UniProt ID | PSAN_ARATH | |
---|---|---|
UniProt AC | P49107 | |
Protein Name | Photosystem I reaction center subunit N, chloroplastic | |
Gene Name | PSAN | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 171 | |
Subcellular Localization |
Plastid, chloroplast thylakoid membrane Peripheral membrane protein Lumenal side. |
|
Protein Description | May function in mediating the binding of the antenna complexes to the PSI reaction center and core antenna. Plays an important role in docking plastocyanin to the PSI complex. Does not bind pigments.. | |
Protein Sequence | MAAMNSSVLTCSYAIAGSGSVELNQKVGLVNSSVGFGQKKQMIMPVIKAQRVVGDDVDGSNGRRSAMVFLAATLFSTAAVSASANAGVIDEYLERSKTNKELNDKKRLATSGANFARAFTVQFGSCKFPENFTGCQDLAKQKKVPFISEDIALECEGKDKYKCGSNVFWKW | |
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 |
---|---|---|---|---|---|
65 | Phosphorylation | DGSNGRRSAMVFLAA CCCCCHHHHHHHHHH | 21.25 | 25368622 | |
73 | Phosphorylation | AMVFLAATLFSTAAV HHHHHHHHHHHHHHH | 23.80 | 25368622 | |
76 | Phosphorylation | FLAATLFSTAAVSAS HHHHHHHHHHHHHHH | 21.90 | 25368622 | |
77 | Phosphorylation | LAATLFSTAAVSASA HHHHHHHHHHHHHHC | 15.99 | 25368622 | |
83 | Phosphorylation | STAAVSASANAGVID HHHHHHHHCCCCHHH | 17.98 | 25368622 | |
87 | Acetylation | VSASANAGVIDEYLE HHHHCCCCHHHHHHH | 19.40 | 18431481 | |
92 | Nitration | NAGVIDEYLERSKTN CCCHHHHHHHHHCCC | 15.32 | - | |
120 | Phosphorylation | ANFARAFTVQFGSCK CCHHHEEEEECCCCC | 16.65 | 19376835 | |
125 | Phosphorylation | AFTVQFGSCKFPENF EEEEECCCCCCCCCC | 18.54 | 19376835 | |
133 | Phosphorylation | CKFPENFTGCQDLAK CCCCCCCCCHHHHHH | 48.94 | 24243849 |
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 PSAN_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSAN_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 PSAN_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PSAN_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Sorting signals, N-terminal modifications and abundance of thechloroplast proteome."; Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,Sun Q., van Wijk K.J.; PLoS ONE 3:E1994-E1994(2008). Cited for: IDENTIFICATION BY MASS SPECTROMETRY, AND ACETYLATION AT GLY-87. |