UniProt ID | MLO2_ARATH | |
---|---|---|
UniProt AC | Q9SXB6 | |
Protein Name | MLO-like protein 2 | |
Gene Name | MLO2 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 573 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. |
|
Protein Description | May be involved in modulation of pathogen defense and leaf cell death. Activity seems to be regulated by Ca(2+)-dependent calmodulin binding and seems not to require heterotrimeric G proteins (By similarity).. | |
Protein Sequence | MADQVKERTLEETSTWAVAVVCFVLLFISIVLEHSIHKIGTWFKKKHKQALFEALEKVKAELMLLGFISLLLTIGQTPISNICISQKVASTMHPCSAAEEAKKYGKKDAGKKDDGDGDKPGRRLLLELAESYIHRRSLATKGYDKCAEKGKVAFVSAYGIHQLHIFIFVLAVVHVVYCIVTYAFGKIKMRTWKSWEEETKTIEYQYSNDPERFRFARDTSFGRRHLNFWSKTRVTLWIVCFFRQFFGSVTKVDYLALRHGFIMAHFAPGNESRFDFRKYIQRSLEKDFKTVVEISPVIWFVAVLFLLTNSYGLRSYLWLPFIPLVVILIVGTKLEVIITKLGLRIQEKGDVVRGAPVVQPGDDLFWFGKPRFILFLIHLVLFTNAFQLAFFAWSTYEFNLNNCFHESTADVVIRLVVGAVVQILCSYVTLPLYALVTQMGSKMKPTVFNDRVATALKKWHHTAKNETKHGRHSGSNTPFSSRPTTPTHGSSPIHLLHNFNNRSVENYPSSPSPRYSGHGHHEHQFWDPESQHQEAETSTHHSLAHESSEPVLASVELPPIRTSKSLRDFSFKK | |
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 |
---|---|---|---|---|---|
207 | Phosphorylation | KTIEYQYSNDPERFR CEEEEECCCCHHHHH | 21.16 | 30407730 | |
473 | Phosphorylation | ETKHGRHSGSNTPFS CCCCCCCCCCCCCCC | 42.42 | 29654922 | |
475 | Phosphorylation | KHGRHSGSNTPFSSR CCCCCCCCCCCCCCC | 40.31 | 25561503 | |
477 | Phosphorylation | GRHSGSNTPFSSRPT CCCCCCCCCCCCCCC | 27.66 | 29654922 | |
503 | Phosphorylation | LHNFNNRSVENYPSS EECCCCCCCCCCCCC | 35.59 | 23776212 | |
507 | Phosphorylation | NNRSVENYPSSPSPR CCCCCCCCCCCCCCC | 7.32 | 23776212 | |
509 | Phosphorylation | RSVENYPSSPSPRYS CCCCCCCCCCCCCCC | 44.51 | 23776212 | |
510 | Phosphorylation | SVENYPSSPSPRYSG CCCCCCCCCCCCCCC | 25.54 | 27532006 | |
512 | Phosphorylation | ENYPSSPSPRYSGHG CCCCCCCCCCCCCCC | 24.77 | 30291188 | |
565 | Phosphorylation | PPIRTSKSLRDFSFK CCCCCCCCHHCCCCC | 28.53 | 25561503 | |
570 | Phosphorylation | SKSLRDFSFKK---- CCCHHCCCCCC---- | 40.21 | 23111157 |
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 MLO2_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MLO2_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 MLO2_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
GCR1_ARATH | GCR1 | physical | 21423366 |
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-509; SER-510 ANDSER-512, AND MASS SPECTROMETRY. |