UniProt ID | CP20C_ARATH | |
---|---|---|
UniProt AC | P34791 | |
Protein Name | Peptidyl-prolyl cis-trans isomerase CYP20-3, chloroplastic | |
Gene Name | CYP20-3 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 260 | |
Subcellular Localization | Plastid, chloroplast stroma . Probably associated to membranes. | |
Protein Description | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Required for the light-induced increase of thiol accumulation. Assists the folding or assembly of SAT1 enzyme to form the cysteine synthase complex. Links light and redox signals to the regulation of cysteine biosynthesis in response to stress.. | |
Protein Sequence | MASSSSMQMVHTSRSIAQIGFGVKSQLVSANRTTQSVCFGARSSGIALSSRLHYASPIKQFSGVYATTKHQRTACVKSMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRIYACGELPLDA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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 CP20C_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CP20C_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 CP20C_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SAT1_ARATH | SERAT2;1 | physical | 23671085 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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