Cloned (Comment) | Organism |
---|---|
production of recombinant His6-SUS2 protein (rSUS2) in Escherichia coli | Zea mays |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | SUS2 may be the housekeeping SUS isoform because it is solely cytosolic and therefore cleaves sucrose for metabolic requirements within the cytosol | Zea mays | 5829 | - |
membrane | SUS-SH1 is associated with membranes | Zea mays | 16020 | - |
membrane | SUS1 is associated with membranes | Zea mays | 16020 | - |
microsome | SUS-SH1 is associated with microsomes | Zea mays | - |
- |
additional information | native SUS2 is not associated with membranes in vivo | Zea mays | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Zea mays | SUS2 may function to regulate SUS1 membrane association by formation of SUS1SUS2 hetero-oligomers | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylated at a C-terminal threonine residue only in midvein | Zea mays |
phosphoprotein | phosphorylated at a C-terminal threonine residue only in midvein. SUS-SH1 is phosphorylated in vivo at the Ser10 site in kernels | Zea mays |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
internode | SUS1 is predominant in the internode cortex tissue | Zea mays | - |
kernel | SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels | Zea mays | - |
kernel | SUS2 is particularly abundant in kernels at various pollination stages | Zea mays | - |
kernel | SUSSH1 is predominant in developing kernels | Zea mays | - |
leaf | elongation zone, isoenzyme SUS-SH1 | Zea mays | - |
leaf | elongation zone, isoenzyme SUS2. SUS2 exists predominantly as a hetero-oligomer with SUS1 in kernels | Zea mays | - |
leaf | SUS1 is the predominant isoform of SUS associated with microsomes isolated from the base of the maize leaf elongation zone and from kernels at 20 and 30 days after pollination | Zea mays | - |
root | SUS1 is predominant in etiolated shoots | Zea mays | - |
shoot | SUS1 is predominant in etiolated shoots | Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | SUS2 may function to regulate SUS1 membrane association by formation of SUS1SUS2 hetero-oligomers | Zea mays | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | SUS2 exists predominantly as a heterooligomer with SUS1 | Zea mays |
More | SUS2 predominantly exists as a hetero-oligomer with SUS1 | Zea mays |
oligomer | SUS-SH1 forms only homooligomers | Zea mays |
Synonyms | Comment | Organism |
---|---|---|
SUS-SH1 | - |
Zea mays |
SUS1 | - |
Zea mays |
SUS2 | - |
Zea mays |