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P48552

- NRIP1_HUMAN

UniProt

P48552 - NRIP1_HUMAN

Protein

Nuclear receptor-interacting protein 1

Gene

NRIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Modulates transcriptional activation by steroid receptors such as NR3C1, NR3C2 and ESR1. Also modulates transcriptional repression by nuclear hormone receptors.6 Publications

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. estrogen receptor binding Source: UniProtKB
    3. glucocorticoid receptor binding Source: UniProtKB
    4. nuclear hormone receptor binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription coactivator activity Source: UniProtKB
    7. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiP48552.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor-interacting protein 1
    Alternative name(s):
    Nuclear factor RIP140
    Receptor-interacting protein 140
    Gene namesi
    Name:NRIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:8001. NRIP1.

    Subcellular locationi

    Nucleus 4 Publications
    Note: Localized to discrete foci and redistributes to larger nuclear domains upon binding to ligand-bound NR3C1.

    GO - Cellular componenti

    1. cell junction Source: HPA
    2. histone deacetylase complex Source: Ensembl
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi440 – 4434PIDL → AAAA: Abolishes interaction with CTBP1.
    Mutagenesisi440 – 4423PID → AIA: Abolishes interaction with CTBP1 and attenuates nuclear hormone receptor-dependent transcription repression.
    Mutagenesisi442 – 4432DL → AA: Reduces, but does not completely abolish, interaction with CTBP. Reduces transcriptional repression.
    Mutagenesisi442 – 4432DL → AS: Disrupts interaction with CTBP1, and CTBP2 to a lesser extent. Disrupts transcriptional repression; when associated with 567-AS-568.
    Mutagenesisi446 – 4461K → Q: Disrupts interaction with CTBP1. Decreases lysine acetylation. Disrupts nuclear hormone receptor-dependent transcription repression. 1 Publication
    Mutagenesisi446 – 4461K → R: Does not disrupt nuclear hormone receptor-dependent transcription repression. 1 Publication
    Mutagenesisi567 – 5682NL → AA: Disrupts transcriptional repression.
    Mutagenesisi567 – 5682NL → AS: Disrupts interaction with CTBP1 and CTBP2. Disrupts transcriptional repression; when associated with 442-AS-443.
    Mutagenesisi599 – 6035SMDLT → PIAAS: Does not further disrupt transcriptional repression; when associated with 442-AA-443 and 567-AA-568.
    Mutagenesisi948 – 9492DL → AA: Abolishes CTBP binding but retains transcriptional repressor activity.

    Organism-specific databases

    PharmGKBiPA31780.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11581158Nuclear receptor-interacting protein 1PRO_0000057951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei104 – 1041PhosphoserineBy similarity
    Modified residuei111 – 1111N6-acetyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysineBy similarity
    Modified residuei207 – 2071PhosphothreonineBy similarity
    Modified residuei286 – 2861N6-acetyllysineBy similarity
    Modified residuei310 – 3101N6-acetyllysineBy similarity
    Modified residuei356 – 3561PhosphoserineBy similarity
    Modified residuei378 – 3781PhosphoserineBy similarity
    Modified residuei446 – 4461N6-acetyllysine1 Publication
    Modified residuei481 – 4811N6-acetyllysineBy similarity
    Modified residuei487 – 4871PhosphoserineBy similarity
    Modified residuei518 – 5181PhosphoserineBy similarity
    Modified residuei528 – 5281N6-acetyllysineBy similarity
    Modified residuei542 – 5421PhosphoserineBy similarity
    Modified residuei606 – 6061N6-acetyllysineBy similarity
    Modified residuei671 – 6711PhosphoserineBy similarity
    Modified residuei931 – 9311N6-acetyllysineBy similarity
    Modified residuei1001 – 10011PhosphoserineBy similarity

    Post-translational modificationi

    Acetylation regulates its nuclear translocation and corepressive activity By similarity. Acetylation abolishes interaction with CTBP1. Phosphorylation enhances interaction with YWHAH.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP48552.
    PRIDEiP48552.

    PTM databases

    PhosphoSiteiP48552.

    Expressioni

    Gene expression databases

    ArrayExpressiP48552.
    BgeeiP48552.
    CleanExiHS_NRIP1.
    GenevestigatoriP48552.

    Organism-specific databases

    HPAiHPA046571.

    Interactioni

    Subunit structurei

    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.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CEP70Q8NHQ13EBI-746484,EBI-739624
    DNMT1P263583EBI-746484,EBI-719459
    FHL1Q136426EBI-746484,EBI-912547
    HDAC3O153792EBI-746484,EBI-607682
    LDOC1O957513EBI-746484,EBI-740738
    PRMT1Q998734EBI-746484,EBI-78738
    ZNF366Q8N8952EBI-746484,EBI-2813661

    Protein-protein interaction databases

    BioGridi113843. 54 interactions.
    DIPiDIP-5964N.
    IntActiP48552. 21 interactions.
    MINTiMINT-192711.
    STRINGi9606.ENSP00000327213.

    Structurei

    Secondary structure

    1
    1158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi379 – 3857

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GPOX-ray1.95C366-390[»]
    2GPPX-ray2.60C/D366-390[»]
    ProteinModelPortaliP48552.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP48552.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 415415Interaction with ZNF366Add
    BLAST
    Regioni78 – 333256Repression domain 1Add
    BLAST
    Regioni410 – 700291Repression domain 2Add
    BLAST
    Regioni431 – 47242Required for targeting to small nuclear fociAdd
    BLAST
    Regioni735 – 885151Repression domain 3Add
    BLAST
    Regioni753 – 1158406Interaction with ZNF366Add
    BLAST
    Regioni1118 – 115841Repression domain 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi21 – 255LXXLL motif 1
    Motifi133 – 1375LXXLL motif 2
    Motifi185 – 1895LXXLL motif 3
    Motifi266 – 2705LXXLL motif 4
    Motifi380 – 3845LXXLL motif 5
    Motifi440 – 4467CTBP-binding; principal site
    Motifi500 – 5045LXXLL motif 6
    Motifi565 – 5695CTBP-binding
    Motifi599 – 6035CTBP-bindingSequence Analysis
    Motifi713 – 7175LXXLL motif 7
    Motifi819 – 8235LXXLL motif 8
    Motifi936 – 9405LXXLL motif 9
    Motifi946 – 9505CTBP-binding
    Motifi1061 – 107414Ligand-dependent nuclear receptor bindingBy similarityAdd
    BLAST

    Domaini

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG47583.
    HOGENOMiHOG000236277.
    HOVERGENiHBG052667.
    InParanoidiP48552.
    KOiK17965.
    OMAiVEKDLRC.
    OrthoDBiEOG7H1JJQ.
    PhylomeDBiP48552.
    TreeFamiTF332210.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P48552-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN     50
    FNISGSAFPT CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR 100
    LSDSIMNLNV KKEALLAGMV DSVPKGKQDS TLLASLLQSF SSRLQTVALS 150
    QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV ASSHLKTLLK KSKVKDQKPD 200
    TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL QAVASMVEKR 250
    ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA 300
    MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM 350
    GIIPSSPKNA GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE 400
    RGSIFEESST PTTIDEYSDN NPSFTDDSSG DESSYSNCVP IDLSCKHRTE 450
    KSESDQPVSL DNFTQSLLNT WDPKVPDVDI KEDQDTSKNS KLNSHQKVTL 500
    LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI ESPSTNRTTP 550
    VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM 600
    DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP 650
    SKQLLTGNTD KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG 700
    SEIENLLERR TVLQLLLGNP NKGKSEKKEK TPLRDESTQE HSERALSEQI 750
    LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP FLGMAPAVQR SAPALPVSED 800
    FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR NNEMALLESK 850
    NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL 900
    KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS 950
    PHRSNSVADS KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF 1000
    SYPGVVKTPV SPTFPEHLGC AGSRPESGLL NGCSMPSEKG PIKWVITDAE 1050
    KNEYEKDSPR LTKTNPILYY MLQKGGNSVT SRETQDKDIW REASSAESVS 1100
    QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN GEVYGLLGSV 1150
    LTIKKESE 1158
    Length:1,158
    Mass (Da):126,942
    Last modified:December 1, 2000 - v2
    Checksum:i81FC424968E9A5F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241P → R in CAA59108. (PubMed:7641693)Curated
    Sequence conflicti721 – 7266NKGKSE → TKGRVK in CAA59108. (PubMed:7641693)Curated
    Sequence conflicti954 – 9541S → I in AAH40361. (PubMed:15489334)Curated
    Sequence conflicti1080 – 10801T → A in CAA59108. (PubMed:7641693)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371V → I.
    Corresponds to variant rs9941840 [ dbSNP | Ensembl ].
    VAR_051241
    Natural varianti221 – 2211H → R.1 Publication
    Corresponds to variant rs139263261 [ dbSNP | Ensembl ].
    VAR_023706
    Natural varianti315 – 3151Y → F.
    Corresponds to variant rs2228507 [ dbSNP | Ensembl ].
    VAR_034142
    Natural varianti441 – 4411I → V.1 Publication
    Corresponds to variant rs150468995 [ dbSNP | Ensembl ].
    VAR_023707
    Natural varianti448 – 4481R → G Common polymorphism. 2 Publications
    Corresponds to variant rs2229742 [ dbSNP | Ensembl ].
    VAR_023708
    Natural varianti567 – 5671N → S.
    Corresponds to variant rs9975169 [ dbSNP | Ensembl ].
    VAR_051242
    Natural varianti803 – 8031S → L.1 Publication
    Corresponds to variant rs61750208 [ dbSNP | Ensembl ].
    VAR_023709
    Natural varianti1079 – 10791V → F.1 Publication
    VAR_023710

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84373 mRNA. Translation: CAA59108.1.
    AF248484 Genomic DNA. Translation: AAF62185.1.
    AF127577 Genomic DNA. Translation: AAF35255.1.
    AL163207 Genomic DNA. Translation: CAB90396.1.
    BC040361 mRNA. Translation: AAH40361.1.
    CCDSiCCDS13568.1.
    PIRiS57348.
    RefSeqiNP_003480.2. NM_003489.3.
    XP_005261120.1. XM_005261063.1.
    XP_005261122.1. XM_005261065.1.
    XP_005261123.1. XM_005261066.1.
    XP_006724117.1. XM_006724054.1.
    UniGeneiHs.155017.

    Genome annotation databases

    EnsembliENST00000318948; ENSP00000327213; ENSG00000180530.
    ENST00000400199; ENSP00000383060; ENSG00000180530.
    ENST00000400202; ENSP00000383063; ENSG00000180530.
    GeneIDi8204.
    KEGGihsa:8204.
    UCSCiuc002yjx.2. human.

    Polymorphism databases

    DMDMi9988061.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84373 mRNA. Translation: CAA59108.1 .
    AF248484 Genomic DNA. Translation: AAF62185.1 .
    AF127577 Genomic DNA. Translation: AAF35255.1 .
    AL163207 Genomic DNA. Translation: CAB90396.1 .
    BC040361 mRNA. Translation: AAH40361.1 .
    CCDSi CCDS13568.1.
    PIRi S57348.
    RefSeqi NP_003480.2. NM_003489.3.
    XP_005261120.1. XM_005261063.1.
    XP_005261122.1. XM_005261065.1.
    XP_005261123.1. XM_005261066.1.
    XP_006724117.1. XM_006724054.1.
    UniGenei Hs.155017.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GPO X-ray 1.95 C 366-390 [» ]
    2GPP X-ray 2.60 C/D 366-390 [» ]
    ProteinModelPortali P48552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113843. 54 interactions.
    DIPi DIP-5964N.
    IntActi P48552. 21 interactions.
    MINTi MINT-192711.
    STRINGi 9606.ENSP00000327213.

    PTM databases

    PhosphoSitei P48552.

    Polymorphism databases

    DMDMi 9988061.

    Proteomic databases

    PaxDbi P48552.
    PRIDEi P48552.

    Protocols and materials databases

    DNASUi 8204.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318948 ; ENSP00000327213 ; ENSG00000180530 .
    ENST00000400199 ; ENSP00000383060 ; ENSG00000180530 .
    ENST00000400202 ; ENSP00000383063 ; ENSG00000180530 .
    GeneIDi 8204.
    KEGGi hsa:8204.
    UCSCi uc002yjx.2. human.

    Organism-specific databases

    CTDi 8204.
    GeneCardsi GC21M016333.
    H-InvDB HIX0027827.
    HGNCi HGNC:8001. NRIP1.
    HPAi HPA046571.
    MIMi 602490. gene.
    neXtProti NX_P48552.
    PharmGKBi PA31780.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47583.
    HOGENOMi HOG000236277.
    HOVERGENi HBG052667.
    InParanoidi P48552.
    KOi K17965.
    OMAi VEKDLRC.
    OrthoDBi EOG7H1JJQ.
    PhylomeDBi P48552.
    TreeFami TF332210.

    Enzyme and pathway databases

    SignaLinki P48552.

    Miscellaneous databases

    EvolutionaryTracei P48552.
    GeneWikii NRIP1.
    GenomeRNAii 8204.
    NextBioi 30914.
    PROi P48552.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48552.
    Bgeei P48552.
    CleanExi HS_NRIP1.
    Genevestigatori P48552.

    Family and domain databases

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

    Publicationsi

    1. "Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor."
      Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S., Kushner P.J., Parker M.G.
      EMBO J. 14:3741-3751(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1, SUBCELLULAR LOCATION, VARIANT GLY-448.
      Tissue: Mammary gland.
    2. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Skin.
    4. "Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4."
      Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M.
      J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C2.
    5. "Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids."
      Subramaniam N., Treuter E., Okret S.
      J. Biol. Chem. 274:18121-18127(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C1.
    6. "Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP."
      Vo N., Fjeld C., Goodman R.H.
      Mol. Cell. Biol. 21:6181-6188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND LYS-446, ACETYLATION AT LYS-446.
    7. "Regulation of glucocorticoid receptor activity by 14-3-3-dependent intracellular relocalization of the corepressor RIP140."
      Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.
      Mol. Endocrinol. 15:501-511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH NR3C1 AND YWHAH, SUBCELLULAR LOCATION.
    8. "A new human MR splice variant is a ligand-independent transactivator modulating corticosteroid action."
      Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.
      Mol. Endocrinol. 15:1586-1598(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NR3C2.
    9. "Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140."
      Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A., Zilliacus J.
      Mol. Cell. Biol. 23:4187-4198(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1, SUBCELLULAR LOCATION.
    10. "Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect."
      Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.
      Mol. Endocrinol. 17:287-299(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR1; FOS AND JUN.
    11. "Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140."
      Christian M., Tullet J.M.A., Parker M.G.
      J. Biol. Chem. 279:15645-15651(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443; 567-ASN--LEU-568 AND 948-ASP--LEU-949, IDENTIFICATION OF REPRESSION DOMAINS.
    12. "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
      Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
      Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, SUBCELLULAR LOCATION.
    13. "Modulation of testicular receptor 4 activity by mitogen-activated protein kinase-mediated phosphorylation."
      Huq M.D., Gupta P., Tsai N.P., Wei L.N.
      Mol. Cell. Proteomics 5:2072-2082(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C2.
    14. "ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases."
      Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.
      Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF366.
    15. "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."
      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.
      J. Biol. Chem. 281:37773-37781(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH ESRRG.
    16. "Preliminary molecular genetic analysis of the receptor interacting protein 140 (RIP140) in women affected by endometriosis."
      Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A., Galan J.J., Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A.
      J. Exp. Clin. Assist. Reprod. 2:11-11(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.

    Entry informationi

    Entry nameiNRIP1_HUMAN
    AccessioniPrimary (citable) accession number: P48552
    Secondary accession number(s): Q8IWE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 128 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3