Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P11474

- ERR1_HUMAN

UniProt

P11474 - ERR1_HUMAN

Protein

Steroid hormone receptor ERR1

Gene

ESRRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei124 – 1241Required for DNA-dependent dimerization

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi76 – 15176Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri79 – 9921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri115 – 13420NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ProtInc
    3. protein binding Source: UniProtKB
    4. protein domain specific binding Source: UniProtKB
    5. sequence-specific DNA binding Source: UniProtKB
    6. steroid binding Source: InterPro
    7. steroid hormone receptor activity Source: InterPro
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cartilage development Source: Ensembl
    2. gene expression Source: Reactome
    3. intracellular receptor signaling pathway Source: GOC
    4. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    5. regulation of cell proliferation Source: Ensembl
    6. regulation of osteoblast differentiation Source: Ensembl
    7. regulation of osteoclast differentiation Source: Ensembl
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    SignaLinkiP11474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Steroid hormone receptor ERR1
    Alternative name(s):
    Estrogen receptor-like 1
    Estrogen-related receptor alpha
    Short name:
    ERR-alpha
    Nuclear receptor subfamily 3 group B member 1
    Gene namesi
    Name:ESRRA
    Synonyms:ERR1, ESRL1, NR3B1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3471. ESRRA.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. intercellular bridge Source: HPA
    2. microtubule cytoskeleton Source: HPA
    3. nucleolus Source: HPA
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141K → R: Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403. 2 Publications
    Mutagenesisi19 – 191S → A: 50% loss of phosphorylation but represses transactivation activity in the absence of coactivator. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in response to coactivator; when associated with A-22. 2 Publications
    Mutagenesisi19 – 191S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-22. 2 Publications
    Mutagenesisi22 – 221S → A: 15% loss of phosphorylation but little transactivating activity. Almost complete loss of phosphorylation and 2-fold loss of repression of transactivation activity in the presence of coactivator; when associated with A-19. 2 Publications
    Mutagenesisi22 – 221S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-19. 2 Publications
    Mutagenesisi118 – 1181S → A: Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A. 1 Publication
    Mutagenesisi124 – 1241T → A: Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A. 1 Publication
    Mutagenesisi129 – 1291K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-138, R-160 and R-162. 1 Publication
    Mutagenesisi138 – 1381K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-160 and R-162. 1 Publication
    Mutagenesisi160 – 1601K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-162. 1 Publication
    Mutagenesisi162 – 1621K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-160. 1 Publication
    Mutagenesisi258 – 2625MSVLQ → VSVLE: Almost complete loss of interaction to L2 or to L3 of PPARGC1A.
    Mutagenesisi259 – 2591S → H: Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A. 1 Publication
    Mutagenesisi315 – 3151R → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. 1 Publication
    Mutagenesisi338 – 3381D → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. 1 Publication
    Mutagenesisi341 – 3411H → A: Little effect on binding L3 of PPARGC1A. 1 Publication
    Mutagenesisi343 – 3431E → A: No effect on binding L3 of PPARGC1A. 1 Publication
    Mutagenesisi403 – 4031K → R: Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14. 2 Publications
    Mutagenesisi413 – 4131L → A: Loss of coactivation activity; when associated with A-418. Loss of increased response to coactivator; when associated with A-19 and A-418. 1 Publication
    Mutagenesisi418 – 4181L → A: Loss of coactivation activity; when associated with A-413. Loss of increased response to coactivator activity; when associated with A-19 and A-413. 1 Publication
    Mutagenesisi421 – 4233Missing: Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A.
    Mutagenesisi423 – 4231D → A: Little effect on binding L3 of PPARGC1A.

    Organism-specific databases

    PharmGKBiPA27887.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 423423Steroid hormone receptor ERR1PRO_0000053660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei19 – 191Phosphoserine3 Publications
    Modified residuei22 – 221Phosphoserine3 Publications
    Modified residuei129 – 1291N6-acetyllysine; by PCAF/KAT2B1 Publication
    Modified residuei138 – 1381N6-acetyllysine; by PCAF/KAT2B1 Publication
    Modified residuei160 – 1601N6-acetyllysine; by PCAF/KAT2B1 Publication
    Modified residuei162 – 1621N6-acetyllysine; by PCAF/KAT2B1 Publication
    Cross-linki403 – 403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); partial

    Post-translational modificationi

    Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.3 Publications
    Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4. Sumoylation enhances repression of transcriptional activity, but has no effect on subcellular location nor on DNA binding.3 Publications
    Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP11474.
    PaxDbiP11474.
    PRIDEiP11474.

    PTM databases

    PhosphoSiteiP11474.

    Expressioni

    Inductioni

    Induced by PGC1alpha in a number of specific cell types including heart, kidney and muscle.1 Publication

    Gene expression databases

    ArrayExpressiP11474.
    BgeeiP11474.
    CleanExiHS_ESRRA.
    GenevestigatoriP11474.

    Organism-specific databases

    HPAiHPA053785.

    Interactioni

    Subunit structurei

    Binds DNA as a monomer or a homodimer. Interacts (via the AF2 domain) with coactivator PPARGC1A (via the L3 motif); the interaction greatly enhances transriptional activity of genes involved in energy metabolism. Interacts with PIAS4; the interaction enhances sumoylation.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TRRAPQ9Y4A53EBI-372412,EBI-399128

    Protein-protein interaction databases

    BioGridi108405. 42 interactions.
    DIPiDIP-35053N.
    IntActiP11474. 12 interactions.
    MINTiMINT-215609.
    STRINGi9606.ENSP00000000442.

    Structurei

    Secondary structure

    1
    423
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi195 – 20410
    Helixi224 – 24421
    Helixi249 – 2513
    Helixi254 – 27724
    Beta strandi280 – 2823
    Beta strandi284 – 2874
    Beta strandi290 – 2923
    Helixi294 – 2996
    Turni300 – 3045
    Helixi305 – 31713
    Turni318 – 3203
    Helixi323 – 33513
    Helixi345 – 36420
    Helixi377 – 3826
    Helixi385 – 40016
    Helixi404 – 4063
    Helixi410 – 42112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XB7X-ray2.50A194-423[»]
    2PJLX-ray2.30A/B193-423[»]
    3D24X-ray2.11A/C192-423[»]
    3K6PX-ray2.00A193-423[»]
    ProteinModelPortaliP11474.
    SMRiP11474. Positions 71-422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11474.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7676Repressor domainAdd
    BLAST
    Regioni206 – 402197Ligand binding domainAdd
    BLAST
    Regioni403 – 42321AF-2 domainAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri79 – 9921NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri115 – 13420NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG282629.
    HOGENOMiHOG000233467.
    HOVERGENiHBG108344.
    KOiK08552.
    OMAiGPGEQGS.
    OrthoDBiEOG7288S1.
    PhylomeDBiP11474.
    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.
    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.
    PRINTSiPR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 2 hits.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11474-1) [UniParc]FASTAAdd to Basket

    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

    MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH    50
    KEEEDGEGAG PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK 100
    AFFKRTIQGS IEYSCPASNE CEITKRRRKA CQACRFTKCL RVGMLKEGVR 150
    LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP LAVAGGPRKT AAPVNALVSH 200
    LLVVEPEKLY AMPDPAGPDG HLPAVATLCD LFDREIVVTI SWAKSIPGFS 250
    SLSLSDQMSV LQSVWMEVLV LGVAQRSLPL QDELAFAEDL VLDEEGARAA 300
    GLGELGAALL QLVRRLQALR LEREEYVLLK ALALANSDSV HIEDAEAVEQ 350
    LREALHEALL EYEAGRAGPG GGAERRRAGR LLLTLPLLRQ TAGKVLAHFY 400
    GVKLEGKVPM HKLFLEMLEA MMD 423
    Length:423
    Mass (Da):45,510
    Last modified:November 25, 2008 - v3
    Checksum:iBAE62DAF0BE6BA96
    GO
    Isoform 2 (identifier: P11474-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-191: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:422
    Mass (Da):45,439
    Checksum:i482E152354383842
    GO

    Sequence cautioni

    The sequence CAA35778.1 differs from that shown. Reason: Frameshift at positions 345 and 354.
    The sequence AAB17015.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei191 – 1911Missing in isoform 2. 1 PublicationVSP_035756

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51416 mRNA. Translation: CAA35778.1. Frameshift.
    L38487 mRNA. Translation: AAB17015.1. Different initiation.
    AP001453 Genomic DNA. No translation available.
    CCDSiCCDS41667.1. [P11474-1]
    CCDS60830.1. [P11474-2]
    PIRiA29345.
    RefSeqiNP_001269379.1. NM_001282450.1. [P11474-1]
    NP_001269380.1. NM_001282451.1. [P11474-2]
    NP_004442.3. NM_004451.4. [P11474-1]
    UniGeneiHs.110849.

    Genome annotation databases

    EnsembliENST00000000442; ENSP00000000442; ENSG00000173153. [P11474-1]
    ENST00000405666; ENSP00000384851; ENSG00000173153. [P11474-1]
    ENST00000406310; ENSP00000385971; ENSG00000173153. [P11474-2]
    GeneIDi2101.
    KEGGihsa:2101.
    UCSCiuc001nzq.1. human. [P11474-1]
    uc001nzr.1. human. [P11474-2]

    Polymorphism databases

    DMDMi215274146.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51416 mRNA. Translation: CAA35778.1 . Frameshift.
    L38487 mRNA. Translation: AAB17015.1 . Different initiation.
    AP001453 Genomic DNA. No translation available.
    CCDSi CCDS41667.1. [P11474-1 ]
    CCDS60830.1. [P11474-2 ]
    PIRi A29345.
    RefSeqi NP_001269379.1. NM_001282450.1. [P11474-1 ]
    NP_001269380.1. NM_001282451.1. [P11474-2 ]
    NP_004442.3. NM_004451.4. [P11474-1 ]
    UniGenei Hs.110849.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XB7 X-ray 2.50 A 194-423 [» ]
    2PJL X-ray 2.30 A/B 193-423 [» ]
    3D24 X-ray 2.11 A/C 192-423 [» ]
    3K6P X-ray 2.00 A 193-423 [» ]
    ProteinModelPortali P11474.
    SMRi P11474. Positions 71-422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108405. 42 interactions.
    DIPi DIP-35053N.
    IntActi P11474. 12 interactions.
    MINTi MINT-215609.
    STRINGi 9606.ENSP00000000442.

    Chemistry

    BindingDBi P11474.
    ChEMBLi CHEMBL3429.
    GuidetoPHARMACOLOGYi 622.

    PTM databases

    PhosphoSitei P11474.

    Polymorphism databases

    DMDMi 215274146.

    Proteomic databases

    MaxQBi P11474.
    PaxDbi P11474.
    PRIDEi P11474.

    Protocols and materials databases

    DNASUi 2101.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000000442 ; ENSP00000000442 ; ENSG00000173153 . [P11474-1 ]
    ENST00000405666 ; ENSP00000384851 ; ENSG00000173153 . [P11474-1 ]
    ENST00000406310 ; ENSP00000385971 ; ENSG00000173153 . [P11474-2 ]
    GeneIDi 2101.
    KEGGi hsa:2101.
    UCSCi uc001nzq.1. human. [P11474-1 ]
    uc001nzr.1. human. [P11474-2 ]

    Organism-specific databases

    CTDi 2101.
    GeneCardsi GC11P064073.
    HGNCi HGNC:3471. ESRRA.
    HPAi HPA053785.
    MIMi 601998. gene.
    neXtProti NX_P11474.
    PharmGKBi PA27887.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG282629.
    HOGENOMi HOG000233467.
    HOVERGENi HBG108344.
    KOi K08552.
    OMAi GPGEQGS.
    OrthoDBi EOG7288S1.
    PhylomeDBi P11474.
    TreeFami TF323751.

    Enzyme and pathway databases

    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_15525. Nuclear Receptor transcription pathway.
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    SignaLinki P11474.

    Miscellaneous databases

    EvolutionaryTracei P11474.
    GeneWikii Estrogen-related_receptor_alpha.
    GenomeRNAii 2101.
    NextBioi 8503.
    PROi P11474.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11474.
    Bgeei P11474.
    CleanExi HS_ESRRA.
    Genevestigatori P11474.

    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.
    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 PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 2 hits.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a new class of steroid hormone receptors."
      Giguere V., Yang N., Segui P., Evans R.M.
      Nature 331:91-94(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Kidney.
    2. "Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter."
      Yang N., Shigeta H., Shi H., Teng C.T.
      J. Biol. Chem. 271:5795-5804(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Uterus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "SV40 early-to-late switch involves titration of cellular transcriptional repressors."
      Wiley S.R., Kraus R.J., Zuo F., Murray E.E., Loritz K., Mertz J.E.
      Genes Dev. 7:2206-2219(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 69-76.
    5. "The orphan nuclear receptor estrogen-related receptor alpha is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene."
      Sladek R., Bader J.-A., Giguere V.
      Mol. Cell. Biol. 17:5400-5409(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha)."
      Schreiber S.N., Knutti D., Brogli K., Uhlmann T., Kralli A.
      J. Biol. Chem. 278:9013-9018(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPARGC1A, INDUCTION, FUNCTION.
    7. "A single nucleotide in an estrogen-related receptor alpha site can dictate mode of binding and peroxisome proliferator-activated receptor gamma coactivator 1alpha activation of target promoters."
      Barry J.B., Laganiere J., Giguere V.
      Mol. Endocrinol. 20:302-310(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING SPECIFICITY, INTERACTION WITH PPARGC1A, HOMODIMERIZATION, FUNCTION, MUTAGENESIS OF SER-118 AND THR-124.
    8. "Phosphorylation-dependent sumoylation of estrogen-related receptor alpha1."
      Vu E.H., Kraus R.J., Mertz J.E.
      Biochemistry 46:9795-9804(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22, FUNCTION, MUTAGENESIS OF LYS-14; SER-19; SER-22; LYS-403; LEU-413 AND LEU-418.
    9. "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-14 AND LYS-403, PHOSPHORYLATION AT SER-19 AND SER-22, INTERACTION WITH PIAS4, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-14; SER-19; SER-22 AND LYS-403.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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 AT LYS-129; LYS-138; LYS-160 AND LYS-162 BY PCAF/KAT2B, MUTAGENESIS OF LYS-129; LYS-138; LYS-160 AND LYS-162, DEACETYLATION BY SIRT1 AND HDAC8.
    12. "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.
    13. "Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha."
      Kallen J., Schlaeppi J.-M., Bitsch F., Filipuzzi I., Schilb A., Riou V., Graham A., Strauss A., Geiser M., Fournier B.
      J. Biol. Chem. 279:49330-49337(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 193-423 IN COMPLEX WITH THE L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, HOMODIMERIZATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop."
      Greschik H., Althage M., Flaig R., Sato Y., Chavant V., Peluso-Iltis C., Choulier L., Cronet P., Rochel N., Schuele R., Stroemstedt P.E., Moras D.
      J. Biol. Chem. 283:20220-20230(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 180-423 IN COMPLEX WITH THE L3 SITE-CONTAINING PEPTIDE OF COACTIVATOR PPARGC1A, INTERACTION WITH PPARGC1A, MUTAGENESIS OF 258-MET--GLN-262; SER-259; ARG-315; ASP-338; HIS-341; GLU-343 AND 421-MET--ASP-423.

    Entry informationi

    Entry nameiERR1_HUMAN
    AccessioniPrimary (citable) accession number: P11474
    Secondary accession number(s): Q14514
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3