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Protein

Steroid hormone receptor ERR1

Gene

Esrra

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei124Required for DNA-dependent dimerizationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi76 – 151Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
Zinc fingeri79 – 99NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri115 – 134NR C4-typePROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2151201. Transcriptional activation of mitochondrial biogenesis.
R-MMU-383280. Nuclear Receptor transcription pathway.

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, Estrra, Nr3b1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1346831. Esrra.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • intercellular bridge Source: Ensembl
  • microtubule cytoskeleton Source: Ensembl
  • nucleolus Source: Ensembl
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype; mice are viable, fertile and display no gross anatomical alterations, with the exception of reduced body weight and peripheral fat deposits. Mice are resistant to a high-fat diet-induced obesity.1 Publication

Chemistry databases

ChEMBLiCHEMBL1914280.
GuidetoPHARMACOLOGYi622.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000536611 – 422Steroid hormone receptor ERR1Add BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei19PhosphoserineCombined sources1 Publication1
Modified residuei22PhosphoserineCombined sources1
Modified residuei129N6-acetyllysine; by PCAF/KAT2BBy similarity1
Modified residuei138N6-acetyllysine; by PCAF/KAT2BBy similarity1
Modified residuei160N6-acetyllysine; by PCAF/KAT2BBy similarity1
Modified residuei162N6-acetyllysine; by PCAF/KAT2BBy similarity1
Cross-linki189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

Post-translational modificationi

Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.By similarity
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 (By similarity).By similarity
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO08580.
MaxQBiO08580.
PaxDbiO08580.
PeptideAtlasiO08580.
PRIDEiO08580.

PTM databases

iPTMnetiO08580.
PhosphoSitePlusiO08580.

Expressioni

Tissue specificityi

Most highly expressed in kidney, heart, and brown adipocytes. Also found in utERus, cervix and vagina.

Developmental stagei

Expressed in an organ specific mannER through mid-to late embryonic development with persistent high-level expression in brown adipose tissue and intestinal mucosa.

Inductioni

Activated by diethylstilbestrol (DES) and estradiol in the uterus.

Gene expression databases

BgeeiENSMUSG00000024955.
CleanExiMM_ESRRA.
ExpressionAtlasiO08580. baseline and differential.
GenevisibleiO08580. MM.

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 transcriptional activity of genes involved in energy metabolism. Interacts with PIAS4; the interaction enhances sumoylation (By similarity).By similarity

Protein-protein interaction databases

BioGridi204937. 6 interactors.
IntActiO08580. 2 interactors.
STRINGi10090.ENSMUSP00000025906.

Structurei

3D structure databases

ProteinModelPortaliO08580.
SMRiO08580.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 76Repressor domainAdd BLAST76
Regioni205 – 401Ligand binding domainBy similarityAdd BLAST197
Regioni402 – 422AF-2 domainBy similarityAdd BLAST21

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri79 – 99NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri115 – 134NR C4-typePROSITE-ProRule annotationAdd BLAST20

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233467.
HOVERGENiHBG108344.
InParanoidiO08580.
KOiK08552.
OMAiCHPGHKE.
OrthoDBiEOG091G0DYP.
TreeFamiTF323751.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR027289. Oest-rel_rcp.
IPR024178. Oest_rcpt/oest-rel_rcp.
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]

Sequencei

Sequence statusi: Complete.

O08580-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVTLASG PAPARCLPGH
60 70 80 90 100
KEEEDGEGAG SGEQGSGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK
110 120 130 140 150
AFFKRTIQGS IEYSCPASNE CEITKRRRKA CQACRFTKCL RVGMLKEGVR
160 170 180 190 200
LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP LAVAGGPRKT APVNALVSHL
210 220 230 240 250
LVVEPEKLYA MPDPASPDGH LPAVATLCDL FDREIVVTIS WAKSIPGFSS
260 270 280 290 300
LSLSDQMSVL QSVWMEVLVL GVAQRSLPLQ DELAFAEDLV LDEEGARAAG
310 320 330 340 350
LGDLGAALLQ LVRRLQALRL EREEYVLLKA LALANSDSVH IEDAEAVEQL
360 370 380 390 400
REALHEALLE YEAGRAGPGG GAERRRAGRL LLTLPLLRQT AGKVLAHFYG
410 420
VKLEGKVPMH KLFLEMLEAM MD
Length:422
Mass (Da):45,464
Last modified:July 27, 2011 - v4
Checksum:i2F54EEA1BD3B511D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti275R → G in AAB51250 (PubMed:9271417).Curated1
Sequence conflicti308Missing in AAB51250 (PubMed:9271417).Curated1
Sequence conflicti408 – 412PMHKL → HAQV in AAB51250 (PubMed:9271417).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85259 mRNA. Translation: AAB51250.1.
AK156371 mRNA. Translation: BAE33690.1.
BC138586 mRNA. Translation: AAI38587.1.
BC171958 mRNA. Translation: AAI71958.1.
CCDSiCCDS29509.1.
RefSeqiNP_031979.2. NM_007953.2.
UniGeneiMm.386776.

Genome annotation databases

EnsembliENSMUST00000025906; ENSMUSP00000025906; ENSMUSG00000024955.
GeneIDi26379.
KEGGimmu:26379.
UCSCiuc008gjg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85259 mRNA. Translation: AAB51250.1.
AK156371 mRNA. Translation: BAE33690.1.
BC138586 mRNA. Translation: AAI38587.1.
BC171958 mRNA. Translation: AAI71958.1.
CCDSiCCDS29509.1.
RefSeqiNP_031979.2. NM_007953.2.
UniGeneiMm.386776.

3D structure databases

ProteinModelPortaliO08580.
SMRiO08580.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204937. 6 interactors.
IntActiO08580. 2 interactors.
STRINGi10090.ENSMUSP00000025906.

Chemistry databases

ChEMBLiCHEMBL1914280.
GuidetoPHARMACOLOGYi622.

PTM databases

iPTMnetiO08580.
PhosphoSitePlusiO08580.

Proteomic databases

EPDiO08580.
MaxQBiO08580.
PaxDbiO08580.
PeptideAtlasiO08580.
PRIDEiO08580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025906; ENSMUSP00000025906; ENSMUSG00000024955.
GeneIDi26379.
KEGGimmu:26379.
UCSCiuc008gjg.1. mouse.

Organism-specific databases

CTDi2101.
MGIiMGI:1346831. Esrra.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233467.
HOVERGENiHBG108344.
InParanoidiO08580.
KOiK08552.
OMAiCHPGHKE.
OrthoDBiEOG091G0DYP.
TreeFamiTF323751.

Enzyme and pathway databases

ReactomeiR-MMU-2151201. Transcriptional activation of mitochondrial biogenesis.
R-MMU-383280. Nuclear Receptor transcription pathway.

Miscellaneous databases

ChiTaRSiEsrra. mouse.
PROiO08580.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024955.
CleanExiMM_ESRRA.
ExpressionAtlasiO08580. baseline and differential.
GenevisibleiO08580. MM.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR027289. Oest-rel_rcp.
IPR024178. Oest_rcpt/oest-rel_rcp.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiERR1_MOUSE
AccessioniPrimary (citable) accession number: O08580
Secondary accession number(s): B2RRU9, Q3U110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.