Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Reticulon-3  

UniProtKB / Swiss-Prot ID :  RTN3_MOUSE

Gene Name (Synonyms) : 
Rtn3  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein (By similarity). 

Protein Function :  May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress (By similarity). 

Transmembrane Topology (topPTM) : RTN3_MOUSE 

Protein Sequence MAESSAATQSPSVSSSSSGAEPSALGGGGGSPGACPALGAKSCGSSCADSFVSSSSSQPVSIFSTSQAGL...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHCCCCCCCEEEECCHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
31PhosphoserineGGGGSPGAC
CCCCCCCCC
24.36Phosphositeplus
Link-
217PhosphoserineTYSLSPSEL
EEECCCCCC
22.05Phosphositeplus
Link-
225PhosphoserineLPVASVEKD
CCCCCCCCC
30.92Phosphositeplus
Link-
230PhosphoserineVEKDSPESP
CCCCCCCCC
41.45PhosphoELM
Link-
230PhosphoserineVEKDSPESP
CCCCCCCCC
41.45Phosphositeplus
Link-
230PhosphoserineVEKDSPESP
CCCCCCCCC
41.45SysPTM
Link-
230Phosphoserine.VEKDSPESP
CCCCCCCCC
41.45UniProtKB
Link-
233PhosphoserineDSPESPFEV
CCCCCCHHE
37.97Phosphositeplus
Link-
467PhosphoserineTEVDSSGES
ECCCCCCCC
45.47Phosphositeplus
Link-
468PhosphoserineEVDSSGESD
CCCCCCCCC
41.96Phosphositeplus
Link-
524PhosphothreonineAQPETPTQK
CCCCCCCCC
38.02PhosphoELM
Link-
524PhosphothreonineAQPETPTQK
CCCCCCCCC
38.02Phosphositeplus
Link-
524PhosphothreonineAQPETPTQK
CCCCCCCCC
38.02SysPTM
Link-
524Phosphothreonine.AQPETPTQK
CCCCCCCCC
38.02UniProtKB
Link-
526PhosphothreoninePETPTQKSL
CCCCCCCCC
56.92PhosphoELM
Link-
526PhosphothreoninePETPTQKSL
CCCCCCCCC
56.92Phosphositeplus
Link-
526PhosphothreoninePETPTQKSL
CCCCCCCCC
56.92SysPTM
Link-
526Phosphothreonine.PETPTQKSL
CCCCCCCCC
56.92UniProtKB
Link-
529PhosphoserinePTQKSLEGE
CCCCCCCCC
23.10Phosphositeplus
Link-
596PhosphoserineDTDGSSPED
CCCCCCCCC
45.59Phosphositeplus
Link-
597PhosphoserineTDGSSPEDL
CCCCCCCCC
37.53Phosphositeplus
Link-
597PhosphoserineTDGSSPEDL
CCCCCCCCC
37.53SysPTM
Link-
671PhosphothreonineGGAPTMSPD
CCCCCCCCC
29.73PhosphoELM
Link-
671PhosphothreonineGGAPTMSPD
CCCCCCCCC
29.73Phosphositeplus
Link-
671PhosphothreonineGGAPTMSPD
CCCCCCCCC
29.73SysPTM
Link-
671Phosphothreonine.GGAPTMSPD
CCCCCCCCC
29.73UniProtKB
Link-
673PhosphoserineAPTMSPDLE
CCCCCCCCC
20.10PhosphoELM
Link-
673PhosphoserineAPTMSPDLE
CCCCCCCCC
20.10Phosphositeplus
Link-
673PhosphoserineAPTMSPDLE
CCCCCCCCC
20.10SysPTM
Link-
673Phosphoserine.APTMSPDLE
CCCCCCCCC
20.10UniProtKB
Link-
752PhosphoserineTRIDSISSL
CCCCCCCCC
23.23Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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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-230; THR-524; THR-526;THR-671 AND SER-673, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures