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P62509 (ERR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen-related receptor gamma
Alternative name(s):
Estrogen receptor-related protein 3
Nuclear receptor subfamily 3 group B member 3
Gene names
Name:Esrrg
Synonyms:Err3, Kiaa0832, Nr3b3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Orphan receptor that acts as transcription activator in the absence of bound ligand. Binds specifically to an estrogen response element and activates reporter genes controlled by estrogen response elements. Induces the expression of PERM1 in the skeletal muscle. Ref.1

Subunit structure

Homodimer. Interacts with NRIP1, NCOA1 and NCOR2 By similarity. Binds TLE1, PNRC1 and PNRC2 By similarity. Binds GRIP1. Ref.1 Ref.5

Subcellular location

Nucleus Probable.

Tissue specificity

Highly expressed in the heart, brain and kidney and low expression in the liver. Ref.1

Post-translational modification

Acetylated by PCAF/KAT2 (in vitro) By similarity.

Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and represses transcriptional activity By similarity.

Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus repressing transcriptional activity By similarity.

Miscellaneous

No physiological activating ligand is known for this orphan receptor, but 4-hydroxytamoxifen and diethylstilbestrol act as inverse agonists and deactivate ESRRG By similarity.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence BAC41450.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmulticellular organismal development

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1PubMed 12715898. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleus

Non-traceable author statement PubMed 10072763. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

calmodulin binding

Non-traceable author statement PubMed 12715898. Source: UniProtKB

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Non-traceable author statement PubMed 10072763. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: UniProtKB

retinoic acid receptor activity

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

steroid binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CREBZFQ9NS373EBI-5274019,EBI-632965From a different organism.
CrebzfQ91ZR33EBI-5274019,EBI-5274001

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62509-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P62509-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Estrogen-related receptor gamma
PRO_0000053666

Regions

DNA binding125 – 20076Nuclear receptor
Zinc finger128 – 14821NR C4-type
Zinc finger164 – 18825NR C4-type

Amino acid modifications

Modified residue451Phosphoserine Probable
Cross-link40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 2323Missing in isoform 2.
VSP_010766

Experimental info

Mutagenesis4491L → A: Loss of transcriptional activation; when associated with A-450. Ref.1
Mutagenesis4501F → A: Loss of transcriptional activation; when associated with A-449. Ref.1
Mutagenesis4531M → A: Loss of transcriptional activation; when associated with A-454. Ref.1
Mutagenesis4541L → A: Loss of transcriptional activation; when associated with A-453. Ref.1
Sequence conflict1531K → N in BAC41450. Ref.2

Secondary structure

.............................. 458
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 63D36CFD37573152

FASTA45851,306
        10         20         30         40         50         60 
MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT DSVNHHSPGG 

        70         80         90        100        110        120 
SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL YDDCSSTIVE DPQTKCEYML 

       130        140        150        160        170        180 
NSMPKRLCLV CGDIASGYHY GVASCEACKA FFKRTIQGNI EYSCPATNEC EITKRRRKSC 

       190        200        210        220        230        240 
QACRFMKCLK VGMLKEGVRL DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH 

       250        260        270        280        290        300 
LLVAEPEKIY AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL 

       310        320        330        340        350        360 
LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL QLVKKYKSMK 

       370        380        390        400        410        420 
LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ DYEAGQHMED PRRAGKMLMT 

       430        440        450 
LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF LEMLEAKV 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 63F81CDBE3A9C2D5
Show »

FASTA43548,581

References

« Hide 'large scale' references
[1]"Hormone-independent transcriptional activation and coactivator binding by novel orphan nuclear receptor ERR3."
Hong H., Yang L., Stallcup M.R.
J. Biol. Chem. 274:22618-22626(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH GRIP1, MUTAGENESIS OF LEU-449; PHE-450; MET-453 AND LEU-454, FUNCTION, TISSUE SPECIFICITY.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H.
DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Kidney.
[4]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[5]"Structural basis for the deactivation of the estrogen-related receptor gamma by diethylstilbestrol or 4-hydroxytamoxifen and determinants of selectivity."
Greschik H., Flaig R., Renaud J.-P., Moras D.
J. Biol. Chem. 279:33639-33646(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 229-458 IN COMPLEXES WITH INVERSE AGONISTS, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF117254 mRNA. Translation: AAD48369.1.
AB093266 mRNA. Translation: BAC41450.1. Different initiation.
AK052731 mRNA. Translation: BAC35120.1.
BC082324 mRNA. Translation: AAH82324.1.
CCDSCCDS15606.1. [P62509-1]
CCDS56666.1. [P62509-2]
RefSeqNP_001230721.1. NM_001243792.1. [P62509-2]
NP_036065.1. NM_011935.3. [P62509-1]
XP_006497227.1. XM_006497164.1. [P62509-2]
XP_006497228.1. XM_006497165.1. [P62509-2]
XP_006497229.1. XM_006497166.1. [P62509-2]
XP_006497230.1. XM_006497167.1. [P62509-2]
XP_006497231.1. XM_006497168.1. [P62509-2]
XP_006497232.1. XM_006497169.1. [P62509-2]
XP_006497233.1. XM_006497170.1. [P62509-2]
UniGeneMm.388156.
Mm.421613.
Mm.89989.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9PX-ray2.13A/B/C/D232-458[»]
1S9QX-ray2.20A/B229-456[»]
ProteinModelPortalP62509.
SMRP62509. Positions 120-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204939. 4 interactions.
IntActP62509. 2 interactions.

Chemistry

BindingDBP62509.

PTM databases

PhosphoSiteP62509.

Proteomic databases

PRIDEP62509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027906; ENSMUSP00000027906; ENSMUSG00000026610. [P62509-1]
ENSMUST00000110938; ENSMUSP00000106563; ENSMUSG00000026610. [P62509-2]
ENSMUST00000110939; ENSMUSP00000106564; ENSMUSG00000026610. [P62509-2]
GeneID26381.
KEGGmmu:26381.
UCSCuc007eaa.2. mouse. [P62509-1]

Organism-specific databases

CTD2104.
MGIMGI:1347056. Esrrg.
RougeSearch...

Phylogenomic databases

eggNOGNOG282629.
GeneTreeENSGT00730000110346.
HOGENOMHOG000233467.
HOVERGENHBG108344.
InParanoidP62509.
KOK08554.
OMAHVEDPRR.
PhylomeDBP62509.
TreeFamTF323751.

Gene expression databases

ArrayExpressP62509.
BgeeP62509.
CleanExMM_ESRRG.
GenevestigatorP62509.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR027289. Oest-rel_rcp.
IPR024178. Oest_rcpt/oest-rel_rcp.
IPR003078. Retinoic_acid_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.
PRINTSPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304297.
PROP62509.
SOURCESearch...

Entry information

Entry nameERR3_MOUSE
AccessionPrimary (citable) accession number: P62509
Secondary accession number(s): O75454 expand/collapse secondary AC list , O96021, Q8CHC9, Q9R1F3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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