PGRC2_MOUSE - dbPTM
PGRC2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGRC2_MOUSE
UniProt AC Q80UU9
Protein Name Membrane-associated progesterone receptor component 2
Gene Name Pgrmc2
Organism Mus musculus (Mouse).
Sequence Length 217
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description Receptor for steroids..
Protein Sequence MAAGDGDVKLSTLGSGGESGGDGSPGGAGATAARSSWVAALLATGGEMLLNVALVALVLLGAYRLWVRWGRRGLCSGPGAGEESPAATLPRMKKRDFSLEQLRQYDGARTPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHSKQD
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
15PhosphorylationVKLSTLGSGGESGGD
EEEEECCCCCCCCCC		46.8928066266
19PhosphorylationTLGSGGESGGDGSPG
ECCCCCCCCCCCCCC		51.8828066266
24PhosphorylationGESGGDGSPGGAGAT
CCCCCCCCCCCHHHH		25.7228066266
31PhosphorylationSPGGAGATAARSSWV
CCCCHHHHHHHHHHH		21.6728066266
75S-nitrosocysteineRWGRRGLCSGPGAGE
HCCCCCCCCCCCCCC		5.00-
75S-palmitoylationRWGRRGLCSGPGAGE
HCCCCCCCCCCCCCC		5.0028526873
75S-nitrosylationRWGRRGLCSGPGAGE
HCCCCCCCCCCCCCC		5.0021278135
76PhosphorylationWGRRGLCSGPGAGEE
CCCCCCCCCCCCCCC		53.7320531401
84PhosphorylationGPGAGEESPAATLPR
CCCCCCCCCCCCCCC		18.6125521595
88PhosphorylationGEESPAATLPRMKKR
CCCCCCCCCCCHHHC		39.1325159016
98PhosphorylationRMKKRDFSLEQLRQY
CHHHCCCCHHHHHHC		34.9726824392
110PhosphorylationRQYDGARTPRILLAV
HHCCCCCCCEEEEEE		19.1824899341
120UbiquitinationILLAVNGKVFDVTKG
EEEEECCEEEEECCC		34.2322790023
126UbiquitinationGKVFDVTKGSKFYGP
CEEEEECCCCCCCCC		62.1222790023
129UbiquitinationFDVTKGSKFYGPAGP
EEECCCCCCCCCCCC		51.8022790023
153S-palmitoylationSRGLATFCLDKDALR
CCCCCHHHCCHHHHH		4.1128526873
185UbiquitinationREWEMQFKEKYDYVG
HHHHHHHHHHHCCHH		36.0822790023
187AcetylationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.9723201123
187UbiquitinationWEMQFKEKYDYVGRL
HHHHHHHHHCCHHCC		43.9722790023
188PhosphorylationEMQFKEKYDYVGRLL
HHHHHHHHCCHHCCC		17.3823984901
190PhosphorylationQFKEKYDYVGRLLKP
HHHHHHCCHHCCCCC		11.1720469934
202PhosphorylationLKPGEEPSEYTDEED
CCCCCCCCCCCCCCC		46.6524925903
204PhosphorylationPGEEPSEYTDEEDTK
CCCCCCCCCCCCCCC		24.6725521595
205PhosphorylationGEEPSEYTDEEDTKD
CCCCCCCCCCCCCCC		32.6527087446
210PhosphorylationEYTDEEDTKDHSKQD
CCCCCCCCCCCCCCC		41.4724925903
214PhosphorylationEEDTKDHSKQD----
CCCCCCCCCCC----		41.9927742792
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGRC2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGRC2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGRC2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND THR-205, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASSSPECTROMETRY.

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