RTN1_MOUSE - dbPTM
RTN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTN1_MOUSE
UniProt AC Q8K0T0
Protein Name Reticulon-1
Gene Name Rtn1
Organism Mus musculus (Mouse).
Sequence Length 780
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description May be involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells..
Protein Sequence MAAPPDLQDEPLSLGSPGSQWFGGRGDGEDEATAVMGARPAQQDGEPAWGSGAGAGVTSSRELCSGPARSPPVAMETASTGMAAVPDALDHSPSSTLKDGEGACYTSLISDVCYPPREDSAYFTGILQKENGHITTSESPEEPETPGPSLPEVPGMEPQGLLSSDSGIEMTPAESTEVNKILADPLDQMKAEAYKYIDITRPQEAKGQEEQHPGLEDKDLDFKDKDTEVSTKAEGVRAPNQPAPVEGKLIKDHLFEESTFAPYIDELSDEQHRVSLVTAPVKITLTEIEPPLMTATQETIPEKQDLCLKPSPDTVPTVTVSEPEDDSPGSVTPPSSGTEPSAAESQGKGSVSEDELIAAIKEAKGLSYETTESPRPVGQVADKPKTKTRSGLPTIPSPLDQEASSAESGDSEIELVSEDPMASEDALPSGYVSFGHVSGPPPSPASPSIQYSILREEREAELDSELIIESCDASSASEESPKREQDSPPMKPGALDAIREETGSRATEERAPSHQGPVEPDPMLSFAPAAALQSRPEPSSGDGASVPEPPRSQQQKPEEEAVSSSQSPTATEIPGPLGSGLMPPLPFFNKQKAIDLLYWRDIKQTGIVFGSFLLLLFSLTQFSVVSVVAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKAYLELEITLSQEQIQKYTDCLQLYVNSTLKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLLMAVVSMFTLPVVYVKHQAQVDQYLGLVRTHINTVVAKIQAKIPGAKRHAE
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
13PhosphorylationDLQDEPLSLGSPGSQ
CCCCCCCCCCCCCCC		41.20-
16PhosphorylationDEPLSLGSPGSQWFG
CCCCCCCCCCCCCCC		31.2322817900
65PhosphorylationTSSRELCSGPARSPP
CCCCHHCCCCCCCCC		61.5125521595
70PhosphorylationLCSGPARSPPVAMET
HCCCCCCCCCCEECC		35.3424925903
77PhosphorylationSPPVAMETASTGMAA
CCCCEECCCCCCCCC		16.9024925903
79PhosphorylationPVAMETASTGMAAVP
CCEECCCCCCCCCCC		32.6729472430
80PhosphorylationVAMETASTGMAAVPD
CEECCCCCCCCCCCC		28.6324925903
92PhosphorylationVPDALDHSPSSTLKD
CCCHHCCCCCCCCCC		26.5825521595
94PhosphorylationDALDHSPSSTLKDGE
CHHCCCCCCCCCCCC		38.6824925903
95PhosphorylationALDHSPSSTLKDGEG
HHCCCCCCCCCCCCC		40.9424925903
96PhosphorylationLDHSPSSTLKDGEGA
HCCCCCCCCCCCCCC		42.0124925903
105PhosphorylationKDGEGACYTSLISDV
CCCCCCEEEEECCCC		9.99-
107PhosphorylationGEGACYTSLISDVCY
CCCCEEEEECCCCCC		9.3821082442
136PhosphorylationKENGHITTSESPEEP
EECCEECCCCCCCCC		29.8729899451
137PhosphorylationENGHITTSESPEEPE
ECCEECCCCCCCCCC		27.6829899451
190UbiquitinationADPLDQMKAEAYKYI
CCHHHHHHHHHHHEE		37.13-
263PhosphorylationEESTFAPYIDELSDE
CCCCCHHHHHHCCCC		19.9929899451
268PhosphorylationAPYIDELSDEQHRVS
HHHHHHCCCCCCEEE		36.7329899451
275PhosphorylationSDEQHRVSLVTAPVK
CCCCCEEEEEECCEE		19.6529899451
278O-linked_GlycosylationQHRVSLVTAPVKITL
CCEEEEEECCEEEEE		30.4569101409
311PhosphorylationQDLCLKPSPDTVPTV
CCCCCCCCCCCCCEE		33.5420415495
314PhosphorylationCLKPSPDTVPTVTVS
CCCCCCCCCCEEEEC		31.5920415495
317PhosphorylationPSPDTVPTVTVSEPE
CCCCCCCEEEECCCC		25.1925293948
319PhosphorylationPDTVPTVTVSEPEDD
CCCCCEEEECCCCCC		22.3125293948
321PhosphorylationTVPTVTVSEPEDDSP
CCCEEEECCCCCCCC		37.7620415495
327PhosphorylationVSEPEDDSPGSVTPP
ECCCCCCCCCCCCCC		43.4119060867
330PhosphorylationPEDDSPGSVTPPSSG
CCCCCCCCCCCCCCC		26.6320415495
332PhosphorylationDDSPGSVTPPSSGTE
CCCCCCCCCCCCCCC		31.0519060867
335PhosphorylationPGSVTPPSSGTEPSA
CCCCCCCCCCCCCCH		42.4725293948
336PhosphorylationGSVTPPSSGTEPSAA
CCCCCCCCCCCCCHH		56.3525293948
338PhosphorylationVTPPSSGTEPSAAES
CCCCCCCCCCCHHHH		46.8225293948
341PhosphorylationPSSGTEPSAAESQGK
CCCCCCCCHHHHCCC		33.6025293948
345PhosphorylationTEPSAAESQGKGSVS
CCCCHHHHCCCCCCC		39.2325293948
350PhosphorylationAESQGKGSVSEDELI
HHHCCCCCCCHHHHH		26.4225521595
352PhosphorylationSQGKGSVSEDELIAA
HCCCCCCCHHHHHHH		40.8225521595
373PhosphorylationLSYETTESPRPVGQV
CCCCCCCCCCCCCCC		24.9029899451
470PhosphorylationDSELIIESCDASSAS
CCEEHHHHCCCCCCC		13.5927841257
474PhosphorylationIIESCDASSASEESP
HHHHCCCCCCCCCCC		17.1225521595
477PhosphorylationSCDASSASEESPKRE
HCCCCCCCCCCCCCC		43.7922817900
480PhosphorylationASSASEESPKREQDS
CCCCCCCCCCCCCCC		31.5025521595
487PhosphorylationSPKREQDSPPMKPGA
CCCCCCCCCCCCCCH		30.5125521595
504PhosphorylationAIREETGSRATEERA
HHHHHHCCCCCCCCC		26.6029899451
539PhosphorylationLQSRPEPSSGDGASV
HHCCCCCCCCCCCCC		45.3429899451
552PhosphorylationSVPEPPRSQQQKPEE
CCCCCCCHHCCCCHH		37.8124925903
563PhosphorylationKPEEEAVSSSQSPTA
CCHHHHHCCCCCCCC		31.1829899451
564PhosphorylationPEEEAVSSSQSPTAT
CHHHHHCCCCCCCCC		26.2924925903
565PhosphorylationEEEAVSSSQSPTATE
HHHHHCCCCCCCCCC		27.4629899451
567PhosphorylationEAVSSSQSPTATEIP
HHHCCCCCCCCCCCC		26.6024925903
569PhosphorylationVSSSQSPTATEIPGP
HCCCCCCCCCCCCCC		52.0029899451
571PhosphorylationSSQSPTATEIPGPLG
CCCCCCCCCCCCCCC		36.6024925903
579PhosphorylationEIPGPLGSGLMPPLP
CCCCCCCCCCCCCCC		36.1124925903
598PhosphorylationQKAIDLLYWRDIKQT
HHHHHHEECCCHHHH		13.00-
641PhosphorylationAALSATISFRIYKSV
HHHHHHHHHHHHHHH		12.2428973931
646UbiquitinationTISFRIYKSVLQAVQ
HHHHHHHHHHHHHHH		31.55-
753NitrationHQAQVDQYLGLVRTH
HHHHHHHHHHHHHHH		9.77-
763PhosphorylationLVRTHINTVVAKIQA
HHHHHHHHHHHHHHH		18.76-
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 RTN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTN1_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 RTN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RTN1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-70; SER-92; SER-350 ANDSER-352, AND MASS SPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-352, ANDMASS SPECTROMETRY.

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