UniProt ID | GPA1_ARATH | |
---|---|---|
UniProt AC | P18064 | |
Protein Name | Guanine nucleotide-binding protein alpha-1 subunit {ECO:0000303|PubMed:2111018} | |
Gene Name | GPA1 {ECO:0000303|PubMed:2111018} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 383 | |
Subcellular Localization | Cell membrane . | |
Protein Description | Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate (IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. But, together with GCR1 and GB1, acts as a negative regulator of ABA during seed germination and early seedling development. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1.. | |
Protein Sequence | MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKLVKKTFKLVDETLRRRNLLEAGLL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | N-myristoyl glycine | ------MGLLCSRSR ------CCCCCCCCC | 27.62 | - | |
2 | Myristoylation | ------MGLLCSRSR ------CCCCCCCCC | 27.62 | 12912986 | |
5 | S-palmitoylation | ---MGLLCSRSRHHT ---CCCCCCCCCCCC | 3.69 | 17158913 | |
12 | Phosphorylation | CSRSRHHTEDTDENT CCCCCCCCCCCCCHH | 29.45 | 19880383 | |
15 | Phosphorylation | SRHHTEDTDENTQAA CCCCCCCCCCHHHHH | 38.69 | 19880383 | |
19 | Phosphorylation | TEDTDENTQAAEIER CCCCCCHHHHHHHHH | 19.96 | 20374526 | |
49 | Phosphorylation | LLLGAGESGKSTIFK HHHCCCCCCCCHHHH | 51.07 | 19880383 | |
166 | Phosphorylation | QVPDCTKYLMENLKR CCCHHHHHHHHHHHH | 7.98 | 20374526 |
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 GPA1_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GPA1_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 GPA1_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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