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Entry version 135 (08 May 2019)
Sequence version 3 (13 Jul 2010)
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Protein

Androgen receptor

Gene

AR

Organism
Sus scrofa (Pig)
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

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

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_section">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 sitei682AndrogenBy similarity1
Binding sitei729AndrogenBy similarity1
Binding sitei854AndrogenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi535 – 608Nuclear receptorPROSITE-ProRule annotationAdd BLAST74
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri536 – 556NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri572 – 596NR 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

GO - Biological processi

<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

<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:
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_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:AR
Synonyms:NR3C4
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
<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
  • UP000008227 <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: 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

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 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_00000537101 – 896Androgen receptorAdd BLAST896

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 residuei65Phosphoserine; by CDK9By similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei215Phosphotyrosine; by CSKBy similarity1
Modified residuei248PhosphoserineBy similarity1
Modified residuei259Phosphotyrosine; by CSK and TNK2By similarity1
Modified residuei299Phosphotyrosine; by CSKBy similarity1
Modified residuei338Phosphotyrosine; by CSKBy similarity1
Modified residuei349Phosphotyrosine; by CSKBy similarity1
Modified residuei354Phosphotyrosine; by CSKBy similarity1
Modified residuei355Phosphotyrosine; by CSK and TNK2By similarity1
<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-linki378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei385Phosphotyrosine; by CSKBy similarity1
Cross-linki497Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei511Phosphotyrosine; by CSKBy similarity1
Modified residuei528Phosphotyrosine; by CSKBy similarity1
Modified residuei627Phosphoserine; by STK4/MST1By similarity1
Cross-linki822Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki824Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei892Phosphotyrosine; by CSKBy similarity1

<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

Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-511 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-65 by CDK9 regulates AR promoter selectivity and cell growth (By similarity).By similarity
Sumoylated on Lys-378 (major) and Lys-497 (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
Q9GKL7

PRoteomics IDEntifications database

More...
PRIDEi
Q9GKL7

<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 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, PELP1, PQBP1, RANBP9, RBAK, SPDEF, SRA1, TGFB1I1 and RREB1.

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

Interacts with SLC30A9 and RAD54L2/ARIP4.

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.

Interacts with ZNF318.

Interacts with BUD31.

Interacts with ARID4A.

Interacts with ARID4B.

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 similarity

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>Sitei697Interaction with coactivator LXXL and FXXFY motifsBy similarity1
Sitei874Interaction with coactivator FXXLF and FXXFY motifsBy similarity1

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000013166

<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
Q9GKL7

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_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>Domaini645 – 876NR 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 – 563Interaction with ZNF318By similarityAdd BLAST563
Regioni1 – 534ModulatingBy similarityAdd BLAST534
Regioni528 – 895Interaction with LPXNBy similarityAdd BLAST368
Regioni548 – 638Interaction with HIPK3By similarityAdd BLAST91
Regioni568 – 895Interaction with CCAR1By similarityAdd BLAST328
Regioni601 – 895Interaction 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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi55 – 62Poly-Gln8
Compositional biasi69 – 75Poly-Gln7
Compositional biasi180 – 189Poly-Gln10
Compositional biasi364 – 373Poly-Pro10
Compositional biasi388 – 394Poly-Ala7
Compositional biasi441 – 446Poly-Gly6

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri536 – 556NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri572 – 596NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3575 Eukaryota
ENOG410XRZC LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000037950

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9GKL7

KEGG Orthology (KO)

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KOi
K08557

Database of Orthologous Groups

More...
OrthoDBi
615449at2759

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

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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>. 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_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.

Q9GKL7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEVQLGLGRV YPRPPSKTFR GAFQNLFQSV REVIQNPGPR HPEAASAAPP
60 70 80 90 100
GARLQQQQLQ QQETSPRRQQ QQQQQPSEDG SPQVQSRGPT GYLALDEKQQ
110 120 130 140 150
PSQQQSAPEC HPESGCTPEP GAASAASKGL QQQPPAPPDE DDSAAPSTLS
160 170 180 190 200
LLGPTFPGLS SCSTDLKDIL SEAGTMQLLQ QQQQQQQQQE AVSEGNSSGR
210 220 230 240 250
AREATGAPIS SKDSYLGGSS TISDSAKELC KAVSVSMGLG VEALEHLSPG
260 270 280 290 300
EQLRGDCMYA PLLTGPPSVR PTPCAPLAEC KGSLLDDGPG KSNEETAEYS
310 320 330 340 350
PFKAGYTKGL DSESLGCSSG GEAGGSGTLE LPSALSLYKS GALDDVAAYP
360 370 380 390 400
SRDYYNFPLA LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD
410 420 430 440 450
LASLHGGGAP GPGSGSPSAT SSSSWHTLFT AEESQLYGPC GGGGGGSAGE
460 470 480 490 500
AGAVAPYGYT RPPQGLAGQE GDLAIPDIWY PGGVVSRVPY PSPSCVKSEM
510 520 530 540 550
GPWMESYSGP YGDMRLEPTR DHVLPIDYYF PPQKTCLICG DEASGCHYGA
560 570 580 590 600
LTCGSCKVFF KRAAEGKQKY LCASRNDCTI DKFRRKNCPS CRLRKCYEAG
610 620 630 640 650
MTLGARKLKK LGNLKLQEEG EASSATSPTE EPAQKLTVSH IEGYECQPIF
660 670 680 690 700
LNVLEAIEPG VVCAGHDNNQ PDSFAALLSS LNELGERQLV HVVKWAKALP
710 720 730 740 750
GFRNLHVDDQ MAVIQYSWMG LMVFAMGWRS FTNVNSRMLY FAPDLVFNEY
760 770 780 790 800
RMHKSRMYSQ CVRMRHLSQE FGWLQITPQE FLCMKALLLF SIIPVDGLKN
810 820 830 840 850
QKFFDELRMN YIKELDRIIA CKRKNPTSCS RRFYQLTKLL DSVQPIAREL
860 870 880 890
HQFTFDLLIK SHMVSVDFPE MMAEIISVQV PKILSGKVKP IYFHTQ
Length:896
Mass (Da):97,137
Last modified:July 13, 2010 - 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:i43DD668E3FFDC796
GO

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 conflicti13R → W in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti75Missing in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti256D → G in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti323A → E in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti352R → N in AAG37994 (Ref. 1) Curated1
Sequence conflicti363G → R in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti410P → S in AAG40566 (PubMed:11086548).Curated1
Sequence conflicti820 – 823ACKR → VMQE in AAG40566 (PubMed:11086548).Curated4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF202775 mRNA Translation: AAG37994.1
AF161717 mRNA Translation: AAG40566.1

NCBI Reference Sequences

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RefSeqi
NP_999479.2, NM_214314.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
397582

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:397582

<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
AF202775 mRNA Translation: AAG37994.1
AF161717 mRNA Translation: AAG40566.1
RefSeqiNP_999479.2, NM_214314.2

3D structure databases

SMRiQ9GKL7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013166

Proteomic databases

PaxDbiQ9GKL7
PRIDEiQ9GKL7

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397582
KEGGissc:397582

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
367

Phylogenomic databases

eggNOGiKOG3575 Eukaryota
ENOG410XRZC LUCA
HOGENOMiHOG000037950
InParanoidiQ9GKL7
KOiK08557
OrthoDBi615449at2759

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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_PIG
<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: Q9GKL7
Secondary accession number(s): Q9GKN9
<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: June 21, 2004
Last sequence update: July 13, 2010
Last modified: May 8, 2019
This is version 135 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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