UniProt ID | CDKA1_ARATH | |
---|---|---|
UniProt AC | P24100 | |
Protein Name | Cyclin-dependent kinase A-1 | |
Gene Name | CDKA-1 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 294 | |
Subcellular Localization | Cytoplasm. Nucleus. Mainly cytoplasmic. Nuclear distribution increases after binding to ICK1/KRP1. | |
Protein Description | Involved in the control of the cell cycle. Essential for both G1/S and G2/M (mitosis) phase transitions. Functions in cell morphogenesis as well as cell proliferation. Required for cell division (entry into mitosis) of the generative cell in male gametogenesis. Required to trigger guard mother cells (GMC) symmetric divisions at the late stage of stomatal development, probably via the regulation of G1 to S transition in the cell cycle. Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division when in the presence of CYCD3-2. [PubMed: 24687979] | |
Protein Sequence | MDQYEKVEKIGEGTYGVVYKARDKVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHSNIVKLQDVVHSEKRLYLVFEYLDLDLKKHMDSTPDFSKDLHMIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNSLKLADFGLARAFGIPVRTFTHEVVTLWYRAPEILLGSHHYSTPVDIWSVGCIFAEMISQKPLFPGDSEIDQLFKIFRIMGTPYEDTWRGVTSLPDYKSAFPKWKPTDLETFVPNLDPDGVDLLSKMLLMDPTKRINARAALEHEYFKDLGGMP | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | EKIGEGTYGVVYKAR EECCCCCCEEEEEEE | 20.84 | 16856985 | |
159 | Phosphorylation | AFGIPVRTFTHEVVT HHCCCEEECCCCHHH | 32.87 | 23776212 | |
161 | Phosphorylation | GIPVRTFTHEVVTLW CCCEEECCCCHHHHH | 19.26 | 19880383 | |
166 | Phosphorylation | TFTHEVVTLWYRAPE ECCCCHHHHHHCCCH | 19.42 | 23776212 | |
169 | Phosphorylation | HEVVTLWYRAPEILL CCHHHHHHCCCHHHH | 10.46 | 19376835 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
161 | T | Phosphorylation |
| 17369369 |
* 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 CDKA1_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY. | |
"T-loop phosphorylation of Arabidopsis CDKA;1 is required for itsfunction and can be partially substituted by an aspartate residue."; Dissmeyer N., Nowack M.K., Pusch S., Stals H., Inze D., Grini P.E.,Schnittger A.; Plant Cell 19:972-985(2007). Cited for: FUNCTION, PHOSPHORYLATION AT THR-161, AND MUTAGENESIS OF THR-161. |