| UniProt ID | MTN1_ARATH | |
|---|---|---|
| UniProt AC | Q9T0I8 | |
| Protein Name | 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 1 | |
| Gene Name | MTN1 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 267 | |
| Subcellular Localization | ||
| Protein Description | Enzyme of the methionine cycle that catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis. Inactive towards S-adenosylhomocysteine (SAH/AdoHcy).. | |
| Protein Sequence | MAPHGDGLSDIEEPEVDAQSEILRPISSVVFVIAMQAEALPLVNKFGLSETTDSPLGKGLPWVLYHGVHKDLRINVVCPGRDAALGIDSVGTVPASLITFASIQALKPDIIINAGTCGGFKVKGANIGDVFLVSDVVFHDRRIPIPMFDLYGVGLRQAFSTPNLLKELNLKIGRLSTGDSLDMSTQDETLIIANDATLKDMEGAAVAYVADLLKIPVVFLKAVTDLVDGDKPTAEEFLQNLTVVTAALEGTATKVINFINGRNLSDL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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| 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 MTN1_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MTN1_ARATH !! | ||||||
* 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 MTN1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CNBL3_ARATH | CBL3 | physical | 18945934 | |
| CNBL2_ARATH | CBL2 | physical | 21798944 | |
| MTN1_ARATH | MTN1 | physical | 26259190 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASSSPECTROMETRY. | |