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P62508 (ERR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen-related receptor gamma
Alternative name(s):
ERR gamma-2
Estrogen receptor-related protein 3
Nuclear receptor subfamily 3 group B member 3
Gene names
Name:ESRRG
Synonyms:ERR3, ERRG2, KIAA0832, NR3B3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity. Induces the expression of PERM1 in the skeletal muscle. Ref.14 Ref.15 Ref.17 Ref.18

Subunit structure

Homodimer. Binds TLE1, PNRC1 and PNRC2. Binds GRIP1 By similarity. Interacts with NRIP1, NCOA1 and NCOR2. Ref.12 Ref.20

Subcellular location

Nucleus Probable.

Tissue specificity

Expressed in the heart, kidney, brain, lung, bone marrow, adrenal gland, trachea, spinal cord and thyroid gland. Ref.3 Ref.12

Developmental stage

Expressed at high levels in fetal brain and also in the fetal kidney, lung and liver. Ref.3

Post-translational modification

Acetylated by PCAF/KAT2 (in vitro). Ref.16

Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and represses transcriptional activity. Ref.13 Ref.14 Ref.15

Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus repressing transcriptional activity. Ref.13 Ref.14 Ref.15

Miscellaneous

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

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence AAH08218.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA74855.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPARGC1AQ9UBK23EBI-2834260,EBI-765486

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62508-1)

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: P62508-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Isoform 3 (identifier: P62508-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     234-234: Y → LLWSDPAD
Isoform 4 (identifier: P62508-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     158-196: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P62508-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MDSVELCLPESFSLHYEEE → MWRECDWGLGAVKSDLACVPSAKR
     234-234: Y → LLWSDPAD
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Estrogen-related receptor gamma
PRO_0000053665

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) Ref.13 Ref.14 Ref.15

Natural variations

Alternative sequence1 – 2323Missing in isoform 2, isoform 3 and isoform 4.
VSP_003702
Alternative sequence1 – 1919MDSVE…HYEEE → MWRECDWGLGAVKSDLACVP SAKR in isoform 5.
VSP_047156
Alternative sequence158 – 19639Missing in isoform 4.
VSP_045980
Alternative sequence2341Y → LLWSDPAD in isoform 3 and isoform 5.
VSP_013301
Natural variant501T → M. Ref.7
Corresponds to variant rs11572693 [ dbSNP | Ensembl ].
VAR_019229

Experimental info

Mutagenesis381F → A or E: No effect on transcriptional activity. Ref.14
Mutagenesis391I → A: 4-fold increase in transcriptional activity. Ref.14
Mutagenesis401K → R: Abolishes sumoylation. 7-fold increase in transcriptional activity. Ref.13 Ref.14 Ref.15
Mutagenesis411T → A: No effect on transcriptional activity. Ref.14
Mutagenesis421E → A: 4-fold increase in transcriptional activity. Ref.14
Mutagenesis441S → A or E: No effect on transcriptional activity. Ref.14
Mutagenesis451S → A: Abolishes sumoylation. Increased transcriptional activity. Ref.14 Ref.15
Mutagenesis451S → D: No change in sumoylation nor transcriptional activity. Ref.14 Ref.15
Sequence conflict191E → K in AAQ93376. Ref.4
Sequence conflict1511F → S in AAC39899. Ref.3
Sequence conflict1551T → K in AAC39899. Ref.3
Sequence conflict1581G → A in AAC39899. Ref.3
Sequence conflict2271V → A in BAG54746. Ref.5
Sequence conflict2711L → C in AAC39899. Ref.3
Sequence conflict3131V → F in AAC39899. Ref.3
Sequence conflict4491L → P in CAH18320. Ref.5
Sequence conflict4581V → VC in AAC39899. Ref.3

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] [UniParc].

Checksum: 63F81CDBE3A9C2D5
Show »

FASTA43548,581
Isoform 3 [UniParc].

Checksum: 09B8CD0EE90CAEF5
Show »

FASTA44249,316
Isoform 4 [UniParc].

Checksum: 614E044D8A31361C
Show »

FASTA39644,073
Isoform 5 [UniParc].

Checksum: C0C4BD53ABAF5CE4
Show »

FASTA47052,462

References

« Hide 'large scale' references
[1]"Identification of two hERR2-related novel nuclear receptors utilizing bioinformatics and inverse PCR."
Chen F., Zhang Q., McDonald T., Davidoff M.J., Bailey W., Bai C., Liu Q., Caskey C.T.
Gene 228:101-109(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"Isolation of a gene encoding a novel member of the nuclear receptor superfamily from the critical region of Usher syndrome type IIa at 1q41."
Eudy J.D., Yao S.F., Weston M.D., Ma-Edmonds M., Talmadge C.B., Cheng J.J., Kimberling W.J., Sumegi J.
Genomics 50:382-384(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[4]"Human ERRgamma, a third member of the estrogen receptor-related receptor (ERR) subfamily of orphan nuclear receptors: tissue-specific isoforms are expressed during development and in the adult."
Heard D.J., Norby P.L., Holloway J., Vissing H.
Mol. Endocrinol. 14:382-392(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney, Retina and Skeletal muscle.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
Tissue: Brain and Placenta.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[7]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-50.
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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] (ISOFORMS 2 AND 3).
Tissue: Eye and Placenta.
[11]"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] OF 1-129 (ISOFORM 1).
Tissue: Brain.
[12]"Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRgamma."
Hentschke M., Borgmeyer U.
Biochem. Biophys. Res. Commun. 312:975-982(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TLE1 AND PNRC2, TISSUE SPECIFICITY.
[13]"PDSM, a motif for phosphorylation-dependent SUMO modification."
Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L.
Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-40, MUTAGENESIS OF LYS-40.
[14]"Transcriptional ERRgamma2-mediated activation is regulated by sentrin-specific proteases."
Hentschke M., Suesens U., Borgmeyer U.
Biochem. J. 419:167-176(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, MUTAGENESIS OF PHE-38; ILE-39; LYS-40; THR-41; GLU-42; SER-44 AND SER-45.
[15]"Phosphorylation-dependent sumoylation regulates estrogen-related receptor-alpha and -gamma transcriptional activity through a synergy control motif."
Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.
Mol. Endocrinol. 22:570-584(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-40, PHOSPHORYLATION AT SER-45, FUNCTION, MUTAGENESIS OF LYS-40 AND SER-45.
[16]"An acetylation switch modulates the transcriptional activity of estrogen-related receptor alpha."
Wilson B.J., Tremblay A.M., Deblois G., Sylvain-Drolet G., Giguere V.
Mol. Endocrinol. 24:1349-1358(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION BY PCAF/KAT2B.
[17]"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."
Cho Y., Hazen B.C., Russell A.P., Kralli A.
J. Biol. Chem. 288:25207-25218(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3."
Greschik H., Wurtz J.-M., Sanglier S., Bourguet W., van Dorsselaer A., Moras D., Renaud J.-P.
Mol. Cell 9:303-313(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 229-458 IN COMPLEXES WITH INVERSE AGONISTS AND NCOA1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Structure-guided synthesis of tamoxifen analogs with improved selectivity for the orphan ERRgamma."
Chao E.Y.H., Collins J.L., Gaillard S., Miller A.B., Wang L., Orband-Miller L.A., Nolte R.T., McDonnell D.P., Willson T.M., Zuercher W.J.
Bioorg. Med. Chem. Lett. 16:821-824(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 233-458 IN COMPLEX WITH INVERSE AGONIST.
[20]"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 (1.70 ANGSTROMS) OF 229-458 IN COMPLEXES WITH AGONIST AND INVERSE AGONIST; NRIP1 AND NCOR2, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF094518 mRNA. Translation: AAC99410.1.
AB020639 mRNA. Translation: BAA74855.2. Different initiation.
AF058291 mRNA. Translation: AAC39899.1.
AY388456 mRNA. Translation: AAQ93376.1.
AY388457 mRNA. Translation: AAQ93377.1.
AY388458 mRNA. Translation: AAQ93378.1.
AY388459 mRNA. Translation: AAQ93379.1.
AY388460 mRNA. Translation: AAQ93380.1.
AY388461 mRNA. Translation: AAQ93381.1.
AK131193 mRNA. Translation: BAG54746.1.
AK290945 mRNA. Translation: BAF83634.1.
AK291028 mRNA. Translation: BAF83717.1.
AK291647 mRNA. Translation: BAF84336.1.
CR749497 mRNA. Translation: CAH18320.1.
AY528719 Genomic DNA. Translation: AAS00098.1.
AL445650, AL512650, AC096635 Genomic DNA. Translation: CAH70618.1.
AL445650, AC096635, AL512650 Genomic DNA. Translation: CAH70619.1.
AL512650, AC096635, AL445650 Genomic DNA. Translation: CAH71594.1.
AL512650, AC096635, AL445650 Genomic DNA. Translation: CAH71595.1.
AC096634 Genomic DNA. No translation available.
AL391216 Genomic DNA. No translation available.
AL512626 Genomic DNA. No translation available.
AL513312 Genomic DNA. No translation available.
AL603752 Genomic DNA. No translation available.
CH471100 Genomic DNA. Translation: EAW93335.1.
BC008218 mRNA. Translation: AAH08218.1. Sequence problems.
BC064700 mRNA. Translation: AAH64700.1.
AF117255 mRNA. Translation: AAD48370.1.
CCDSCCDS1517.1. [P62508-2]
CCDS41468.1.
CCDS58060.1. [P62508-4]
CCDS58061.1. [P62508-5]
RefSeqNP_001127757.1. NM_001134285.2. [P62508-2]
NP_001230434.1. NM_001243505.1.
NP_001230435.1. NM_001243506.1.
NP_001230436.1. NM_001243507.1. [P62508-4]
NP_001230438.1. NM_001243509.1. [P62508-2]
NP_001230439.1. NM_001243510.1. [P62508-2]
NP_001230440.1. NM_001243511.1. [P62508-2]
NP_001230441.1. NM_001243512.1. [P62508-2]
NP_001230442.1. NM_001243513.1. [P62508-2]
NP_001230443.1. NM_001243514.1. [P62508-2]
NP_001230444.1. NM_001243515.1. [P62508-2]
NP_001230447.1. NM_001243518.1. [P62508-5]
NP_001230448.1. NM_001243519.1. [P62508-2]
NP_001429.2. NM_001438.3. [P62508-1]
NP_996317.1. NM_206594.2. [P62508-2]
NP_996318.1. NM_206595.2. [P62508-2]
XP_006711268.1. XM_006711205.1. [P62508-2]
XP_006711269.1. XM_006711206.1. [P62508-2]
XP_006711270.1. XM_006711207.1. [P62508-2]
XP_006711271.1. XM_006711208.1. [P62508-2]
XP_006711272.1. XM_006711209.1. [P62508-2]
UniGeneHs.444225.
Hs.738938.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KV6X-ray2.70A/B229-458[»]
1TFCX-ray2.40A/B229-458[»]
1VJBX-ray3.20A/B229-458[»]
2E2RX-ray1.60A222-458[»]
2EWPX-ray2.30A/B/C/D/E233-458[»]
2GP7X-ray2.45A/B/C/D229-458[»]
2GPOX-ray1.95A229-458[»]
2GPPX-ray2.60A/B229-458[»]
2GPUX-ray1.70A229-458[»]
2GPVX-ray2.85A/B/C/D/E/F229-458[»]
2P7AX-ray2.30A229-458[»]
2P7GX-ray2.10A229-458[»]
2P7ZX-ray2.50A229-458[»]
2ZASX-ray2.00A222-458[»]
2ZBSX-ray1.80A222-458[»]
2ZKCX-ray1.70A222-458[»]
ProteinModelPortalP62508.
SMRP62508. Positions 120-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108407. 24 interactions.
IntActP62508. 6 interactions.
MINTMINT-4824700.

Chemistry

BindingDBP62508.
ChEMBLCHEMBL4245.
DrugBankDB00255. Diethylstilbestrol.
GuidetoPHARMACOLOGY624.

PTM databases

PhosphoSiteP62508.

Polymorphism databases

DMDM50402102.

Proteomic databases

MaxQBP62508.
PaxDbP62508.
PRIDEP62508.

Protocols and materials databases

DNASU2104.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359162; ENSP00000352077; ENSG00000196482. [P62508-2]
ENST00000360012; ENSP00000353108; ENSG00000196482. [P62508-2]
ENST00000361395; ENSP00000354584; ENSG00000196482. [P62508-2]
ENST00000361525; ENSP00000355225; ENSG00000196482. [P62508-2]
ENST00000366937; ENSP00000355904; ENSG00000196482. [P62508-5]
ENST00000366938; ENSP00000355905; ENSG00000196482. [P62508-2]
ENST00000366940; ENSP00000355907; ENSG00000196482. [P62508-2]
ENST00000391890; ENSP00000375761; ENSG00000196482. [P62508-3]
ENST00000408911; ENSP00000386171; ENSG00000196482. [P62508-1]
ENST00000463665; ENSP00000418629; ENSG00000196482. [P62508-4]
ENST00000487276; ENSP00000419155; ENSG00000196482. [P62508-2]
ENST00000493603; ENSP00000419594; ENSG00000196482. [P62508-2]
ENST00000493748; ENSP00000417374; ENSG00000196482. [P62508-2]
GeneID2104.
KEGGhsa:2104.
UCSCuc001hkw.2. human.

Organism-specific databases

CTD2104.
GeneCardsGC01M216676.
HGNCHGNC:3474. ESRRG.
HPAHPA044678.
MIM602969. gene.
neXtProtNX_P62508.
PharmGKBPA27891.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG282629.
HOVERGENHBG108344.
InParanoidP62508.
KOK08554.
OMAHVEDPRR.
OrthoDBEOG7288S1.
PhylomeDBP62508.
TreeFamTF323751.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP62508.

Gene expression databases

ArrayExpressP62508.
BgeeP62508.
GenevestigatorP62508.

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

ChiTaRSESRRG. human.
EvolutionaryTraceP62508.
GeneWikiEstrogen-related_receptor_gamma.
GenomeRNAi2104.
NextBio8511.
PROP62508.
SOURCESearch...

Entry information

Entry nameERR3_HUMAN
AccessionPrimary (citable) accession number: P62508
Secondary accession number(s): A8K4I0 expand/collapse secondary AC list , A8K6I2, B3KY84, E9PGB7, F8W8J3, O75454, O96021, Q68DA0, Q6P274, Q6PK28, Q6TS38, Q9R1F3, Q9UNJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM