P62508 (ERR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.14 Ref.15 Ref.16
Subunit structure	Homodimer. Binds TLE1, PNRC1 and PNRC2. Binds GRIP1 By similarity. Interacts with NRIP1, NCOA1 and NCOR2. Ref.12 Ref.18
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	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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	AF-2 domain binding Inferred from sequence or structural similarity. 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...

Alternative products

This entry describes 4 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 458

458

Estrogen-related receptor gamma

PRO_0000053665

Regions

DNA binding

125 – 200

76

Nuclear receptor

Zinc finger

128 – 148

21

NR C4-type

Zinc finger

164 – 188

25

NR C4-type

Amino acid modifications

Modified residue

45

1

Phosphoserine Probable

Cross-link

40

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.13 Ref.14 Ref.15

Natural variations

Alternative sequence

1 – 23

23

Missing in isoform 2, isoform 3 and isoform 4.

VSP_003702

Alternative sequence

158 – 196

39

Missing in isoform 4.

VSP_045980

Alternative sequence

234

1

Y → LLWSDPAD in isoform 3.

VSP_013301

Natural variant

50

1

T → M. Ref.7
Corresponds to variant rs11572693 [ dbSNP | Ensembl ].

VAR_019229

Experimental info

Mutagenesis

38

1

F → A or E: No effect on transcriptional activity. Ref.14

Mutagenesis

39

1

I → A: 4-fold increase in transcriptional activity. Ref.14

Mutagenesis

40

1

K → R: Abolishes sumoylation. 7-fold increase in transcriptional activity. Ref.13 Ref.14 Ref.15

Mutagenesis

41

1

T → A: No effect on transcriptional activity. Ref.14

Mutagenesis

42

1

E → A: 4-fold increase in transcriptional activity. Ref.14

Mutagenesis

44

1

S → A or E: No effect on transcriptional activity. Ref.14

Mutagenesis

45

1

S → A: Abolishes sumoylation. Increased transcriptional activity. Ref.14 Ref.15

Mutagenesis

45

1

S → D: No change in sumoylation nor transcriptional activity. Ref.14 Ref.15

Sequence conflict

19

1

E → K in AAQ93376. Ref.4

Sequence conflict

151

1

F → S in AAC39899. Ref.3

Sequence conflict

155

1

T → K in AAC39899. Ref.3

Sequence conflict

158

1

G → A in AAC39899. Ref.3

Sequence conflict

227

1

V → A in BAG54746. Ref.5

Sequence conflict

271

1

L → C in AAC39899. Ref.3

Sequence conflict

313

1

V → F in AAC39899. Ref.3

Sequence conflict

449

1

L → P in CAH18320. Ref.5

Sequence conflict

458

1

V → VC in AAC39899. Ref.3

Secondary structure

1

.

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458

Helix Strand Turn

Details...

Helix

236 – 243

8

Beta strand

255 – 257

3

Helix

261 – 283

23

Helix

289 – 291

3

Helix

294 – 316

23

Turn

317 – 319

3

Beta strand

320 – 322

3

Beta strand

324 – 327

4

Beta strand

330 – 332

3

Helix

334 – 339

6

Helix

343 – 359

17

Helix

363 – 375

13

Helix

385 – 406

22

Helix

413 – 418

6

Helix

421 – 441

21

Helix

448 – 454

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 63D36CFD37573152	FASTA	458	51,306
	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
	Isoform 2 (Short) [UniParc] [UniParc]. Checksum: 63F81CDBE3A9C2D5	FASTA	435	48,581
	10 20 30 40 50 60 MSNKDRHIDS SCSSFIKTEP SSPASLTDSV NHHSPGGSSD ASGSYSSTMN GHQNGLDSPP 70 80 90 100 110 120 LYPSAPILGG SGPVRKLYDD CSSTIVEDPQ TKCEYMLNSM PKRLCLVCGD IASGYHYGVA 130 140 150 160 170 180 SCEACKAFFK RTIQGNIEYS CPATNECEIT KRRRKSCQAC RFMKCLKVGM LKEGVRLDRV 190 200 210 220 230 240 RGGRQKYKRR IDAENSPYLN PQLVQPAKKP YNKIVSHLLV AEPEKIYAMP DPTVPDSDIK 250 260 270 280 290 300 ALTTLCDLAD RELVVIIGWA KHIPGFSTLS LADQMSLLQS AWMEILILGV VYRSLSFEDE 310 320 330 340 350 360 LVYADDYIMD EDQSKLAGLL DLNNAILQLV KKYKSMKLEK EEFVTLKAIA LANSDSMHIE 370 380 390 400 410 420 DVEAVQKLQD VLHEALQDYE AGQHMEDPRR AGKMLMTLPL LRQTSTKAVQ HFYNIKLEGK 430 VPMHKLFLEM LEAKV
	Isoform 3 [UniParc]. Checksum: 09B8CD0EE90CAEF5	FASTA	442	49,316
	10 20 30 40 50 60 MSNKDRHIDS SCSSFIKTEP SSPASLTDSV NHHSPGGSSD ASGSYSSTMN GHQNGLDSPP 70 80 90 100 110 120 LYPSAPILGG SGPVRKLYDD CSSTIVEDPQ TKCEYMLNSM PKRLCLVCGD IASGYHYGVA 130 140 150 160 170 180 SCEACKAFFK RTIQGNIEYS CPATNECEIT KRRRKSCQAC RFMKCLKVGM LKEGVRLDRV 190 200 210 220 230 240 RGGRQKYKRR IDAENSPYLN PQLVQPAKKP LLWSDPADNK IVSHLLVAEP EKIYAMPDPT 250 260 270 280 290 300 VPDSDIKALT TLCDLADREL VVIIGWAKHI PGFSTLSLAD QMSLLQSAWM EILILGVVYR 310 320 330 340 350 360 SLSFEDELVY ADDYIMDEDQ SKLAGLLDLN NAILQLVKKY KSMKLEKEEF VTLKAIALAN 370 380 390 400 410 420 SDSMHIEDVE AVQKLQDVLH EALQDYEAGQ HMEDPRRAGK MLMTLPLLRQ TSTKAVQHFY 430 440 NIKLEGKVPM HKLFLEMLEA KV
	Isoform 4 [UniParc]. Checksum: 614E044D8A31361C	FASTA	396	44,073
	10 20 30 40 50 60 MSNKDRHIDS SCSSFIKTEP SSPASLTDSV NHHSPGGSSD ASGSYSSTMN GHQNGLDSPP 70 80 90 100 110 120 LYPSAPILGG SGPVRKLYDD CSSTIVEDPQ TKCEYMLNSM PKRLCLVCGD IASGYHYGVA 130 140 150 160 170 180 SCEACKAFFK RTIQGVRLDR VRGGRQKYKR RIDAENSPYL NPQLVQPAKK PYNKIVSHLL 190 200 210 220 230 240 VAEPEKIYAM PDPTVPDSDI KALTTLCDLA DRELVVIIGW AKHIPGFSTL SLADQMSLLQ 250 260 270 280 290 300 SAWMEILILG VVYRSLSFED ELVYADDYIM DEDQSKLAGL LDLNNAILQL VKKYKSMKLE 310 320 330 340 350 360 KEEFVTLKAI ALANSDSMHI EDVEAVQKLQ DVLHEALQDY EAGQHMEDPR RAGKMLMTLP 370 380 390 LLRQTSTKAV QHFYNIKLEG KVPMHKLFLE MLEAKV

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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, MASS SPECTROMETRY.
[17]	"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.
[18]	"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.

Web resources

NIEHS-SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00025743.
IPI00427737.
IPI00554597.
IPI00940244.

RefSeq

NP_001127757.1. NM_001134285.2.
NP_001230434.1. NM_001243505.1.
NP_001230435.1. NM_001243506.1.
NP_001230436.1. NM_001243507.1.
NP_001230438.1. NM_001243509.1.
NP_001230439.1. NM_001243510.1.
NP_001230440.1. NM_001243511.1.
NP_001230441.1. NM_001243512.1.
NP_001230442.1. NM_001243513.1.
NP_001230443.1. NM_001243514.1.
NP_001230444.1. NM_001243515.1.
NP_001230447.1. NM_001243518.1.
NP_001230448.1. NM_001243519.1.
NP_001429.2. NM_001438.3.
NP_996317.1. NM_206594.2.
NP_996318.1. NM_206595.2.

UniGene

Hs.444225.
Hs.738938.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KV6	X-ray	2.70	A/B	229-458	[»]
1TFC	X-ray	2.40	A/B	229-458	[»]
1VJB	X-ray	3.20	A/B	229-458	[»]
2E2R	X-ray	1.60	A	222-458	[»]
2EWP	X-ray	2.30	A/B/C/D/E	233-458	[»]
2GP7	X-ray	2.45	A/B/C/D	229-458	[»]
2GPO	X-ray	1.95	A	229-458	[»]
2GPP	X-ray	2.60	A/B	229-458	[»]
2GPU	X-ray	1.70	A	229-458	[»]
2GPV	X-ray	2.85	A/B/C/D/E/F	229-458	[»]
2P7A	X-ray	2.30	A	229-458	[»]
2P7G	X-ray	2.10	A	229-458	[»]
2P7Z	X-ray	2.50	A	229-458	[»]
2ZAS	X-ray	2.00	A	222-458	[»]
2ZBS	X-ray	1.80	A	222-458	[»]
2ZKC	X-ray	1.70	A	222-458	[»]

ProteinModelPortal

P62508.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62508. 3 interactions.

MINT

MINT-4824700.

PTM databases

PhosphoSite

P62508.

Polymorphism databases

DMDM

50402102.

Proteomic databases

PaxDb

P62508.

PRIDE

P62508.

Protocols and materials databases

DNASU

2104.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359162; ENSP00000352077; ENSG00000196482.
ENST00000360012; ENSP00000353108; ENSG00000196482.
ENST00000361395; ENSP00000354584; ENSG00000196482.
ENST00000361525; ENSP00000355225; ENSG00000196482.
ENST00000366938; ENSP00000355905; ENSG00000196482.
ENST00000366940; ENSP00000355907; ENSG00000196482.
ENST00000391890; ENSP00000375761; ENSG00000196482.
ENST00000408911; ENSP00000386171; ENSG00000196482.
ENST00000463665; ENSP00000418629; ENSG00000196482.
ENST00000487276; ENSP00000419155; ENSG00000196482.
ENST00000493603; ENSP00000419594; ENSG00000196482.
ENST00000493748; ENSP00000417374; ENSG00000196482.

GeneID

2104.

KEGG

hsa:2104.

UCSC

uc001hkw.2. human.
uc001hkz.2. human.

Organism-specific databases

CTD

2104.

GeneCards

GC01M216676.

HGNC

HGNC:3474. ESRRG.

HPA

HPA044678.

MIM

602969. gene.

neXtProt

NX_P62508.

PharmGKB

PA27891.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG282629.

HOVERGEN

HBG108344.

InParanoid

P62508.

KO

K08554.

Enzyme and pathway databases

Reactome

REACT_71. Gene Expression.

SignaLink

P62508.

Gene expression databases

ArrayExpress

P62508.

Bgee

P62508.

Genevestigator

P62508.

GermOnline

ENSG00000196482. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.
3.30.50.10. 1 hit.

InterPro

IPR008946. 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]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PIRSF

PIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.

PRINTS

PR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P62508.

ChEMBL

CHEMBL4245.

ChiTaRS

ESRRG. human.

DrugBank

DB00255. Diethylstilbestrol.

EvolutionaryTrace

P62508.

GenomeRNAi

2104.

NextBio

8511.

SOURCE

Search...

Entry information

Entry name

ERR3_HUMAN

Accession

Primary (citable) accession number: P62508
Secondary accession number(s): A8K4I0 , A8K6I2, B3KY84, E9PGB7, 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:	May 29, 2013
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.