Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P06401

- PRGR_HUMAN

UniProt

P06401 - PRGR_HUMAN

Protein

Progesterone receptor

Gene

PGR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 193 (01 Oct 2014)
      Sequence version 4 (21 Mar 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation.
    Isoform A: inactive in stimulating c-Src/MAPK signaling on hormone stimulation.
    Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi567 – 63973Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri567 – 58721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri603 – 62725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. enzyme binding Source: UniProtKB
    3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
    4. protein binding Source: UniProtKB
    5. receptor binding Source: UniProtKB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    7. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    8. steroid binding Source: UniProtKB-KW
    9. steroid hormone receptor activity Source: ProtInc
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. epithelial cell maturation Source: Ensembl
    3. gene expression Source: Reactome
    4. negative regulation of gene expression Source: UniProtKB
    5. ovulation from ovarian follicle Source: Ensembl
    6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    7. progesterone receptor signaling pathway Source: Ensembl
    8. regulation of epithelial cell proliferation Source: Ensembl
    9. signal transduction Source: ProtInc
    10. tertiary branching involved in mammary gland duct morphogenesis Source: Ensembl
    11. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Lipid-binding, Metal-binding, Steroid-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_116022. Nuclear signaling by ERBB4.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP06401.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Progesterone receptor
    Short name:
    PR
    Alternative name(s):
    Nuclear receptor subfamily 3 group C member 3
    Gene namesi
    Name:PGR
    Synonyms:NR3C3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:8910. PGR.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nucleoplasmic shuttling is both homone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G1 and G2/M phases.
    Isoform A : Nucleus. Cytoplasm
    Note: Mainly nuclear.
    Isoform 4 : Mitochondrion outer membrane 1 Publication

    GO - Cellular componenti

    1. mitochondrial outer membrane Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71K → R: Some loss of sumoylation; when associated with R-531. Complete loss of sumoylation; when associated with R-388 and R-531. 1 Publication
    Mutagenesisi294 – 2941S → 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. 3 Publications
    Mutagenesisi294 – 2941S → D: Decreases protein stability and increases progesterone-induced transcriptional activity. 3 Publications
    Mutagenesisi344 – 3441S → 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. 2 Publications
    Mutagenesisi345 – 3451S → 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. 2 Publications
    Mutagenesisi388 – 3881K → 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. 3 Publications
    Mutagenesisi400 – 4001S → A: Abolishes CDK2-induced activity in the absence, but not in the presence, of progestin. Delayed nuclear translocation in presence of progestin. 2 Publications
    Mutagenesisi531 – 5311K → R: Some loss of sumoylation; when associated with R-7. Completely abolishes sumoylation; when associated with R-7 and R-388. 1 Publication

    Organism-specific databases

    PharmGKBiPA266.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 933933Progesterone receptorPRO_0000053693Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei81 – 811Phosphoserine2 Publications
    Modified residuei102 – 1021Phosphoserine2 Publications
    Modified residuei130 – 1301Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine5 Publications
    Modified residuei190 – 1901Phosphoserine4 Publications
    Modified residuei213 – 2131Phosphoserine1 Publication
    Modified residuei294 – 2941Phosphoserine; by MAPK17 Publications
    Modified residuei345 – 3451Phosphoserine; by MAPK3 Publications
    Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Cross-linki388 – 388Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
    Modified residuei400 – 4001Phosphoserine; by CDK23 Publications
    Cross-linki531 – 531Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei676 – 6761Phosphoserine1 Publication

    Post-translational modificationi

    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 G2/M phase of the cell cycle. Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1.13 Publications
    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-294.9 Publications
    Ubiquitination is hormone-dependent and represses sumoylation on the same site. Promoted by MAPK-mediated phosphorylation on Ser-294.7 Publications
    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.1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP06401.
    PaxDbiP06401.
    PRIDEiP06401.

    PTM databases

    PhosphoSiteiP06401.

    Expressioni

    Gene expression databases

    ArrayExpressiP06401.
    BgeeiP06401.
    CleanExiHS_PGR.
    GenevestigatoriP06401.

    Organism-specific databases

    HPAiCAB000068.
    CAB055100.
    HPA004751.
    HPA008428.
    HPA017176.

    Interactioni

    Subunit structurei

    Interacts with SMARD1 and UNC45A. Interacts with CUEDC2; the interaction promotes ubiquitination, decreases sumoylation, and repesses 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 PRMT2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CUEDC2Q9H4679EBI-78539,EBI-1248228
    STAT3P407633EBI-78539,EBI-518675

    Protein-protein interaction databases

    BioGridi111260. 65 interactions.
    DIPiDIP-5967N.
    IntActiP06401. 8 interactions.
    MINTiMINT-1505587.
    STRINGi9606.ENSP00000325120.

    Structurei

    Secondary structure

    1
    933
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni568 – 5703
    Beta strandi576 – 5783
    Beta strandi581 – 5833
    Helixi585 – 59612
    Turni613 – 6186
    Helixi620 – 63011
    Helixi686 – 6949
    Helixi711 – 73525
    Helixi739 – 7413
    Helixi744 – 77128
    Beta strandi774 – 7796
    Beta strandi782 – 7843
    Helixi786 – 7883
    Helixi792 – 81120
    Helixi815 – 82612
    Beta strandi828 – 8303
    Helixi838 – 85720
    Helixi863 – 89634
    Helixi898 – 9014
    Helixi907 – 92115
    Beta strandi925 – 9273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A28X-ray1.80A/B678-933[»]
    1E3KX-ray2.80A/B676-933[»]
    1SQNX-ray1.45A/B673-933[»]
    1SR7X-ray1.46A/B676-933[»]
    1ZUCX-ray2.00A/B676-933[»]
    2C7AX-ray2.50A/B563-640[»]
    2OVHX-ray2.00A678-933[»]
    2OVMX-ray2.60A678-933[»]
    2W8YX-ray1.80A/B678-933[»]
    3D90X-ray2.26A/B676-933[»]
    3G8OX-ray1.90A/B673-933[»]
    3HQ5X-ray2.10A/B678-933[»]
    3KBAX-ray2.00A/B681-933[»]
    3ZR7X-ray1.65A/B678-933[»]
    3ZRAX-ray1.90A/B678-933[»]
    3ZRBX-ray1.80A/B678-933[»]
    4A2JX-ray2.00A/B678-933[»]
    4APUX-ray1.90A/B678-933[»]
    ProteinModelPortaliP06401.
    SMRiP06401. Positions 563-933.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06401.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 566566Modulating, Pro-RichAdd
    BLAST
    Regioni681 – 933253Steroid-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi183 – 1875Nuclear localization signalSequence Analysis

    Domaini

    Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

    Sequence similaritiesi

    Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri567 – 58721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri603 – 62725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG273252.
    HOGENOMiHOG000290653.
    HOVERGENiHBG007583.
    InParanoidiP06401.
    KOiK08556.
    OMAiRPCQGQD.
    OrthoDBiEOG751NF2.
    PhylomeDBiP06401.
    TreeFamiTF106510.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR000128. Progest_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF02161. Prog_receptor. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PRINTSiPR00544. PROGESTRONER.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTiSM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view]
    SUPFAMiSSF48508. SSF48508. 2 hits.
    PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: P06401-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA    50
    IPISLDGLLF PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS 100
    SSPPEKDSGL LDSVLDTLLA PSGPGQSQPS PPACEVTSSW CLFGPELPED 150
    PPAAPATQRV LSPLMSRSGC KVGDSSGTAA AHKVLPRGLS PARQLLLPAS 200
    ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK PRALGGAAAG 250
    GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV 300
    MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS 350
    TPVAVGDFPD CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS 400
    PRSYLVAGAN PAAFPDFPLG PPPPLPPRAT PSRPGEAAVT AAPASASVSS 450
    ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC KAPGASGCLL PRDGLPSTSA 500
    SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP YLNYLRPDSE 550
    ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 600
    YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA 650
    LDAVALPQPV GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY 700
    AGHDNTKPDT SSSLLTSLNQ LGERQLLSVV KWSKSLPGFR NLHIDDQITL 750
    IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP DLILNEQRMK ESSFYSLCLT 800
    MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ FEEMRSSYIR 850
    ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 900
    LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK 933
    Length:933
    Mass (Da):98,981
    Last modified:March 21, 2006 - v4
    Checksum:i80452E54FF3A0454
    GO
    Isoform A (identifier: P06401-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-164: Missing.

    Show »
    Length:769
    Mass (Da):82,295
    Checksum:iFE676F25282983F3
    GO
    Isoform 3 (identifier: P06401-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-594: Missing.

    Show »
    Length:339
    Mass (Da):38,798
    Checksum:i4496D6B5A4EC95FD
    GO
    Isoform 4 (identifier: P06401-4) [UniParc]FASTAAdd to Basket

    Also known as: PR-M

    The sequence of this isoform differs from the canonical sequence as follows:
         1-16: MTELKAKGPRAPHVAG → MEFIYIYMNFFFFFSV
         17-635: Missing.

    Show »
    Length:314
    Mass (Da):36,318
    Checksum:iA85692E905BFB9B3
    GO
    Isoform 5 (identifier: P06401-5) [UniParc]FASTAAdd to Basket

    Also known as: delta4

    The sequence of this isoform differs from the canonical sequence as follows:
         636-737: Missing.

    Show »
    Length:831
    Mass (Da):87,747
    Checksum:iEC4882171DD1C48B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti226 – 2261G → S in CAA36018. (PubMed:2328727)Curated
    Sequence conflicti256 – 2561V → S in CAA36018. (PubMed:2328727)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501A → T.1 Publication
    Corresponds to variant rs11571143 [ dbSNP | Ensembl ].
    VAR_019221
    Natural varianti120 – 1201A → V.1 Publication
    Corresponds to variant rs11571144 [ dbSNP | Ensembl ].
    VAR_019222
    Natural varianti186 – 1861P → L.1 Publication
    Corresponds to variant rs11571145 [ dbSNP | Ensembl ].
    VAR_019223
    Natural varianti301 – 3011M → R.1 Publication
    Corresponds to variant rs11571146 [ dbSNP | Ensembl ].
    VAR_019224
    Natural varianti344 – 3441S → T.2 Publications
    Corresponds to variant rs3740753 [ dbSNP | Ensembl ].
    VAR_016117
    Natural varianti347 – 3471C → S.
    Corresponds to variant rs11571147 [ dbSNP | Ensembl ].
    VAR_025555
    Natural varianti444 – 4441A → S.1 Publication
    Corresponds to variant rs11571150 [ dbSNP | Ensembl ].
    VAR_019225
    Natural varianti529 – 5291V → L.1 Publication
    Corresponds to variant rs11571151 [ dbSNP | Ensembl ].
    VAR_019226
    Natural varianti536 – 5361Q → P.1 Publication
    Corresponds to variant rs11571152 [ dbSNP | Ensembl ].
    VAR_019227
    Natural varianti625 – 6251R → I.
    Corresponds to variant rs2020874 [ dbSNP | Ensembl ].
    VAR_014627
    Natural varianti651 – 6511L → V.1 Publication
    Corresponds to variant rs11571222 [ dbSNP | Ensembl ].
    VAR_019228
    Natural varianti660 – 6601V → L.3 Publications
    Corresponds to variant rs1042838 [ dbSNP | Ensembl ].
    VAR_016118
    Natural varianti865 – 8651S → L.1 Publication
    Corresponds to variant rs2020880 [ dbSNP | Ensembl ].
    VAR_014628

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 594594Missing in isoform 3. 1 PublicationVSP_046942Add
    BLAST
    Alternative sequencei1 – 164164Missing in isoform A. CuratedVSP_003706Add
    BLAST
    Alternative sequencei1 – 1616MTELK…PHVAG → MEFIYIYMNFFFFFSV in isoform 4. 1 PublicationVSP_047454Add
    BLAST
    Alternative sequencei17 – 635619Missing in isoform 4. 1 PublicationVSP_047455Add
    BLAST
    Alternative sequencei636 – 737102Missing in isoform 5. 1 PublicationVSP_053543Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51730 mRNA. Translation: CAA36018.1.
    M15716 mRNA. Translation: AAA60081.1.
    AF016381 mRNA. Translation: AAD01587.1.
    AB084248 mRNA. Translation: BAB91074.1.
    DQ234979 Genomic DNA. Translation: ABB72139.1.
    AY212933 mRNA. Translation: AAO61671.1.
    AK304853 mRNA. Translation: BAG65592.1.
    AY525610 Genomic DNA. Translation: AAS00096.1.
    AP001533 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66999.1.
    CH471065 Genomic DNA. Translation: EAW67000.1.
    CCDSiCCDS59229.1. [P06401-3]
    CCDS8310.1. [P06401-1]
    PIRiS09971. QRHUP.
    RefSeqiNP_000917.3. NM_000926.4. [P06401-1]
    NP_001189403.1. NM_001202474.3. [P06401-2]
    NP_001258090.1. NM_001271161.2.
    NP_001258091.1. NM_001271162.1. [P06401-3]
    UniGeneiHs.32405.
    Hs.742403.

    Genome annotation databases

    EnsembliENST00000263463; ENSP00000263463; ENSG00000082175. [P06401-5]
    ENST00000325455; ENSP00000325120; ENSG00000082175. [P06401-1]
    ENST00000534013; ENSP00000436561; ENSG00000082175. [P06401-3]
    GeneIDi5241.
    KEGGihsa:5241.
    UCSCiuc001pgh.2. human. [P06401-1]
    uc001pgi.3. human.

    Polymorphism databases

    DMDMi90110048.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Progesterone receptor entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51730 mRNA. Translation: CAA36018.1 .
    M15716 mRNA. Translation: AAA60081.1 .
    AF016381 mRNA. Translation: AAD01587.1 .
    AB084248 mRNA. Translation: BAB91074.1 .
    DQ234979 Genomic DNA. Translation: ABB72139.1 .
    AY212933 mRNA. Translation: AAO61671.1 .
    AK304853 mRNA. Translation: BAG65592.1 .
    AY525610 Genomic DNA. Translation: AAS00096.1 .
    AP001533 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66999.1 .
    CH471065 Genomic DNA. Translation: EAW67000.1 .
    CCDSi CCDS59229.1. [P06401-3 ]
    CCDS8310.1. [P06401-1 ]
    PIRi S09971. QRHUP.
    RefSeqi NP_000917.3. NM_000926.4. [P06401-1 ]
    NP_001189403.1. NM_001202474.3. [P06401-2 ]
    NP_001258090.1. NM_001271161.2.
    NP_001258091.1. NM_001271162.1. [P06401-3 ]
    UniGenei Hs.32405.
    Hs.742403.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A28 X-ray 1.80 A/B 678-933 [» ]
    1E3K X-ray 2.80 A/B 676-933 [» ]
    1SQN X-ray 1.45 A/B 673-933 [» ]
    1SR7 X-ray 1.46 A/B 676-933 [» ]
    1ZUC X-ray 2.00 A/B 676-933 [» ]
    2C7A X-ray 2.50 A/B 563-640 [» ]
    2OVH X-ray 2.00 A 678-933 [» ]
    2OVM X-ray 2.60 A 678-933 [» ]
    2W8Y X-ray 1.80 A/B 678-933 [» ]
    3D90 X-ray 2.26 A/B 676-933 [» ]
    3G8O X-ray 1.90 A/B 673-933 [» ]
    3HQ5 X-ray 2.10 A/B 678-933 [» ]
    3KBA X-ray 2.00 A/B 681-933 [» ]
    3ZR7 X-ray 1.65 A/B 678-933 [» ]
    3ZRA X-ray 1.90 A/B 678-933 [» ]
    3ZRB X-ray 1.80 A/B 678-933 [» ]
    4A2J X-ray 2.00 A/B 678-933 [» ]
    4APU X-ray 1.90 A/B 678-933 [» ]
    ProteinModelPortali P06401.
    SMRi P06401. Positions 563-933.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111260. 65 interactions.
    DIPi DIP-5967N.
    IntActi P06401. 8 interactions.
    MINTi MINT-1505587.
    STRINGi 9606.ENSP00000325120.

    Chemistry

    BindingDBi P06401.
    ChEMBLi CHEMBL208.
    DrugBanki DB00304. Desogestrel.
    DB01395. Drospirenone.
    DB00378. Dydrogesterone.
    DB00823. Ethynodiol Diacetate.
    DB00294. Etonogestrel.
    DB00367. Levonorgestrel.
    DB00603. Medroxyprogesterone.
    DB00351. Megestrol.
    DB00834. Mifepristone.
    DB00717. Norethindrone.
    DB00957. Norgestimate.
    DB00506. Norgestrel.
    DB00396. Progesterone.
    GuidetoPHARMACOLOGYi 627.

    PTM databases

    PhosphoSitei P06401.

    Polymorphism databases

    DMDMi 90110048.

    Proteomic databases

    MaxQBi P06401.
    PaxDbi P06401.
    PRIDEi P06401.

    Protocols and materials databases

    DNASUi 5241.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263463 ; ENSP00000263463 ; ENSG00000082175 . [P06401-5 ]
    ENST00000325455 ; ENSP00000325120 ; ENSG00000082175 . [P06401-1 ]
    ENST00000534013 ; ENSP00000436561 ; ENSG00000082175 . [P06401-3 ]
    GeneIDi 5241.
    KEGGi hsa:5241.
    UCSCi uc001pgh.2. human. [P06401-1 ]
    uc001pgi.3. human.

    Organism-specific databases

    CTDi 5241.
    GeneCardsi GC11M100943.
    HGNCi HGNC:8910. PGR.
    HPAi CAB000068.
    CAB055100.
    HPA004751.
    HPA008428.
    HPA017176.
    MIMi 607311. gene.
    neXtProti NX_P06401.
    PharmGKBi PA266.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273252.
    HOGENOMi HOG000290653.
    HOVERGENi HBG007583.
    InParanoidi P06401.
    KOi K08556.
    OMAi RPCQGQD.
    OrthoDBi EOG751NF2.
    PhylomeDBi P06401.
    TreeFami TF106510.

    Enzyme and pathway databases

    Reactomei REACT_116022. Nuclear signaling by ERBB4.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P06401.

    Miscellaneous databases

    EvolutionaryTracei P06401.
    GeneWikii Progesterone_receptor.
    GenomeRNAii 5241.
    NextBioi 20248.
    PROi P06401.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06401.
    Bgeei P06401.
    CleanExi HS_PGR.
    Genevestigatori P06401.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR000128. Progest_rcpt.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF02161. Prog_receptor. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PRINTSi PR00544. PROGESTRONER.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 2 hits.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B."
      Kastner P., Krust A., Turcotte B., Stropp U., Tora L., Gronemeyer H., Chambon P.
      EMBO J. 9:1603-1614(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, VARIANT THR-344.
    2. "Complete amino acid sequence of the human progesterone receptor deduced from cloned cDNA."
      Misrahi M., Atger M., D'Auriol L., Loosfelt H., Meriel C., Fridlansky F., Guiochon-Mantel A., Galibert F., Milgrom E.
      Biochem. Biophys. Res. Commun. 143:740-748(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-660.
    3. Kieback D.G., Agoulnik I.U., Tong X.-W.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-660.
    4. "Progesterone Receptor, alternative splicing variant, mRNA."
      Hisatomi H., Wakita K., Kohno N., Nagao K., Hirata H., Hikiji K.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Mammary tumor.
    5. "The human progesterone receptor shows evidence of adaptive evolution associated with its ability to act as a transcription factor."
      Chen C., Opazo J.C., Erez O., Uddin M., Santolaya-Forgas J., Goodman M., Grossman L.I., Romero R., Wildman D.E.
      Mol. Phylogenet. Evol. 47:637-649(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Cloning and expression of a novel, truncated, progesterone receptor."
      Saner K.J., Welter B.H., Zhang F., Hansen E., Dupont B., Wei Y., Price T.M.
      Mol. Cell. Endocrinol. 200:155-163(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT LEU-660.
      Tissue: Adipose tissue and Aorta.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Uterus.
    8. NIEHS SNPs program
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-50; VAL-120; LEU-186; ARG-301; THR-344; SER-444; LEU-529; PRO-536; VAL-651 AND LEU-865.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "Identification of a phosphorylation site in the hinge region of the human progesterone receptor and additional amino-terminal phosphorylation sites."
      Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L.
      J. Biol. Chem. 276:8475-8483(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "A truncated progesterone receptor (PR-M) localizes to the mitochondrion and controls cellular respiration."
      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.
      Mol. Endocrinol. 27:741-753(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 204-217, FUNCTION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).
      Tissue: Heart.
    13. "Identification of a group of Ser-Pro motif hormone-inducible phosphorylation sites in the human progesterone receptor."
      Zhang Y., Beck C.A., Poletti A., Edwards D.P., Weigel N.L.
      Mol. Endocrinol. 9:1029-1040(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-81 AND SER-162.
    14. "Stoichiometry and site-specific phosphorylation of human progesterone receptor in native target cells and in the baculovirus expression system."
      Beck C.A., Zhang Y., Altmann M., Weigel N.L., Edwards D.P.
      J. Biol. Chem. 271:19546-19555(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345.
    15. "Phosphorylation of human progesterone receptor by cyclin-dependent kinase 2 on three sites that are authentic basal phosphorylation sites in vivo."
      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.
      Mol. Endocrinol. 11:823-832(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-400.
    16. "Differential hormone-dependent phosphorylation of progesterone receptor A and B forms revealed by a phosphoserine site-specific monoclonal antibody."
      Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T., Weigel N.L., Edwards D.P.
      Mol. Endocrinol. 14:52-65(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-190 AND SER-294.
    17. "Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome."
      Lange C.A., Shen T., Horwitz K.B.
      Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-294, UBIQUITINATION, MUTAGENESIS OF SER-294; SER-344 AND SER-345.
    18. "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha."
      Qi C., Chang J., Zhu Y., Yeldandi A.V., Rao S.M., Zhu Y.-J.
      J. Biol. Chem. 277:28624-28630(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT2.
    19. "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation."
      Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.
      Mol. Cell. Biol. 23:6210-6220(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMARD1.
    20. "Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation of cyclin-dependent protein kinase 2."
      Pierson-Mullany L.K., Lange C.A.
      Mol. Cell. Biol. 24:10542-10557(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-400.
    21. "Human progesterone receptor displays cell cycle-dependent changes in transcriptional activity."
      Narayanan R., Edwards D.P., Weigel N.L.
      Mol. Cell. Biol. 25:2885-2898(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION, FUNCTION.
    22. "GCUNC-45 is a novel regulator for the progesterone receptor/hsp90 chaperoning pathway."
      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.
      Mol. Cell. Biol. 26:1722-1730(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC45A.
    23. "PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus."
      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.
      Nucleic Acids Res. 34:5552-5566(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-7; LYS-388 AND LYS-531, INTERACTION WITH PIAS3, FUNCTION, MUTAGENESIS OF LYS-7; LYS-388 AND LYS-531.
    24. "CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome."
      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.
      EMBO J. 26:1831-1842(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION AT LYS-388, FUNCTION, MUTAGENESIS OF LYS-388.
    25. "Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells."
      Daniel A.R., Faivre E.J., Lange C.A.
      Mol. Endocrinol. 21:2890-2906(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, MUTAGENESIS OF SER-294 AND LYS-388.
    26. "Linkage of progestin and epidermal growth factor signaling: phosphorylation of progesterone receptors mediates transcriptional hypersensitivity and increased ligand-independent breast cancer cell growth."
      Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A., Lange C.A.
      Steroids 72:188-201(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-294.
    27. "Progesterone receptor rapid signaling mediates serine 345 phosphorylation and tethering to specificity protein 1 transcription factors."
      Faivre E.J., Daniel A.R., Hillard C.J., Lange C.A.
      Mol. Endocrinol. 22:823-837(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-294; SER-345 AND SER-400, INTERACTION WITH SP1, FUNCTION, MUTAGENESIS OF SER-344; SER-345 AND SER-400.
    28. "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors."
      Pedram A., Razandi M., Deschenes R.J., Levin E.R.
      Mol. Biol. Cell 23:188-199(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION.
    29. "Atomic structure of progesterone complexed with its receptor."
      Williams S.P., Sigler P.B.
      Nature 393:392-396(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 682-933.
    30. "Molecular and pharmacological properties of a potent and selective novel nonsteroidal progesterone receptor agonist tanaproget."
      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.
      J. Biol. Chem. 280:28468-28475(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 676-933.

    Entry informationi

    Entry nameiPRGR_HUMAN
    AccessioniPrimary (citable) accession number: P06401
    Secondary accession number(s): A7LQ08
    , A7X8B0, B4E3T0, Q8TDS3, Q9UPF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 193 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3