A7X8B7 · PRGR_GORGO
- ProteinProgesterone receptor
- GenePGR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids933 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation.
Features
Showing features for dna binding, binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProgesterone receptor
- Short namesPR
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Gorilla
Accessions
- Primary accessionA7X8B7
Proteomes
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000375854 | 1-933 | Progesterone receptor | |||
Sequence: MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGIPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK | ||||||
Modified residue | 20 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 81 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 162 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 190 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 213 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 294 | Phosphoserine; by MAPK1 | ||||
Sequence: S | ||||||
Modified residue | 345 | Phosphoserine; by MAPK | ||||
Sequence: S | ||||||
Cross-link | 388 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||||
Sequence: K | ||||||
Cross-link | 388 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | ||||||
Modified residue | 400 | Phosphoserine; by CDK2 | ||||
Sequence: S | ||||||
Cross-link | 531 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Modified residue | 676 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388. Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone. Basal phosphorylation on Ser-81, Ser-162, Ser-190 and Ser-400 is increased in response to progesterone and can be phosphorylated in vitro by the CDK2-A1 complex. Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS. Phosphorylation at this site by CDK2 is ligand-independent, and increases nuclear translocation and transcriptional activity. Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1 (By similarity).
Sumoylation is hormone-dependent and represses transcriptional activity. Sumoylation on all three sites is enhanced by PIAS3. Desumoylated by SENP1. Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294 (By similarity).
Ubiquitination is hormone-dependent and represses sumoylation on the same site (By similarity).
Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity).
Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (By similarity).
In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (By similarity).
Promoted by MAPK-mediated phosphorylation on Ser-294 (By similarity).
Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (By similarity).
In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (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).
Keywords
- PTM
Expression
Gene expression databases
Interaction
Subunit
Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and represses transcriptional activity. Interacts with PIAS3; the interaction promotes sumoylation of PR in a hormone-dependent manner, inhibits DNA-binding, and alters nuclear export. Interacts with SP1; the interaction requires ligand-induced phosphorylation on Ser-345 by ERK1/2-MAPK. Interacts with PRMT2. Interacts with NCOA2 and NCOA1. Interacts with KLF9. Interacts with GTF2B (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-164 | AF3; mediates transcriptional activation | ||||
Sequence: MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPL | ||||||
Region | 1-256 | Disordered | ||||
Sequence: MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAV | ||||||
Region | 1-566 | Modulating, Pro-Rich | ||||
Sequence: MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPYPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLETLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQGVLSPLMSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKI | ||||||
Motif | 55-59 | LXXL motif 1 | ||||
Sequence: LDGLL | ||||||
Compositional bias | 68-84 | Polar residues | ||||
Sequence: DPSDEKTQDQQSLSDVE | ||||||
Motif | 115-119 | LXXL motif 2 | ||||
Sequence: LETLL | ||||||
Compositional bias | 120-135 | Polar residues | ||||
Sequence: APSGPGQSQPSPPACE | ||||||
Region | 165-305 | Mediates transcriptional transrepression | ||||
Sequence: MSRSGGKAGDSSGTAAAHKVLPRGLSPSRQLLLPVSGSPHWSGAPVKPSPQPAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIH | ||||||
Motif | 183-187 | Nuclear localization signal | ||||
Sequence: KVLPR | ||||||
Region | 331-378 | Disordered | ||||
Sequence: GGAGAASAFAPPRSSPSASSTPVAVGDFPDCAYPPDAEPKDDAYPLYS | ||||||
Compositional bias | 415-433 | Pro residues | ||||
Sequence: PDFPLGPPPPLPPRAPPSR | ||||||
Region | 415-452 | Disordered | ||||
Sequence: PDFPLGPPPPLPPRAPPSRPGEAAVTAAPASASVSSAS | ||||||
Region | 456-546 | AF1; mediates transcriptional activation | ||||
Sequence: STLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLR | ||||||
Zinc finger | 567-587 | NR C4-type | ||||
Sequence: CLICGDEASGCHYGVLTCGSC | ||||||
Zinc finger | 603-627 | NR C4-type | ||||
Sequence: CAGRNDCIVDKIRRKNCPACRLRKC | ||||||
Domain | 679-913 | NR LBD | ||||
Sequence: QDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVI | ||||||
Region | 687-933 | AF2; mediates transcriptional activation | ||||
Sequence: LINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK |
Domain
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.
Sequence similarities
Belongs to the nuclear hormone receptor family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length933
- Mass (Da)98,830
- Last updated2007-10-23 v1
- Checksum9C1080538291E6E6
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3RJR5 | G3RJR5_GORGO | 831 | |||
A0A2I2YH06 | A0A2I2YH06_GORGO | 764 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 68-84 | Polar residues | ||||
Sequence: DPSDEKTQDQQSLSDVE | ||||||
Compositional bias | 120-135 | Polar residues | ||||
Sequence: APSGPGQSQPSPPACE | ||||||
Compositional bias | 415-433 | Pro residues | ||||
Sequence: PDFPLGPPPPLPPRAPPSR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ234982 EMBL· GenBank· DDBJ | ABB72142.1 EMBL· GenBank· DDBJ | Genomic DNA |