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

UniProtKB / Swiss-Prot ID :  TMT1_YEAST

Gene Name (Synonyms) : 
TMT1, TAM1 YER175CSYGP-ORF63  

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

Subcellular Localization :  Cytoplasm. 

Protein Function :  Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate and 3-isopropylmalate at high affinity and of other molecules like cis-aconitate, isocitrate, and citrate at lower velocities and affinities. The function of trans-aconitate methylation appears to be in reducing the toxicity of this spontaneous breakdown product of cis-aconitate. The role of 3-isopropylmalate methylation is unclear but may represent a metabolic branch at 3-isopropylmalate, where some of the material is taken in the pathway leading to leucine and some is taken in a pathway to the 3-isopropylmalate methyl ester, a molecule that provides a signal to switch from vegetative to invasive growth in response to amino acid starvation. 

Protein Sequence MSTFSASDFNSERYSSSRPSYPSDFYKMIDEYHDGERKLLVDVGCGPGTATLQMAQELKPFEQIIGSDLS...
Predicted Secondary Structure  -
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
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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
14PhosphotyrosineNSERYSSSR
14.62SysPTM
Link
14Phosphotyrosine.NSERYSSSR
14.62UniProtKB
Link
17PhosphoserineRYSSSRPSY
42.12SysPTM
Link
17Phosphoserine.RYSSSRPSY
42.12UniProtKB
Link
20PhosphoserineSSRPSYPSD
48.87SysPTM
Link
20Phosphoserine.SSRPSYPSD
48.87UniProtKB
Link
84PhosphoserineIKEGSPDTY
22.24SysPTM
Link
84Phosphoserine.IKEGSPDTY
22.24UniProtKB
Link
87PhosphothreonineGSPDTYKNV
39.52SysPTM
Link
87Phosphothreonine.GSPDTYKNV
39.52UniProtKB
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
"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 TYR-14; SER-17; SER-20;SER-84 AND THR-87, 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