| UniProt ID | PSBA_ARATH | |
|---|---|---|
| UniProt AC | P83755 | |
| Protein Name | Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379} | |
| Gene Name | psbA {ECO:0000255|HAMAP-Rule:MF_01379} | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 353 | |
| Subcellular Localization |
Plastid, chloroplast thylakoid membrane Multi-pass membrane protein . |
|
| Protein Description | Photosystem II (PSII) is a light-driven water: plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.. | |
| Protein Sequence | MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MTAILERRE ------CCCHHHHHH | 23.54 | 11113141 | |
| 2 | Phosphorylation | ------MTAILERRE ------CCCHHHHHH | 23.54 | 27531888 | |
| 227 | Phosphorylation | TSSLIRETTENESAN HHHHHHHHCCCCCCC | 29.57 | 28295753 | |
| 228 | Phosphorylation | SSLIRETTENESANE HHHHHHHCCCCCCCC | 31.87 | 28295753 | |
| 232 | Phosphorylation | RETTENESANEGYRF HHHCCCCCCCCCCCC | 48.23 | 25561503 | |
| 237 | Nitration | NESANEGYRFGQEEE CCCCCCCCCCCCHHH | 9.15 | - | |
| 262 | Nitration | FGRLIFQYASFNNSR HHHHHHEHHCCCCCC | 8.08 | - |
| 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 PSBA_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSBA_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 PSBA_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ALB3_ARATH | ALB3 | physical | 15988575 | |
| PSBA_ARATH | psbA | physical | 15988575 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Mass spectrometric resolution of reversible protein phosphorylationin photosynthetic membranes of Arabidopsis thaliana."; Vener A.V., Harms A., Sussman M.R., Vierstra R.D.; J. Biol. Chem. 276:6959-6966(2001). Cited for: PROTEIN SEQUENCE OF 2-7, PHOSPHORYLATION AT THR-2, ACETYLATION ATTHR-2, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Mass spectrometric resolution of reversible protein phosphorylationin photosynthetic membranes of Arabidopsis thaliana."; Vener A.V., Harms A., Sussman M.R., Vierstra R.D.; J. Biol. Chem. 276:6959-6966(2001). Cited for: PROTEIN SEQUENCE OF 2-7, PHOSPHORYLATION AT THR-2, ACETYLATION ATTHR-2, AND MASS SPECTROMETRY. | |