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Nuclear receptor-interacting protein 1 (Nuclear factor RIP140) (Receptor-interacting protein 140)

 NRIP1_HUMAN             Reviewed;        1158 AA.
P48552; Q8IWE8;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
30-AUG-2017, entry version 156.
RecName: Full=Nuclear receptor-interacting protein 1;
AltName: Full=Nuclear factor RIP140;
AltName: Full=Receptor-interacting protein 140;
Name=NRIP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1,
SUBCELLULAR LOCATION, AND VARIANT GLY-448.
TISSUE=Mammary gland;
PubMed=7641693;
Cavailles V., Dauvois S., L'Horset F., Lopez G., Hoare S.,
Kushner P.J., Parker M.G.;
"Nuclear factor RIP140 modulates transcriptional activation by the
estrogen receptor.";
EMBO J. 14:3741-3751(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH NR2C2.
PubMed=9556573; DOI=10.1074/jbc.273.18.10948;
Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I.,
Jetten A.M.;
"Regulation of peroxisome proliferator-activated receptor alpha-
induced transactivation by the nuclear orphan receptor TAK1/TR4.";
J. Biol. Chem. 273:10948-10957(1998).
[5]
FUNCTION, AND INTERACTION WITH NR3C1.
PubMed=10364267; DOI=10.1074/jbc.274.25.18121;
Subramaniam N., Treuter E., Okret S.;
"Receptor interacting protein RIP140 inhibits both positive and
negative gene regulation by glucocorticoids.";
J. Biol. Chem. 274:18121-18127(1999).
[6]
FUNCTION, INTERACTION WITH CTBP1, MUTAGENESIS OF 440-PRO--LEU-443 AND
LYS-446, AND ACETYLATION AT LYS-446.
PubMed=11509661; DOI=10.1128/MCB.21.18.6181-6188.2001;
Vo N., Fjeld C., Goodman R.H.;
"Acetylation of nuclear hormone receptor-interacting protein RIP140
regulates binding of the transcriptional corepressor CtBP.";
Mol. Cell. Biol. 21:6181-6188(2001).
[7]
INTERACTION WITH NR3C1 AND YWHAH, IDENTIFICATION IN A COMPLEX WITH
NR3C1 AND YWHAH, AND SUBCELLULAR LOCATION.
PubMed=11266503; DOI=10.1210/mend.15.4.0624;
Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
Gustafsson J.-A.;
"Regulation of glucocorticoid receptor activity by 14-3-3-dependent
intracellular relocalization of the corepressor RIP140.";
Mol. Endocrinol. 15:501-511(2001).
[8]
FUNCTION, AND INTERACTION WITH NR3C2.
PubMed=11518808; DOI=10.1210/mend.15.9.0689;
Zennaro M.-C., Souque A., Viengchareun S., Poisson E., Lombes M.;
"A new human MR splice variant is a ligand-independent transactivator
modulating corticosteroid action.";
Mol. Endocrinol. 15:1586-1598(2001).
[9]
INTERACTION WITH NR3C1, AND SUBCELLULAR LOCATION.
PubMed=12773562; DOI=10.1128/MCB.23.12.4187-4198.2003;
Tazawa H., Osman W., Shoji Y., Treuter E., Gustafsson J.-A.,
Zilliacus J.;
"Regulation of subnuclear localization is associated with a mechanism
for nuclear receptor corepression by RIP140.";
Mol. Cell. Biol. 23:4187-4198(2003).
[10]
FUNCTION, AND INTERACTION WITH ESR1; FOS AND JUN.
PubMed=12554755; DOI=10.1210/me.2002-0324;
Teyssier C., Belguise K., Galtier F., Cavailles V., Chalbos D.;
"Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-
induced activator protein-1 activity by reversing glucocorticoid
receptor-interacting protein 1 effect.";
Mol. Endocrinol. 17:287-299(2003).
[11]
INTERACTION WITH CTBP1 AND CTBP2, MUTAGENESIS OF 442-ASP--LEU-443;
567-ASN--LEU-568 AND 948-ASP--LEU-949, AND IDENTIFICATION OF
REPRESSION DOMAINS.
PubMed=14736873; DOI=10.1074/jbc.M313906200;
Christian M., Tullet J.M.A., Parker M.G.;
"Characterization of four autonomous repression domains in the
corepressor receptor interacting protein 140.";
J. Biol. Chem. 279:15645-15651(2004).
[12]
FUNCTION, INTERACTION WITH CTBP1; CTBP2; HDAC1; HDAC2; HDAC5 AND
HDAC6, MUTAGENESIS OF 442-ASP--LEU-443 AND 567-ASN--LEU-568, AND
SUBCELLULAR LOCATION.
PubMed=15060175; DOI=10.1093/nar/gkh524;
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
"Multiple domains of the receptor-interacting protein 140 contribute
to transcription inhibition.";
Nucleic Acids Res. 32:1957-1966(2004).
[13]
INTERACTION WITH NR2C2.
PubMed=16887930; DOI=10.1074/mcp.M600180-MCP200;
Huq M.D., Gupta P., Tsai N.P., Wei L.N.;
"Modulation of testicular receptor 4 activity by mitogen-activated
protein kinase-mediated phosphorylation.";
Mol. Cell. Proteomics 5:2072-2082(2006).
[14]
INTERACTION WITH ZNF366.
PubMed=17085477; DOI=10.1093/nar/gkl875;
Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M.,
Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L.,
Kamalati T., Ali S.;
"ZNF366 is an estrogen receptor corepressor that acts through CtBP and
histone deacetylases.";
Nucleic Acids Res. 34:6126-6136(2006).
[15]
FUNCTION, INTERACTION WITH RORA, AND INDUCTION.
PubMed=21628546; DOI=10.1177/0748730411401579;
Poliandri A.H., Gamsby J.J., Christian M., Spinella M.J., Loros J.J.,
Dunlap J.C., Parker M.G.;
"Modulation of clock gene expression by the transcriptional
coregulator receptor interacting protein 140 (RIP140).";
J. Biol. Rhythms 26:187-199(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-807, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218; SER-671 AND
SER-807, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-756 AND LYS-1105, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-111; LYS-170; LYS-195;
LYS-198; LYS-372; LYS-508; LYS-756; LYS-802; LYS-850; LYS-901;
LYS-931; LYS-1105; LYS-1115 AND LYS-1154, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 366-390 IN COMPLEX WITH
ESRRG.
PubMed=16990259; DOI=10.1074/jbc.M608410200;
Wang L., Zuercher W.J., Consler T.G., Lambert M.H., Miller A.B.,
Orband-Miller L.A., McKee D.D., Willson T.M., Nolte R.T.;
"X-ray crystal structures of the estrogen-related receptor-gamma
ligand binding domain in three functional states reveal the molecular
basis of small molecule regulation.";
J. Biol. Chem. 281:37773-37781(2006).
[21]
VARIANTS ARG-221; VAL-441; GLY-448; LEU-803 AND PHE-1079.
PubMed=16131398; DOI=10.1186/1743-1050-2-11;
Caballero V., Ruiz R., Sainz J.A., Cruz M., Lopez-Nevot M.A.,
Galan J.J., Real L.M., de Castro F., Lopez-Villaverde V., Ruiz A.;
"Preliminary molecular genetic analysis of the receptor interacting
protein 140 (RIP140) in women affected by endometriosis.";
J. Exp. Clin. Assist. Reprod. 2:11-11(2005).
-!- FUNCTION: Modulates transcriptional activation by steroid
receptors such as NR3C1, NR3C2 and ESR1. Also modulates
transcriptional repression by nuclear hormone receptors. Positive
regulator of the circadian clock gene expression: stimulates
transcription of ARNTL/BMAL1, CLOCK and CRY1 by acting as a
coactivator for RORA and RORC. {ECO:0000269|PubMed:10364267,
ECO:0000269|PubMed:11509661, ECO:0000269|PubMed:11518808,
ECO:0000269|PubMed:12554755, ECO:0000269|PubMed:15060175,
ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693}.
-!- SUBUNIT: Interacts with RARA and RXRB homodimers and RARA/RXRB
heterodimers in the presence of ligand. Interacts with HDAC1 and
HDAC3 via its N-terminal domain. Interacts with NR2C1 (sumoylated
form and via the ligand-binding domain); the interaction results
in promoting the repressor activity of NR2C1 (By similarity).
Interacts with CTBP1, CTBP2, ESR1, HDAC1, HDAC2, HDAC5, HDAC6,
NR2C2, NR3C1, NR3C2, YWHAH, JUN and FOS. Found in a complex with
both NR3C1 and YWHAH. Interacts with ZNF366. Interacts with RORA.
{ECO:0000250|UniProtKB:Q8CBD1, ECO:0000269|PubMed:10364267,
ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11509661,
ECO:0000269|PubMed:11518808, ECO:0000269|PubMed:12554755,
ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:14736873,
ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:16887930,
ECO:0000269|PubMed:16990259, ECO:0000269|PubMed:17085477,
ECO:0000269|PubMed:21628546, ECO:0000269|PubMed:7641693,
ECO:0000269|PubMed:9556573}.
-!- INTERACTION:
O15145:ARPC3; NbExp=3; IntAct=EBI-746484, EBI-351829;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-746484, EBI-739624;
P26358:DNMT1; NbExp=3; IntAct=EBI-746484, EBI-719459;
Q13642:FHL1; NbExp=6; IntAct=EBI-746484, EBI-912547;
O15379:HDAC3; NbExp=2; IntAct=EBI-746484, EBI-607682;
O95751:LDOC1; NbExp=3; IntAct=EBI-746484, EBI-740738;
Q99873:PRMT1; NbExp=4; IntAct=EBI-746484, EBI-78738;
P10276:RARA; NbExp=4; IntAct=EBI-746484, EBI-413374;
P10276-2:RARA; NbExp=3; IntAct=EBI-746484, EBI-10197061;
Q8N895:ZNF366; NbExp=2; IntAct=EBI-746484, EBI-2813661;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11266503,
ECO:0000269|PubMed:12773562, ECO:0000269|PubMed:15060175,
ECO:0000269|PubMed:7641693}. Note=Localized to discrete foci and
redistributes to larger nuclear domains upon binding to ligand-
bound NR3C1.
-!- INDUCTION: Expressed in a circadian manner in the liver (at
protein level). {ECO:0000269|PubMed:21628546}.
-!- DOMAIN: Contains 9 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which have
different affinities for nuclear receptors. The C-terminal
LTKTNPILYYMLQK motif is required for ligand-dependent interaction
with RAAR and RXRB homodimers and heterodimers, for the
corepressor activity, and for the formation of an HDAC3 complex
with RARA/RXRB (By similarity). Contains at least four autonomous
repression domains (RD1-4). RD1 functions via a histone
deacetylase (HDAC)-independent mechanism, whereas RD2, RD3 and RD4
can function by HDAC-dependent or independent mechanisms,
depending on cell type. RD2 is dependent on CTBP binding.
{ECO:0000250}.
-!- PTM: Acetylation regulates its nuclear translocation and
corepressive activity (By similarity). Acetylation abolishes
interaction with CTBP1. Phosphorylation enhances interaction with
YWHAH. {ECO:0000250, ECO:0000269|PubMed:11509661}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NRIP1ID44067ch21q11.html";
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EMBL; X84373; CAA59108.1; -; mRNA.
EMBL; AF248484; AAF62185.1; -; Genomic_DNA.
EMBL; AF127577; AAF35255.1; -; Genomic_DNA.
EMBL; AL163207; CAB90396.1; -; Genomic_DNA.
EMBL; BC040361; AAH40361.1; -; mRNA.
CCDS; CCDS13568.1; -.
PIR; S57348; S57348.
RefSeq; NP_003480.2; NM_003489.3.
RefSeq; XP_005261120.1; XM_005261063.3.
RefSeq; XP_005261122.1; XM_005261065.3.
RefSeq; XP_011528049.1; XM_011529747.1.
RefSeq; XP_011528050.1; XM_011529748.2.
RefSeq; XP_011528051.1; XM_011529749.2.
RefSeq; XP_011528053.1; XM_011529751.2.
RefSeq; XP_011528054.1; XM_011529752.1.
RefSeq; XP_016883962.1; XM_017028473.1.
RefSeq; XP_016883963.1; XM_017028474.1.
RefSeq; XP_016883964.1; XM_017028475.1.
RefSeq; XP_016883965.1; XM_017028476.1.
UniGene; Hs.155017; -.
PDB; 2GPO; X-ray; 1.95 A; C=366-390.
PDB; 2GPP; X-ray; 2.60 A; C/D=366-390.
PDB; 4S14; X-ray; 3.54 A; C=499-510.
PDB; 4S15; X-ray; 1.90 A; C/D=499-510.
PDB; 5NTN; X-ray; 1.90 A; P/Q/R/S=493-512.
PDB; 5NTW; X-ray; 1.64 A; P/Q/R/S=493-512.
PDB; 5NU1; X-ray; 1.85 A; P/Q=493-512.
PDBsum; 2GPO; -.
PDBsum; 2GPP; -.
PDBsum; 4S14; -.
PDBsum; 4S15; -.
PDBsum; 5NTN; -.
PDBsum; 5NTW; -.
PDBsum; 5NU1; -.
ProteinModelPortal; P48552; -.
SMR; P48552; -.
BioGrid; 113843; 58.
DIP; DIP-5964N; -.
IntAct; P48552; 26.
MINT; MINT-192711; -.
STRING; 9606.ENSP00000327213; -.
DrugBank; DB06884; 4-HYDROXY-N'-(4-ISOPROPYLBENZYL)BENZOHYDRAZIDE.
iPTMnet; P48552; -.
PhosphoSitePlus; P48552; -.
BioMuta; NRIP1; -.
DMDM; 9988061; -.
EPD; P48552; -.
MaxQB; P48552; -.
PaxDb; P48552; -.
PeptideAtlas; P48552; -.
PRIDE; P48552; -.
DNASU; 8204; -.
Ensembl; ENST00000318948; ENSP00000327213; ENSG00000180530.
Ensembl; ENST00000400199; ENSP00000383060; ENSG00000180530.
Ensembl; ENST00000400202; ENSP00000383063; ENSG00000180530.
GeneID; 8204; -.
KEGG; hsa:8204; -.
UCSC; uc002yjx.2; human.
CTD; 8204; -.
DisGeNET; 8204; -.
GeneCards; NRIP1; -.
H-InvDB; HIX0027827; -.
HGNC; HGNC:8001; NRIP1.
HPA; HPA046571; -.
HPA; HPA060036; -.
MIM; 602490; gene.
neXtProt; NX_P48552; -.
OpenTargets; ENSG00000180530; -.
PharmGKB; PA31780; -.
eggNOG; ENOG410IFW7; Eukaryota.
eggNOG; ENOG410XPVS; LUCA.
GeneTree; ENSGT00390000007999; -.
HOGENOM; HOG000236277; -.
HOVERGEN; HBG052667; -.
InParanoid; P48552; -.
KO; K17965; -.
OMA; YMLQKGG; -.
OrthoDB; EOG091G07UX; -.
PhylomeDB; P48552; -.
TreeFam; TF332210; -.
Reactome; R-HSA-1368082; RORA activates gene expression.
Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
Reactome; R-HSA-400253; Circadian Clock.
SignaLink; P48552; -.
SIGNOR; P48552; -.
ChiTaRS; NRIP1; human.
EvolutionaryTrace; P48552; -.
GeneWiki; NRIP1; -.
GenomeRNAi; 8204; -.
PRO; PR:P48552; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000180530; -.
CleanEx; HS_NRIP1; -.
ExpressionAtlas; P48552; baseline and differential.
Genevisible; P48552; HS.
GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0035257; F:nuclear hormone receptor binding; IPI:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:BHF-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0001543; P:ovarian follicle rupture; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026649; NRIP1.
InterPro; IPR031405; NRIP1_RD1.
InterPro; IPR031406; NRIP1_RD2.
InterPro; IPR031407; NRIP1_RD3.
InterPro; IPR031408; NRIP1_RD4.
PANTHER; PTHR15088; PTHR15088; 1.
Pfam; PF15687; NRIP1_repr_1; 1.
Pfam; PF15688; NRIP1_repr_2; 1.
Pfam; PF15689; NRIP1_repr_3; 1.
Pfam; PF15690; NRIP1_repr_4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Biological rhythms;
Complete proteome; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 1158 Nuclear receptor-interacting protein 1.
/FTId=PRO_0000057951.
REGION 1 415 Interaction with ZNF366.
{ECO:0000269|PubMed:17085477}.
REGION 78 333 Repression domain 1.
REGION 410 700 Repression domain 2.
REGION 431 472 Required for targeting to small nuclear
foci.
REGION 735 885 Repression domain 3.
REGION 753 1158 Interaction with ZNF366.
{ECO:0000269|PubMed:17085477}.
REGION 1118 1158 Repression domain 4.
MOTIF 21 25 LXXLL motif 1.
MOTIF 133 137 LXXLL motif 2.
MOTIF 185 189 LXXLL motif 3.
MOTIF 266 270 LXXLL motif 4.
MOTIF 380 384 LXXLL motif 5.
MOTIF 440 446 CTBP-binding; principal site.
MOTIF 500 504 LXXLL motif 6.
MOTIF 565 569 CTBP-binding.
MOTIF 599 603 CTBP-binding. {ECO:0000255}.
MOTIF 713 717 LXXLL motif 7.
MOTIF 819 823 LXXLL motif 8.
MOTIF 936 940 LXXLL motif 9.
MOTIF 946 950 CTBP-binding.
MOTIF 1061 1074 Ligand-dependent nuclear receptor
binding. {ECO:0000250}.
MOD_RES 104 104 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 111 111 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 158 158 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 207 207 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 286 286 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 310 310 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 446 446 N6-acetyllysine.
{ECO:0000269|PubMed:11509661}.
MOD_RES 481 481 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 487 487 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 528 528 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 542 542 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 564 564 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 606 606 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 807 807 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 931 931 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8CBD1}.
MOD_RES 1001 1001 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CBD1}.
CROSSLNK 111 111 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 170 170 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 195 195 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 198 198 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 372 372 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 508 508 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 756 756 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 802 802 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 850 850 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 901 901 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 931 931 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 1105 1105 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1115 1115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1154 1154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 37 37 V -> I (in dbSNP:rs9941840).
/FTId=VAR_051241.
VARIANT 221 221 H -> R (in dbSNP:rs139263261).
{ECO:0000269|PubMed:16131398}.
/FTId=VAR_023706.
VARIANT 315 315 Y -> F (in dbSNP:rs2228507).
/FTId=VAR_034142.
VARIANT 441 441 I -> V (in dbSNP:rs150468995).
{ECO:0000269|PubMed:16131398}.
/FTId=VAR_023707.
VARIANT 448 448 R -> G (common polymorphism;
dbSNP:rs2229742).
{ECO:0000269|PubMed:16131398,
ECO:0000269|PubMed:7641693}.
/FTId=VAR_023708.
VARIANT 567 567 N -> S (in dbSNP:rs9975169).
/FTId=VAR_051242.
VARIANT 803 803 S -> L (in dbSNP:rs61750208).
{ECO:0000269|PubMed:16131398}.
/FTId=VAR_023709.
VARIANT 1079 1079 V -> F (in dbSNP:rs140803495).
{ECO:0000269|PubMed:16131398}.
/FTId=VAR_023710.
MUTAGEN 440 443 PIDL->AAAA: Abolishes interaction with
CTBP1. {ECO:0000269|PubMed:11509661}.
MUTAGEN 440 442 PID->AIA: Abolishes interaction with
CTBP1 and attenuates nuclear hormone
receptor-dependent transcription
repression.
MUTAGEN 442 443 DL->AA: Reduces, but does not completely
abolish, interaction with CTBP. Reduces
transcriptional repression.
{ECO:0000269|PubMed:14736873,
ECO:0000269|PubMed:15060175}.
MUTAGEN 442 443 DL->AS: Disrupts interaction with CTBP1,
and CTBP2 to a lesser extent. Disrupts
transcriptional repression; when
associated with 567-AS-568.
{ECO:0000269|PubMed:14736873,
ECO:0000269|PubMed:15060175}.
MUTAGEN 446 446 K->Q: Disrupts interaction with CTBP1.
Decreases lysine acetylation. Disrupts
nuclear hormone receptor-dependent
transcription repression.
{ECO:0000269|PubMed:11509661}.
MUTAGEN 446 446 K->R: Does not disrupt nuclear hormone
receptor-dependent transcription
repression.
{ECO:0000269|PubMed:11509661}.
MUTAGEN 567 568 NL->AA: Disrupts transcriptional
repression. {ECO:0000269|PubMed:14736873,
ECO:0000269|PubMed:15060175}.
MUTAGEN 567 568 NL->AS: Disrupts interaction with CTBP1
and CTBP2. Disrupts transcriptional
repression; when associated with 442-AS-
443. {ECO:0000269|PubMed:14736873,
ECO:0000269|PubMed:15060175}.
MUTAGEN 599 603 SMDLT->PIAAS: Does not further disrupt
transcriptional repression; when
associated with 442-AA-443 and 567-AA-
568.
MUTAGEN 948 949 DL->AA: Abolishes CTBP binding but
retains transcriptional repressor
activity. {ECO:0000269|PubMed:14736873}.
CONFLICT 124 124 P -> R (in Ref. 1; CAA59108).
{ECO:0000305}.
CONFLICT 721 726 NKGKSE -> TKGRVK (in Ref. 1; CAA59108).
{ECO:0000305}.
CONFLICT 954 954 S -> I (in Ref. 3; AAH40361).
{ECO:0000305}.
CONFLICT 1080 1080 T -> A (in Ref. 1; CAA59108).
{ECO:0000305}.
HELIX 379 385 {ECO:0000244|PDB:2GPO}.
HELIX 500 505 {ECO:0000244|PDB:4S15}.
SEQUENCE 1158 AA; 126942 MW; 81FC424968E9A5F6 CRC64;
MTHGEELGSD VHQDSIVLTY LEGLLMHQAA GGSGTAVDKK SAGHNEEDQN FNISGSAFPT
CQSNGPVLNT HTYQGSGMLH LKKARLLQSS EDWNAAKRKR LSDSIMNLNV KKEALLAGMV
DSVPKGKQDS TLLASLLQSF SSRLQTVALS QQIRQSLKEQ GYALSHDSLK VEKDLRCYGV
ASSHLKTLLK KSKVKDQKPD TNLPDVTKNL IRDRFAESPH HVGQSGTKVM SEPLSCAARL
QAVASMVEKR ASPATSPKPS VACSQLALLL SSEAHLQQYS REHALKTQNA NQAASERLAA
MARLQENGQK DVGSYQLPKG MSSHLNGQAR TSSSKLMASK SSATVFQNPM GIIPSSPKNA
GYKNSLERNN IKQAANNSLL LHLLKSQTIP KPMNGHSHSE RGSIFEESST PTTIDEYSDN
NPSFTDDSSG DESSYSNCVP IDLSCKHRTE KSESDQPVSL DNFTQSLLNT WDPKVPDVDI
KEDQDTSKNS KLNSHQKVTL LQLLLGHKNE ENVEKNTSPQ GVHNDVSKFN TQNYARTSVI
ESPSTNRTTP VSTPPLLTSS KAGSPINLSQ HSLVIKWNSP PYVCSTQSEK LTNTASNHSM
DLTKSKDPPG EKPAQNEGAQ NSATFSASKL LQNLAQCGMQ SSMSVEEQRP SKQLLTGNTD
KPIGMIDRLN SPLLSNKTNA VEENKAFSSQ PTGPEPGLSG SEIENLLERR TVLQLLLGNP
NKGKSEKKEK TPLRDESTQE HSERALSEQI LMVKIKSEPC DDLQIPNTNV HLSHDAKSAP
FLGMAPAVQR SAPALPVSED FKSEPVSPQD FSFSKNGLLS RLLRQNQDSY LADDSDRSHR
NNEMALLESK NLCMVPKKRK LYTEPLENPF KKMKNNIVDA ANNHSAPEVL YGSLLNQEEL
KFSRNDLEFK YPAGHGSASE SEHRSWARES KSFNVLKQLL LSENCVRDLS PHRSNSVADS
KKKGHKNNVT NSKPEFSISS LNGLMYSSTQ PSSCMDNRTF SYPGVVKTPV SPTFPEHLGC
AGSRPESGLL NGCSMPSEKG PIKWVITDAE KNEYEKDSPR LTKTNPILYY MLQKGGNSVT
SRETQDKDIW REASSAESVS QVTAKEELLP TAETKASFFN LRSPYNSHMG NNASRPHSAN
GEVYGLLGSV LTIKKESE


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