Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5QJV7 (ERR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Esrra
Synonyms:Nr3b1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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 By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

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.

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.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR3 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence AAI04702.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAQ17212.1 differs from that shown. Reason: Frameshift at positions 408 and 413.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from mutant phenotype PubMed 17170100. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 17170100. Source: RGD

regulation of cell proliferation

Inferred from mutant phenotype PubMed 11381083. Source: RGD

regulation of ossification

Inferred from mutant phenotype PubMed 12193582. Source: RGD

regulation of osteoblast differentiation

Inferred from mutant phenotype PubMed 11381083. Source: RGD

regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 12193582. Source: RGD

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

steroid binding

Inferred from electronic annotation. Source: InterPro

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Steroid hormone receptor ERR1
PRO_0000295232

Regions

DNA binding76 – 15176Nuclear receptor
Zinc finger79 – 9921NR C4-type
Zinc finger115 – 13420NR C4-type
Region1 – 7676Repressor domain By similarity
Region205 – 401197Ligand binding domain By similarity
Region402 – 42221AF-2 domain By similarity

Sites

Site1241Required for DNA-dependent dimerization By similarity

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue221Phosphoserine By similarity
Modified residue1291N6-acetyllysine; by PCAF/KAT2B By similarity
Modified residue1381N6-acetyllysine; by PCAF/KAT2B By similarity
Modified residue1601N6-acetyllysine; by PCAF/KAT2B By similarity
Modified residue1621N6-acetyllysine; by PCAF/KAT2B By similarity
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QJV7 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 2F54EEA1BD3B511D

FASTA42245,464
        10         20         30         40         50         60 
MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVTLASG PAPARCLPGH KEEEDGEGAG 

        70         80         90        100        110        120 
SGEQGSGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE 

       130        140        150        160        170        180 
CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP 

       190        200        210        220        230        240 
LAVAGGPRKT APVNALVSHL LVVEPEKLYA MPDPASPDGH LPAVATLCDL FDREIVVTIS 

       250        260        270        280        290        300 
WAKSIPGFSS LSLSDQMSVL QSVWMEVLVL GVAQRSLPLQ DELAFAEDLV LDEEGARAAG 

       310        320        330        340        350        360 
LGDLGAALLQ LVRRLQALRL EREEYVLLKA LALANSDSVH IEDAEAVEQL REALHEALLE 

       370        380        390        400        410        420 
YEAGRAGPGG GAERRRAGRL LLTLPLLRQT AGKVLAHFYG VKLEGKVPMH KLFLEMLEAM 


MD 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY280663 mRNA. Translation: AAQ17212.1. Frameshift.
BC104701 mRNA. Translation: AAI04702.1. Different initiation.
RefSeqNP_001008511.2. NM_001008511.2.
UniGeneRn.130171.

3D structure databases

ProteinModelPortalQ5QJV7.
SMRQ5QJV7. Positions 71-421.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ5QJV7.

Proteomic databases

PaxDbQ5QJV7.
PRIDEQ5QJV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028697; ENSRNOP00000028697; ENSRNOG00000021139.
GeneID293701.
KEGGrno:293701.
UCSCRGD:1583866. rat.

Organism-specific databases

CTD2101.
RGD1583866. Esrra.

Phylogenomic databases

eggNOGNOG282629.
GeneTreeENSGT00730000110346.
HOGENOMHOG000233467.
HOVERGENHBG108344.
InParanoidQ5QJV7.
KOK08552.
OMAGPGEQGS.
OrthoDBEOG7288S1.
PhylomeDBQ5QJV7.
TreeFamTF323751.

Gene expression databases

GenevestigatorQ5QJV7.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF002527. ER-like_NR. 1 hit.
PIRSF500939. ERR1-2-3. 1 hit.
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio636801.
PROQ5QJV7.

Entry information

Entry nameERR1_RAT
AccessionPrimary (citable) accession number: Q5QJV7
Secondary accession number(s): Q3MHT1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families