dbPTM

PGRC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PGRC1_HUMAN
UniProt AC	O00264
Protein Name	Membrane-associated progesterone receptor component 1
Gene Name	PGRMC1 {ECO:0000312\|HGNC:HGNC:16090}
Organism	Homo sapiens (Human).
Sequence Length	195
Subcellular Localization	Microsome membrane Single-pass membrane protein . Smooth endoplasmic reticulum membrane Single-pass membrane protein .
Protein Description	Component of a progesterone-binding protein complex. [PubMed: 28396637 Binds progesterone]
Protein Sequence	MAAEDVVATGADPSDLESGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASGDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTFKYHHVGKLLKEGEEPTVYSDEEEPKDESARKND

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Methylation	FLLYKIVRGDQPAAS HHHHHHHHCCCCCCC	46.58	115487317
54	Phosphorylation	RGDQPAASGDSDDDE HCCCCCCCCCCCCCC	45.28	22167270
57	Phosphorylation	QPAASGDSDDDEPPP CCCCCCCCCCCCCCC	46.60	19664994
74	Phosphorylation	RLKRRDFTPAELRRF CCCCCCCCHHHHHCC	26.36	23911959
79	Methylation	DFTPAELRRFDGVQD CCCHHHHHCCCCCCC	28.82	115487297
96	Ubiquitination	ILMAINGKVFDVTKG EEEEECCEEEEECCC	34.93	21890473
96	Ubiquitination	ILMAINGKVFDVTKG EEEEECCEEEEECCC	34.93	21890473
96	Acetylation	ILMAINGKVFDVTKG EEEEECCEEEEECCC	34.93	133443
101	Phosphorylation	NGKVFDVTKGRKFYG CCEEEEECCCCCCCC	29.62	-
102	Ubiquitination	GKVFDVTKGRKFYGP CEEEEECCCCCCCCC	57.47	21890473
102	Malonylation	GKVFDVTKGRKFYGP CEEEEECCCCCCCCC	57.47	26320211
102	Ubiquitination	GKVFDVTKGRKFYGP CEEEEECCCCCCCCC	57.47	21890473
105	Ubiquitination	FDVTKGRKFYGPEGP EEECCCCCCCCCCCC	52.16	21890473
105	Acetylation	FDVTKGRKFYGPEGP EEECCCCCCCCCCCC	52.16	27452117
105	Malonylation	FDVTKGRKFYGPEGP EEECCCCCCCCCCCC	52.16	26320211
107	Phosphorylation	VTKGRKFYGPEGPYG ECCCCCCCCCCCCCC	34.50	28152594
113	Phosphorylation	FYGPEGPYGVFAGRD CCCCCCCCCEECCCC	36.46	27273156
119	Methylation	PYGVFAGRDASRGLA CCCEECCCCCCCCCC	32.65	115487307
120	Ubiquitination	YGVFAGRDASRGLAT CCEECCCCCCCCCCH	48.23	-
129	Glutathionylation	SRGLATFCLDKEALK CCCCCHHHCCHHHHH	4.11	22555962
132	Ubiquitination	LATFCLDKEALKDEY CCHHHCCHHHHHHHC	31.75	21890473
136	Ubiquitination	CLDKEALKDEYDDLS HCCHHHHHHHCCCHH	56.41	-
139	Phosphorylation	KEALKDEYDDLSDLT HHHHHHHCCCHHHCH	25.54	-
143	Phosphorylation	KDEYDDLSDLTAAQQ HHHCCCHHHCHHHHH	37.25	-
146	Phosphorylation	YDDLSDLTAAQQETL CCCHHHCHHHHHHHH	25.57	30622161
152	Phosphorylation	LTAAQQETLSDWESQ CHHHHHHHHHHHHHH	27.50	30622161
154	Phosphorylation	AAQQETLSDWESQFT HHHHHHHHHHHHHHH	48.36	30622161
163	Acetylation	WESQFTFKYHHVGKL HHHHHHHEEHHHHHH	40.39	23236377
163	Ubiquitination	WESQFTFKYHHVGKL HHHHHHHEEHHHHHH	40.39	-
169	Ubiquitination	FKYHHVGKLLKEGEE HEEHHHHHHHHCCCC	49.94	-
169	Acetylation	FKYHHVGKLLKEGEE HEEHHHHHHHHCCCC	49.94	25953088
172	Ubiquitination	HHVGKLLKEGEEPTV HHHHHHHHCCCCCCC	74.28	21906983
178	Phosphorylation	LKEGEEPTVYSDEEE HHCCCCCCCCCCCCC	35.04	29255136
180	Phosphorylation	EGEEPTVYSDEEEPK CCCCCCCCCCCCCCC	16.94	29255136
181	Phosphorylation	GEEPTVYSDEEEPKD CCCCCCCCCCCCCCC	33.92	29255136
187	Ubiquitination	YSDEEEPKDESARKN CCCCCCCCCHHHHCC	76.92	-
190	Phosphorylation	EEEPKDESARKND-- CCCCCCHHHHCCC--	43.43	23401153

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
Oops, there are no upstream regulatory protein records of PGRC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PGRC1_HUMAN !!

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 PGRC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EFHD1_HUMAN	EFHD1	physical	17353931
DAAF5_HUMAN	DNAAF5	physical	17353931
ABCD3_HUMAN	ABCD3	physical	17353931
SFXN1_HUMAN	SFXN1	physical	17353931
OST48_HUMAN	DDOST	physical	17353931
SPCS2_HUMAN	SPCS2	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
RS20_HUMAN	RPS20	physical	22939629
BAP31_HUMAN	BCAP31	physical	21081644
NCPR_HUMAN	POR	physical	21081644
CALX_HUMAN	CANX	physical	21081644
INSI1_HUMAN	INSIG1	physical	21081644
CR3L1_HUMAN	CREB3L1	physical	25416956
ATLA3_HUMAN	ATL3	physical	26344197
ITBP1_HUMAN	ITGB1BP1	physical	25814554

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
DB00514	Dextromethorphan
DB00540	Nortriptyline

Regulatory Network of PGRC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-57, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-178;TYR-180 AND SER-181, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-178 AND SER-181,AND MASS SPECTROMETRY.	19413330 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASSSPECTROMETRY.	18318008 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; THR-74 AND SER-181,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-57; THR-74 ANDSER-181, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASSSPECTROMETRY.	19367720 [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-181, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.	16565220 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; TYR-180 AND SER-181,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-181, AND MASSSPECTROMETRY.	15302935 [Abstract]