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Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)

 ERR1_HUMAN              Reviewed;         423 AA.
P11474; Q14514;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
11-DEC-2019, entry version 218.
RecName: Full=Steroid hormone receptor ERR1;
AltName: Full=Estrogen receptor-like 1;
AltName: Full=Estrogen-related receptor alpha;
Short=ERR-alpha;
AltName: Full=Nuclear receptor subfamily 3 group B member 1;
Name=ESRRA; Synonyms=ERR1, ESRL1, NR3B1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=3267207; DOI=10.1038/331091a0;
Giguere V., Yang N., Segui P., Evans R.M.;
"Identification of a new class of steroid hormone receptors.";
Nature 331:91-94(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=8621448; DOI=10.1074/jbc.271.10.5795;
Yang N., Shigeta H., Shi H., Teng C.T.;
"Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated
response of human lactoferrin gene promoter.";
J. Biol. Chem. 271:5795-5804(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
Hattori M., Rogers J., Lander E.S., Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
PROTEIN SEQUENCE OF 69-76.
PubMed=8224847; DOI=10.1101/gad.7.11.2206;
Wiley S.R., Kraus R.J., Zuo F., Murray E.E., Loritz K., Mertz J.E.;
"SV40 early-to-late switch involves titration of cellular transcriptional
repressors.";
Genes Dev. 7:2206-2219(1993).
[5]
FUNCTION.
PubMed=9271417; DOI=10.1128/mcb.17.9.5400;
Sladek R., Bader J.-A., Giguere V.;
"The orphan nuclear receptor estrogen-related receptor alpha is a
transcriptional regulator of the human medium-chain acyl coenzyme A
dehydrogenase gene.";
Mol. Cell. Biol. 17:5400-5409(1997).
[6]
INTERACTION WITH PPARGC1A, INDUCTION, AND FUNCTION.
PubMed=12522104; DOI=10.1074/jbc.m212923200;
Schreiber S.N., Knutti D., Brogli K., Uhlmann T., Kralli A.;
"The transcriptional coactivator PGC-1 regulates the expression and
activity of the orphan nuclear receptor estrogen-related receptor alpha
(ERRalpha).";
J. Biol. Chem. 278:9013-9018(2003).
[7]
DNA-BINDING SPECIFICITY, INTERACTION WITH PPARGC1A, HOMODIMERIZATION,
FUNCTION, AND MUTAGENESIS OF SER-118 AND THR-124.
PubMed=16150865; DOI=10.1210/me.2005-0313;
Barry J.B., Laganiere J., Giguere V.;
"A single nucleotide in an estrogen-related receptor alpha site can dictate
mode of binding and peroxisome proliferator-activated receptor gamma
coactivator 1alpha activation of target promoters.";
Mol. Endocrinol. 20:302-310(2006).
[8]
SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22,
FUNCTION, AND MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403; LEU-413 AND
LEU-418.
PubMed=17676930; DOI=10.1021/bi700316g;
Vu E.H., Kraus R.J., Mertz J.E.;
"Phosphorylation-dependent sumoylation of estrogen-related receptor
alpha1.";
Biochemistry 46:9795-9804(2007).
[9]
SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22,
INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
LYS-14; SER-19; SER-22 AND LYS-403.
PubMed=18063693; DOI=10.1210/me.2007-0357;
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
"Phosphorylation-dependent sumoylation regulates estrogen-related receptor-
alpha and -gamma transcriptional activity through a synergy control
motif.";
Mol. Endocrinol. 22:570-584(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-22, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
ACETYLATION AT LYS-129; LYS-138; LYS-160 AND LYS-162 BY PCAF/KAT2B,
MUTAGENESIS OF LYS-129; LYS-138; LYS-160 AND LYS-162, AND DEACETYLATION BY
SIRT1 AND HDAC8.
PubMed=20484414; DOI=10.1210/me.2009-0441;
Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.;
"An acetylation switch modulates the transcriptional activity of estrogen-
related receptor alpha.";
Mol. Endocrinol. 24:1349-1358(2010).
[12]
INTERACTION WITH MAPK15, AND SUBCELLULAR LOCATION.
PubMed=21190936; DOI=10.1074/jbc.m110.179523;
Rossi M., Colecchia D., Iavarone C., Strambi A., Piccioni F.,
Verrotti di Pianella A., Chiariello M.;
"Extracellular signal-regulated kinase 8 (ERK8) controls estrogen-related
receptor alpha (ERRalpha) cellular localization and inhibits its
transcriptional activity.";
J. Biol. Chem. 286:8507-8522(2011).
[13]
FUNCTION.
PubMed=23836911; DOI=10.1074/jbc.m113.489674;
Cho Y., Hazen B.C., Russell A.P., Kralli A.;
"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-
1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1
(Perm1) is a tissue-specific regulator of oxidative capacity in skeletal
muscle cells.";
J. Biol. Chem. 288:25207-25218(2013).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189 AND LYS-403, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-403, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-189 AND LYS-403, 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).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 193-423 IN COMPLEX WITH THE L3
SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, HOMODIMERIZATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15337744; DOI=10.1074/jbc.m407999200;
Kallen J., Schlaeppi J.-M., Bitsch F., Filipuzzi I., Schilb A., Riou V.,
Graham A., Strauss A., Geiser M., Fournier B.;
"Evidence for ligand-independent transcriptional activation of the human
estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha
ligand binding domain in complex with peroxisome proliferator-activated
receptor coactivator-1alpha.";
J. Biol. Chem. 279:49330-49337(2004).
[18]
X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 180-423 IN COMPLEX WITH THE L3
SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, INTERACTION WITH PPARGC1A,
AND MUTAGENESIS OF 258-MET--GLN-262; SER-259; ARG-315; ASP-338; HIS-341;
GLU-343 AND 421-MET--ASP-423.
PubMed=18441008; DOI=10.1074/jbc.m801920200;
Greschik H., Althage M., Flaig R., Sato Y., Chavant V., Peluso-Iltis C.,
Choulier L., Cronet P., Rochel N., Schuele R., Stroemstedt P.E., Moras D.;
"Communication between the ERRalpha homodimer interface and the PGC-1alpha
binding surface via the helix 8-9 loop.";
J. Biol. Chem. 283:20220-20230(2008).
-!- FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a
single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-
chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and
may act as an important regulator of MCAD promoter. Binds to the C1
region of the lactoferrin gene promoter. Requires dimerization and the
coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex
is a regulator of energy metabolism. Induces the expression of PERM1 in
the skeletal muscle. {ECO:0000269|PubMed:12522104,
ECO:0000269|PubMed:16150865, ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:23836911,
ECO:0000269|PubMed:9271417}.
-!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the AF2
domain) with coactivator PPARGC1A (via the L3 motif); the interaction
greatly enhances transcriptional activity of genes involved in energy
metabolism. Interacts with PIAS4; the interaction enhances sumoylation.
Interacts with MAPK15; promotes re-localization of ESRRA to the
cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA
transcriptional activity. {ECO:0000269|PubMed:12522104,
ECO:0000269|PubMed:15337744, ECO:0000269|PubMed:16150865,
ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:18441008}.
-!- INTERACTION:
Q16665:HIF1A; NbExp=3; IntAct=EBI-372412, EBI-447269;
Q8N2W9:PIAS4; NbExp=3; IntAct=EBI-372412, EBI-473160;
Q9UBK2:PPARGC1A; NbExp=19; IntAct=EBI-372412, EBI-765486;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
ECO:0000269|PubMed:18063693, ECO:0000269|PubMed:21190936}. Cytoplasm
{ECO:0000269|PubMed:21190936}. Note=Co-localizes to the cytoplasm only
in presence of MAPK15. {ECO:0000269|PubMed:21190936}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11474-1; Sequence=Displayed;
Name=2;
IsoId=P11474-2; Sequence=VSP_035756;
-!- INDUCTION: Induced by PGC1alpha in a number of specific cell types
including heart, kidney and muscle. {ECO:0000269|PubMed:12522104}.
-!- PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14
increasing repression of transcriptional activity.
{ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693}.
-!- PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by
phosphorylation on Ser-19, cofactor activation, and by interaction with
PIAS4. Sumoylation enhances repression of transcriptional activity, but
has no effect on subcellular location nor on DNA binding.
{ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693}.
-!- PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-
138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional
activity probably by inhibiting DNA-binding activity; deacetylation
involves SIRT1 and HDAC8 and increases DNA-binding.
{ECO:0000269|PubMed:20484414}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB17015.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=CAA35778.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ESRRAID44408ch11q13.html";
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EMBL; X51416; CAA35778.1; ALT_FRAME; mRNA.
EMBL; L38487; AAB17015.1; ALT_INIT; mRNA.
EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS41667.1; -. [P11474-1]
CCDS; CCDS60830.1; -. [P11474-2]
PIR; A29345; A29345.
RefSeq; NP_001269379.1; NM_001282450.1. [P11474-1]
RefSeq; NP_001269380.1; NM_001282451.1. [P11474-2]
RefSeq; NP_004442.3; NM_004451.4. [P11474-1]
PDB; 1XB7; X-ray; 2.50 A; A=194-423.
PDB; 2PJL; X-ray; 2.30 A; A/B=193-423.
PDB; 3D24; X-ray; 2.11 A; A/C=192-423.
PDB; 3K6P; X-ray; 2.00 A; A=193-423.
PDBsum; 1XB7; -.
PDBsum; 2PJL; -.
PDBsum; 3D24; -.
PDBsum; 3K6P; -.
SMR; P11474; -.
BioGrid; 108405; 40.
DIP; DIP-35053N; -.
IntAct; P11474; 29.
MINT; P11474; -.
STRING; 9606.ENSP00000384851; -.
BindingDB; P11474; -.
ChEMBL; CHEMBL3429; -.
DrugBank; DB06833; 1-CYCLOHEXYL-N-{[1-(4-METHYLPHENYL)-1H-INDOL-3-YL]METHYL}METHANAMINE.
DrugBank; DB04468; Afimoxifene.
DrugBank; DB06732; beta-Naphthoflavone.
DrugBank; DB00255; Diethylstilbestrol.
DrugBank; DB07776; Flavone.
DrugBank; DB01645; Genistein.
DrugBank; DB00197; Troglitazone.
DrugCentral; P11474; -.
GuidetoPHARMACOLOGY; 622; -.
iPTMnet; P11474; -.
PhosphoSitePlus; P11474; -.
BioMuta; ESRRA; -.
DMDM; 215274146; -.
EPD; P11474; -.
jPOST; P11474; -.
MassIVE; P11474; -.
PaxDb; P11474; -.
PeptideAtlas; P11474; -.
PRIDE; P11474; -.
ProteomicsDB; 52781; -. [P11474-1]
ProteomicsDB; 52782; -. [P11474-2]
ABCD; P11474; -.
DNASU; 2101; -.
Ensembl; ENST00000000442; ENSP00000000442; ENSG00000173153. [P11474-1]
Ensembl; ENST00000405666; ENSP00000384851; ENSG00000173153. [P11474-1]
Ensembl; ENST00000406310; ENSP00000385971; ENSG00000173153. [P11474-2]
GeneID; 2101; -.
KEGG; hsa:2101; -.
UCSC; uc001nzr.3; human. [P11474-1]
CTD; 2101; -.
DisGeNET; 2101; -.
EuPathDB; HostDB:ENSG00000173153.13; -.
GeneCards; ESRRA; -.
HGNC; HGNC:3471; ESRRA.
HPA; HPA053785; -.
MIM; 601998; gene.
neXtProt; NX_P11474; -.
OpenTargets; ENSG00000173153; -.
PharmGKB; PA27887; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000160341; -.
HOGENOM; HOG000233467; -.
InParanoid; P11474; -.
KO; K08552; -.
OMA; KRPRCPF; -.
OrthoDB; 669799at2759; -.
PhylomeDB; P11474; -.
TreeFam; TF323751; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
SignaLink; P11474; -.
SIGNOR; P11474; -.
ChiTaRS; ESRRA; human.
EvolutionaryTrace; P11474; -.
GeneWiki; Estrogen-related_receptor_alpha; -.
GenomeRNAi; 2101; -.
Pharos; P11474; Tchem.
PRO; PR:P11474; -.
Proteomes; UP000005640; Chromosome 11.
RNAct; P11474; protein.
Bgee; ENSG00000173153; Expressed in 207 organ(s), highest expression level in apex of heart.
ExpressionAtlas; P11474; baseline and differential.
Genevisible; P11474; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0045171; C:intercellular bridge; IDA:HPA.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; ISA:NTNU_SB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
GO; GO:0004879; F:nuclear receptor activity; TAS:ProtInc.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0005496; F:steroid binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051216; P:cartilage development; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:1900078; P:positive regulation of cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0045670; P:regulation of osteoclast differentiation; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 1.10.565.10; -; 1.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR-like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR027289; Oest-rel_rcp.
InterPro; IPR024178; Oest_rcpt/oest-rel_rcp.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PIRSF; PIRSF002527; ER-like_NR; 1.
PIRSF; PIRSF500939; ERR1-2-3; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cytoplasm;
Direct protein sequencing; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1..423
/note="Steroid hormone receptor ERR1"
/id="PRO_0000053660"
DOMAIN 193..421
/note="NR LBD"
/evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
DNA_BIND 76..151
/note="Nuclear receptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 79..99
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
ZN_FING 115..134
/note="NR C4-type"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
REGION 1..76
/note="Repressor domain"
REGION 403..423
/note="AF-2 domain"
SITE 124
/note="Required for DNA-dependent dimerization"
MOD_RES 19
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"
MOD_RES 22
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:17676930, ECO:0000269|PubMed:18063693"
MOD_RES 129
/note="N6-acetyllysine; by PCAF/KAT2B"
/evidence="ECO:0000269|PubMed:20484414"
MOD_RES 138
/note="N6-acetyllysine; by PCAF/KAT2B"
/evidence="ECO:0000269|PubMed:20484414"
MOD_RES 160
/note="N6-acetyllysine; by PCAF/KAT2B"
/evidence="ECO:0000269|PubMed:20484414"
MOD_RES 162
/note="N6-acetyllysine; by PCAF/KAT2B"
/evidence="ECO:0000269|PubMed:20484414"
CROSSLNK 14
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO)"
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
CROSSLNK 189
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733"
CROSSLNK 403
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO); alternate"
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
CROSSLNK 403
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364, ECO:0000244|PubMed:28112733"
VAR_SEQ 191
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:8621448"
/id="VSP_035756"
MUTAGEN 14
/note="K->R: Some loss of sumoylation. Complete loss of
sumoylation; when associated with R-403."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 19
/note="S->A: 50% loss of phosphorylation but represses
transactivation activity in the absence of coactivator.
Almost complete loss of phosphorylation and 2-fold loss of
repression of transactivation activity in response to
coactivator; when associated with A-22."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 19
/note="S->D: Represses transactivation activity in response
to coactivator as for wild type; when associated with D-
22."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 22
/note="S->A: 15% loss of phosphorylation but little
transactivating activity. Almost complete loss of
phosphorylation and 2-fold loss of repression of
transactivation activity in the presence of coactivator;
when associated with A-19."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 22
/note="S->D: Represses transactivation activity in response
to coactivator as for wild type; when associated with D-
19."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 118
/note="S->A: Binds DNA as a monomer or as a dimer as for
wild type. No effect on interaction with PPARGC1A."
/evidence="ECO:0000269|PubMed:16150865"
MUTAGEN 124
/note="T->A: Binds DNA predominantly as a monomer. Loss of
interaction with PPARGC1A."
/evidence="ECO:0000269|PubMed:16150865"
MUTAGEN 129
/note="K->R: Abolishes acetylation by PCAF/KAT2B; when
associated with R-138, R-160 and R-162."
/evidence="ECO:0000269|PubMed:20484414"
MUTAGEN 138
/note="K->R: Abolishes acetylation by PCAF/KAT2B; when
associated with R-129, R-160 and R-162."
/evidence="ECO:0000269|PubMed:20484414"
MUTAGEN 160
/note="K->R: Abolishes acetylation by PCAF/KAT2B; when
associated with R-129, R-138 and R-162."
/evidence="ECO:0000269|PubMed:20484414"
MUTAGEN 162
/note="K->R: Abolishes acetylation by PCAF/KAT2B; when
associated with R-129, R-138 and R-160."
/evidence="ECO:0000269|PubMed:20484414"
MUTAGEN 258..262
/note="MSVLQ->VSVLE: Almost complete loss of interaction to
L2 or to L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 259
/note="S->H: Little effect on binding L2 of PPARGC1A.
Greatly reduced binding to L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 315
/note="R->A: Almost complete loss of interaction to L2 or
to L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 338
/note="D->A: Almost complete loss of interaction to L2 or
to L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 341
/note="H->A: Little effect on binding L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 343
/note="E->A: No effect on binding L3 of PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 403
/note="K->R: Decrease in sumoylation. No effect on
transcriptional activity. Complete loss of sumoylation;
when associated with R-14."
/evidence="ECO:0000269|PubMed:17676930,
ECO:0000269|PubMed:18063693"
MUTAGEN 413
/note="L->A: Loss of coactivation activity; when associated
with A-418. Loss of increased response to coactivator; when
associated with A-19 and A-418."
/evidence="ECO:0000269|PubMed:17676930"
MUTAGEN 418
/note="L->A: Loss of coactivation activity; when associated
with A-413. Loss of increased response to coactivator
activity; when associated with A-19 and A-413."
/evidence="ECO:0000269|PubMed:17676930"
MUTAGEN 421..423
/note="Missing: Greatly reduced interaction with L3 motif
of PPARGC1A. Less effect on binding to L2 motif of
PPARGC1A."
/evidence="ECO:0000269|PubMed:18441008"
MUTAGEN 423
/note="D->A: Little effect on binding L3 of PPARGC1A."
HELIX 195..204
/evidence="ECO:0000244|PDB:3K6P"
HELIX 224..244
/evidence="ECO:0000244|PDB:3K6P"
HELIX 249..251
/evidence="ECO:0000244|PDB:3K6P"
HELIX 254..277
/evidence="ECO:0000244|PDB:3K6P"
STRAND 280..282
/evidence="ECO:0000244|PDB:3K6P"
STRAND 284..287
/evidence="ECO:0000244|PDB:3K6P"
STRAND 290..292
/evidence="ECO:0000244|PDB:3K6P"
HELIX 294..299
/evidence="ECO:0000244|PDB:3K6P"
TURN 300..304
/evidence="ECO:0000244|PDB:3K6P"
HELIX 305..317
/evidence="ECO:0000244|PDB:3K6P"
TURN 318..320
/evidence="ECO:0000244|PDB:3K6P"
HELIX 323..335
/evidence="ECO:0000244|PDB:3K6P"
HELIX 345..364
/evidence="ECO:0000244|PDB:3K6P"
HELIX 377..382
/evidence="ECO:0000244|PDB:3K6P"
HELIX 385..400
/evidence="ECO:0000244|PDB:3K6P"
HELIX 404..406
/evidence="ECO:0000244|PDB:2PJL"
HELIX 410..421
/evidence="ECO:0000244|PDB:3K6P"
SEQUENCE 423 AA; 45510 MW; BAE62DAF0BE6BA96 CRC64;
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH KEEEDGEGAG
PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE
CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP
LAVAGGPRKT AAPVNALVSH LLVVEPEKLY AMPDPAGPDG HLPAVATLCD LFDREIVVTI
SWAKSIPGFS SLSLSDQMSV LQSVWMEVLV LGVAQRSLPL QDELAFAEDL VLDEEGARAA
GLGELGAALL QLVRRLQALR LEREEYVLLK ALALANSDSV HIEDAEAVEQ LREALHEALL
EYEAGRAGPG GGAERRRAGR LLLTLPLLRQ TAGKVLAHFY GVKLEGKVPM HKLFLEMLEA
MMD


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Related Genes :
[ESRRA ERR1 ESRL1 NR3B1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Err1 Estrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen receptor-like 1) (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrra Nr3b1] Steroid hormone receptor ERR1 (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[Esrrb Err-2 Err2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[ESRRB ERRB2 ESRL2 NR3B2] Steroid hormone receptor ERR2 (ERR beta-2) (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[Esrrb Err2 Esrl2 Nr3b2] Steroid hormone receptor ERR2 (Estrogen receptor-like 2) (Estrogen-related receptor beta) (ERR-beta) (Nuclear receptor subfamily 3 group B member 2)
[Esrrg Err3 Kiaa0832 Nr3b3] Estrogen-related receptor gamma (Estrogen receptor-related protein 3) (Nuclear receptor subfamily 3 group B member 3)
[ESRRA NR3B1] Steroid hormone receptor ERR1 (Estrogen-related receptor alpha) (ERR-alpha) (Nuclear receptor subfamily 3 group B member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esr1 Esr Estr Estra Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[Esr1 Esr Estr Nr3a1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[NR1D2] Nuclear receptor subfamily 1 group D member 2 (Orphan nuclear hormone receptor BD73) (Rev-erb alpha-related receptor) (RVR) (Rev-erb-beta) (V-erbA-related protein 1-related) (EAR-1R)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[THRA EAR7 ERBA1 NR1A1 THRA1 THRA2] Thyroid hormone receptor alpha (Nuclear receptor subfamily 1 group A member 1) (V-erbA-related protein 7) (EAR-7) (c-erbA-1) (c-erbA-alpha)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[ESR2 ESTRB NR3A2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Estrb Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[Esr2 Erbeta Nr3a2] Estrogen receptor beta (ER-beta) (Nuclear receptor subfamily 3 group A member 2)
[RXRA NR2B1] Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
[RARA NR1B1] Retinoic acid receptor alpha (RAR-alpha) (Nuclear receptor subfamily 1 group B member 1)
[NR5A2 B1F CPF FTF] Nuclear receptor subfamily 5 group A member 2 (Alpha-1-fetoprotein transcription factor) (B1-binding factor) (hB1F) (CYP7A promoter-binding factor) (Hepatocytic transcription factor) (Liver receptor homolog 1) (LRH-1)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[GPER1 CEPR CMKRL2 DRY12 GPER GPR30] G-protein coupled estrogen receptor 1 (Chemoattractant receptor-like 2) (Flow-induced endothelial G-protein coupled receptor 1) (FEG-1) (G protein-coupled estrogen receptor 1) (G-protein coupled receptor 30) (GPCR-Br) (IL8-related receptor DRY12) (Lymphocyte-derived G-protein coupled receptor) (LYGPR) (Membrane estrogen receptor) (mER)
[ESR1 ESR NR3A1] Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (Fragment)
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)

Bibliography :