PGRC2_HUMAN - dbPTM
PGRC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGRC2_HUMAN
UniProt AC O15173
Protein Name Membrane-associated progesterone receptor component 2
Gene Name PGRMC2
Organism Homo sapiens (Human).
Sequence Length 223
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description Receptor for steroids..
Protein Sequence MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGLGAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
90PhosphorylationGAGAGEESPATSLPR
CCCCCCCCCCCCCCC		18.6119664994
93PhosphorylationAGEESPATSLPRMKK
CCCCCCCCCCCCHHH		33.8930266825
94PhosphorylationGEESPATSLPRMKKR
CCCCCCCCCCCHHHC		38.1822167270
100MalonylationTSLPRMKKRDFSLEQ
CCCCCHHHCCCCHHH		48.1026320211
104PhosphorylationRMKKRDFSLEQLRQY
CHHHCCCCHHHHHHC		34.9723401153
109MethylationDFSLEQLRQYDGSRN
CCCHHHHHHCCCCCC		32.48115487343
114PhosphorylationQLRQYDGSRNPRILL
HHHHCCCCCCCEEEE		26.4519664994
117PhosphorylationQYDGSRNPRILLAVN
HCCCCCCCEEEEEEC		24.47-
118PhosphorylationYDGSRNPRILLAVNG
CCCCCCCEEEEEECC		35.42-
124UbiquitinationPRILLAVNGKVFDVT
CEEEEEECCEEEEEC		38.67-
126AcetylationILLAVNGKVFDVTKG
EEEEECCEEEEECCC		34.23133447
126UbiquitinationILLAVNGKVFDVTKG
EEEEECCEEEEECCC		34.2321890473
1262-HydroxyisobutyrylationILLAVNGKVFDVTKG
EEEEECCEEEEECCC		34.23-
128PhosphorylationLAVNGKVFDVTKGSK
EEECCEEEEECCCCC		7.7224719451
1322-HydroxyisobutyrylationGKVFDVTKGSKFYGP
CEEEEECCCCCCCCC		62.12-
132UbiquitinationGKVFDVTKGSKFYGP
CEEEEECCCCCCCCC		62.12-
133MethylationKVFDVTKGSKFYGPA
EEEEECCCCCCCCCC		27.05-
1352-HydroxyisobutyrylationFDVTKGSKFYGPAGP
EEECCCCCCCCCCCC		51.80-
135AcetylationFDVTKGSKFYGPAGP
EEECCCCCCCCCCCC		51.8025953088
135UbiquitinationFDVTKGSKFYGPAGP
EEECCCCCCCCCCCC		51.8021890473
137PhosphorylationVTKGSKFYGPAGPYG
ECCCCCCCCCCCCCC		26.4128152594
143PhosphorylationFYGPAGPYGIFAGRD
CCCCCCCCCEEECCC		23.1821253578
149MethylationPYGIFAGRDASRGLA
CCCEEECCCCCCCCC		32.65115487335
150UbiquitinationYGIFAGRDASRGLAT
CCEEECCCCCCCCCH		48.2321890473
156UbiquitinationRDASRGLATFCLDKD
CCCCCCCCHHHCCHH		11.0623000965
159UbiquitinationSRGLATFCLDKDALR
CCCCCHHHCCHHHHH		4.1121890473
159GlutathionylationSRGLATFCLDKDALR
CCCCCHHHCCHHHHH		4.1122555962
162AcetylationLATFCLDKDALRDEY
CCHHHCCHHHHHHCC		31.7725825284
162UbiquitinationLATFCLDKDALRDEY
CCHHHCCHHHHHHCC		31.77-
166MethylationCLDKDALRDEYDDLS
HCCHHHHHHCCCCHH		36.11115487327
167PhosphorylationLDKDALRDEYDDLSD
CCHHHHHHCCCCHHH		60.71-
169PhosphorylationKDALRDEYDDLSDLN
HHHHHHCCCCHHHCC		21.0327642862
173MethylationRDEYDDLSDLNAVQM
HHCCCCHHHCCCCHH		47.23-
173PhosphorylationRDEYDDLSDLNAVQM
HHCCCCHHHCCCCHH		47.23-
180SulfoxidationSDLNAVQMESVREWE
HHCCCCHHHHHHHHH		3.1328465586
186AcetylationQMESVREWEMQFKEK
HHHHHHHHHHHHHHH		8.87-
186UbiquitinationQMESVREWEMQFKEK
HHHHHHHHHHHHHHH		8.8723000965
190MethylationVREWEMQFKEKYDYV
HHHHHHHHHHHHCCH		12.16-
191UbiquitinationREWEMQFKEKYDYVG
HHHHHHHHHHHCCHH		36.0821890473
193MalonylationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.9726320211
193UbiquitinationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.9721890473
193AcetylationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.9723749302
193PhosphorylationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.97-
1932-HydroxyisobutyrylationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.97-
194PhosphorylationEMQFKEKYDYVGRLL
HHHHHHHHCCHHCCC		17.3826074081
196PhosphorylationQFKEKYDYVGRLLKP
HHHHHHCCHHCCCCC		11.1725884760
197PhosphorylationFKEKYDYVGRLLKPG
HHHHHCCHHCCCCCC		3.08-
208PhosphorylationLKPGEEPSEYTDEED
CCCCCCCCCCCCHHH		46.6529255136
210PhosphorylationPGEEPSEYTDEEDTK
CCCCCCCCCCHHHCC		24.6723927012
211PhosphorylationGEEPSEYTDEEDTKD
CCCCCCCCCHHHCCC		32.6529255136
215UbiquitinationSEYTDEEDTKDHNKQ
CCCCCHHHCCCCCCC		57.9421890473
216PhosphorylationEYTDEEDTKDHNKQD
CCCCHHHCCCCCCCC		41.4729255136
217AcetylationYTDEEDTKDHNKQD-
CCCHHHCCCCCCCC-		70.12-
217UbiquitinationYTDEEDTKDHNKQD-
CCCHHHCCCCCCCC-		70.1221890473
220PhosphorylationEEDTKDHNKQD----
HHHCCCCCCCC----		54.54-
226UbiquitinationHNKQD----------
CCCCC----------		-
232Phosphorylation----------------
----------------		20166139
234Phosphorylation------------------
------------------		20166139
235Phosphorylation-------------------
-------------------		18452278
240Phosphorylation------------------------
------------------------		20166139
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 PGRC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGRC2_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 PGRC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGRC2_HUMAN !!
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
There are no disease associations of PTM sites.
Regulatory Network of PGRC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-90, AND MASSSPECTROMETRY.
"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-90; SER-208 AND TYR-210,AND MASS SPECTROMETRY.
"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-208 AND THR-211, ANDMASS SPECTROMETRY.
"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-90 AND THR-211, AND MASSSPECTROMETRY.
"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-90, AND MASSSPECTROMETRY.
"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 THR-211, AND MASSSPECTROMETRY.
"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 TYR-210 AND THR-211, ANDMASS SPECTROMETRY.

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