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Protein

Steroid hormone receptor ERR1

Gene

Esrra

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.

Sites

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

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  4. sequence-specific DNA binding Source: UniProtKB
  5. steroid binding Source: InterPro
  6. steroid hormone receptor activity Source: InterPro
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. cartilage development Source: RGD
  2. positive regulation of transcription, DNA-templated Source: RGD
  3. regulation of cell proliferation Source: RGD
  4. regulation of ossification Source: RGD
  5. regulation of osteoblast differentiation Source: RGD
  6. regulation of osteoclast differentiation Source: RGD
  7. regulation of transcription, DNA-templated Source: UniProtKB
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_285313. PPARA activates gene expression.
REACT_304415. Transcriptional activation of mitochondrial biogenesis.
REACT_334119. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Steroid hormone receptor ERR1
Alternative name(s):
Estrogen-related receptor alpha
Short name:
ERR-alpha
Nuclear receptor subfamily 3 group B member 1
Gene namesi
Name:Esrra
Synonyms:Nr3b1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1583866. Esrra.

Subcellular locationi

  1. Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. intercellular bridge Source: Ensembl
  2. microtubule cytoskeleton Source: Ensembl
  3. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Steroid hormone receptor ERR1PRO_0000295232Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei22 – 221PhosphoserineBy similarity
Modified residuei129 – 1291N6-acetyllysine; by PCAF/KAT2BBy similarity
Modified residuei138 – 1381N6-acetyllysine; by PCAF/KAT2BBy similarity
Modified residuei160 – 1601N6-acetyllysine; by PCAF/KAT2BBy similarity
Modified residuei162 – 1621N6-acetyllysine; by PCAF/KAT2BBy similarity
Cross-linki402 – 402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By 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

PaxDbiQ5QJV7.
PRIDEiQ5QJV7.

PTM databases

PhosphoSiteiQ5QJV7.

Expressioni

Gene expression databases

GenevestigatoriQ5QJV7.

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

Structurei

3D structure databases

ProteinModelPortaliQ5QJV7.
SMRiQ5QJV7. Positions 71-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7676Repressor domainBy similarityAdd
BLAST
Regioni205 – 401197Ligand binding domainBy similarityAdd
BLAST
Regioni402 – 42221AF-2 domainBy similarityAdd
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.
InParanoidiQ5QJV7.
KOiK08552.
OMAiGPGEQGS.
OrthoDBiEOG7288S1.
PhylomeDBiQ5QJV7.
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]

Sequencei

Sequence statusi: Complete.

Q5QJV7-1 [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 10, 2007 - v2
Checksum:i2F54EEA1BD3B511D
GO

Sequence cautioni

The sequence AAI04702.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAQ17212.1 differs from that shown. Reason: Frameshift at positions 408 and 413. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY280663 mRNA. Translation: AAQ17212.1. Frameshift.
BC104701 mRNA. Translation: AAI04702.1. Different initiation.
RefSeqiNP_001008511.2. NM_001008511.2.
UniGeneiRn.130171.

Genome annotation databases

EnsembliENSRNOT00000028697; ENSRNOP00000028697; ENSRNOG00000021139.
GeneIDi293701.
KEGGirno:293701.
UCSCiRGD:1583866. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY280663 mRNA. Translation: AAQ17212.1. Frameshift.
BC104701 mRNA. Translation: AAI04702.1. Different initiation.
RefSeqiNP_001008511.2. NM_001008511.2.
UniGeneiRn.130171.

3D structure databases

ProteinModelPortaliQ5QJV7.
SMRiQ5QJV7. Positions 71-421.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ5QJV7.

Proteomic databases

PaxDbiQ5QJV7.
PRIDEiQ5QJV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028697; ENSRNOP00000028697; ENSRNOG00000021139.
GeneIDi293701.
KEGGirno:293701.
UCSCiRGD:1583866. rat.

Organism-specific databases

CTDi2101.
RGDi1583866. Esrra.

Phylogenomic databases

eggNOGiNOG282629.
GeneTreeiENSGT00760000118887.
HOGENOMiHOG000233467.
HOVERGENiHBG108344.
InParanoidiQ5QJV7.
KOiK08552.
OMAiGPGEQGS.
OrthoDBiEOG7288S1.
PhylomeDBiQ5QJV7.
TreeFamiTF323751.

Enzyme and pathway databases

ReactomeiREACT_285313. PPARA activates gene expression.
REACT_304415. Transcriptional activation of mitochondrial biogenesis.
REACT_334119. Nuclear Receptor transcription pathway.

Miscellaneous databases

NextBioi636801.
PROiQ5QJV7.

Gene expression databases

GenevestigatoriQ5QJV7.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression study of estrogen receptor-related receptor alpha in rat ovary."
    Lui K., Chen S., Chan F.L.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "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].
    Tissue: Heart.

Entry informationi

Entry nameiERR1_RAT
AccessioniPrimary (citable) accession number: Q5QJV7
Secondary accession number(s): Q3MHT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: April 1, 2015
This is version 86 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.