280N.
    IntActi Q8CBD1. 4 interactions.
    STRINGi 10090.ENSMUSP00000112959.

    PTM databases

    PhosphoSitei Q8CBD1.

    Proteomic databases

    PRIDEi Q8CBD1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054178 ; ENSMUSP00000051726 ; ENSMUSG00000048490 .
    ENSMUST00000121927 ; ENSMUSP00000112959 ; ENSMUSG00000048490 .
    GeneIDi 268903.
    KEGGi mmu:268903.
    UCSCi uc007zrx.1. mouse.

    Organism-specific databases

    CTDi 8204.
    MGIi MGI:1315213. Nrip1.

    Phylogenomic databases

    eggNOGi NOG47583.
    GeneTreei ENSGT00390000007999.
    HOGENOMi HOG000236277.
    HOVERGENi HBG052667.
    InParanoidi Q8CBD1.
    KOi K17965.
    OMAi VEKDLRC.
    OrthoDBi EOG7H1JJQ.
    PhylomeDBi Q8CBD1.
    TreeFami TF332210.

    Miscellaneous databases

    NextBioi 392571.
    PROi Q8CBD1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CBD1.
    CleanExi MM_NRIP1.
    Genevestigatori Q8CBD1.

    Family and domain databases

    InterProi IPR026649. NRIP1.
    [Graphical view ]
    PANTHERi PTHR15088. PTHR15088. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2."
      Lee C.-H., Chinpaisal C., Wei L.-N.
      Mol. Cell. Biol. 18:6745-6755(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH NR2C1 AND RARA.
      Strain: ICRImported.
      Tissue: Embryo1 Publication.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6JImported and NOD.
      Tissue: CerebellumImported, HeartImported and Spleen.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6Imported.
      Tissue: BrainImported.
    4. "Post-translational modification of nuclear co-repressor receptor-interacting protein 140 by acetylation."
      Huq M.D.M., Wei L.-N.
      Mol. Cell. Proteomics 4:975-983(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 101-112; 155-170; 283-298; 305-320; 476-492; 517-537; 606-630 AND 930-938, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, ACETYLATION AT LYS-111; LYS-158; LYS-287; LYS-311; LYS-482; LYS-529; LYS-607 AND LYS-932.
    5. "Mapping of phosphorylation sites of nuclear corepressor receptor interacting protein 140 by liquid chromatography-tandem mass spectroscopy."
      Huq M.D.M., Khan S.A., Park S.W., Wei L.-N.
      Proteomics 5:2157-2166(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 101-112; 199-212; 343-360; 375-387; 476-492; 517-548; 670-678 AND 1001-1009, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-104; THR-207; SER-358; SER-380; SER-488; SER-519; SER-531; SER-543; SER-672 AND SER-1003.
    6. "Characterization of receptor-interacting protein 140 in retinoid receptor activities."
      Lee C.-H., Wei L.-N.
      J. Biol. Chem. 274:31320-31326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RARA AND RXRB.
    7. "Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing."
      Wei L.-N., Hu X., Chandra D., Seto E., Farooqui M.
      J. Biol. Chem. 275:40782-40787(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1 AND HDAC3.
    8. "The nuclear receptor co-repressor Nrip1 (RIP140) is essential for female fertility."
      White R., Leonardsson G., Rosewell I., Jacobs M.A., Milligan S., Parker M.G.
      Nat. Med. 6:1368-1374(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    9. "Ligand-dependent formation of retinoid receptors, receptor-interacting protein 140 (RIP140), and histone deacetylase complex is mediated by a novel receptor-interacting motif of RIP140."
      Wei L.-N., Farooqui M., Hu X.
      J. Biol. Chem. 276:16107-16112(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RARA AND RXRB, IDENTIFICATION IN A COMPLEX WITH HDAC3.
    10. "Effects of retinoid ligands on RIP140: molecular interaction with retinoid receptors and biological activity."
      Farooqui M., Franco P.J., Thompson J., Kagechika H., Chandraratna R.A.S., Banaszak L., Wei L.-N.
      Biochemistry 42:971-979(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RARA AND RXRB, MUTAGENESIS OF ASN-1067; PRO-1068 AND MET-1073.
    11. "Receptor interacting protein 140 as a thyroid hormone-dependent, negative co-regulator for the induction of cellular retinoic acid binding protein I gene."
      Wei L.-N., Hu X.
      Mol. Cell. Endocrinol. 218:39-48(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: FUNCTION, TISSUE SPECIFICITY.
    13. "Multiple signaling defects in the absence of RIP140 impair both cumulus expansion and follicle rupture."
      Tullet J.M.A., Pocock V., Steel J.H., White R., Milligan S., Parker M.G.
      Endocrinology 146:4127-4137(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
      Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
      Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C1.
    15. "Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression."
      Gupta P., Ho P.C., Huq M.M., Ha S.G., Park S.W., Khan A.A., Tsai N.P., Wei L.N.
      Proc. Natl. Acad. Sci. U.S.A. 105:11424-11429(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C1.

    Entry informationi

    Entry nameiNRIP1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CBD1
    Secondary accession number(s): Q3U166, Q8C3Y8, Q9Z2K2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 8, 2005
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3