Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein MON2  

UniProtKB / Swiss-Prot ID :  MON2_YEAST

Gene Name (Synonyms) : 
MON2, YSL2 YNL297C N0453  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Golgi apparatus membrane; Peripheral membrane protein. Note=Late Golgi. 

Protein Function :  Required for traffic between late Golgi and early endosomes. Required for endocytosis and maintenance of vacuolar structure. 

Protein Sequence MAMNTGGFDSMQRQLEAELRSLSSESKRRNSTIRHASDKSIEILKRVHSFEELERHPDFALPFVLACQSR...
Predicted Secondary Structure  -
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
564PhosphoserineTRNISTSSV
26.28SysPTM
Link-
564Phosphoserine.TRNISTSSV
26.28UniProtKB
Link-
565PhosphothreonineRNISTSSVT
22.63SysPTM
Link-
565Phosphothreonine.RNISTSSVT
22.63UniProtKB
Link-
567PhosphoserineISTSSVTTS
24.46SysPTM
Link-
567Phosphoserine.ISTSSVTTS
24.46UniProtKB
Link-
569PhosphothreonineTSSVTTSPV
24.41SysPTM
Link-
569Phosphothreonine.TSSVTTSPV
24.41UniProtKB
Link-
571PhosphoserineSVTTSPVES
19.99SysPTM
Link-
571Phosphoserine.SVTTSPVES
19.99UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
- top -

Disease Reference
Drug Reference
- top -
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND MASSSPECTROMETRY.
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; THR-565; SER-567;THR-569 AND SER-571, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-567, ANDMASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures