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UniProtKB - P15207 (ANDR_RAT)

Entry version 213 (23 Feb 2022)
Sequence version 1 (01 Apr 1990)
Previous versions | rss
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Protein

Androgen receptor

Gene

Ar

Organism
Rattus norvegicus (Rat)
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

Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3 (By similarity).

By similarity2 Publications

Miscellaneous

In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites.
Transcriptional activity is enhanced by binding to RANBP9.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei68817beta-hydroxy-5alpha-androstan-3-oneCombined sources1 Publication1
Binding sitei73517beta-hydroxy-5alpha-androstan-3-oneCombined sources1 Publication1
Binding sitei86017beta-hydroxy-5alpha-androstan-3-oneCombined sources1 Publication1

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 bindingi541 – 614Nuclear receptorPROSITE-ProRule annotationAdd BLAST74
<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 fingeri542 – 562NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri578 – 602NR 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 functionDNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Steroid-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-RNO-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand
R-RNO-383280, Nuclear Receptor transcription pathway
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-RNO-5689880, Ub-specific processing proteases

<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:
Androgen receptor
Alternative name(s):
Dihydrotestosterone receptor
Nuclear receptor subfamily 3 group C member 4
<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:Ar
Synonyms:Nr3c4
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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

Organism-specific databases

Rat genome database

More...RGDi		2147, Ar

<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

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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Defects in Ar are a cause of androgen insensitivity. Rats with this syndrome are called testicular feminized (TFM).1 Publication

Keywords - Diseasei

Disease variant

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3072

DrugCentral

More...DrugCentrali		P15207

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		628

<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_00000537121 – 902Androgen receptorAdd BLAST902

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei61Phosphoserine; by CDK9By similarity1
Modified residuei75PhosphoserineBy similarity1
Modified residuei221Phosphotyrosine; by CSKBy similarity1
Modified residuei254PhosphoserineBy similarity1
Modified residuei265Phosphotyrosine; by CSK and TNK2By similarity1
Modified residuei290PhosphoserineCombined sources1
Modified residuei305Phosphotyrosine; by CSKBy similarity1
Modified residuei344Phosphotyrosine; by CSKBy similarity1
Modified residuei355Phosphotyrosine; by CSKBy similarity1
Modified residuei360Phosphotyrosine; by CSKBy similarity1
Modified residuei361Phosphotyrosine; by CSK and TNK2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei391Phosphotyrosine; by CSKBy similarity1
Cross-linki503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei517Phosphotyrosine; by CSKBy similarity1
Modified residuei534Phosphotyrosine; by CSKBy similarity1
Modified residuei633PhosphoserineCombined sources1
Cross-linki828Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki830Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei898Phosphotyrosine; by CSKBy 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

Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-517 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity). Phosphorylation by TNK2 enhances the DNA-binding and transcriptional activity. Phosphorylation at Ser-61 by CDK9 regulates AR promoter selectivity and cell growth. Phosphorylation by PAK6 leads to AR-mediated transcription inhibition (By similarity).By similarity
Sumoylated on Lys-384 (major) and Lys-503 (By similarity). Ubiquitinated. Deubiquitinated by USP26 (By similarity). 'Lys-6' and 'Lys-27'-linked polyubiquitination by RNF6 modulates AR transcriptional activity and specificity (By similarity).By similarity
Palmitoylated by ZDHHC7 and ZDHHC21. Palmitoylation is required for plasma membrane targeting and for rapid intracellular signaling via ERK and AKT kinases and cAMP generation (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...PaxDbi		P15207

PRoteomics IDEntifications database

More...PRIDEi		P15207

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15207

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

More...PhosphoSitePlusi		P15207

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highest levels in the seminal vesicle, ventral prostate and coagulating gland with lower levels in the kidney and levator ani muscle.

<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.

Part of a ternary complex containing AR, EFCAB6/DJBP and PARK7.

Interacts with HIPK3 and NR0B2 in the presence of androgen. The ligand binding domain interacts with KAT7/HBO1 in the presence of dihydrotestosterone.

Interacts with EFCAB6/DJBP, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1, ZNF318 and RREB1.

Interacts with ZMIZ1/ZIMP10 and ZMIZ2/ZMIP7 which both enhance its transactivation activity.

Interacts with SLC30A9 and RAD54L2/ARIP4.

Interacts with MACROD1 (via macro domain) (By similarity).

Interacts via the ligand-binding domain with LXXLL and FXXLF motifs from NCOA1, NCOA2, NCOA3, NCOA4 and MAGEA11. The AR N-terminal poly-Gln region binds Ran resulting in enhancement of AR-mediated transactivation. Ran-binding decreases as the poly-Gln length increases.

Interacts with HIP1 (via coiled coil domain).

Interacts (via ligand-binding domain) with TRIM68.

Interacts with TNK2.

Interacts with USP26.

Interacts with RNF6.

Interacts (regulated by RNF6 probably through polyubiquitination) with RNF14; regulates AR transcriptional activity.

Interacts with PRMT2 and TRIM24.

Interacts with RACK1.

Interacts with RANBP10; this interaction enhances dihydrotestosterone-induced AR transcriptional activity.

Interacts with PRPF6 in a hormone-independent way; this interaction enhances dihydrotestosterone-induced AR transcriptional activity.

Interacts with STK4/MST1.

Interacts with ZIPK/DAPK3.

Interacts with LPXN.

Interacts with MAK.

Part of a complex containing AR, MAK and NCOA3.

Interacts with CRY1.

Interacts with CCAR1 and GATA2 (By similarity).

Interacts with BUD31 (By similarity).

Interacts with ARID4A (By similarity).

Interacts with ARID4B (By similarity).

Interacts (via NR LBD domain) with ZBTB7A; the interaction is direct and androgen-dependent (By similarity).

Interacts with NCOR1 (By similarity).

Interacts with NCOR2 (By similarity).

Interacts with CRY2 in a ligand-dependent manner (By similarity).

By similarity7 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>Sitei703Interaction with coactivator LXXL and FXXFY motifsBy similarity1
Sitei880Interaction with coactivator FXXLF and FXXFY motifsBy similarity1

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		246396, 3 interactors

Database of interacting proteins

More...DIPi		DIP-5963N

Protein interaction database and analysis system

More...IntActi		P15207, 1 interactor

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000009129

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P15207

<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

1902
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P15207

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P15207

<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>Domaini651 – 882NR LBDPROSITE-ProRule annotationAdd BLAST232

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 – 569Interaction with ZNF318By similarityAdd BLAST569
Regioni1 – 540ModulatingAdd BLAST540
Regioni35 – 146DisorderedSequence analysisAdd BLAST112
Regioni194 – 224DisorderedSequence analysisAdd BLAST31
Regioni439 – 465DisorderedSequence analysisAdd BLAST27
Regioni534 – 901Interaction with LPXNBy similarityAdd BLAST368
Regioni554 – 644Interaction with HIPK31 PublicationAdd BLAST91
Regioni574 – 901Interaction with CCAR1By similarityAdd BLAST328
Regioni607 – 901Interaction with KAT7By similarityAdd BLAST295

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi59 – 74Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi89 – 105Polar residuesSequence analysisAdd BLAST17

<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. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (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 fingeri542 – 562NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri578 – 602NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3575, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15207

Database of Orthologous Groups

More...OrthoDBi		615449at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P15207

TreeFam database of animal gene trees

More...TreeFami		TF350286

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
IPR001103, Andrgn_rcpt
IPR035500, NHR-like_dom_sf
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02166, Androgen_recep, 1 hit
PF00104, Hormone_recep, 1 hit
PF00105, zf-C4, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00521, ANDROGENR
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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P15207-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEVQLGLGRV YPRPPSKTYR GAFQNLFQSV REAIQNPGPR HPEAASIAPP 
        60         70         80         90        100
GACLQQRQET SPRRRRRQQH PEDGSPQAHI RGTTGYLALE EEQQPSQQQS 
       110        120        130        140        150
ASEGHPESGC LPEPGAATAP GKGLPQQPPA PPDQDDSAAP STLSLLGPTF 
       160        170        180        190        200
PGLSSCSADI KDILSEAGTM QLLQQQQQQQ QQQQQQQQQQ QQQQQEVISE 
       210        220        230        240        250
GSSSVRAREA TGAPSSSKDS YLGGNSTISD SAKELCKAVS VSMGLGVEAL 
       260        270        280        290        300
EHLSPGEQLR GDCMYASLLG GPPAVRPTPC APLAECKGLS LDEGPGKGTE 
       310        320        330        340        350
ETAEYSSFKG GYAKGLEGES LGCSGSSEAG SSGTLEIPSS LSLYKSGAVD 
       360        370        380        390        400
EAAAYQNRDY YNFPLALSGP PHPPPPTHPH ARIKLENPSD YGSAWAAAAA 
       410        420        430        440        450
QCRYGDLASL HGGSVAGPST GSPPATASSS WHTLFTAEEG QLYGPGGGGG 
       460        470        480        490        500
SSSPSDAGPV APYGYTRPPQ GLASQEGDFS ASEVWYPGGV VNRVPYPSPS 
       510        520        530        540        550
CVKSEMGPWM ENYSGPYGDM RLDSTRDHVL PIDYYFPPQK TCLICGDEAS 
       560        570        580        590        600
GCHYGALTCG SCKVFFKRAA EGKQKYLCAS RNDCTIDKFR RKNCPSCRLR 
       610        620        630        640        650
KCYEAGMTLG ARKLKKLGNL KLQEEGENSS AGSPTEDPSQ KMTVSHIEGY 
       660        670        680        690        700
ECQPIFLNVL EAIEPGVVCA GHDNNQPDSF AALLSSLNEL GERQLVHVVK 
       710        720        730        740        750
WAKALPGFRN LHVDDQMAVI QYSWMGLMVF AMGWRSFTNV NSRMLYFAPD 
       760        770        780        790        800
LVFNEYRMHK SRMYSQCVRM RHLSQEFGWL QITPQEFLCM KALLLFSIIP 
       810        820        830        840        850
VDGLKNQKFF DELRMNYIKE LDRIIACKRK NPTSCSRRFY QLTKLLDSVQ 
       860        870        880        890        900
PIARELHQFT FDLLIKSHMV SVDFPEMMAE IISVQVPKIL SGKVKPIYFH 

TQ
Length:902
Mass (Da):98,218
Last modified:April 1, 1990 - 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:i43F4064759FDCBED
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JSI8A0A0G2JSI8_RAT
Androgen receptor
Ar rCG_36439
902Annotation 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti195Missing in AAA40734 (PubMed:2341409).Curated1
Sequence conflicti389S → L in AAA40759 (PubMed:3174628).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti735R → Q in TFM; has only 10-15% of the androgen-binding capacity of wild-type AR. 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
M20133 mRNA Translation: AAA40733.1
M23264 mRNA Translation: AAA40759.1
J05454 Genomic DNA Translation: AAA40734.1

Protein sequence database of the Protein Information Resource

More...PIRi		B40494

NCBI Reference Sequences

More...RefSeqi		NP_036634.1, NM_012502.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24208

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:24208

<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
M20133 mRNA Translation: AAA40733.1
M23264 mRNA Translation: AAA40759.1
J05454 Genomic DNA Translation: AAA40734.1
PIRiB40494
RefSeqiNP_036634.1, NM_012502.1

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
1I37X-ray2.00A647-902[»]
1I38X-ray2.00A647-902[»]
1R4IX-ray3.10A/B533-637[»]
1XNNX-ray2.20A647-902[»]
2IHQX-ray2.00A647-902[»]
2NW4X-ray3.00A647-902[»]
3G0WX-ray1.95A647-902[»]
SMRiP15207
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi246396, 3 interactors
DIPiDIP-5963N
IntActiP15207, 1 interactor
STRINGi10116.ENSRNOP00000009129

Chemistry databases

BindingDBiP15207
ChEMBLiCHEMBL3072
DrugCentraliP15207
GuidetoPHARMACOLOGYi628

PTM databases

iPTMnetiP15207
PhosphoSitePlusiP15207

Proteomic databases

PaxDbiP15207
PRIDEiP15207

Genome annotation databases

GeneIDi24208
KEGGirno:24208

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		367
RGDi2147, Ar

Phylogenomic databases

eggNOGiKOG3575, Eukaryota
InParanoidiP15207
OrthoDBi615449at2759
PhylomeDBiP15207
TreeFamiTF350286

Enzyme and pathway databases

ReactomeiR-RNO-3371497, HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand
R-RNO-383280, Nuclear Receptor transcription pathway
R-RNO-4090294, SUMOylation of intracellular receptors
R-RNO-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-RNO-5689880, Ub-specific processing proteases

Miscellaneous databases

EvolutionaryTraceiP15207

Protein Ontology

More...PROi		PR:P15207

Family and domain databases

Gene3Di1.10.565.10, 1 hit
3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR001103, Andrgn_rcpt
IPR035500, NHR-like_dom_sf
IPR000536, Nucl_hrmn_rcpt_lig-bd
IPR001628, Znf_hrmn_rcpt
IPR013088, Znf_NHR/GATA
PfamiView protein in Pfam
PF02166, Androgen_recep, 1 hit
PF00104, Hormone_recep, 1 hit
PF00105, zf-C4, 1 hit
PRINTSiPR00521, ANDROGENR
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

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 nameiANDR_RAT
<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: P15207
Secondary accession number(s): Q63049
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 23, 2022
This is version 213 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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