dbPTM

CMTA4_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CMTA4_ARATH
UniProt AC	Q9FYG2
Protein Name	Calmodulin-binding transcription activator 4 {ECO:0000303\|PubMed:11925432}
Gene Name	CAMTA4 {ECO:0000303\|PubMed:11925432}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1016
Subcellular Localization	Nucleus .
Protein Description	Transcription activator that binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved together with CAMTA2 and CAMTA3 in the positive regulation of a general stress response. [PubMed: 25039701]
Protein Sequence	MSSVAEDNSFTCDIATIFVAICRNPPANPSDSLFQYEISTLYQEAHSRWLKPPEVLFILQNHESLTLTNTAPQRPTSGSLLLFNKRVLKFFRKDGHQWRRKRDGRAIAEAHERLKVGNAEALNCYYAHGEQDPTFRRRIYWMLDPEYEHIVLVHYRDVSEREEGQQTGGQVYQFAPILSTQNVSYNQYIGDSSDIYQQSSTSPGVAEVNSNLEGSASSSEFGQALKMLKEQLSIGDEHVNSVDPHYIQPESLDSLQFLEYSDIDHLAQPTTVYQRPENNKLERCYGGNFGAQYSAKNDSNKLERCYGGYVGGAEYHSSNLMLVKNGSGPSGGTGGSGDQGSESWKDVLEACEASIPLNSEGSTPSSAKGLLAGLQEDSNWSYSNQVDQSTFLLPQDLGSFQLPASYSALVAPENNGEYCGMMEDGMKIGLPFEQEMRVTGAHNQKFTIQDISPDWGYANETTKVIIIGSFLCDPTESTWSCMFGNAQVPFEIIKEGVIRCEAPQCGPGKVNLCITSGDGLLCSEIREFEYREKPDTCCPKCSEPQTSDMSTSPNELILLVRFVQTLLSDRSSERKSNLESGNDKLLTKLKADDDQWRHVIGTIIDGSASSTSTVDWLLQELLKDKLDTWLSSRSCDEDYITCSLSKQEQGIIHMVAGLGFEWAFYPILAHGVNVDFRDIKGWSALHWAAQFGSEKMVAALIASGASAGAVTDPSRQDPNGKTAASIAASNGHKGLAGYLSEVALTNHLSSLTLEETENSKDTAQVQTEKTLNSISEQSPSGNEDQVSLKDTLAAVRNAAQAAARIQAAFRAHSFRKRKQREAALVACLQEYGMYCEDIEGISAMSKLTFGKGRNYNSAALSIQKNFRGYKDRKCFLELRQKVVKIQAHVRGYQIRKNYKVICWAVRILDKVVLRWRRKGVGLRGFRQDVESTEDSEDEDILKVFRKQKVDVAVNEAFSRVLSMSNSPEARQQYHRVLKRYCQTKAELGKTETLVGEDDDGLFDIADMEYDTLFSLP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
931	Phosphorylation	GFRQDVESTEDSEDE CCCCCCCCCCCCCCH	36.62	23776212
932	Phosphorylation	FRQDVESTEDSEDED CCCCCCCCCCCCCHH	30.24	23776212
935	Phosphorylation	DVESTEDSEDEDILK CCCCCCCCCCHHHHH	40.49	30291188
962	Phosphorylation	EAFSRVLSMSNSPEA HHHHHHHHCCCCHHH	19.80	24808101
964	Phosphorylation	FSRVLSMSNSPEARQ HHHHHHCCCCHHHHH	30.68	25561503
966	Phosphorylation	RVLSMSNSPEARQQY HHHHCCCCHHHHHHH	19.46	25561503

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
Oops, there are no upstream regulatory protein records of CMTA4_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CMTA4_ARATH !!

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 CMTA4_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CMTA4_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CMTA4_ARATH

Related Literatures of Post-Translational Modification

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-962, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-935, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	19245862 [Abstract]
"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 SER-935, AND MASSSPECTROMETRY.	18433157 [Abstract]