PGRC1_MOUSE - dbPTM
PGRC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PGRC1_MOUSE
UniProt AC O55022
Protein Name Membrane-associated progesterone receptor component 1
Gene Name Pgrmc1 {ECO:0000312|MGI:MGI:1858305}
Organism Mus musculus (Mouse).
Sequence Length 195
Subcellular Localization Microsome membrane
Single-pass membrane protein . Endoplasmic reticulum membrane
Single-pass membrane protein .
Protein Description Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs)..
Protein Sequence MAAEDVVATGADPSELEGGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDETARKNE
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
54PhosphorylationRGDQPGASGDNDDDE
HCCCCCCCCCCCCCC		53.2325293948
74PhosphorylationRLKRRDFTPAELRRF
CCCCCCCCHHHHHCC		26.3621082442
96UbiquitinationILMAINGKVFDVTKG
EEEEECCEEEEECCC		34.9322790023
102MalonylationGKVFDVTKGRKFYGP
CEEEEECCCCCCCCC		57.4726320211
102UbiquitinationGKVFDVTKGRKFYGP
CEEEEECCCCCCCCC		57.47-
105MalonylationFDVTKGRKFYGPEGP
EEECCCCCCCCCCCC		52.1626320211
105AcetylationFDVTKGRKFYGPEGP
EEECCCCCCCCCCCC		52.1622826441
105UbiquitinationFDVTKGRKFYGPEGP
EEECCCCCCCCCCCC		52.16-
113PhosphorylationFYGPEGPYGVFAGRD
CCCCCCCCCEECCCC		36.4629514104
129S-nitrosylationSRGLATFCLDKEALK
CCCCCHHHCCHHHHH		4.1122178444
132UbiquitinationLATFCLDKEALKDEY
CCHHHCCHHHHHHCC		31.7522790023
136AcetylationCLDKEALKDEYDDLS
HCCHHHHHHCCCCHH		56.4123954790
139PhosphorylationKEALKDEYDDLSDLT
HHHHHHCCCCHHHCC		25.5422802335
143PhosphorylationKDEYDDLSDLTPAQQ
HHCCCCHHHCCHHHH		37.2523984901
146PhosphorylationYDDLSDLTPAQQETL
CCCHHHCCHHHHHHH		22.9019060867
163UbiquitinationWDSQFTFKYHHVGKL
CCHHHHEEEECHHHH		40.3922790023
163AcetylationWDSQFTFKYHHVGKL
CCHHHHEEEECHHHH		40.3923954790
169UbiquitinationFKYHHVGKLLKEGEE
EEEECHHHHHHCCCC		49.9422790023
172UbiquitinationHHVGKLLKEGEEPTV
ECHHHHHHCCCCCCC		74.2822790023
178PhosphorylationLKEGEEPTVYSDDEE
HHCCCCCCCCCCCCC		35.0425521595
180PhosphorylationEGEEPTVYSDDEEPK
CCCCCCCCCCCCCCC		14.6225521595
181PhosphorylationGEEPTVYSDDEEPKD
CCCCCCCCCCCCCCC		33.9624925903
190PhosphorylationDEEPKDETARKNE--
CCCCCCHHHHCCC--		41.7325521595
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
181SPhosphorylationKinaseMAPK14P47811
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PGRC1_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 PGRC1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PGRC1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PGRC1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-181, 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 SER-181, AND MASSSPECTROMETRY.
"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 TYR-180 AND SER-181, ANDMASS SPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of mouse liver using immobilized metalaffinity purification and linear ion trap mass spectrometry.";
Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
Cited for: PHOSPHORYLATION AT SER-181.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASSSPECTROMETRY.

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