PGR
entrez
5241
canonical
uniprot
P06401
canonical
ensembl
ENSG00000082175
resolver
ensp
ENSP00000263463
resolver
ensp
ENSP00000325120
resolver
ensp
ENSP00000436561
resolver
ensp
ENSP00000782611
resolver
genesymbol
PGR
resolver
genesymbol_syn
NR3C3
resolver
hgnc
HGNC:8910
resolver
uniprot
A7LQ08
resolver
uniprot
A7X8B0
resolver
uniprot
B4E3T0
resolver
uniprot
Q8TDS3
resolver
uniprot
Q9UPF7
resolver
uniprot_entry
PRGR_HUMAN
resolver
uniprot_sec
A7LQ08
resolver
uniprot_sec
A7X8B0
resolver
uniprot_sec
B4E3T0
resolver
uniprot_sec
Q8TDS3
resolver
uniprot_sec
Q9UPF7
resolver
amino_acid_sequence
MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
uniprot
proteins
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. Depending on the isoform, progesterone receptor functions as a transcriptional activator or repressor. {ECO:0000269|PubMed:10757795, ECO:0000269|PubMed:1587864, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:9407067, ECO:0000305}.; FUNCTION: [Isoform A]: Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2. {ECO:0000269|PubMed:7969170, ECO:0000269|PubMed:8180103, ECO:0000269|PubMed:8264658, ECO:0000305, ECO:0000305|PubMed:10757795}.; FUNCTION: [Isoform B]: Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. {ECO:0000269|PubMed:7969170}.; FUNCTION: [Isoform 4]: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.
uniprot
proteins
mass_dalton
98981
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="K->R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531."; /evidence="ECO:0000269|PubMed:17020914"; MUTAGEN 55; /note="L->A: Reduces transcriptional activation; when associated with A-58 and A-59."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 58; /note="L->A: Reduces transcriptional activation; when associated with A-55 and A-59."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 59; /note="L->A: Reduces transcriptional activation; when associated with A-55 and A-58."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 115; /note="L->A: Reduces transcriptional activation; when associated with A-118 and A-119."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 118; /note="L->A: Reduces transcriptional activation; when associated with A-115 and A-119."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 119; /note="L->A: Reduces transcriptional activation; when associated with A-115 and A-118."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 140; /note="W->A,F,R: Reduces transcriptional activation."; /evidence="ECO:0000269|PubMed:11546784"; MUTAGEN 294; /note="S->A: No effect on interaction with CUEDC2. Impaired progesterone-induced transcriptional activity. No CUEDC2- nor progestin-mediated protein degradation. No change in sumoylation; when associated with A-344 and A-345."; /evidence="ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17717077"; MUTAGEN 294; /note="S->D: Decreases protein stability and increases progesterone-induced transcriptional activity."; /evidence="ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17717077"; MUTAGEN 344; /note="S->A: No interaction with SP1. No change in progestin-induced protein degradation; when associated with A-345. No change in sumoylation; when associated with A-294 and A-345."; /evidence="ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:18202149"; MUTAGEN 345; /note="S->A: No change in progestin-induced protein degradation; when associated with A-344. No change in sumoylation; when associated with A-294 and A-344."; /evidence="ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:18202149"; MUTAGEN 388; /note="K->R: Great loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-531. Loss of CUEDC2-mediated protein degradation. Increased ligand-dependent transcriptional activity."; /evidence="ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17717077"; MUTAGEN 400; /note="S->A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin."; /evidence="ECO:0000269|PubMed:15572662, ECO:0000269|PubMed:18202149"; MUTAGEN 531; /note="K->R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388."; /evidence="ECO:0000269|PubMed:17020914
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on multiple serine sites. Several of these sites are hormone-dependent. Phosphorylation on Ser-294 occurs preferentially on isoform B, 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 G(2)/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1. {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:11110801, ECO:0000269|PubMed:15572662, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:7476977, ECO:0000269|PubMed:8702648, ECO:0000269|PubMed:9171245}.; PTM: 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. {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17347654, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:8702648}.; PTM: Ubiquitination is hormone-dependent and represses sumoylation on the same site (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Promoted by MAPK-mediated phosphorylation on Ser-294 (PubMed:10628747, PubMed:10655479, PubMed:15798179, PubMed:17173941, PubMed:17717077, PubMed:18202149, PubMed:8702648). Ubiquitinated by UBR5, leading to its degradation: UBR5 specifically recognizes and binds ligand-bound PGR when it is not associated with coactivators (NCOAs) (PubMed:37478846). In presence of NCOAs, the UBR5-degron is not accessible, preventing its ubiquitination and degradation (PubMed:37478846). {ECO:0000269|PubMed:10628747, ECO:0000269|PubMed:10655479, ECO:0000269|PubMed:15798179, ECO:0000269|PubMed:17173941, ECO:0000269|PubMed:17717077, ECO:0000269|PubMed:18202149, ECO:0000269|PubMed:37478846, ECO:0000269|PubMed:8702648}.; PTM: 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. {ECO:0000269|PubMed:22031296}.
uniprot
proteins
protein_family
NR3 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10628747
uniprot
proteins
pubmed
10655479
uniprot
proteins
pubmed
10757795
uniprot
proteins
pubmed
11041221
uniprot
proteins
pubmed
11110801
uniprot
proteins
pubmed
11546784
uniprot
proteins
pubmed
12039952
uniprot
proteins
pubmed
12644308
uniprot
proteins
pubmed
12917342
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1517211
uniprot
proteins
pubmed
15572662
uniprot
proteins
pubmed
15798179
uniprot
proteins
pubmed
1587864
uniprot
proteins
pubmed
15937332
uniprot
proteins
pubmed
16478993
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17020914
uniprot
proteins
pubmed
17173941
uniprot
proteins
pubmed
17347654
uniprot
proteins
pubmed
17717077
uniprot
proteins
pubmed
18202149
uniprot
proteins
pubmed
18375150
uniprot
proteins
pubmed
22031296
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
2328727
uniprot
proteins
pubmed
23518922
uniprot
proteins
pubmed
3551956
uniprot
proteins
pubmed
37478846
uniprot
proteins
pubmed
7476977
uniprot
proteins
pubmed
7969170
uniprot
proteins
pubmed
8180103
uniprot
proteins
pubmed
8264658
uniprot
proteins
pubmed
8702648
uniprot
proteins
pubmed
9171245
uniprot
proteins
pubmed
9407067
uniprot
proteins
pubmed
9620806
uniprot
proteins
sequence_length
933
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus. Cytoplasm. Note=Mainly nuclear.; SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion outer membrane {ECO:0000269|PubMed:23518922}.
uniprot
proteins