| UniProt ID | ACCA_ARATH | |
|---|---|---|
| UniProt AC | Q9LD43 | |
| Protein Name | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic | |
| Gene Name | CAC3 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 769 | |
| Subcellular Localization |
Plastid, chloroplast inner membrane Peripheral membrane protein Stromal side . |
|
| Protein Description | Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity).. | |
| Protein Sequence | MASISHSSLALGGASSASASDYLRSSSNGVNGVPLKTLGRAVFTTIRRKDLAVTSRLKKGKKFEHPWPANPDPNVKGGVLSYLAEFKPLGDTQKPVTLDFEKPLVELEKKIVDVRKMANETGLDFTEQIITLENKYRQALKDLYTHLTPIQRVNIARHPNRPTFLDHIHNITDKFMELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIANNLRTMFGLKVPILSIVIGEGGSGGALAIGCANKMLMLENAVFYVASPEACAAILWKTSKAAPEAAEKLRITSKELVKLNVADGIIPEPLGGAHADPSWTSQQIKIAINENMNEFGKMSGEELLKHRMAKYRKIGVFIEGEPIEPSRKINMKKREAVFSDSRKLQGEVDKLKEQILKAKETSTEAEPSSEVLNEMIEKLKSEIDDEYTEAAIAVGLEERLTAMREEFSKASSEEHLMHPVLIEKIEKLKEEFNTRLTDAPNYESLKSKLNMLRDFSRAKAASEATSLKKEINKRFQEAVDRPEIREKVEAIKAEVASSGASSFDELPDALKEKVLKTKGEVEAEMAGVLKSMGLELDAVKQNQKDTAEQIYAANENLQEKLEKLNQEITSKIEEVVRTPEIKSMVELLKVETAKASKTPGVTEAYQKIEALEQQIKQKIAEALNTSGLQEKQDELEKELAAARELAAEESDGSVKEDDDDDEDSSESGKSEMVNPSFA | |
| 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 |
|---|---|---|---|---|---|
| 383 | Sulfoxidation | KIAINENMNEFGKMS HHHHHCCHHHHHCCC | 4.08 | 23289948 | |
| 623 | Sulfoxidation | MAGVLKSMGLELDAV HHHHHHHCCCCHHHH | 7.30 | 25693801 | |
| 675 | Sulfoxidation | RTPEIKSMVELLKVE CCHHHHHHHHHHHHH | 2.00 | 25693801 | |
| 741 | Phosphorylation | RELAAEESDGSVKED HHHHHHHCCCCCCCC | 38.48 | 24601666 | |
| 744 | Phosphorylation | AAEESDGSVKEDDDD HHHHCCCCCCCCCCC | 34.70 | 24601666 | |
| 755 | Phosphorylation | DDDDDEDSSESGKSE CCCCCCCCCCCCCCC | 33.68 | 23776212 | |
| 756 | Phosphorylation | DDDDEDSSESGKSEM CCCCCCCCCCCCCCC | 48.37 | 23776212 | |
| 758 | Phosphorylation | DDEDSSESGKSEMVN CCCCCCCCCCCCCCC | 54.17 | 23776212 | |
| 761 | Phosphorylation | DSSESGKSEMVNPSF CCCCCCCCCCCCCCC | 34.15 | 23776212 | |
| 767 | Phosphorylation | KSEMVNPSFA----- CCCCCCCCCC----- | 28.71 | 23776212 |
| 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 ACCA_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACCA_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 ACCA_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ACCA_ARATH !! | ||||
| 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-741, AND MASSSPECTROMETRY. | |
