dbPTM

PRGR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRGR_HUMAN
UniProt AC	P06401
Protein Name	Progesterone receptor
Gene Name	PGR
Organism	Homo sapiens (Human).
Sequence Length	933
Subcellular Localization	Nucleus. Cytoplasm. 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. Isoform A: Nucleus. Cytoplasm. Mainly nuclear. Isoform 4: Mitochondrion out
Protein 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. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor.; 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.; 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.; Isoform 4: Increases mitochondrial membrane potential and cellular respiration upon stimulation by progesterone..
Protein Sequence	MTELKAKGPRAPHVAGGPPSPEVGSPLLCRPAAGPFPGSQTSDTLPEVSAIPISLDGLLFPRPCQGQDPSDEKTQDQQSLSDVEGAYSRAEATRGAGGSSSSPPEKDSGLLDSVLDTLLAPSGPGQSQPSPPACEVTSSWCLFGPELPEDPPAAPATQRVLSPLMSRSGCKVGDSSGTAAAHKVLPRGLSPARQLLLPASESPHWSGAPVKPSPQAAAVEVEEEDGSESEESAGPLLKGKPRALGGAAAGGGAAAVPPGAAAGGVALVPKEDSRFSAPRVALVEQDAPMAPGRSPLATTVMDFIHVPILPLNHALLAARTRQLLEDESYDGGAGAASAFAPPRSSPCASSTPVAVGDFPDCAYPPDAEPKDDAYPLYSDFQPPALKIKEEEEGAEASARSPRSYLVAGANPAAFPDFPLGPPPPLPPRATPSRPGEAAVTAAPASASVSSASSSGSTLECILYKAEGAPPQQGPFAPPPCKAPGASGCLLPRDGLPSTSASAAAAGAAPALYPALGLNGLPQLGYQAAVLKEGLPQVYPPYLNYLRPDSEASQSPQYSFESLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVVRALDAVALPQPVGVPNESQALSQRFTFSPGQDIQLIPPLINLLMSIEPDVIYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKESSFYSLCLTMWQIPQEFVKLQVSQEEFLCMKVLLLLNTIPLEGLRSQTQFEEMRSSYIRELIKAIGLRQKGVVSSSQRFYQLTKLLDNLHDLVKQLHLYCLNTFIQSRALSVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Sumoylation	-MTELKAKGPRAPHV -CCCCCCCCCCCCCC	68.79	-
7	Sumoylation	-MTELKAKGPRAPHV -CCCCCCCCCCCCCC	68.79	17020914
20	Phosphorylation	HVAGGPPSPEVGSPL CCCCCCCCCCCCCCC	36.50	27362937
25	Phosphorylation	PPSPEVGSPLLCRPA CCCCCCCCCCCCCCC	19.97	27362937
26 (in isoform 2)	Phosphorylation	-	24.35	-
63 (in isoform 2)	Phosphorylation	-	18.28	-
79	Phosphorylation	EKTQDQQSLSDVEGA CCCCCHHHHHHHHHH	24.98	28102081
81	Phosphorylation	TQDQQSLSDVEGAYS CCCHHHHHHHHHHHH	44.87	8702648
87	Phosphorylation	LSDVEGAYSRAEATR HHHHHHHHHHHHHHC	15.00	27642862
88	Phosphorylation	SDVEGAYSRAEATRG HHHHHHHHHHHHHCC	25.20	-
99	Phosphorylation	ATRGAGGSSSSPPEK HHCCCCCCCCCCCHH	26.57	28102081
100	Phosphorylation	TRGAGGSSSSPPEKD HCCCCCCCCCCCHHC	37.80	28102081
101	Phosphorylation	RGAGGSSSSPPEKDS CCCCCCCCCCCHHCC	48.86	25849741
102	Phosphorylation	GAGGSSSSPPEKDSG CCCCCCCCCCHHCCC	46.55	8702648
112 (in isoform 2)	Phosphorylation	-	41.56	-
130 (in isoform 2)	Phosphorylation	-	35.56	-
130	Phosphorylation	GPGQSQPSPPACEVT CCCCCCCCCCCCEEE	35.56	22817900
137	Phosphorylation	SPPACEVTSSWCLFG CCCCCEEECCEEECC	8.51	27251275
138	Phosphorylation	PPACEVTSSWCLFGP CCCCEEECCEEECCC	27.32	27251275
139	Phosphorylation	PACEVTSSWCLFGPE CCCEEECCEEECCCC	16.67	27251275
162	Phosphorylation	PATQRVLSPLMSRSG CHHHHHHHHHHCCCC	17.09	8702648
164 (in isoform 2)	Phosphorylation	-	4.35	-
166	Phosphorylation	RVLSPLMSRSGCKVG HHHHHHHCCCCCCCC	30.86	23186163
183	Acetylation	SGTAAAHKVLPRGLS CCCHHHHHHCCCCCC	40.52	60665199
183	Ubiquitination	SGTAAAHKVLPRGLS CCCHHHHHHCCCCCC	40.52	-
190	Phosphorylation	KVLPRGLSPARQLLL HHCCCCCCHHHHHHC	21.24	10628747
213	Phosphorylation	SGAPVKPSPQAAAVE CCCCCCCCCCCEEEE	24.75	22817900
222	Ubiquitination	QAAAVEVEEEDGSES CCEEEEEEECCCCCC	42.01	22817900
224	Ubiquitination	AAVEVEEEDGSESEE EEEEEEECCCCCCCH	54.92	22817900
227	Phosphorylation	EVEEEDGSESEESAG EEEECCCCCCCHHCC	50.72	25849741
229	Phosphorylation	EEEDGSESEESAGPL EECCCCCCCHHCCCC	48.65	28102081
232	Phosphorylation	DGSESEESAGPLLKG CCCCCCHHCCCCCCC	34.18	28102081
236 (in isoform 2)	Phosphorylation	-	8.26	-
273	Phosphorylation	ALVPKEDSRFSAPRV EEEECCCCCCCCCEE	36.00	27174698
276	Phosphorylation	PKEDSRFSAPRVALV ECCCCCCCCCEEEEE	35.93	27174698
294	Phosphorylation	APMAPGRSPLATTVM CCCCCCCCCCCCCHH	30.13	8702648
328	Phosphorylation	RQLLEDESYDGGAGA HHHHHCCCCCCCCCC	40.63	27251275
344	Phosphorylation	SAFAPPRSSPCASST CCCCCCCCCCCCCCC	44.39	30278072
345	Phosphorylation	AFAPPRSSPCASSTP CCCCCCCCCCCCCCC	25.85	8702648
349	Phosphorylation	PRSSPCASSTPVAVG CCCCCCCCCCCEEEC	41.27	28348404
350	Phosphorylation	RSSPCASSTPVAVGD CCCCCCCCCCEEECC	20.43	30278072
351	Phosphorylation	SSPCASSTPVAVGDF CCCCCCCCCEEECCC	21.20	30278072
377	Phosphorylation	KDDAYPLYSDFQPPA CCCCCCCCCCCCCCC	11.16	27642862
386	Ubiquitination	DFQPPALKIKEEEEG CCCCCCCCCCHHHHC	54.56	22817900
388	Sumoylation	QPPALKIKEEEEGAE CCCCCCCCHHHHCHH	58.44	17347654
388	Ubiquitination	QPPALKIKEEEEGAE CCCCCCCCHHHHCHH	58.44	22817900
388	Sumoylation	QPPALKIKEEEEGAE CCCCCCCCHHHHCHH	58.44	-
390 (in isoform 2)	Phosphorylation	-	57.24	-
394 (in isoform 2)	Phosphorylation	-	16.68	-
397	Phosphorylation	EEEGAEASARSPRSY HHHCHHCCCCCCCCE	18.73	25849741
400	Phosphorylation	GAEASARSPRSYLVA CHHCCCCCCCCEEEE	25.12	30278072
464	Methylation	TLECILYKAEGAPPQ EEEEEEEECCCCCCC	36.19	-
512 (in isoform 2)	Phosphorylation	-	6.64	-
531	Sumoylation	GYQAAVLKEGLPQVY HHHHHHHHCCCCCCC	43.04	17020914
531	Sumoylation	GYQAAVLKEGLPQVY HHHHHHHHCCCCCCC	43.04	-
549	Phosphorylation	LNYLRPDSEASQSPQ CCCCCCCCCCCCCCC	37.43	22817900
552	Phosphorylation	LRPDSEASQSPQYSF CCCCCCCCCCCCCCH	27.43	22817900
554	Phosphorylation	PDSEASQSPQYSFES CCCCCCCCCCCCHHH	16.10	22817900
558	Phosphorylation	ASQSPQYSFESLPQK CCCCCCCCHHHCCCE	19.79	22817900
561	Phosphorylation	SPQYSFESLPQKICL CCCCCHHHCCCEEEE	43.25	22817900
666	Phosphorylation	PVGVPNESQALSQRF CCCCCCHHHHHHHCC	27.65	27251275
676	Phosphorylation	LSQRFTFSPGQDIQL HHHCCCCCCCCCCHH	25.68	17020914
735	Phosphorylation	SVVKWSKSLPGFRNL HHHHHHHCCCCCCCC	33.99	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
81	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
81	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
81	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
162	S	Phosphorylation	Kinase	CDK2	P24941	PSP
164	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
190	S	Phosphorylation	Kinase	CDK2	P24941	PSP
213	S	Phosphorylation	Kinase	CDK2	P24941	PSP
294	S	Phosphorylation	Kinase	CDK2	P24941	PSP
294	S	Phosphorylation	Kinase	MK01	P28482	PhosphoELM
294	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
345	S	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
345	S	Phosphorylation	Kinase	MAPK	-	Uniprot
390	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
400	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
400	S	Phosphorylation	Kinase	PKCA	P17252	PSP
400	S	Phosphorylation	Kinase	PKCD	Q05655	PSP
676	S	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	BRCA1	P38398	PMID:21531767
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:26693071

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
81	S	Phosphorylation	7476977
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.
102	S	Phosphorylation	11110801
Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone.
162	S	Phosphorylation	11110801
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.
162	S	Phosphorylation	11110801
Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle.
190	S	Phosphorylation	11110801
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.
190	S	Phosphorylation	11110801
Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle.
294	S	Phosphorylation	8702648
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
294	S	ubiquitylation	8702648
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
294	S	ubiquitylation	8702648
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
294	S	Sumoylation	8702648
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
294	S	Sumoylation	8702648
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
294	S	Phosphorylation	8702648
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
294	S	Phosphorylation	8702648
Promoted by MAPK-mediated phosphorylation on Ser-294.
294	S	Phosphorylation	8702648
Phosphorylation at Ser-162 and Ser-294, but not at Ser-190, is impaired during the G(2)/M phase of the cell cycle.
345	S	Phosphorylation	11110801
Phosphorylation on Ser-102 and Ser-345 also requires induction by hormone.
345	S	Phosphorylation	11110801
Phosphorylation on Ser-345 by ERK1/2 MAPK is required for interaction with SP1.
388	K	Phosphorylation	17020914
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
388	K	ubiquitylation	17020914
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
388	K	ubiquitylation	17020914
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
388	K	Sumoylation	17020914
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
388	K	Sumoylation	17020914
Phosphorylation on Ser-294 occurs preferentially on isoform B, is highly hormone-dependent and modulates ubiquitination and sumoylation on Lys-388.
388	K	Phosphorylation	17020914
Sumoylation on Lys-388, the main site of sumoylation, is repressed by ubiquitination on the same site, and modulated by phosphorylation at Ser-294.
400	S	Phosphorylation	9171245
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.
400	S	Phosphorylation	9171245
Increased levels of phosphorylation on Ser-400 also in the presence of EGF, heregulin, IGF, PMA and FBS.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PRGR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE3A_HUMAN	UBE3A	physical	9891052
KLF9_HUMAN	KLF9	physical	12672823
MPIP2_HUMAN	CDC25B	physical	11689696
UBR5_HUMAN	UBR5	physical	12011095
TF65_HUMAN	RELA	physical	8626413
NCOA1_HUMAN	NCOA1	physical	12529333
HMGB1_HUMAN	HMGB1	physical	9671457
HMGB2_HUMAN	HMGB2	physical	9671457
NCOR2_HUMAN	NCOR2	physical	10757795
CUED2_HUMAN	CUEDC2	physical	17347654
MK01_HUMAN	MAPK1	physical	17081988
SMCE1_HUMAN	SMARCE1	physical	19609353
ARI1A_HUMAN	ARID1A	physical	19609353
GNAI1_HUMAN	GNAI1	physical	16484338
NR0B1_HUMAN	NR0B1	physical	12771131
SP1_HUMAN	SP1	physical	18202149
PRDM2_HUMAN	PRDM2	physical	15282304
FGFR2_HUMAN	FGFR2	physical	21464042
STA5A_HUMAN	STAT5A	physical	21464042
STA5B_HUMAN	STAT5B	physical	21464042
BATF3_HUMAN	BATF3	physical	12101239
JDP2_HUMAN	JDP2	physical	12101239
BATF3_RAT	Batf3	physical	12101239
JDP2_RAT	Jdp2	physical	12101239
NCOA1_HUMAN	NCOA1	physical	21273440
NCOA3_HUMAN	NCOA3	physical	19357364
NCOA1_HUMAN	NCOA1	physical	16728408
NCOA2_HUMAN	NCOA2	physical	16728408
NCOA3_HUMAN	NCOA3	physical	16728408
KAT2B_HUMAN	KAT2B	physical	16728408
CDK2_HUMAN	CDK2	physical	15601848
CCNA1_HUMAN	CCNA1	physical	15601848
SRC_HUMAN	SRC	physical	15601848
ESR1_HUMAN	ESR1	physical	22396492
CSN5_HUMAN	COPS5	physical	10722692
NCOA1_HUMAN	NCOA1	physical	10722692
BPTF_HUMAN	BPTF	physical	21447625
CHIP_HUMAN	STUB1	physical	20661446
FKBP5_HUMAN	FKBP5	physical	20661446
FKBP4_HUMAN	FKBP4	physical	20661446
PPP5_HUMAN	PPP5C	physical	20661446
DNJC7_HUMAN	DNAJC7	physical	20661446
BRCA1_HUMAN	BRCA1	physical	16109739
MAGAB_HUMAN	MAGEA11	physical	22891251
KAT2B_HUMAN	KAT2B	physical	9223281
XRCC6_HUMAN	XRCC6	physical	10750018
XRCC5_HUMAN	XRCC5	physical	10750018
PARP1_HUMAN	PARP1	physical	10750018
PRKDC_HUMAN	PRKDC	physical	10750018
SRC_HUMAN	SRC	physical	15937332
PRGR_HUMAN	PGR	physical	15937332
SPOP_HUMAN	SPOP	physical	26693071
MAS5_YEAST	YDJ1	physical	11809754
DNJA1_HUMAN	DNAJA1	physical	11809754

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01431	Allylestrenol
DB01406	Danazol
DB00304	Desogestrel
DB01395	Drospirenone
DB00378	Dydrogesterone
DB00823	Ethynodiol
DB00294	Etonogestrel
DB00588	Fluticasone Propionate
DB00367	Levonorgestrel
DB00603	Medroxyprogesterone Acetate
DB00351	Megestrol acetate
DB00834	Mifepristone
DB06713	Norelgestromin
DB00717	Norethindrone
DB00957	Norgestimate
DB00396	Progesterone
DB00421	Spironolactone

Regulatory Network of PRGR_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Progesterone receptor rapid signaling mediates serine 345phosphorylation and tethering to specificity protein 1 transcriptionfactors."; Faivre E.J., Daniel A.R., Hillard C.J., Lange C.A.; Mol. Endocrinol. 22:823-837(2008). Cited for: PHOSPHORYLATION AT SER-294; SER-345 AND SER-400, INTERACTION WITH SP1,FUNCTION, AND MUTAGENESIS OF SER-344; SER-345 AND SER-400.	18202149 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Linkage of progestin and epidermal growth factor signaling:phosphorylation of progesterone receptors mediates transcriptionalhypersensitivity and increased ligand-independent breast cancer cellgrowth."; Daniel A.R., Qiu M., Faivre E.J., Ostrander J.H., Skildum A.,Lange C.A.; Steroids 72:188-201(2007). Cited for: PHOSPHORYLATION AT SER-294, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-294.	17173941 [Abstract]
"Phosphorylation-dependent antagonism of sumoylation derepressesprogesterone receptor action in breast cancer cells."; Daniel A.R., Faivre E.J., Lange C.A.; Mol. Endocrinol. 21:2890-2906(2007). Cited for: PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, ANDMUTAGENESIS OF SER-294 AND LYS-388.	17717077 [Abstract]
"Human progesterone receptor displays cell cycle-dependent changes intranscriptional activity."; Narayanan R., Edwards D.P., Weigel N.L.; Mol. Cell. Biol. 25:2885-2898(2005). Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-294, SUBCELLULAR LOCATION,AND FUNCTION.	15798179 [Abstract]
"Phosphorylation of progesterone receptor serine 400 mediates ligand-independent transcriptional activity in response to activation ofcyclin-dependent protein kinase 2."; Pierson-Mullany L.K., Lange C.A.; Mol. Cell. Biol. 24:10542-10557(2004). Cited for: PHOSPHORYLATION AT SER-400, FUNCTION, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-400.	15572662 [Abstract]
"Phosphorylation of human progesterone receptors at serine-294 bymitogen-activated protein kinase signals their degradation by the 26Sproteasome."; Lange C.A., Shen T., Horwitz K.B.; Proc. Natl. Acad. Sci. U.S.A. 97:1032-1037(2000). Cited for: PHOSPHORYLATION AT SER-294, UBIQUITINATION, AND MUTAGENESIS OFSER-294; SER-344 AND SER-345.	10655479 [Abstract]
"Differential hormone-dependent phosphorylation of progesteronereceptor A and B forms revealed by a phosphoserine site-specificmonoclonal antibody."; Clemm D.L., Sherman L., Boonyaratanakornkit V., Schrader W.T.,Weigel N.L., Edwards D.P.; Mol. Endocrinol. 14:52-65(2000). Cited for: PHOSPHORYLATION AT SER-190 AND SER-294.	10628747 [Abstract]
"Phosphorylation of human progesterone receptor by cyclin-dependentkinase 2 on three sites that are authentic basal phosphorylation sitesin 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). Cited for: PHOSPHORYLATION AT SER-162; SER-190 AND SER-400.	9171245 [Abstract]
"Stoichiometry and site-specific phosphorylation of human progesteronereceptor in native target cells and in the baculovirus expressionsystem."; Beck C.A., Zhang Y., Altmann M., Weigel N.L., Edwards D.P.; J. Biol. Chem. 271:19546-19555(1996). Cited for: PHOSPHORYLATION AT SER-81; SER-102; SER-162; SER-294 AND SER-345.	8702648 [Abstract]
"Identification of a group of Ser-Pro motif hormone-induciblephosphorylation 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). Cited for: PHOSPHORYLATION AT SER-81 AND SER-162.	7476977 [Abstract]
"Identification of a phosphorylation site in the hinge region of thehuman progesterone receptor and additional amino-terminalphosphorylation sites."; Knotts T.A., Orkiszewski R.S., Cook R.G., Edwards D.P., Weigel N.L.; J. Biol. Chem. 276:8475-8483(2001). 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, ANDMASS SPECTROMETRY.	11110801 [Abstract]
Sumoylation
Reference	PubMed
"Phosphorylation-dependent antagonism of sumoylation derepressesprogesterone receptor action in breast cancer cells."; Daniel A.R., Faivre E.J., Lange C.A.; Mol. Endocrinol. 21:2890-2906(2007). Cited for: PHOSPHORYLATION AT SER-294, SUMOYLATION AT LYS-388, FUNCTION, ANDMUTAGENESIS OF SER-294 AND LYS-388.	17717077 [Abstract]
"CUE domain containing 2 regulates degradation of progesteronereceptor 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). Cited for: INTERACTION WITH CUEDC2, SUMOYLATION AT LYS-388, UBIQUITINATION ATLYS-388, FUNCTION, AND MUTAGENESIS OF LYS-388.	17347654 [Abstract]
"PIAS3 induction of PRB sumoylation represses PRB transactivation bydestabilizing 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). Cited for: SUMOYLATION AT LYS-7; LYS-388 AND LYS-531, INTERACTION WITH PIAS3,FUNCTION, AND MUTAGENESIS OF LYS-7; LYS-388 AND LYS-531.	17020914 [Abstract]

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