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UniProtKB - Q9TV98 (ESR1_HORSE)

Entry version 158 (07 Apr 2021)
Sequence version 1 (01 May 2000)
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Protein

Estrogen receptor

Gene

ESR1

Organism
Equus caballus (Horse)
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 transcript 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

Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades.Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi185 – 250Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionActivator, DNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

<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%5Fand%5Ftaxonomy%5Fsection">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:
Estrogen receptor
Short name:
ER
Alternative name(s):
ER-alpha
Estradiol receptor
Nuclear receptor subfamily 3 group A member 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ESR1
Synonyms:ESR, NR3A1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEquus caballus (Horse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9796 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Laurasiatheria › Perissodactyla › Equidae › Equus ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002281 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced

<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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000536171 – 594Estrogen receptorAdd BLAST594

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi10O-linked (GlcNAc) serineBy similarity1
<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 residuei104Phosphoserine; by CDK2By similarity1
Modified residuei106Phosphoserine; by CDK2By similarity1
Modified residuei118PhosphoserineBy similarity1
Modified residuei167Phosphoserine; by CK2By similarity1
Modified residuei260Asymmetric dimethylarginine; by PRMT1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi447S-palmitoyl cysteineBy similarity1
Modified residuei536Phosphotyrosine; by Tyr-kinasesBy similarity1
Glycosylationi570O-linked (GlcNAc) threonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated; regulated by LATS1 via DCAF1 it leads to ESR1 proteasomal degradation. Deubiquitinated by OTUB1.By similarity
Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity (By similarity). Phosphorylated by LMTK3 (in vitro) (By similarity).By similarity
Palmitoylated at Cys-447 by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation, but not for signaling mediated by the nuclear hormone receptor (By similarity).By similarity
Dimethylated by PRMT1 at Arg-260. The methylation may favor cytoplasmic localization. Demethylated by JMJD6 at Arg-260.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		Q9TV98

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds DNA as a homodimer. Can form a heterodimer with ESR2.

Interacts with coactivator NCOA5.

Interacts with NCOA7; the interaction is ligand-inducible.

Interacts with AKAP13, CUEDC2, HEXIM1, KDM5A, MAP1S, PELP1, SMARD1, and UBE1C.

Interacts with MUC1; the interaction is stimulated by 7 beta-estradiol (E2) and enhances ERS1-mediated transcription.

Interacts with DNTTIP2, and UIMC1.

Interacts with KMT2D/MLL2.

Interacts with ATAD2; the interaction is enhanced by estradiol.

Interacts with KIF18A and LDB1.

Interacts with RLIM (via its C-terminus).

Interacts with MACROD1.

Interacts with SH2D4A and PLCG.

Interacts with SH2D4A; the interaction blocks binding to PLCG and inhibits estrogen-induced cell proliferation.

Interacts with DYNLL1.

Interacts with CCDC62; the interaction requires estradiol and appears to enhance the transcription of target genes.

Interacts with NR2C1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth.

Interacts with DNAAF4.

Interacts with PRMT2.

Interacts with PI3KR1 or PIK3R2, SRC and PTK2/FAK1.

Interacts with RBFOX2.

Interacts with EP300; the interaction is estrogen-dependent and enhanced by CITED1.

Interacts with CITED1; the interaction is estrogen-dependent.

Interacts with FAM120B, FOXL2, PHB2 and SLC30A9.

Interacts with coactivators NCOA3 and NCOA6.

Interacts with STK3/MST2 only in the presence of SAV1 and vice-versa. Binds to CSNK1D.

Interacts with NCOA2; NCOA2 can interact with ESR1 AF-1 and AF-2 domains simultaneously and mediate their transcriptional synergy.

Interacts with DDX5.

Interacts with NCOA1; the interaction seems to require a self-association of N-terminal and C-terminal regions.

Interacts with ZNF366, DDX17, NFKB1, RELA, SP1 and SP3.

Interacts with NRIP1.

Interacts with GPER1; the interaction occurs in an estrogen-dependent manner.

Interacts with CLOCK and the interaction is stimulated by estrogen.

Interacts with TRIP4 (ufmylated); estrogen dependent.

Interacts with LMTK3; the interaction phosphorylates ESR1 (in vitro) and protects it against proteasomal degradation.

Interacts with CCAR2 (via N-terminus) in a ligand-independent manner.

Interacts with ZFHX3.

Interacts with SFR1 in a ligand-dependent and -independent manner.

Interacts with DCAF13, LATS1 and DCAF1; regulates ESR1 ubiquitination and ubiquitin-mediated proteasomal degradation.

Interacts (via DNA-binding domain) with POU4F2 (C-terminus); this interaction increases the estrogen receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-estradiol-independent manner.

Interacts with ESRRB isoform 1.

Interacts with UBE3A and WBP2.

Interacts with GTF2B.

Interacts with RBM39. In the absence of hormonal ligand, interacts with TACC1 (By similarity).

By similarity

<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

3D structure databases

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

More...SMRi		Q9TV98

Database of comparative protein structure models

More...ModBasei		Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini311 – 546NR LBDPROSITE-ProRule annotationAdd BLAST236

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 – 184Modulating (transactivation AF-1); mediates interaction with MACROD1By similarityAdd BLAST184
Regioni35 – 174Interaction with DDX5; self-associationBy similarityAdd BLAST140
Regioni35 – 47Required for interaction with NCOA1By similarityAdd BLAST13
Regioni185 – 310Mediates interaction with DNTTIP2By similarityAdd BLAST126
Regioni251 – 310HingeAdd BLAST60
Regioni262 – 594Interaction with AKAP13By similarityAdd BLAST333
Regioni264 – 594Self-associationBy similarityAdd BLAST331
Regioni311 – 594Transactivation AF-2By similarityAdd BLAST284

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi64 – 70Poly-Ala7

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. The modulating domain, also known as A/B or AF-1 domain has a ligand-independent transactivation function. The C-terminus contains a ligand-dependent transactivation domain, also known as E/F or AF-2 domain which overlaps with the ligand binding domain. AF-1 and AF-2 activate transcription independently and synergistically and act in a promoter- and cell-specific manner (By similarity).By similarity

<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 fingeri185 – 205NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri221 – 245NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9TV98

Database of Orthologous Groups

More...OrthoDBi		487299at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.565.10, 1 hit
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
IPR024178, Oest_rcpt/oest-rel_rcp
IPR001292, Oestr_rcpt
IPR024736, Oestrogen-typ_rcpt_final_C_dom
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12743, ESR1_C, 1 hit
PF00104, Hormone_recep, 1 hit
PF02159, Oest_recep, 1 hit
PF00105, zf-C4, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF500101, ER-a, 1 hit
PIRSF002527, ER-like_NR, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00543, OESTROGENR
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9TV98-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTMTLHTKAS GMALLHQIQG NELETLNLPQ FKIPLERPLG EVYVESSKPP 
        60         70         80         90        100
VYDYPEGAAY DFNAAAAASA SVYGQSGLAY GPGSEAAAFG ANGLGGFPPL 
       110        120        130        140        150
NSVSPSQLML LHPPPQLSPY LHPPGQQVPY YLENEPSGYS VCEAGPQAFY 
       160        170        180        190        200
RPNADNRRQG GRERLASSGD KGSMAMESAK ETRYCAVCND YASGYHYGVW 
       210        220        230        240        250
SCEGCKAFFK RSIQGHNDYM CPATNQCTID KNRRKSCQAC RLRKCYEVGM 
       260        270        280        290        300
MKGGIRKDRR GGRMLKHKRQ RDDGEGRNEA GPSGDRRPAN FWPSPLLIKH 
       310        320        330        340        350
TKKISPVLSL TAEQMISALL DAEPPVLYSE YDATRPFNEA SMMGLLTNLA 
       360        370        380        390        400
DRELVHMINW AKRVPGFVDL SLHDQVHLLE CAWLEILMIG LVWRSMEHPG 
       410        420        430        440        450
KLLFAPNLLL DRNQGKCVEG MVEIFDMLLA TSSRLRMMNL QGEEFVCLKS 
       460        470        480        490        500
IILLNSGVYT FLSSTLKSLE EKDHIHRVLD KMTDTLIHLM AKAGLTLQQH 
       510        520        530        540        550
RRLAQLLLIL SHIRHMSNKG MEHLYSMKCK NVVPLYDLLL EMLDAHRLHA 
       560        570        580        590 
PANHGGAPME ETNQSQLATT GSTSPHSMQT YYITGEAEGF PNTI
Length:594
Mass (Da):66,104
Last modified:May 1, 2000 - v1
<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:iDD36CA7C24C74B95
GO

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
AF124093 mRNA Translation: AAD17316.1

NCBI Reference Sequences

More...RefSeqi		NP_001075241.1, NM_001081772.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		791249

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecb:791249

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124093 mRNA Translation: AAD17316.1
RefSeqiNP_001075241.1, NM_001081772.1

3D structure databases

SMRiQ9TV98
ModBaseiSearch...

Proteomic databases

PaxDbiQ9TV98

Genome annotation databases

GeneIDi791249
KEGGiecb:791249

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2099

Phylogenomic databases

InParanoidiQ9TV98
OrthoDBi487299at2759

Family and domain databases

Gene3Di1.10.565.10, 1 hit
3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500, NHR-like_dom_sf
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001723, Nuclear_hrmn_rcpt
IPR024178, Oest_rcpt/oest-rel_rcp
IPR001292, Oestr_rcpt
IPR024736, Oestrogen-typ_rcpt_final_C_dom
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA
PfamiView protein in Pfam
PF12743, ESR1_C, 1 hit
PF00104, Hormone_recep, 1 hit
PF02159, Oest_recep, 1 hit
PF00105, zf-C4, 1 hit
PIRSFiPIRSF500101, ER-a, 1 hit
PIRSF002527, ER-like_NR, 1 hit
PRINTSiPR00543, OESTROGENR
PR00398, 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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiESR1_HORSE
<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: Q9TV98
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: April 7, 2021
This is version 158 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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