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P62508

- ERR3_HUMAN

UniProt

P62508 - ERR3_HUMAN

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Protein
Estrogen-related receptor gamma
Gene
ESRRG, ERR3, ERRG2, KIAA0832, NR3B3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi125 – 20076Nuclear receptor
Add
BLAST
Zinc fingeri128 – 14821NR C4-type
Add
BLAST
Zinc fingeri164 – 18825NR C4-type
Add
BLAST

GO - Molecular functioni

  1. AF-2 domain binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. retinoic acid receptor activity Source: InterPro
  4. sequence-specific DNA binding Source: InterPro
  5. steroid binding Source: InterPro
  6. steroid hormone receptor activity Source: InterPro
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. positive regulation of transcription, DNA-templated Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: UniProtKB
  4. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP62508.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ESRRG
Synonyms:ERR3, ERRG2, KIAA0832, NR3B3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3474. ESRRG.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381F → A or E: No effect on transcriptional activity. 1 Publication
Mutagenesisi39 – 391I → A: 4-fold increase in transcriptional activity. 1 Publication
Mutagenesisi40 – 401K → R: Abolishes sumoylation. 7-fold increase in transcriptional activity. 3 Publications
Mutagenesisi41 – 411T → A: No effect on transcriptional activity. 1 Publication
Mutagenesisi42 – 421E → A: 4-fold increase in transcriptional activity. 1 Publication
Mutagenesisi44 – 441S → A or E: No effect on transcriptional activity. 1 Publication
Mutagenesisi45 – 451S → A: Abolishes sumoylation. Increased transcriptional activity. 2 Publications
Mutagenesisi45 – 451S → D: No change in sumoylation nor transcriptional activity. 2 Publications

Organism-specific databases

PharmGKBiPA27891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Estrogen-related receptor gamma
PRO_0000053665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki40 – 40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)3 Publications
Modified residuei45 – 451Phosphoserine Inferred

Post-translational modificationi

Acetylated by PCAF/KAT2 (in vitro).1 Publication
Sumoylation on Lys-40 is enhanced by phosphorylation at Ser-45 and represses transcriptional activity.3 Publications
Phosphorylation on Ser-45 enhances sumoylation on Lys-40 thus repressing transcriptional activity.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62508.
PaxDbiP62508.
PRIDEiP62508.

PTM databases

PhosphoSiteiP62508.

Expressioni

Tissue specificityi

Expressed in the heart, kidney, brain, lung, bone marrow, adrenal gland, trachea, spinal cord and thyroid gland.2 Publications

Developmental stagei

Expressed at high levels in fetal brain and also in the fetal kidney, lung and liver.1 Publication

Gene expression databases

ArrayExpressiP62508.
BgeeiP62508.
GenevestigatoriP62508.

Organism-specific databases

HPAiHPA044678.

Interactioni

Subunit structurei

Homodimer. Binds TLE1, PNRC1 and PNRC2. Binds GRIP1 By similarity. Interacts with NRIP1, NCOA1 and NCOR2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPARGC1AQ9UBK23EBI-2834260,EBI-765486

Protein-protein interaction databases

BioGridi108407. 24 interactions.
IntActiP62508. 6 interactions.
MINTiMINT-4824700.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi236 – 2438
Beta strandi255 – 2573
Helixi261 – 28323
Helixi289 – 2913
Helixi294 – 31623
Turni317 – 3193
Beta strandi320 – 3223
Beta strandi324 – 3274
Beta strandi330 – 3323
Helixi334 – 3396
Helixi343 – 35917
Helixi363 – 37513
Helixi385 – 40622
Helixi413 – 4186
Helixi421 – 44121
Helixi448 – 4547

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP62508.
SMRiP62508. Positions 120-458.

Miscellaneous databases

EvolutionaryTraceiP62508.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG282629.
HOVERGENiHBG108344.
InParanoidiP62508.
KOiK08554.
OMAiHVEDPRR.
OrthoDBiEOG7288S1.
PhylomeDBiP62508.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.
PRINTSiPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62508-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDSVELCLPE SFSLHYEEEL LCRMSNKDRH IDSSCSSFIK TEPSSPASLT    50
DSVNHHSPGG SSDASGSYSS TMNGHQNGLD SPPLYPSAPI LGGSGPVRKL 100
YDDCSSTIVE DPQTKCEYML NSMPKRLCLV CGDIASGYHY GVASCEACKA 150
FFKRTIQGNI EYSCPATNEC EITKRRRKSC QACRFMKCLK VGMLKEGVRL 200
DRVRGGRQKY KRRIDAENSP YLNPQLVQPA KKPYNKIVSH LLVAEPEKIY 250
AMPDPTVPDS DIKALTTLCD LADRELVVII GWAKHIPGFS TLSLADQMSL 300
LQSAWMEILI LGVVYRSLSF EDELVYADDY IMDEDQSKLA GLLDLNNAIL 350
QLVKKYKSMK LEKEEFVTLK AIALANSDSM HIEDVEAVQK LQDVLHEALQ 400
DYEAGQHMED PRRAGKMLMT LPLLRQTSTK AVQHFYNIKL EGKVPMHKLF 450
LEMLEAKV 458
Length:458
Mass (Da):51,306
Last modified:July 19, 2004 - v1
Checksum:i63D36CFD37573152
GO
Isoform 2 (identifier: P62508-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: Short

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

Show »
Length:435
Mass (Da):48,581
Checksum:i63F81CDBE3A9C2D5
GO
Isoform 3 (identifier: P62508-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     234-234: Y → LLWSDPAD

Show »
Length:442
Mass (Da):49,316
Checksum:i09B8CD0EE90CAEF5
GO
Isoform 4 (identifier: P62508-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
     158-196: Missing.

Note: No experimental confirmation available.

Show »
Length:396
Mass (Da):44,073
Checksum:i614E044D8A31361C
GO
Isoform 5 (identifier: P62508-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:470
Mass (Da):52,462
Checksum:iC0C4BD53ABAF5CE4
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501T → M.1 Publication
Corresponds to variant rs11572693 [ dbSNP | Ensembl ].
VAR_019229

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform 2, isoform 3 and isoform 4.
VSP_003702Add
BLAST
Alternative sequencei1 – 1919MDSVE…HYEEE → MWRECDWGLGAVKSDLACVP SAKR in isoform 5.
VSP_047156Add
BLAST
Alternative sequencei158 – 19639Missing in isoform 4.
VSP_045980Add
BLAST
Alternative sequencei234 – 2341Y → LLWSDPAD in isoform 3 and isoform 5.
VSP_013301

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191E → K in AAQ93376. 1 Publication
Sequence conflicti151 – 1511F → S in AAC39899. 1 Publication
Sequence conflicti155 – 1551T → K in AAC39899. 1 Publication
Sequence conflicti158 – 1581G → A in AAC39899. 1 Publication
Sequence conflicti227 – 2271V → A in BAG54746. 1 Publication
Sequence conflicti271 – 2711L → C in AAC39899. 1 Publication
Sequence conflicti313 – 3131V → F in AAC39899. 1 Publication
Sequence conflicti449 – 4491L → P in CAH18320. 1 Publication
Sequence conflicti458 – 4581V → VC in AAC39899. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1517.1. [P62508-2]
CCDS41468.1.
CCDS58060.1. [P62508-4]
CCDS58061.1. [P62508-5]
RefSeqiNP_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]
UniGeneiHs.444225.
Hs.738938.

Genome annotation databases

EnsembliENST00000359162; 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]
GeneIDi2104.
KEGGihsa:2104.
UCSCiuc001hkw.2. human.

Polymorphism databases

DMDMi50402102.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1517.1. [P62508-2 ]
CCDS41468.1.
CCDS58060.1. [P62508-4 ]
CCDS58061.1. [P62508-5 ]
RefSeqi NP_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 ]
UniGenei Hs.444225.
Hs.738938.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P62508.
SMRi P62508. Positions 120-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108407. 24 interactions.
IntActi P62508. 6 interactions.
MINTi MINT-4824700.

Chemistry

BindingDBi P62508.
ChEMBLi CHEMBL4245.
DrugBanki DB00255. Diethylstilbestrol.
GuidetoPHARMACOLOGYi 624.

PTM databases

PhosphoSitei P62508.

Polymorphism databases

DMDMi 50402102.

Proteomic databases

MaxQBi P62508.
PaxDbi P62508.
PRIDEi P62508.

Protocols and materials databases

DNASUi 2104.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359162 ; 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 ]
GeneIDi 2104.
KEGGi hsa:2104.
UCSCi uc001hkw.2. human.

Organism-specific databases

CTDi 2104.
GeneCardsi GC01M216676.
HGNCi HGNC:3474. ESRRG.
HPAi HPA044678.
MIMi 602969. gene.
neXtProti NX_P62508.
PharmGKBi PA27891.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282629.
HOVERGENi HBG108344.
InParanoidi P62508.
KOi K08554.
OMAi HVEDPRR.
OrthoDBi EOG7288S1.
PhylomeDBi P62508.
TreeFami TF323751.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P62508.

Miscellaneous databases

ChiTaRSi ESRRG. human.
EvolutionaryTracei P62508.
GeneWikii Estrogen-related_receptor_gamma.
GenomeRNAii 2104.
NextBioi 8511.
PROi P62508.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62508.
Bgeei P62508.
Genevestigatori P62508.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PIRSFi PIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.
PRINTSi PR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiERR3_HUMAN
AccessioniPrimary (citable) accession number: P62508
Secondary accession number(s): A8K4I0
, A8K6I2, B3KY84, E9PGB7, F8W8J3, O75454, O96021, Q68DA0, Q6P274, Q6PK28, Q6TS38, Q9R1F3, Q9UNJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: September 3, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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