CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002339
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Progesterone receptor 
Protein Synonyms/Alias
 PR; Nuclear receptor subfamily 3 group C member 3 
Gene Name
 PGR 
Gene Synonyms/Alias
 NR3C3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
388QPPALKIKEEEEGAEsumoylation[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
388QPPALKIKEEEEGAEubiquitination[11]
Reference
 [1] Sumoylation of the progesterone receptor and of the steroid receptor coactivator SRC-1.
 Chauchereau A, Amazit L, Quesne M, Guiochon-Mantel A, Milgrom E.
 J Biol Chem. 2003 Apr 4;278(14):12335-43. [PMID: 12529333]
 [2] Functional properties of the N-terminal region of progesterone receptors and their mechanistic relationship to structure.
 Takimoto GS, Tung L, Abdel-Hafiz H, Abel MG, Sartorius CA, Richer JK, Jacobsen BM, Bain DL, Horwitz KB.
 J Steroid Biochem Mol Biol. 2003 Jun;85(2-5):209-19. [PMID: 12943706]
 [3] PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus.
 Man JH, Li HY, Zhang PJ, Zhou T, He K, Pan X, Liang B, Li AL, Zhao J, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM.
 Nucleic Acids Res. 2006;34(19):5552-66. [PMID: 17020914]
 [4] Regulation of the SUMO pathway sensitizes differentiating human endometrial stromal cells to progesterone.
 Jones MC, Fusi L, Higham JH, Abdel-Hafiz H, Horwitz KB, Lam EW, Brosens JJ.
 Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16272-7. [PMID: 17053081]
 [5] CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome.
 Zhang PJ, Zhao J, Li HY, Man JH, He K, Zhou T, Pan X, Li AL, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM.
 EMBO J. 2007 Apr 4;26(7):1831-42. [PMID: 17347654]
 [6] Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells.
 Daniel AR, Faivre EJ, Lange CA.
 Mol Endocrinol. 2007 Dec;21(12):2890-906. [PMID: 17717077]
 [7] Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation.
 Abdel-Hafiz H, Dudevoir ML, Horwitz KB.
 J Biol Chem. 2009 Apr 3;284(14):9099-108. [PMID: 19211567]
 [8] Protein kinases mediate ligand-independent derepression of sumoylated progesterone receptors in breast cancer cells.
 Daniel AR, Lange CA.
 Proc Natl Acad Sci U S A. 2009 Aug 25;106(34):14287-92. [PMID: 19706513]
 [9] Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation.
 Abdel-Hafiz HA, Horwitz KB.
 BMC Mol Biol. 2012 Mar 22;13:10. [PMID: 22439847]
 [10] Phosphorylated and sumoylation-deficient progesterone receptors drive proliferative gene signatures during breast cancer progression.
 Knutson TP, Daniel AR, Fan D, Silverstein KA, Covington KR, Fuqua SA, Lange CA.
 Breast Cancer Res. 2012 Jun 14;14(3):R95. [PMID: 22697792]
 [11] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
Functional Description
 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. 
Sequence Annotation
 DNA_BIND 567 639 Nuclear receptor.
 ZN_FING 567 587 NR C4-type.
 ZN_FING 603 627 NR C4-type.
 REGION 1 566 Modulating, Pro-Rich.
 REGION 681 933 Steroid-binding.
 MOTIF 183 187 Nuclear localization signal (Potential).
 MOD_RES 20 20 Phosphoserine.
 MOD_RES 81 81 Phosphoserine.
 MOD_RES 102 102 Phosphoserine.
 MOD_RES 130 130 Phosphoserine.
 MOD_RES 162 162 Phosphoserine.
 MOD_RES 190 190 Phosphoserine.
 MOD_RES 213 213 Phosphoserine.
 MOD_RES 294 294 Phosphoserine; by MAPK1.
 MOD_RES 345 345 Phosphoserine; by MAPK.
 MOD_RES 400 400 Phosphoserine; by CDK2.
 MOD_RES 676 676 Phosphoserine.
 CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 531 531 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; 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. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 933 AA 
Protein Sequence
MTELKAKGPR APHVAGGPPS PEVGSPLLCR PAAGPFPGSQ TSDTLPEVSA IPISLDGLLF 60
PRPCQGQDPS DEKTQDQQSL SDVEGAYSRA EATRGAGGSS SSPPEKDSGL LDSVLDTLLA 120
PSGPGQSQPS PPACEVTSSW CLFGPELPED PPAAPATQRV LSPLMSRSGC KVGDSSGTAA 180
AHKVLPRGLS PARQLLLPAS ESPHWSGAPV KPSPQAAAVE VEEEDGSESE ESAGPLLKGK 240
PRALGGAAAG GGAAAVPPGA AAGGVALVPK EDSRFSAPRV ALVEQDAPMA PGRSPLATTV 300
MDFIHVPILP LNHALLAART RQLLEDESYD GGAGAASAFA PPRSSPCASS TPVAVGDFPD 360
CAYPPDAEPK DDAYPLYSDF QPPALKIKEE EEGAEASARS PRSYLVAGAN PAAFPDFPLG 420
PPPPLPPRAT PSRPGEAAVT AAPASASVSS ASSSGSTLEC ILYKAEGAPP QQGPFAPPPC 480
KAPGASGCLL PRDGLPSTSA SAAAAGAAPA LYPALGLNGL PQLGYQAAVL KEGLPQVYPP 540
YLNYLRPDSE ASQSPQYSFE SLPQKICLIC GDEASGCHYG VLTCGSCKVF FKRAMEGQHN 600
YLCAGRNDCI VDKIRRKNCP ACRLRKCCQA GMVLGGRKFK KFNKVRVVRA LDAVALPQPV 660
GVPNESQALS QRFTFSPGQD IQLIPPLINL LMSIEPDVIY AGHDNTKPDT SSSLLTSLNQ 720
LGERQLLSVV KWSKSLPGFR NLHIDDQITL IQYSWMSLMV FGLGWRSYKH VSGQMLYFAP 780
DLILNEQRMK ESSFYSLCLT MWQIPQEFVK LQVSQEEFLC MKVLLLLNTI PLEGLRSQTQ 840
FEEMRSSYIR ELIKAIGLRQ KGVVSSSQRF YQLTKLLDNL HDLVKQLHLY CLNTFIQSRA 900
LSVEFPEMMS EVIAAQLPKI LAGMVKPLLF HKK 933 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; IEA:Compara.
 GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
 GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
 GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007267; P:cell-cell signaling; TAS:ProtInc.
 GO:0002070; P:epithelial cell maturation; IEA:Compara.
 GO:0010629; P:negative regulation of gene expression; IEP:UniProtKB.
 GO:0001542; P:ovulation from ovarian follicle; IEA:Compara.
 GO:0050847; P:progesterone receptor signaling pathway; IEA:Compara.
 GO:0050678; P:regulation of epithelial cell proliferation; IEA:Compara.
 GO:0060748; P:tertiary branching involved in mammary gland duct morphogenesis; IEA:Compara.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. 
Interpro
 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. 
Pfam
 PF00104; Hormone_recep
 PF02161; Prog_receptor
 PF00105; zf-C4 
SMART
 SM00430; HOLI
 SM00399; ZnF_C4 
PROSITE
 PS00031; NUCLEAR_REC_DBD_1
 PS51030; NUCLEAR_REC_DBD_2 
PRINTS
 PR00544; PROGESTRONER.
 PR00398; STRDHORMONER.
 PR00047; STROIDFINGER.