| UniProt ID | SAHH2_ARATH | |
|---|---|---|
| UniProt AC | Q9LK36 | |
| Protein Name | Adenosylhomocysteinase 2 | |
| Gene Name | SAHH2 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 485 | |
| Subcellular Localization | ||
| Protein Description | Adenosylhomocysteine is a competitive inhibitor of S-adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine.. | |
| Protein Sequence | MALLVEKTSSGREYKVKDMSQADFGRLEIELAEVEMPGLVSCVTEFGPSQPLKGARITGSLHMTIQTAVLIETLTALGAEVRWCSCNIFSTQDHAAAAIARDSAAVFAWKGETLQEYWWCTERALDWGPGGGPDLIVDDGGDATLLIHEGVKAEEIFAKNGTFPDPTSTDNPEFQIVLSIIKDGLQVDPKKYHKMKERLVGVSEETTTGVKRLYQMQETGALLFPAINVNDSVTKSKFDNLYGCRHSLPDGLMRATDVMIAGKVAVICGYGDVGKGCAAAMKTAGARVIVTEIDPICALQALMEGLQVLTLEDVVSEADIFCTTTGNKDIIMVDHMRKMKNNAIVCNIGHFDNEIDMLGLETYPGVKRITIKPQTDRWVFPDTNSGIIVLAEGRLMNLGCATGHPSFVMSCSFTNQVIAQLELWNEKSSGKYEKKVYVLPKHLDEKVAALHLGKLGARLTKLTKDQSDYVSIPVEGPYKPVHYRY | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 14 | Phosphorylation | KTSSGREYKVKDMSQ ECCCCCEEEEEECHH | 21.52 | 23776212 | |
| 15 | Ubiquitination | TSSGREYKVKDMSQA CCCCCEEEEEECHHH | 37.75 | 17272265 | |
| 20 | Phosphorylation | EYKVKDMSQADFGRL EEEEEECHHHHCCCE | 32.14 | 23776212 | |
| 113 | Phosphorylation | VFAWKGETLQEYWWC EEEECCCCHHHEEEE | 42.27 | 24299221 | |
| 203 | Phosphorylation | KERLVGVSEETTTGV HHHHCCCCHHHCHHH | 24.64 | 24299221 | |
| 219 | Phosphorylation | RLYQMQETGALLFPA HHHHHHHHCCEEEEE | 15.74 | 19376835 | |
| 236 | Phosphorylation | VNDSVTKSKFDNLYG CCCCCCHHHCCCCCC | 29.23 | 24299221 | |
| 332 | Sulfoxidation | TGNKDIIMVDHMRKM CCCCCEEECCCHHHC | 2.71 | 25693801 | |
| 336 | Sulfoxidation | DIIMVDHMRKMKNNA CEEECCCHHHCCCCE | 3.69 | 25693801 | |
| 370 | Phosphorylation | YPGVKRITIKPQTDR CCCEEEEEECCCCCC | 27.29 | 25561503 |
| 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 SAHH2_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAHH2_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 SAHH2_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SAHH1_ARATH | MEE58 | physical | 25293756 |
| 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 THR-219, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants."; Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; Mol. Cell. Proteomics 6:601-610(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15, AND MASSSPECTROMETRY. | |