Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3)

 PRGR_HUMAN              Reviewed;         933 AA.
P06401; A7LQ08; A7X8B0; B4E3T0; Q8TDS3; Q9UPF7;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
21-MAR-2006, sequence version 4.
12-SEP-2018, entry version 231.
RecName: Full=Progesterone receptor;
Short=PR;
AltName: Full=Nuclear receptor subfamily 3 group C member 3;
Name=PGR; Synonyms=NR3C3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE PROMOTER USAGE, AND VARIANT
THR-344.
PubMed=2328727;
Kastner P., Krust A., Turcotte B., Stropp U., Tora L., Gronemeyer H.,
Chambon P.;
"Two distinct estrogen-regulated promoters generate transcripts
encoding the two functionally different human progesterone receptor
forms A and B.";
EMBO J. 9:1603-1614(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-660.
PubMed=3551956; DOI=10.1016/0006-291X(87)91416-1;
Misrahi M., Atger M., D'Auriol L., Loosfelt H., Meriel C.,
Fridlansky F., Guiochon-Mantel A., Galibert F., Milgrom E.;
"Complete amino acid sequence of the human progesterone receptor
deduced from cloned cDNA.";
Biochem. Biophys. Res. Commun. 143:740-748(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-660.
Kieback D.G., Agoulnik I.U., Tong X.-W.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Mammary tumor;
Hisatomi H., Wakita K., Kohno N., Nagao K., Hirata H., Hikiji K.;
"Progesterone Receptor, alternative splicing variant, mRNA.";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=18375150; DOI=10.1016/j.ympev.2007.12.026;
Chen C., Opazo J.C., Erez O., Uddin M., Santolaya-Forgas J.,
Goodman M., Grossman L.I., Romero R., Wildman D.E.;
"The human progesterone receptor shows evidence of adaptive evolution
associated with its ability to act as a transcription factor.";
Mol. Phylogenet. Evol. 47:637-649(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE PROMOTER USAGE,
AND VARIANT LEU-660.
TISSUE=Adipose tissue, and Aorta;
PubMed=12644308; DOI=10.1016/S0303-7207(02)00380-5;
Saner K.J., Welter B.H., Zhang F., Hansen E., Dupont B., Wei Y.,
Price T.M.;
"Cloning and expression of a novel, truncated, progesterone
receptor.";
Mol. Cell. Endocrinol. 200:155-163(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-50; VAL-120;
LEU-186; ARG-301; THR-344; SER-444; LEU-529; PRO-536; VAL-651 AND
LEU-865.
NIEHS SNPs program;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 11-22 AND 673-679, PHOSPHORYLATION AT SER-20;
SER-102; SER-130; SER-162; SER-190; SER-213; SER-345 AND SER-676, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11110801; DOI=10.1074/jbc.M009805200;
Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L.;
"Identification of a phosphorylation site in the hinge region of the
human progesterone receptor and additional amino-terminal
phosphorylation sites.";
J. Biol. Chem. 276:8475-8483(2001).
[12]
PROTEIN SEQUENCE OF 204-217, FUNCTION (ISOFORM 4), AND SUBCELLULAR
LOCATION (ISOFORM 4).
TISSUE=Heart;
PubMed=23518922; DOI=10.1210/me.2012-1292;
Dai Q., Shah A.A., Garde R.V., Yonish B.A., Zhang L., Medvitz N.A.,
Miller S.E., Hansen E.L., Dunn C.N., Price T.M.;
"A truncated progesterone receptor (PR-M) localizes to the
mitochondrion and controls cellular respiration.";
Mol. Endocrinol. 27:741-753(2013).
[13]
FUNCTION.
PubMed=1587864;
Meyer M.E., Quirin-Stricker C., Lerouge T., Bocquel M.T.,
Gronemeyer H.;
"A limiting factor mediates the differential activation of promoters
by the human progesterone receptor isoforms.";
J. Biol. Chem. 267:10882-10887(1992).
[14]
INTERACTION WITH GTF2B.
PubMed=1517211;
Ing N.H., Beekman J.M., Tsai S.Y., Tsai M.J., O'Malley B.W.;
"Members of the steroid hormone receptor superfamily interact with
TFIIB (S300-II).";
J. Biol. Chem. 267:17617-17623(1992).
[15]
FUNCTION (ISOFORM A).
PubMed=8264658; DOI=10.1210/mend.7.10.8264658;
Vegeto E., Shahbaz M.M., Wen D.X., Goldman M.E., O'Malley B.W.,
McDonnell D.P.;
"Human progesterone receptor A form is a cell- and promoter-specific
repressor of human progesterone receptor B function.";
Mol. Endocrinol. 7:1244-1255(1993).
[16]
FUNCTION (ISOFORM A).
PubMed=8180103; DOI=10.1016/0960-0760(94)90190-2;
McDonnell D.P., Shahbaz M.M., Vegeto E., Goldman M.E.;
"The human progesterone receptor A-form functions as a transcriptional
modulator of mineralocorticoid receptor transcriptional activity.";
J. Steroid Biochem. Mol. Biol. 48:425-432(1994).
[17]
FUNCTION.
PubMed=7969170; DOI=10.1128/MCB.14.12.8356;
Wen D.X., Xu Y.F., Mais D.E., Goldman M.E., McDonnell D.P.;
"The A and B isoforms of the human progesterone receptor operate
through distinct signaling pathways within target cells.";
Mol. Cell. Biol. 14:8356-8364(1994).
[18]
PHOSPHORYLATION AT SER-81 AND SER-162.
PubMed=7476977; DOI=10.1210/mend.9.8.7476977;
Zhang Y., Beck C.A., Poletti A., Edwards D.P., Weigel N.L.;
"Identification of a group of Ser-Pro motif hormone-inducible
phosphorylation sites in the human progesterone receptor.";
Mol. Endocrinol. 9:1029-1040(1995).
[19]
PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345.
PubMed=8702648; DOI=10.1074/jbc.271.32.19546;
Beck C.A., Zhang Y., Altmann M., Weigel N.L., Edwards D.P.;
"Stoichiometry and site-specific phosphorylation of human progesterone
receptor in native target cells and in the baculovirus expression
system.";
J. Biol. Chem. 271:19546-19555(1996).
[20]
FUNCTION.
PubMed=9407067; DOI=10.1074/jbc.272.52.32889;
Giangrande P.H., Pollio G., McDonnell D.P.;
"Mapping and characterization of the functional domains responsible
for the differential activity of the A and B isoforms of the human
progesterone receptor.";
J. Biol. Chem. 272:32889-32900(1997).
[21]
PHOSPHORYLATION AT SER-162; SER-190 AND SER-400.
PubMed=9171245; DOI=10.1210/mend.11.6.0006;
Zhang Y., Beck C.A., Poletti A., Clement J.P. IV, Prendergast P.,
Yip T.-T., Hutchens T.W., Edwards D.P., Weigel N.L.;
"Phosphorylation of human progesterone receptor by cyclin-dependent
kinase 2 on three sites that are authentic basal phosphorylation sites
in vivo.";
Mol. Endocrinol. 11:823-832(1997).
[22]
TISSUE SPECIFICITY.
PubMed=11041221; DOI=10.1093/humrep/15.suppl_3.48;
Mote P.A., Balleine R.L., McGowan E.M., Clarke C.L.;
"Heterogeneity of progesterone receptors A and B expression in human
endometrial glands and stroma.";
Hum. Reprod. 15:48-56(2000).
[23]
FUNCTION, AND INTERACTION WITH NCOR2; NCOA2 AND NCOA1.
PubMed=10757795; DOI=10.1128/MCB.20.9.3102-3115.2000;
Giangrande P.H., Kimbrel E.A., Edwards D.P., McDonnell D.P.;
"The opposing transcriptional activities of the two isoforms of the
human progesterone receptor are due to differential cofactor
binding.";
Mol. Cell. Biol. 20:3102-3115(2000).
[24]
PHOSPHORYLATION AT SER-190 AND SER-294.
PubMed=10628747; DOI=10.1210/mend.14.1.0413;
Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T.,
Weigel N.L., Edwards D.P.;
"Differential hormone-dependent phosphorylation of progesterone
receptor A and B forms revealed by a phosphoserine site-specific
monoclonal antibody.";
Mol. Endocrinol. 14:52-65(2000).
[25]
PHOSPHORYLATION AT SER-294, UBIQUITINATION, AND MUTAGENESIS OF
SER-294; SER-344 AND SER-345.
PubMed=10655479; DOI=10.1073/pnas.97.3.1032;
Lange C.A., Shen T., Horwitz K.B.;
"Phosphorylation of human progesterone receptors at serine-294 by
mitogen-activated protein kinase signals their degradation by the 26S
proteasome.";
Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000).
[26]
FUNCTION, AND MUTAGENESIS OF LEU-55; LEU-58; LEU-59; LEU-115; LEU-118;
LEU-119 AND TRP-140.
PubMed=11546784; DOI=10.1074/jbc.M106843200;
Tung L., Shen T., Abel M.G., Powell R.L., Takimoto G.S.,
Sartorius C.A., Horwitz K.B.;
"Mapping the unique activation function 3 in the progesterone B-
receptor upstream segment. Two LXXLL motifs and a tryptophan residue
are required for activity.";
J. Biol. Chem. 276:39843-39851(2001).
[27]
INTERACTION WITH PRMT2.
PubMed=12039952; DOI=10.1074/jbc.M201053200;
Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.;
"Identification of protein arginine methyltransferase 2 as a
coactivator for estrogen receptor alpha.";
J. Biol. Chem. 277:28624-28630(2002).
[28]
INTERACTION WITH SMARD1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[29]
PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-400.
PubMed=15572662; DOI=10.1128/MCB.24.24.10542-10557.2004;
Pierson-Mullany L.K., Lange C.A.;
"Phosphorylation of progesterone receptor serine 400 mediates ligand-
independent transcriptional activity in response to activation of
cyclin-dependent protein kinase 2.";
Mol. Cell. Biol. 24:10542-10557(2004).
[30]
PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION,
AND FUNCTION.
PubMed=15798179; DOI=10.1128/MCB.25.8.2885-2898.2005;
Narayanan R., Edwards D.P., Weigel N.L.;
"Human progesterone receptor displays cell cycle-dependent changes in
transcriptional activity.";
Mol. Cell. Biol. 25:2885-2898(2005).
[31]
INTERACTION WITH UNC45A.
PubMed=16478993; DOI=10.1128/MCB.26.5.1722-1730.2006;
Chadli A., Graham J.D., Abel M.G., Jackson T.A., Gordon D.F.,
Wood W.M., Felts S.J., Horwitz K.B., Toft D.;
"GCUNC-45 is a novel regulator for the progesterone receptor/hsp90
chaperoning pathway.";
Mol. Cell. Biol. 26:1722-1730(2006).
[32]
SUMOYLATION AT LYS-7; LYS-388 AND LYS-531, INTERACTION WITH PIAS3,
FUNCTION, AND MUTAGENESIS OF LYS-7; LYS-388 AND LYS-531.
PubMed=17020914; DOI=10.1093/nar/gkl691;
Man J.-H., Li H.-Y., Zhang P.-J., Zhou T., He K., Pan X., Liang B.,
Li A.-L., Zhao J., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F.,
Zhang X.-M.;
"PIAS3 induction of PRB sumoylation represses PRB transactivation by
destabilizing its retention in the nucleus.";
Nucleic Acids Res. 34:5552-5566(2006).
[33]
INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION AT
LYS-388, FUNCTION, AND MUTAGENESIS OF LYS-388.
PubMed=17347654; DOI=10.1038/sj.emboj.7601602;
Zhang P.-J., Zhao J., Li H.-Y., Man J.-H., He K., Zhou T., Pan X.,
Li A.-L., Gong W.-L., Jin B.-F., Xia Q., Yu M., Shen B.-F.,
Zhang X.-M.;
"CUE domain containing 2 regulates degradation of progesterone
receptor by ubiquitin-proteasome.";
EMBO J. 26:1831-1842(2007).
[34]
PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, AND
MUTAGENESIS OF SER-294 AND LYS-388.
PubMed=17717077; DOI=10.1210/me.2007-0248;
Daniel A.R., Faivre E.J., Lange C.A.;
"Phosphorylation-dependent antagonism of sumoylation derepresses
progesterone receptor action in breast cancer cells.";
Mol. Endocrinol. 21:2890-2906(2007).
[35]
PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-294.
PubMed=17173941; DOI=10.1016/j.steroids.2006.11.009;
Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A.,
Lange C.A.;
"Linkage of progestin and epidermal growth factor signaling:
phosphorylation of progesterone receptors mediates transcriptional
hypersensitivity and increased ligand-independent breast cancer cell
growth.";
Steroids 72:188-201(2007).
[36]
PHOSPHORYLATION AT SER-294; SER-345 AND SER-400, INTERACTION WITH SP1,
FUNCTION, AND MUTAGENESIS OF SER-344; SER-345 AND SER-400.
PubMed=18202149; DOI=10.1210/me.2007-0437;
Faivre E.J., Daniel A.R., Hillard C.J., Lange C.A.;
"Progesterone receptor rapid signaling mediates serine 345
phosphorylation and tethering to specificity protein 1 transcription
factors.";
Mol. Endocrinol. 22:823-837(2008).
[37]
PALMITOYLATION.
PubMed=22031296; DOI=10.1091/mbc.E11-07-0638;
Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
"DHHC-7 and -21 are palmitoylacyltransferases for sex steroid
receptors.";
Mol. Biol. Cell 23:188-199(2012).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[39]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 682-933.
PubMed=9620806; DOI=10.1038/30775;
Williams S.P., Sigler P.B.;
"Atomic structure of progesterone complexed with its receptor.";
Nature 393:392-396(1998).
[40]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 676-933.
PubMed=15937332; DOI=10.1074/jbc.M504144200;
Zhang Z., Olland A.M., Zhu Y., Cohen J., Berrodin T., Chippari S.,
Appavu C., Li S., Wilhem J., Chopra R., Fensome A., Zhang P.,
Wrobel J., Unwalla R.J., Lyttle C.R., Winneker R.C.;
"Molecular and pharmacological properties of a potent and selective
novel nonsteroidal progesterone receptor agonist tanaproget.";
J. Biol. Chem. 280:28468-28475(2005).
-!- 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 transcriptional
activator or repressor. {ECO:0000269|PubMed:10757795,
ECO:0000269|PubMed:1587864, 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.
-!- 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. Isoform A
interacts with NCOR2. Isoform B (but not isoform A) interacts with
NCOA2 and NCOA1. Isoform B (but not isoform A) interacts with
KLF9. Interacts with GTF2B (PubMed:1517211).
{ECO:0000250|UniProtKB:Q00175, ECO:0000269|PubMed:10757795,
ECO:0000269|PubMed:12039952, ECO:0000269|PubMed:12917342,
ECO:0000269|PubMed:1517211, ECO:0000269|PubMed:16478993,
ECO:0000269|PubMed:17020914, ECO:0000269|PubMed:17347654,
ECO:0000269|PubMed:18202149}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-78539, EBI-78539;
Q9H467:CUEDC2; NbExp=9; IntAct=EBI-78539, EBI-1248228;
P03372:ESR1; NbExp=20; IntAct=EBI-78539, EBI-78473;
P40763:STAT3; NbExp=3; IntAct=EBI-78539, EBI-518675;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=B; Synonyms=PRB, PR-B;
IsoId=P06401-1; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=A; Synonyms=PRA, PR-A;
IsoId=P06401-2; Sequence=VSP_003706;
Note=Produced by alternative promoter usage.;
Name=3;
IsoId=P06401-3; Sequence=VSP_046942;
Note=Produced by alternative splicing of isoform B.;
Name=4; Synonyms=PR-M;
IsoId=P06401-4; Sequence=VSP_047454, VSP_047455;
Note=Produced by alternative promoter usage.;
Name=5; Synonyms=delta4;
IsoId=P06401-5; Sequence=VSP_053543;
Note=Produced by alternative splicing of isoform B.;
-!- TISSUE SPECIFICITY: In reproductive tissues the expression of
isoform A and isoform B varies as a consequence of developmental
and hormonal status. Isoform A and isoform B are expressed in
comparable levels in uterine glandular epithelium during the
proliferative phase of the menstrual cycle. Expression of isoform
B but not of isoform A persists in the glands during mid-secretory
phase. In the stroma, isoform A is the predominant form throughout
the cycle. Heterogeneous isoform expression between the glands of
the endometrium basalis and functionalis is implying region-
specific responses to hormonal stimuli.
{ECO:0000269|PubMed:11041221}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain.
-!- 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. Promoted by MAPK-mediated phosphorylation on
Ser-294. {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: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}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pgr/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Progesterone receptor entry;
URL="https://en.wikipedia.org/wiki/Progesterone_receptor";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X51730; CAA36018.1; -; mRNA.
EMBL; M15716; AAA60081.1; -; mRNA.
EMBL; AF016381; AAD01587.1; -; mRNA.
EMBL; AB084248; BAB91074.1; -; mRNA.
EMBL; DQ234979; ABB72139.1; -; Genomic_DNA.
EMBL; AY212933; AAO61671.1; -; mRNA.
EMBL; AK304853; BAG65592.1; -; mRNA.
EMBL; AY525610; AAS00096.1; -; Genomic_DNA.
EMBL; AP001533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW66999.1; -; Genomic_DNA.
EMBL; CH471065; EAW67000.1; -; Genomic_DNA.
CCDS; CCDS59229.1; -. [P06401-3]
CCDS; CCDS8310.1; -. [P06401-1]
PIR; S09971; QRHUP.
RefSeq; NP_000917.3; NM_000926.4. [P06401-1]
RefSeq; NP_001189403.1; NM_001202474.3. [P06401-2]
RefSeq; NP_001258090.1; NM_001271161.2.
RefSeq; NP_001258091.1; NM_001271162.1. [P06401-3]
UniGene; Hs.32405; -.
UniGene; Hs.742403; -.
PDB; 1A28; X-ray; 1.80 A; A/B=678-933.
PDB; 1E3K; X-ray; 2.80 A; A/B=676-933.
PDB; 1SQN; X-ray; 1.45 A; A/B=673-933.
PDB; 1SR7; X-ray; 1.46 A; A/B=676-933.
PDB; 1ZUC; X-ray; 2.00 A; A/B=676-933.
PDB; 2C7A; X-ray; 2.50 A; A/B=563-640.
PDB; 2OVH; X-ray; 2.00 A; A=678-933.
PDB; 2OVM; X-ray; 2.60 A; A=678-933.
PDB; 2W8Y; X-ray; 1.80 A; A/B=678-933.
PDB; 3D90; X-ray; 2.26 A; A/B=676-933.
PDB; 3G8O; X-ray; 1.90 A; A/B=673-933.
PDB; 3HQ5; X-ray; 2.10 A; A/B=678-933.
PDB; 3KBA; X-ray; 2.00 A; A/B=681-933.
PDB; 3ZR7; X-ray; 1.65 A; A/B=678-933.
PDB; 3ZRA; X-ray; 1.90 A; A/B=678-933.
PDB; 3ZRB; X-ray; 1.80 A; A/B=678-933.
PDB; 4A2J; X-ray; 2.00 A; A/B=678-933.
PDB; 4APU; X-ray; 1.90 A; A/B=678-933.
PDB; 4OAR; X-ray; 2.41 A; A=678-933.
PDB; 5CC0; X-ray; 2.40 A; A/B=561-641.
PDBsum; 1A28; -.
PDBsum; 1E3K; -.
PDBsum; 1SQN; -.
PDBsum; 1SR7; -.
PDBsum; 1ZUC; -.
PDBsum; 2C7A; -.
PDBsum; 2OVH; -.
PDBsum; 2OVM; -.
PDBsum; 2W8Y; -.
PDBsum; 3D90; -.
PDBsum; 3G8O; -.
PDBsum; 3HQ5; -.
PDBsum; 3KBA; -.
PDBsum; 3ZR7; -.
PDBsum; 3ZRA; -.
PDBsum; 3ZRB; -.
PDBsum; 4A2J; -.
PDBsum; 4APU; -.
PDBsum; 4OAR; -.
PDBsum; 5CC0; -.
ProteinModelPortal; P06401; -.
SMR; P06401; -.
BioGrid; 111260; 68.
DIP; DIP-5967N; -.
ELM; P06401; -.
IntAct; P06401; 14.
MINT; P06401; -.
STRING; 9606.ENSP00000325120; -.
BindingDB; P06401; -.
ChEMBL; CHEMBL208; -.
DrugBank; DB01431; Allylestrenol.
DrugBank; DB01406; Danazol.
DrugBank; DB00304; Desogestrel.
DrugBank; DB01395; Drospirenone.
DrugBank; DB00378; Dydrogesterone.
DrugBank; DB00823; Ethynodiol diacetate.
DrugBank; DB00294; Etonogestrel.
DrugBank; DB00588; Fluticasone Propionate.
DrugBank; DB06789; Hydroxyprogesterone caproate.
DrugBank; DB00367; Levonorgestrel.
DrugBank; DB00603; Medroxyprogesterone acetate.
DrugBank; DB00351; Megestrol acetate.
DrugBank; DB02998; Methyltrienolone.
DrugBank; DB00834; Mifepristone.
DrugBank; DB06713; Norelgestromin.
DrugBank; DB00717; Norethisterone.
DrugBank; DB00957; Norgestimate.
DrugBank; DB09389; Norgestrel.
DrugBank; DB05253; Proellex.
DrugBank; DB00396; Progesterone.
DrugBank; DB00421; Spironolactone.
DrugBank; DB04787; Tanaproget.
DrugBank; DB08867; Ulipristal.
GuidetoPHARMACOLOGY; 627; -.
SwissLipids; SLP:000001574; -.
iPTMnet; P06401; -.
PhosphoSitePlus; P06401; -.
SwissPalm; P06401; -.
BioMuta; PGR; -.
DMDM; 90110048; -.
MaxQB; P06401; -.
PaxDb; P06401; -.
PeptideAtlas; P06401; -.
PRIDE; P06401; -.
ProteomicsDB; 51901; -.
ProteomicsDB; 51902; -. [P06401-2]
DNASU; 5241; -.
Ensembl; ENST00000263463; ENSP00000263463; ENSG00000082175. [P06401-5]
Ensembl; ENST00000325455; ENSP00000325120; ENSG00000082175. [P06401-1]
Ensembl; ENST00000534013; ENSP00000436561; ENSG00000082175. [P06401-3]
GeneID; 5241; -.
KEGG; hsa:5241; -.
UCSC; uc001pgh.3; human. [P06401-1]
CTD; 5241; -.
DisGeNET; 5241; -.
EuPathDB; HostDB:ENSG00000082175.14; -.
GeneCards; PGR; -.
HGNC; HGNC:8910; PGR.
HPA; CAB000068; -.
HPA; CAB055100; -.
HPA; HPA004751; -.
HPA; HPA008428; -.
HPA; HPA017176; -.
MalaCards; PGR; -.
MIM; 607311; gene.
neXtProt; NX_P06401; -.
OpenTargets; ENSG00000082175; -.
PharmGKB; PA266; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00760000118887; -.
HOGENOM; HOG000290653; -.
HOVERGEN; HBG007583; -.
InParanoid; P06401; -.
KO; K08556; -.
OMA; CAYPPDA; -.
OrthoDB; EOG091G04YC; -.
PhylomeDB; P06401; -.
TreeFam; TF106510; -.
Reactome; R-HSA-1251985; Nuclear signaling by ERBB4.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
SignaLink; P06401; -.
SIGNOR; P06401; -.
ChiTaRS; PGR; human.
EvolutionaryTrace; P06401; -.
GeneWiki; Progesterone_receptor; -.
GenomeRNAi; 5241; -.
PRO; PR:P06401; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000082175; Expressed in 153 organ(s), highest expression level in endometrium.
CleanEx; HS_PGR; -.
ExpressionAtlas; P06401; baseline and differential.
Genevisible; P06401; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0051117; F:ATPase binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl.
GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEP:UniProtKB.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0038001; P:paracrine signaling; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR000128; Progest_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF02161; Prog_receptor; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00544; PROGESTRONER.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 2.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Isopeptide bond; Lipid-binding; Lipoprotein; Membrane; Metal-binding;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Palmitate;
Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Steroid-binding; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 933 Progesterone receptor.
/FTId=PRO_0000053693.
DOMAIN 679 913 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 567 639 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 567 587 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 603 627 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 566 Modulating, Pro-Rich.
REGION 1 164 AF3; mediates transcriptional activation
(in isoform B).
{ECO:0000269|PubMed:11546784}.
REGION 165 305 Mediates transcriptional transrepression
(in isoform A).
{ECO:0000269|PubMed:9407067}.
REGION 456 546 AF1; mediates transcriptional activation.
{ECO:0000269|PubMed:1587864}.
REGION 687 933 AF2; mediates transcriptional activation.
{ECO:0000269|PubMed:1587864}.
MOTIF 55 59 LXXL motif 1.
{ECO:0000305|PubMed:11546784}.
MOTIF 115 119 LXXL motif 2.
{ECO:0000305|PubMed:11546784}.
MOTIF 183 187 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000269|PubMed:11110801}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000269|PubMed:7476977,
ECO:0000269|PubMed:8702648}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000269|PubMed:11110801,
ECO:0000269|PubMed:8702648}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000269|PubMed:11110801}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11110801,
ECO:0000269|PubMed:15798179,
ECO:0000269|PubMed:7476977,
ECO:0000269|PubMed:8702648,
ECO:0000269|PubMed:9171245}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000269|PubMed:10628747,
ECO:0000269|PubMed:11110801,
ECO:0000269|PubMed:15798179,
ECO:0000269|PubMed:9171245}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000269|PubMed:11110801}.
MOD_RES 294 294 Phosphoserine; by MAPK1.
{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:8702648}.
MOD_RES 345 345 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:11110801,
ECO:0000269|PubMed:18202149,
ECO:0000269|PubMed:8702648}.
MOD_RES 400 400 Phosphoserine; by CDK2.
{ECO:0000269|PubMed:15572662,
ECO:0000269|PubMed:18202149,
ECO:0000269|PubMed:9171245}.
MOD_RES 676 676 Phosphoserine.
{ECO:0000269|PubMed:11110801}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17020914}.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:17347654}.
CROSSLNK 531 531 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17020914}.
VAR_SEQ 1 594 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046942.
VAR_SEQ 1 164 Missing (in isoform A). {ECO:0000305}.
/FTId=VSP_003706.
VAR_SEQ 1 16 MTELKAKGPRAPHVAG -> MEFIYIYMNFFFFFSV (in
isoform 4).
{ECO:0000303|PubMed:12644308}.
/FTId=VSP_047454.
VAR_SEQ 17 635 Missing (in isoform 4).
{ECO:0000303|PubMed:12644308}.
/FTId=VSP_047455.
VAR_SEQ 636 737 Missing (in isoform 5).
{ECO:0000303|Ref.4}.
/FTId=VSP_053543.
VARIANT 50 50 A -> T (in dbSNP:rs11571143).
{ECO:0000269|Ref.8}.
/FTId=VAR_019221.
VARIANT 120 120 A -> V (in dbSNP:rs11571144).
{ECO:0000269|Ref.8}.
/FTId=VAR_019222.
VARIANT 186 186 P -> L (in dbSNP:rs11571145).
{ECO:0000269|Ref.8}.
/FTId=VAR_019223.
VARIANT 301 301 M -> R (in dbSNP:rs11571146).
{ECO:0000269|Ref.8}.
/FTId=VAR_019224.
VARIANT 344 344 S -> T (in dbSNP:rs3740753).
{ECO:0000269|PubMed:2328727,
ECO:0000269|Ref.8}.
/FTId=VAR_016117.
VARIANT 347 347 C -> S (in dbSNP:rs11571147).
/FTId=VAR_025555.
VARIANT 444 444 A -> S (in dbSNP:rs11571150).
{ECO:0000269|Ref.8}.
/FTId=VAR_019225.
VARIANT 529 529 V -> L (in dbSNP:rs11571151).
{ECO:0000269|Ref.8}.
/FTId=VAR_019226.
VARIANT 536 536 Q -> P (in dbSNP:rs11571152).
{ECO:0000269|Ref.8}.
/FTId=VAR_019227.
VARIANT 625 625 R -> I (in dbSNP:rs2020874).
/FTId=VAR_014627.
VARIANT 651 651 L -> V (in dbSNP:rs11571222).
{ECO:0000269|Ref.8}.
/FTId=VAR_019228.
VARIANT 660 660 V -> L (in dbSNP:rs1042838).
{ECO:0000269|PubMed:12644308,
ECO:0000269|PubMed:3551956,
ECO:0000269|Ref.3}.
/FTId=VAR_016118.
VARIANT 865 865 S -> L (in dbSNP:rs2020880).
{ECO:0000269|Ref.8}.
/FTId=VAR_014628.
MUTAGEN 7 7 K->R: Some loss of sumoylation; when
associated with R-531. Complete loss of
sumoylation; when associated with R-388
and R-531. {ECO:0000269|PubMed:17020914}.
MUTAGEN 55 55 L->A: Reduces transcriptional activation;
when associated with A-58 and A-59.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 58 58 L->A: Reduces transcriptional activation;
when associated with A-55 and A-59.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 59 59 L->A: Reduces transcriptional activation;
when associated with A-55 and A-58.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 115 115 L->A: Reduces transcriptional activation;
when associated with A-118 and A-119.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 118 118 L->A: Reduces transcriptional activation;
when associated with A-115 and A-119.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 119 119 L->A: Reduces transcriptional activation;
when associated with A-115 and A-118.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 140 140 W->A,F,R: Reduces transcriptional
activation.
{ECO:0000269|PubMed:11546784}.
MUTAGEN 294 294 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.
{ECO:0000269|PubMed:10655479,
ECO:0000269|PubMed:17173941,
ECO:0000269|PubMed:17717077}.
MUTAGEN 294 294 S->D: Decreases protein stability and
increases progesterone-induced
transcriptional activity.
{ECO:0000269|PubMed:10655479,
ECO:0000269|PubMed:17173941,
ECO:0000269|PubMed:17717077}.
MUTAGEN 344 344 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. {ECO:0000269|PubMed:10655479,
ECO:0000269|PubMed:18202149}.
MUTAGEN 345 345 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.
{ECO:0000269|PubMed:10655479,
ECO:0000269|PubMed:18202149}.
MUTAGEN 388 388 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.
{ECO:0000269|PubMed:17020914,
ECO:0000269|PubMed:17347654,
ECO:0000269|PubMed:17717077}.
MUTAGEN 400 400 S->A: Abolishes CDK2-induced activity in
the absence, but not in the presence, of
progestin. Delayed nuclear translocation
in presence of progestin.
{ECO:0000269|PubMed:15572662,
ECO:0000269|PubMed:18202149}.
MUTAGEN 531 531 K->R: Some loss of sumoylation; when
associated with R-7. Completely abolishes
sumoylation; when associated with R-7 and
R-388. {ECO:0000269|PubMed:17020914}.
CONFLICT 226 226 G -> S (in Ref. 1; CAA36018).
{ECO:0000305}.
CONFLICT 256 256 V -> S (in Ref. 1; CAA36018).
{ECO:0000305}.
TURN 568 570 {ECO:0000244|PDB:5CC0}.
STRAND 576 578 {ECO:0000244|PDB:5CC0}.
STRAND 581 583 {ECO:0000244|PDB:5CC0}.
HELIX 585 596 {ECO:0000244|PDB:5CC0}.
STRAND 604 607 {ECO:0000244|PDB:5CC0}.
TURN 613 618 {ECO:0000244|PDB:5CC0}.
HELIX 620 629 {ECO:0000244|PDB:5CC0}.
HELIX 686 694 {ECO:0000244|PDB:1SQN}.
HELIX 711 735 {ECO:0000244|PDB:1SQN}.
HELIX 739 741 {ECO:0000244|PDB:1SQN}.
HELIX 744 771 {ECO:0000244|PDB:1SQN}.
STRAND 774 779 {ECO:0000244|PDB:1SQN}.
STRAND 782 784 {ECO:0000244|PDB:1SQN}.
HELIX 786 788 {ECO:0000244|PDB:1SQN}.
HELIX 792 811 {ECO:0000244|PDB:1SQN}.
HELIX 815 826 {ECO:0000244|PDB:1SQN}.
STRAND 828 830 {ECO:0000244|PDB:1SQN}.
HELIX 838 857 {ECO:0000244|PDB:1SQN}.
HELIX 863 896 {ECO:0000244|PDB:1SQN}.
HELIX 898 901 {ECO:0000244|PDB:1SQN}.
HELIX 907 921 {ECO:0000244|PDB:1SQN}.
STRAND 925 927 {ECO:0000244|PDB:1SQN}.
SEQUENCE 933 AA; 98981 MW; 80452E54FF3A0454 CRC64;
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA IPISLDGLLF
PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS SSPPEKDSGL LDSVLDTLLA
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGC KVGDSSGTAA
AHKVLPRGLS PARQLLLPAS ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS TPVAVGDFPD
CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS PRSYLVAGAN PAAFPDFPLG
PPPPLPPRAT PSRPGEAAVT AAPASASVSS ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC
KAPGASGCLL PRDGLPSTSA SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA LDAVALPQPV
GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY AGHDNTKPDT SSSLLTSLNQ
LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP
DLILNEQRMK ESSFYSLCLT MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ
FEEMRSSYIR ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK


Related products :

Catalog number Product name Quantity
E1273r ELISA kit Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Progesterone receptor,Rat,Rattus norvegicus 96T
E1273m ELISA Mouse,Mus musculus,Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Pr,Progesterone receptor 96T
U1273m CLIA Mouse,Mus musculus,Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Pr,Progesterone receptor 96T
U1273r CLIA Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Progesterone receptor,Rat,Rattus norvegicus 96T
E1273r ELISA Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Progesterone receptor,Rat,Rattus norvegicus 96T
E1273m ELISA kit Mouse,Mus musculus,Nr3c3,Nuclear receptor subfamily 3 group C member 3,Pgr,PR,Pr,Progesterone receptor 96T
U1273h CLIA Homo sapiens,Human,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
E1273h ELISA kit Homo sapiens,Human,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
E1273Rb ELISA kit NR3C3,Nuclear receptor subfamily 3 group C member 3,Oryctolagus cuniculus,PGR,PR,Progesterone receptor,Rabbit 96T
U1273Rb CLIA NR3C3,Nuclear receptor subfamily 3 group C member 3,Oryctolagus cuniculus,PGR,PR,Progesterone receptor,Rabbit 96T
E1273Rb ELISA NR3C3,Nuclear receptor subfamily 3 group C member 3,Oryctolagus cuniculus,PGR,PR,Progesterone receptor,Rabbit 96T
E1273h ELISA Homo sapiens,Human,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
EIAAB27810 Gfrp,Hmr,Mouse,Mus musculus,N10,Nr4a1,Nuclear hormone receptor NUR_77,Nuclear protein N10,Nuclear receptor subfamily 4 group A member 1,Nur77,Orphan nuclear receptor HMR
E1273c ELISA kit Chicken,Gallus gallus,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
E1273c ELISA Chicken,Gallus gallus,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
U1273c CLIA Chicken,Gallus gallus,NR3C3,Nuclear receptor subfamily 3 group C member 3,PGR,PR,Progesterone receptor 96T
EIAAB27783 Homo sapiens,Human,Liver X receptor beta,LXRB,NER,NR1H2,Nuclear receptor NER,Nuclear receptor subfamily 1 group H member 2,Oxysterols receptor LXR-beta,Ubiquitously-expressed nuclear receptor,UNR
EIAAB27782 Liver X receptor beta,Lxrb,Nr1h2,Nuclear receptor subfamily 1 group H member 2,Orphan nuclear receptor OR-1,Oxysterols receptor LXR-beta,Rat,Rattus norvegicus,Ubiquitously-expressed nuclear receptor,U
EIAAB27785 Homo sapiens,Human,NR1I2,Nuclear receptor subfamily 1 group I member 2,Orphan nuclear receptor PAR1,Orphan nuclear receptor PXR,Pregnane X receptor,PXR,Steroid and xenobiotic receptor,SXR
EIAAB27820 CHN,CSMF,Homo sapiens,Human,MINOR,Mitogen-induced nuclear orphan receptor,Neuron-derived orphan receptor 1,NOR1,NR4A3,Nuclear hormone receptor NOR-1,Nuclear receptor subfamily 4 group A member 3,TEC
EIAAB27793 Homo sapiens,Human,NR2C1,Nuclear receptor subfamily 2 group C member 1,Orphan nuclear receptor TR2,Testicular receptor 2,TR2
EIAAB27790 Mouse,mTR2,Mus musculus,Nr2c1,Nuclear receptor subfamily 2 group C member 1,Orphan nuclear receptor TR2,Testicular receptor 2,Tr2,Tr2-11
EIAAB27787 CAR,Car,Constitutive androstane receptor,Mouse,Mus musculus,Nr1i3,Nuclear receptor subfamily 1 group I member 3,Orphan nuclear receptor MB67
EIAAB27786 Nr1i2,Nuclear receptor subfamily 1 group I member 2,Orphan nuclear receptor PXR,Pregnane X receptor,Pxr,Rat,Rattus norvegicus
EIAAB27784 Mouse,Mus musculus,Nr1i2,Nuclear receptor subfamily 1 group I member 2,Orphan nuclear receptor PXR,Pregnane X receptor,Pxr


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur