| UniProt ID | C98A3_ARATH | |
|---|---|---|
| UniProt AC | O22203 | |
| Protein Name | Cytochrome P450 98A3 | |
| Gene Name | CYP98A3 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 508 | |
| Subcellular Localization |
Membrane Single-pass membrane protein . |
|
| Protein Description | Cytochrome P450 which catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. Can use p-coumarate, p-coumaraldehyde, p-coumaroyl methyl ester, 5-O-(4-coumaroyl) D-quinate and 5-O-(4-coumaroyl) shikimate as substrates, but not p-coumaryl alcohol, p-coumaroyl CoA, 1-O-p-coumaroyl-beta-D-glucose, p-hydroxy-cinnamyl alcohol, cinnamate, caffeate or ferulate. Has a weak activity on tri(p-coumaroyl)spermidine, but none on triferuloylspermidine. Hydroxylates preferentially the 5-O-isomer, but can also convert the 4-O- and 3-O-isomers with a lower efficiency. Involved in the biosynthesis of the coumarins scopoletin and scopolin. Essential for the biosynthesis of lignin.. | |
| Protein Sequence | MSWFLIAVATIAAVVSYKLIQRLRYKFPPGPSPKPIVGNLYDIKPVRFRCYYEWAQSYGPIISVWIGSILNVVVSSAELAKEVLKEHDQKLADRHRNRSTEAFSRNGQDLIWADYGPHYVKVRKVCTLELFTPKRLESLRPIREDEVTAMVESVFRDCNLPENRAKGLQLRKYLGAVAFNNITRLAFGKRFMNAEGVVDEQGLEFKAIVSNGLKLGASLSIAEHIPWLRWMFPADEKAFAEHGARRDRLTRAIMEEHTLARQKSSGAKQHFVDALLTLKDQYDLSEDTIIGLLWDMITAGMDTTAITAEWAMAEMIKNPRVQQKVQEEFDRVVGLDRILTEADFSRLPYLQCVVKESFRLHPPTPLMLPHRSNADVKIGGYDIPKGSNVHVNVWAVARDPAVWKNPFEFRPERFLEEDVDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMMSHLLHHFVWTPPQGTKPEEIDMSENPGLVTYMRTPVQAVATPRLPSDLYKRVPYDM | |
| 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 |
|---|---|---|---|---|---|
| 172 | Ubiquitination | AKGLQLRKYLGAVAF HHHHHHHHHHHHHHC | 54.11 | 17272265 | |
| 189 | Ubiquitination | ITRLAFGKRFMNAEG HHHHHHCCCHHCCCC | 35.69 | 17272265 | |
| 486 | Phosphorylation | GLVTYMRTPVQAVAT CCEEEECCCCCCCCC | 15.98 | 24894044 | |
| 501 | Phosphorylation | PRLPSDLYKRVPYDM CCCCHHHHHCCCCCC | 11.18 | 24894044 |
| 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 C98A3_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of C98A3_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 C98A3_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of C98A3_ARATH !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Ubiquitylation | |
| Reference | PubMed |
| "Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants."; Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; Mol. Cell. Proteomics 6:601-610(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-189, AND MASSSPECTROMETRY. | |