CCA1_ARATH - dbPTM
CCA1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CCA1_ARATH
UniProt AC P92973
Protein Name Protein CCA1 {ECO:0000303|PubMed:9144958}
Gene Name CCA1 {ECO:0000303|PubMed:9144958}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 608
Subcellular Localization Nucleus . Moves into the nucleus very soo after translation. This translocation is unaffected by light and dark.
Protein Description Transcription factor involved in the circadian clock and in the phytochrome regulation. Binds to the promoter regions of APRR1/TOC1 and TCP21/CHE to repress their transcription. Binds to the promoter regions of CAB2A and CAB2B to promote their transcription. Represses both LHY and itself..
Protein Sequence METNSSGEDLVIKTRKPYTITKQRERWTEEEHNRFIEALRLYGRAWQKIEEHVATKTAVQIRSHAQKFFSKVEKEAEAKGVAMGQALDIAIPPPRPKRKPNNPYPRKTGSGTILMSKTGVNDGKESLGSEKVSHPEMANEDRQQSKPEEKTLQEDNCSDCFTHQYLSAASSMNKSCIETSNASTFREFLPSREEGSQNNRVRKESNSDLNAKSLENGNEQGPQTYPMHIPVLVPLGSSITSSLSHPPSEPDSHPHTVAGDYQSFPNHIMSTLLQTPALYTAATFASSFWPPDSSGGSPVPGNSPPNLAAMAAATVAAASAWWAANGLLPLCAPLSSGGFTSHPPSTFGPSCDVEYTKASTLQHGSVQSREQEHSEASKARSSLDSEDVENKSKPVCHEQPSATPESDAKGSDGAGDRKQVDRSSCGSNTPSSSDDVEADASERQEDGTNGEVKETNEDTNKPQTSESNARRSRISSNITDPWKSVSDEGRIAFQALFSREVLPQSFTYREEHREEEQQQQEQRYPMALDLNFTAQLTPVDDQEEKRNTGFLGIGLDASKLMSRGRTGFKPYKRCSMEAKESRILNNNPIIHVEQKDPKRMRLETQAST
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
5Phosphorylation---METNSSGEDLVI
---CCCCCCCCCEEE
47.3314978263
6Phosphorylation--METNSSGEDLVIK
--CCCCCCCCCEEEE
48.5514593172
562PhosphorylationLDASKLMSRGRTGFK
CCHHHHHHCCCCCCC
41.8622074104
566PhosphorylationKLMSRGRTGFKPYKR
HHHHCCCCCCCCCCC
50.2022074104

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
5SPhosphorylationKinaseCK2-FAMILY-GPS
5SPhosphorylationKinaseCK2-Uniprot
6SPhosphorylationKinaseCK2-FAMILY-GPS
6SPhosphorylationKinaseCK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
5SPhosphorylation

14978263
6SPhosphorylation

14978263
431SPhosphorylation

14978263
432SPhosphorylation

14978263
433SPhosphorylation

14978263
484SPhosphorylation

14978263

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 CCA1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK2D_ARATHCKB3physical
9724822
CSK2C_ARATHCKB2physical
9724822
CSK2B_ARATHCKB1physical
9724822
CSK21_ARATHCKA1physical
9724822
LHY_ARATHLHYgenetic
17483414
APRR1_ARATHTOC1genetic
17483414
CSK2D_ARATHCKB3physical
10535927
LHY_ARATHLHYgenetic
17540692
APRR1_ARATHTOC1genetic
17540692
LHY_ARATHLHYgenetic
17519251
APRR1_ARATHTOC1genetic
17519251
LHY_ARATHLHYgenetic
17504813
TIC_ARATHTICgenetic
17496120
CCA1_ARATHCCA1physical
14978263
TCP2_ARATHTCP2physical
21183706
TCP11_ARATHAT2G37000physical
21183706
DET1_ARATHDET1physical
21884973
CCA1_ARATHCCA1physical
22715042
LHY_ARATHLHYphysical
22715042
CCA1_ARATHCCA1physical
19218364
LHY_ARATHLHYgenetic
19218364
LHY_ARATHLHYphysical
19218364

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CCA1_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"CK2 phosphorylation of CCA1 is necessary for its circadian oscillatorfunction in Arabidopsis.";
Daniel X., Sugano S., Tobin E.M.;
Proc. Natl. Acad. Sci. U.S.A. 101:3292-3297(2004).
Cited for: INTERACTION WITH CKB3, MUTAGENESIS OF SER-5; SER-6; SER-431; SER-432;SER-433 AND SER-484, AND PHOSPHORYLATION AT SER-5 AND SER-6.

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