| UniProt ID | GLGL1_ARATH | |
|---|---|---|
| UniProt AC | P55229 | |
| Protein Name | Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic | |
| Gene Name | ADG2 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 522 | |
| Subcellular Localization | Plastid, chloroplast. | |
| Protein Description | This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.. | |
| Protein Sequence | MVVSADCRISLSAPSCIRSSSTGLTRHIKLGSFCNGELMGKKLNLSQLPNIRLRSSTNFSQKRILMSLNSVAGESKVQELETEKRDPRTVASIILGGGAGTRLFPLTKRRAKPAVPIGGAYRLIDVPMSNCINSGINKVYILTQYNSASLNRHLARAYNSNGLGFGDGYVEVLAATQTPGESGKRWFQGTADAVRQFHWLFEDARSKDIEDVLILSGDHLYRMDYMDFIQDHRQSGADISISCIPIDDRRASDFGLMKIDDKGRVISFSEKPKGDDLKAMAVDTTILGLSKEEAEKKPYIASMGVYVFKKEILLNLLRWRFPTANDFGSEIIPFSAKEFYVNAYLFNDYWEDIGTIRSFFEANLALTEHPGAFSFYDAAKPIYTSRRNLPPSKIDNSKLIDSIISHGSFLTNCLIEHSIVGIRSRVGSNVQLKDTVMLGADYYETEAEVAALLAEGNVPIGIGENTKIQECIIDKNARVGKNVIIANSEGIQEADRSSDGFYIRSGITVILKNSVIKDGVVI | |
| 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 |
|---|---|---|---|---|---|
| 57 | Phosphorylation | NIRLRSSTNFSQKRI CCCCCCCCCCCHHHH | 41.34 | 19880383 | |
| 60 | Phosphorylation | LRSSTNFSQKRILMS CCCCCCCCHHHHHHH | 36.54 | 19880383 | |
| 89 | Phosphorylation | TEKRDPRTVASIILG HCCCCCHHEEEEEEC | 26.30 | 24299221 | |
| 101 | Phosphorylation | ILGGGAGTRLFPLTK EECCCCHHHCCCCCC | 24.54 | 29654922 | |
| 190 | Phosphorylation | GKRWFQGTADAVRQF CCCEECCCHHHHHHH | 15.58 | 25561503 | |
| 252 | Phosphorylation | PIDDRRASDFGLMKI ECCCCCHHHCCCEEE | 31.49 | 25561503 | |
| 267 | Phosphorylation | DDKGRVISFSEKPKG CCCCCEEEEECCCCC | 21.62 | 25561503 | |
| 428 | Phosphorylation | GIRSRVGSNVQLKDT EECCCCCCCCEEECE | 30.85 | 19376835 |
| 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 GLGL1_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLGL1_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 GLGL1_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of GLGL1_ARATH !! | ||||
| 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-428, AND MASSSPECTROMETRY. | |