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UniProtKB - P11474 (ERR1_HUMAN)

Entry version 210 (13 Feb 2019)
Sequence version 3 (25 Nov 2008)
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Protein

Steroid hormone receptor ERR1

Gene

ESRRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei124Required for DNA-dependent dimerization1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi76 – 151Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri79 – 99NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri115 – 134NR C4-typePROSITE-ProRule annotationAdd BLAST20

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1989781 PPARA activates gene expression
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-8939902 Regulation of RUNX2 expression and activity

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P11474

SIGNOR Signaling Network Open Resource

More...SIGNORi		P11474

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ESRRA
Synonyms:ERR1, ESRL1, NR3B1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000173153.13

Human Gene Nomenclature Database

More...HGNCi		HGNC:3471 ESRRA

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601998 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P11474

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14K → R: Some loss of sumoylation. Complete loss of sumoylation; when associated with R-403. 2 Publications1
Mutagenesisi19S → 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 Publications1
Mutagenesisi19S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-22. 2 Publications1
Mutagenesisi22S → 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 Publications1
Mutagenesisi22S → D: Represses transactivation activity in response to coactivator as for wild type; when associated with D-19. 2 Publications1
Mutagenesisi118S → A: Binds DNA as a monomer or as a dimer as for wild type. No effect on interaction with PPARGC1A. 1 Publication1
Mutagenesisi124T → A: Binds DNA predominantly as a monomer. Loss of interaction with PPARGC1A. 1 Publication1
Mutagenesisi129K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-138, R-160 and R-162. 1 Publication1
Mutagenesisi138K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-160 and R-162. 1 Publication1
Mutagenesisi160K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-162. 1 Publication1
Mutagenesisi162K → R: Abolishes acetylation by PCAF/KAT2B; when associated with R-129, R-138 and R-160. 1 Publication1
Mutagenesisi258 – 262MSVLQ → VSVLE: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. 1 Publication5
Mutagenesisi259S → H: Little effect on binding L2 of PPARGC1A. Greatly reduced binding to L3 of PPARGC1A. 1 Publication1
Mutagenesisi315R → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. 1 Publication1
Mutagenesisi338D → A: Almost complete loss of interaction to L2 or to L3 of PPARGC1A. 1 Publication1
Mutagenesisi341H → A: Little effect on binding L3 of PPARGC1A. 1 Publication1
Mutagenesisi343E → A: No effect on binding L3 of PPARGC1A. 1 Publication1
Mutagenesisi403K → R: Decrease in sumoylation. No effect on transcriptional activity. Complete loss of sumoylation; when associated with R-14. 2 Publications1
Mutagenesisi413L → 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 Publication1
Mutagenesisi418L → 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 Publication1
Mutagenesisi421 – 423Missing : Greatly reduced interaction with L3 motif of PPARGC1A. Less effect on binding to L2 motif of PPARGC1A. 1 Publication3
Mutagenesisi423D → A: Little effect on binding L3 of PPARGC1A. 1

Organism-specific databases

DisGeNET

More...DisGeNETi		2101

Open Targets

More...OpenTargetsi		ENSG00000173153

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27887

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3429

Drug and drug target database

More...DrugBanki		DB06833 1-CYCLOHEXYL-N-{[1-(4-METHYLPHENYL)-1H-INDOL-3-YL]METHYL}METHANAMINE
DB00197 Troglitazone

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		622

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ESRRA

Domain mapping of disease mutations (DMDM)

More...DMDMi		215274146

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000536601 – 423Steroid hormone receptor ERR1Add BLAST423

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)2 Publications
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19PhosphoserineCombined sources2 Publications1
Modified residuei22PhosphoserineCombined sources2 Publications1
Modified residuei129N6-acetyllysine; by PCAF/KAT2B1 Publication1
Modified residuei138N6-acetyllysine; by PCAF/KAT2B1 Publication1
Modified residuei160N6-acetyllysine; by PCAF/KAT2B1 Publication1
Modified residuei162N6-acetyllysine; by PCAF/KAT2B1 Publication1
Cross-linki189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate2 Publications
Cross-linki403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity.2 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.2 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

Encyclopedia of Proteome Dynamics

More...EPDi		P11474

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P11474

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P11474

PeptideAtlas

More...PeptideAtlasi		P11474

PRoteomics IDEntifications database

More...PRIDEi		P11474

ProteomicsDB human proteome resource

More...ProteomicsDBi		52781
52782 [P11474-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P11474

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P11474

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000173153 Expressed in 207 organ(s), highest expression level in apex of heart

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P11474 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P11474 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA053785

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. Interacts with MAPK15; promotes re-localization of ESRRA to the cytoplasm through a XPO1-dependent mechanism then inhibits ESRRA transcriptional activity.5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108405, 39 interactors

Database of interacting proteins

More...DIPi		DIP-35053N

Protein interaction database and analysis system

More...IntActi		P11474, 28 interactors

Molecular INTeraction database

More...MINTi		P11474

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000000442

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P11474

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1423
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XB7X-ray2.50A194-423[»]
2PJLX-ray2.30A/B193-423[»]
3D24X-ray2.11A/C192-423[»]
3K6PX-ray2.00A193-423[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P11474

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P11474

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P11474

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini193 – 421NR LBDPROSITE-ProRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 76Repressor domainAdd BLAST76
Regioni403 – 423AF-2 domainAdd BLAST21

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the nuclear hormone receptor family. NR3 subfamily.Curated

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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575 Eukaryota
ENOG410XRZC LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160341

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000233467

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG108344

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11474

KEGG Orthology (KO)

More...KOi		K08552

Identification of Orthologs from Complete Genome Data

More...OMAi		CHSGHKE

Database of Orthologous Groups

More...OrthoDBi		669799at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P11474

TreeFam database of animal gene trees

More...TreeFami		TF323751

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.50.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR035500 NHR_like_dom_sf
IPR000536 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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002527 ER-like_NR, 1 hit
PIRSF500939 ERR1-2-3, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00398 STRDHORMONER
PR00047 STROIDFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48508 SSF48508, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GWT5F5GWT5_HUMAN
Steroid hormone receptor ERR1
ESRRA
109Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YGT3H0YGT3_HUMAN
Steroid hormone receptor ERR1
ESRRA
198Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F5H0E9F5H0E9_HUMAN
Steroid hormone receptor ERR1
ESRRA
162Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB17015 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA35778 differs from that shown. Reason: Frameshift at positions 345 and 354.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_035756191Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X51416 mRNA Translation: CAA35778.1 Frameshift.
L38487 mRNA Translation: AAB17015.1 Different initiation.
AP001453 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS41667.1 [P11474-1]
CCDS60830.1 [P11474-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A29345

NCBI Reference Sequences

More...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]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.110849

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000000442; ENSP00000000442; ENSG00000173153 [P11474-1]
ENST00000405666; ENSP00000384851; ENSG00000173153 [P11474-1]
ENST00000406310; ENSP00000385971; ENSG00000173153 [P11474-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2101

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2101

UCSC genome browser

More...UCSCi		uc001nzr.3 human [P11474-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

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

Protein-protein interaction databases

BioGridi108405, 39 interactors
DIPiDIP-35053N
IntActiP11474, 28 interactors
MINTiP11474
STRINGi9606.ENSP00000000442

Chemistry databases

BindingDBiP11474
ChEMBLiCHEMBL3429
DrugBankiDB06833 1-CYCLOHEXYL-N-{[1-(4-METHYLPHENYL)-1H-INDOL-3-YL]METHYL}METHANAMINE
DB00197 Troglitazone
GuidetoPHARMACOLOGYi622

PTM databases

iPTMnetiP11474
PhosphoSitePlusiP11474

Polymorphism and mutation databases

BioMutaiESRRA
DMDMi215274146

Proteomic databases

EPDiP11474
jPOSTiP11474
PaxDbiP11474
PeptideAtlasiP11474
PRIDEiP11474
ProteomicsDBi52781
52782 [P11474-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		2101
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000000442; ENSP00000000442; ENSG00000173153 [P11474-1]
ENST00000405666; ENSP00000384851; ENSG00000173153 [P11474-1]
ENST00000406310; ENSP00000385971; ENSG00000173153 [P11474-2]
GeneIDi2101
KEGGihsa:2101
UCSCiuc001nzr.3 human [P11474-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2101
DisGeNETi2101
EuPathDBiHostDB:ENSG00000173153.13

GeneCards: human genes, protein and diseases

More...GeneCardsi		ESRRA
HGNCiHGNC:3471 ESRRA
HPAiHPA053785
MIMi601998 gene
neXtProtiNX_P11474
OpenTargetsiENSG00000173153
PharmGKBiPA27887

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
GeneTreeiENSGT00940000160341
HOGENOMiHOG000233467
HOVERGENiHBG108344
InParanoidiP11474
KOiK08552
OMAiCHSGHKE
OrthoDBi669799at2759
PhylomeDBiP11474
TreeFamiTF323751

Enzyme and pathway databases

ReactomeiR-HSA-1989781 PPARA activates gene expression
R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis
R-HSA-383280 Nuclear Receptor transcription pathway
R-HSA-8939902 Regulation of RUNX2 expression and activity
SignaLinkiP11474
SIGNORiP11474

Miscellaneous databases

EvolutionaryTraceiP11474

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Estrogen-related_receptor_alpha

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2101

Protein Ontology

More...PROi		PR:P11474

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000173153 Expressed in 207 organ(s), highest expression level in apex of heart
ExpressionAtlasiP11474 baseline and differential
GenevisibleiP11474 HS

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500 NHR_like_dom_sf
IPR000536 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
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PIRSFiPIRSF002527 ER-like_NR, 1 hit
PIRSF500939 ERR1-2-3, 1 hit
PRINTSiPR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 1 hit
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERR1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11474
Secondary accession number(s): Q14514
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 25, 2008
Last modified: February 13, 2019
This is version 210 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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