CDKA1_ARATH - dbPTM
CDKA1_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
15PhosphorylationEKIGEGTYGVVYKAR
EECCCCCCEEEEEEE
20.8416856985
159PhosphorylationAFGIPVRTFTHEVVT
HHCCCEEECCCCHHH
32.8723776212
161PhosphorylationGIPVRTFTHEVVTLW
CCCEEECCCCHHHHH
19.2619880383
166PhosphorylationTFTHEVVTLWYRAPE
ECCCCHHHHHHCCCH
19.4223776212
169PhosphorylationHEVVTLWYRAPEILL
CCHHHHHHCCCHHHH
10.4619376835

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseFBL17Q8W104
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
161TPhosphorylation

17369369

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KRP1_ARATHICK1physical
9753775
CKS1_ARATHCKS1physical
17426018
CKS2_ARATHCKS2physical
17426018
PSD2A_ARATHRPN1Aphysical
17426018
PSDE_ARATHAT5G23540physical
17426018
PSD8A_ARATHRPN12aphysical
17426018
CCD21_ARATHCYCD2;1physical
17426018
KRP6_ARATHKRP6physical
17426018
PGMC1_ARATHAT1G23190physical
17426018
PSD2B_ARATHRPN1Bphysical
17426018
CDKE1_ARATHCDKE;1physical
17426018
CCD41_ARATHCYCD4;1physical
17426018
CCD42_ARATHCYCD4;2physical
17426018
KRP4_ARATHKRP4physical
17426018
PP273_ARATHemb1796physical
17426018
CPNA1_ARATHCPN60Aphysical
17426018
VATA_ARATHVHA-Aphysical
17426018
TON1A_ARATHTON1Aphysical
17426018
CCU31_ARATHCYCP1;1physical
15197472
CCU11_ARATHCYCP2;1physical
15197472
CCU22_ARATHCYCP3;2physical
15197472
CCU41_ARATHCYCP4;1physical
15197472
CCU43_ARATHCYCP4;2physical
15197472
CCU42_ARATHCYCP4;3physical
15197472
CCU21_ARATHcycp3;1physical
15197472
KRP1_ARATHICK1physical
10758489
KRP2_ARATHKRP2physical
10758489
KRP5_ARATHICK3physical
10758489
CCD11_ARATHCYCD1;1physical
12857813
CCD41_ARATHCYCD4;1physical
12857813
CKS1_ARATHCKS1physical
9276444
CCD42_ARATHCYCD4;2physical
16408177
HACD_ARATHPAS2physical
16698944
CKS1_ARATHCKS1physical
20407024
KRP4_ARATHKRP4physical
20407024
CCD42_ARATHCYCD4;2physical
20407024
KRP1_ARATHICK1physical
20407024
CCD51_ARATHCYCD5;1physical
20407024
RBR1_ARATHRBR1physical
20407024
WEE1_ARATHWEE1physical
20407024
CCD11_ARATHCYCD1;1physical
20407024
CCD41_ARATHCYCD4;1physical
20407024
KRP6_ARATHKRP6physical
20407024
KRP7_ARATHICK5physical
20407024
KRP3_ARATHICK6physical
20407024
CCB12_ARATHCYC1BATphysical
20407024
CCD33_ARATHCYCD3;3physical
20407024
CCD31_ARATHCYCD3;1physical
20407024
CCD21_ARATHCYCD2;1physical
20407024
CCA23_ARATHCYCA2;3physical
20407024
KRP2_ARATHKRP2physical
20407024
KRP5_ARATHICK3physical
20407024
CDKE1_ARATHCDKE;1physical
20407024
CKS2_ARATHCKS2physical
20407024
CDKA1_ARATHCDC2physical
20407024
CKB11_ARATHCDKB1;1physical
20407024
CKB12_ARATHCDKB1;2physical
20407024
CKB21_ARATHCDKB2;1physical
20407024
CDKD1_ARATHCDKD1;1physical
20407024
CDKD2_ARATHCAK4physical
20407024
CDKD3_ARATHCDKD1;3physical
20407024
CDKF1_ARATHCAK1ATphysical
20407024
CCA11_ARATHCYCA1;1physical
20407024
CCA21_ARATHCYCA2;1physical
20407024
CCA22_ARATHCYC3Bphysical
20407024
CCA24_ARATHCYCA2;4physical
20407024
CCA31_ARATHCYCA3;1physical
20407024
CCA32_ARATHCYCA3;2physical
20407024
CCA34_ARATHCYCA3;4physical
20407024
CCB23_ARATHCYCB2;3physical
20407024
CCB31_ARATHCYCB3;1physical
20407024
CCD32_ARATHCYCD3;2physical
20407024
CCD61_ARATHCYCD6;1physical
20407024
CCH11_ARATHCYCH;1physical
20407024
DPB_ARATHDPBphysical
20407024
E2FA_ARATHE2F3physical
20407024
APC10_ARATHAPC10physical
20706207
CKS2_ARATHCKS2physical
20706207
CCD41_ARATHCYCD4;1physical
20706207
KRP6_ARATHKRP6physical
20706207
IF2B_ARATHEIF2 BETAphysical
20706207
ARAK_ARATHARA1physical
20706207
PGMC1_ARATHAT1G23190physical
20706207
PP273_ARATHemb1796physical
20706207
UGDH2_ARATHAT3G29360physical
20706207
PRS6B_ARATHRPT3physical
20706207
PSD1A_ARATHAT2G32730physical
20706207
PSMD6_ARATHAT4G24820physical
20706207
CFIS2_ARATHAT4G25550physical
20706207
PAP1_ARATHFIBphysical
20706207
RB45A_ARATHRBP45Aphysical
20706207
Y1141_ARATHAT1G11410physical
20706207
VAL1_ARATHHSI2physical
20706207
UGDH1_ARATHUGD1physical
20706207
CKS1_ARATHCKS1physical
22098373
KRP1_ARATHICK1physical
22098373
CCD31_ARATHCYCD3;1physical
22098373
CDT1A_ARATHCDT1Aphysical
22098373
H11_ARATHAT1G06760physical
22098373
CCB12_ARATHCYC1BATphysical
22098373
MT2A_ARATHMT2Aphysical
22098373
GPX2_ARATHGPX2physical
22098373
GSTF2_ARATHGSTF2physical
22098373
MD37E_ARATHHSC70-1physical
22098373
KRP6_ARATHKRP6physical
23617622
EDE1_ARATHEDE1physical
21558460
CKS1_ARATHCKS1physical
25521792
CKS2_ARATHCKS2physical
25521792
CCD41_ARATHCYCD4;1physical
25521792
CCD42_ARATHCYCD4;2physical
25521792
KRP3_ARATHICK6physical
25521792
NSF_ARATHNSFphysical
25521792

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDKA1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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