CHERP_MOUSE - dbPTM
CHERP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHERP_MOUSE
UniProt AC Q8CGZ0
Protein Name Calcium homeostasis endoplasmic reticulum protein
Gene Name Cherp {ECO:0000312|MGI:MGI:106417}
Organism Mus musculus (Mouse).
Sequence Length 936
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region . Endoplasmic reticulum . Distributed throughout the cytoplasm and also localizes to the perinuclear region. Colocalizes with ITPR1 (By similarity).
Protein Description Involved in calcium homeostasis, growth and proliferation..
Protein Sequence MEMPMPPDDQELRNVIDKLAQFVARNGPEFEKMTMEKQKDNPKFSFLFGGEFYSYYKCKLALEQQQLICKQQAPELEPTSAMPPLPQPPLAPTASLTPAQGTPSMDELIQQSQWSLQQQEQHLLALRQEQVTTAVAHAVEQQMQKLLEETQLDMSEFDNLLQPIIDTCTKDAISAGKNWMFSNAKSPPHCELMAGHLRNRITADGAHFELRLHLIYLINDVLHHCQRKQARELLAALQKVVVPIYCTSFLAVEEDKQQKIARLLQLWEKNGYFDDSIIQQLQSPALGLGQYQATLINEYSSVVQPVQLAFQQQIQSLKTQHEEFVSSLAQQQQQQQQQQQQQPQPQPQPQIQLPQMEADVKATPPPPAPPPASAPAPTIPPTTQPDDNKPPIQMPGSSEYDTSAGVQDPAAAGPRGPGPHEQIPPNKPPWFDQPHPVAPWGQQQPPEQPPYPHHQGGPPHCPPWNNSHEGMWGEQRGDPGWNGQRDAPWNNQPDPNWNNQFEGPWNNQHEPPPWGGAQREPPFRMQRPPHFRGPFPPHQQHPQFNQPPHPHNFNRFPPRFMQDDFPPRHPFERPPYPHRFDYPQGDFPADMGPPHHHPGHRMPHPGINEHPPWAGPQHPDFGPPPHGFNGQPPHMRRQGPPHINHDDPSLVPNVPYFDLPAGLMAPLVKLEDHEYKPLDPKDIRLPPPMPPSERLLAAVEAFYSPPSHDRPRNSEGWEQNGLYEFFRAKMRARRRKGQEKRNSGPSRSRSRSKSRGRSSSRSSSRSSKSSRSSSRSHSRSRSRSSSRSRSRSRSRSRSSRSRSRSRSRSRSKSYSPGRRRRSRSRSPTPPSAAGLGSNSAPPIPDSRLGEENKGHQMLVKMGWSGSGGLGAKEQGIQDPIKGGDVRDKWDQYKGVGVALDDPYENYRRNKSYSFIARMKARDEFSTFGTRKEEKED
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
1Acetylation-------MEMPMPPD
-------CCCCCCCC		10.06-
18AcetylationELRNVIDKLAQFVAR
HHHHHHHHHHHHHHH		34.30-
18UbiquitinationELRNVIDKLAQFVAR
HHHHHHHHHHHHHHH		34.30-
177UbiquitinationKDAISAGKNWMFSNA
HHHHHCCCCCCCCCC		47.34-
186PhosphorylationWMFSNAKSPPHCELM
CCCCCCCCCCCCHHH		41.0529233185
216PhosphorylationELRLHLIYLINDVLH
HHHHHHHHHHHHHHH		14.1123567750
703PhosphorylationLAAVEAFYSPPSHDR
HHHHHHHCCCCCCCC		27.5826643407
704PhosphorylationAAVEAFYSPPSHDRP
HHHHHHCCCCCCCCC		24.7129514104
707PhosphorylationEAFYSPPSHDRPRNS
HHHCCCCCCCCCCCC		41.2126643407
723PhosphorylationGWEQNGLYEFFRAKM
HHHHCCHHHHHHHHH		16.4622817900
798PhosphorylationRSRSRSRSSRSRSRS
HHHHHHHHHHHHHHH		31.2020531401
799PhosphorylationSRSRSRSSRSRSRSR
HHHHHHHHHHHHHHH		32.9119854140
801PhosphorylationSRSRSSRSRSRSRSR
HHHHHHHHHHHHHHH		36.2320531401
811PhosphorylationRSRSRSRSKSYSPGR
HHHHHHHCCCCCCCC		27.4827681418
813PhosphorylationRSRSRSKSYSPGRRR
HHHHHCCCCCCCCCC		31.9023737553
814PhosphorylationSRSRSKSYSPGRRRR
HHHHCCCCCCCCCCC		23.7123737553
815PhosphorylationRSRSKSYSPGRRRRS
HHHCCCCCCCCCCCC		28.1523737553
822PhosphorylationSPGRRRRSRSRSPTP
CCCCCCCCCCCCCCC		32.5618388127
824PhosphorylationGRRRRSRSRSPTPPS
CCCCCCCCCCCCCCC		38.0518388127
826PhosphorylationRRRSRSRSPTPPSAA
CCCCCCCCCCCCCCC		34.0825521595
828PhosphorylationRSRSRSPTPPSAAGL
CCCCCCCCCCCCCCC		49.4225521595
831PhosphorylationSRSPTPPSAAGLGSN
CCCCCCCCCCCCCCC		31.7727087446
837PhosphorylationPSAAGLGSNSAPPIP
CCCCCCCCCCCCCCC		32.4327087446
839PhosphorylationAAGLGSNSAPPIPDS
CCCCCCCCCCCCCCC		43.8021082442
846PhosphorylationSAPPIPDSRLGEENK
CCCCCCCCCCCCCCC		24.8525619855
864PhosphorylationMLVKMGWSGSGGLGA
EEEECCCCCCCCCCC		19.8326643407
866PhosphorylationVKMGWSGSGGLGAKE
EECCCCCCCCCCCHH		24.9525266776
881UbiquitinationQGIQDPIKGGDVRDK
HCCCCCCCCCCHHHH		63.33-
888AcetylationKGGDVRDKWDQYKGV
CCCCHHHHHHHCCCE		41.95-
903PhosphorylationGVALDDPYENYRRNK
EEECCCHHHHHHCCC		24.6526026062
910MalonylationYENYRRNKSYSFIAR
HHHHHCCCCCHHHHH		49.3026320211
911PhosphorylationENYRRNKSYSFIARM
HHHHCCCCCHHHHHH		29.5628725479
912PhosphorylationNYRRNKSYSFIARMK
HHHCCCCCHHHHHHH		14.8121743459
913PhosphorylationYRRNKSYSFIARMKA
HHCCCCCHHHHHHHH		19.7828725479
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 CHERP_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND THR-828, ANDMASS SPECTROMETRY.
"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-822, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND MASSSPECTROMETRY.

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