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P11474

- ERR1_HUMAN

UniProt

P11474 - ERR1_HUMAN

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Protein

Steroid hormone receptor ERR1

Gene

ESRRA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 domain specific binding Source: UniProtKB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  7. sequence-specific DNA binding Source: UniProtKB
  8. steroid binding Source: InterPro
  9. steroid hormone receptor activity Source: InterPro
  10. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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

BgeeiP11474.
CleanExiHS_ESRRA.
ExpressionAtlasiP11474. baseline.
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. 44 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.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233467.
HOVERGENiHBG108344.
InParanoidiP11474.
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

        10         20         30         40         50
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVALAPG PAPTRCLPGH
60 70 80 90 100
KEEEDGEGAG PGEQGGGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK
110 120 130 140 150
AFFKRTIQGS IEYSCPASNE CEITKRRRKA CQACRFTKCL RVGMLKEGVR
160 170 180 190 200
LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP LAVAGGPRKT AAPVNALVSH
210 220 230 240 250
LLVVEPEKLY AMPDPAGPDG HLPAVATLCD LFDREIVVTI SWAKSIPGFS
260 270 280 290 300
SLSLSDQMSV LQSVWMEVLV LGVAQRSLPL QDELAFAEDL VLDEEGARAA
310 320 330 340 350
GLGELGAALL QLVRRLQALR LEREEYVLLK ALALANSDSV HIEDAEAVEQ
360 370 380 390 400
LREALHEALL EYEAGRAGPG GGAERRRAGR LLLTLPLLRQ TAGKVLAHFY
410 420
GVKLEGKVPM HKLFLEMLEA MMD
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. 44 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.
GeneTreei ENSGT00760000118887.
HOGENOMi HOG000233467.
HOVERGENi HBG108344.
InParanoidi P11474.
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

Bgeei P11474.
CleanExi HS_ESRRA.
ExpressionAtlasi P11474. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 168 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