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Q8CBD1

- NRIP1_MOUSE

UniProt

Q8CBD1 - NRIP1_MOUSE

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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

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. receptor binding Source: UniProtKB
  3. retinoic acid receptor binding Source: UniProtKB
  4. retinoid X receptor binding Source: UniProtKB
  5. transcription coactivator activity Source: Ensembl
  6. 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
Complete GO annotation...

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. cell junction Source: Ensembl
  2. histone deacetylase complex Source: UniProtKB
  3. nuclear speck Source: MGI
  4. nucleus Source: UniProtKB
Complete GO annotation...

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

        10         20         30         40         50
MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAINKK SAGHKEEDQN
60 70 80 90 100
FNLSGSAFPS CQSNGPTVST QTYQGSGMLH LKKARLLQSS EDWNAAKRKR
110 120 130 140 150
LSDSIVNLNV KKEALLAGMV DSVPKGKQDS TLLASLLQSF SSRLQTVALS
160 170 180 190 200
QQIRQSLKEQ GYALSHESLK VEKDLRCYGV ASSHLKTLLK KSKTKDQKSG
210 220 230 240 250
PTLPDVTPNL IRDSFVESSH PAVGQSGTKV MSEPLSCAAR LQAVASMVEK
260 270 280 290 300
RASPAASPKP SVACSQLALL LSSEAHLQQY SREHALKTQN AHQVASERLA
310 320 330 340 350
AMARLQENGQ KDVGSSQLSK GVSGHLNGQA RALPASKLVA NKNNAATFQS
360 370 380 390 400
PMGVVPSSPK NTSYKNSLER NNLKQAANNS LLLHLLKSQT IPTPMNGHSQ
410 420 430 440 450
NERASSFESS TPTTIDEYSD NNPSFTDDSS GDESSYSNCV PIDLSCKHRI
460 470 480 490 500
EKPEAERPVS LENLTQSLLN TWDPKIPGVD IKEDQDTSTN SKLNSHQKVT
510 520 530 540 550
LLQLLLGHKS EETVERNASP QDIHSDGTKF SPQNYTRTSV IESPSTNRTT
560 570 580 590 600
PVSTPPLYTA SQAESPINLS QHSLVIKWNS PPYACSTPAS KLTNTAPSHL
610 620 630 640 650
MDLTKGKESQ AEKPAPSEGA QNSATFSASK LLQNLAQCGL QSSGPGEEQR
660 670 680 690 700
PCKQLLSGNP DKPLGLIDRL NSPLLSNKTN AAEESKAFSS QPAGPEPGLP
710 720 730 740 750
GCEIENLLER RTVLQLLLGN SSKGKNEKKE KTPARDEAPQ EHSERAANEQ
760 770 780 790 800
ILMVKIKSEP CDDFQTHNTN LPLNHDAKSA PFLGVTPAIH RSTAALPVSE
810 820 830 840 850
DFKSEPASPQ DFSFSKNGLL SRLLRQNQES YPADEQDKSH RNSELPTLES
860 870 880 890 900
KNICMVPKKR KLYTEPLENP FKKMKNTAVD TANHHSGPEV LYGSLLHQEE
910 920 930 940 950
LKFSRNELDY KYPAGHSSAS DGDHRSWARE SKSFNVLKQL LLSENCVRDL
960 970 980 990 1000
SPHRSDSVPD TKKKGHKNNA PGSKPEFGIS SLNGLMYSSP QPGSCVTDHR
1010 1020 1030 1040 1050
TFSYPGMVKT PLSPPFPEHL GCVGSRPEPG LLNGCSVPGE KGPIKWVIAD
1060 1070 1080 1090 1100
MDKNEYEKDS PRLTKTNPIL YYMLQKGGGN SVTTQETQDK DIWREPASAE
1110 1120 1130 1140 1150
SLSQVTVKEE LLPAAETKAS FFNLRSPYNS HMGNNASRPH STNGEVYGLL
1160
GNALTIKKES E
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

« Hide 'large scale' publications
  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 29, 2014
This is version 93 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