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P62508

- ERR3_HUMAN

UniProt

P62508 - ERR3_HUMAN

Protein

Estrogen-related receptor gamma

Gene

ESRRG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    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.By similarity4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi125 – 20076Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri128 – 14821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri164 – 18825NR C4-typePROSITE-ProRule annotationAdd
    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

    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 Curated

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    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 gammaPRO_0000053665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki40 – 40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei45 – 451Phosphoserine2 Publications

    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.By similarity3 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

    1
    458
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62508.

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri128 – 14821NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri164 – 18825NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191E → K in AAQ93376. (PubMed:10707956)Curated
    Sequence conflicti151 – 1511F → S in AAC39899. (PubMed:9676434)Curated
    Sequence conflicti155 – 1551T → K in AAC39899. (PubMed:9676434)Curated
    Sequence conflicti158 – 1581G → A in AAC39899. (PubMed:9676434)Curated
    Sequence conflicti227 – 2271V → A in BAG54746. (PubMed:14702039)Curated
    Sequence conflicti271 – 2711L → C in AAC39899. (PubMed:9676434)Curated
    Sequence conflicti313 – 3131V → F in AAC39899. (PubMed:9676434)Curated
    Sequence conflicti449 – 4491L → P in CAH18320. (PubMed:14702039)Curated
    Sequence conflicti458 – 4581V → VC in AAC39899. (PubMed:9676434)Curated

    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. 5 PublicationsVSP_003702Add
    BLAST
    Alternative sequencei1 – 1919MDSVE…HYEEE → MWRECDWGLGAVKSDLACVP SAKR in isoform 5. CuratedVSP_047156Add
    BLAST
    Alternative sequencei158 – 19639Missing in isoform 4. 1 PublicationVSP_045980Add
    BLAST
    Alternative sequencei234 – 2341Y → LLWSDPAD in isoform 3 and isoform 5. 1 PublicationVSP_013301

    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

    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: October 1, 2014
    This is version 131 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