CNBL2_ARATH - dbPTM
CNBL2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNBL2_ARATH
UniProt AC Q8LAS7
Protein Name Calcineurin B-like protein 2
Gene Name CBL2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 226
Subcellular Localization Vacuole membrane
Lipid-anchor . The tonoplast localization is S-acylation dependent and is abolished by 2-bromopalmitate (2-BP) treatment.
Protein Description Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Binds four calcium ions per subunit. Mediates the activation of AKT1 by CIPK proteins (CIPK6, CIPK16, and CIPK23) in response to low potassium conditions and in the context of stomatal movement. Mediates the inactivation of the proton pump AHA2 by CIPK11. Probably involved in regulating signaling responses to abscisic acid..
Protein Sequence MSQCVDGIKHLCTSVLGCFDLDLYKQSGGLGDPELLARDTVFSVSEIEALYELFKKISSAVIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPIDDKIHFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLKDTVIEDIIDKTFEEADTKHDGKIDKEEWRSLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVEDT
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
4S-palmitoylation----MSQCVDGIKHL
----CCCHHHHHHHH
2.0622547024
12S-palmitoylationVDGIKHLCTSVLGCF
HHHHHHHHHHHHHCC
2.3922547024
18S-palmitoylationLCTSVLGCFDLDLYK
HHHHHHHCCCHHHHH
1.7822547024
51PhosphorylationVSEIEALYELFKKIS
HHHHHHHHHHHHHHH
20.0319880383
212PhosphorylationQYLKDITTTFPSFVF
HHHHHHHHHCCHHHC
27.1230407730
213PhosphorylationYLKDITTTFPSFVFH
HHHHHHHHCCHHHCC
25.5430407730
216PhosphorylationDITTTFPSFVFHSQV
HHHHHCCHHHCCCCC
29.8322547024
221PhosphorylationFPSFVFHSQVEDT--
CCHHHCCCCCCCC--
25.1830407730
226PhosphorylationFHSQVEDT-------
CCCCCCCC-------
27.3130407730

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
216SPhosphorylationKinaseCIPK11O22932
Uniprot
216SPhosphorylationKinaseCIPK14Q9LZW4
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNBL2_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 CNBL2_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CIPKB_ARATHSIP4physical
17483306
CIPKB_ARATHSIP4physical
11402167
CIPK9_ARATHCIPK9physical
11402167
CIPKO_ARATHSOS2physical
11402167
CIPK1_ARATHCIPK1physical
11230129
CIPKD_ARATHCIPK13physical
11230129
CIPKE_ARATHSR1physical
11230129
CIPKD_ARATHCIPK13physical
14730130
CIPKI_ARATHCIPK18physical
14730130
CIPK7_ARATHCIPK7physical
14730130
CIPKE_ARATHSR1physical
14730130
CIPKE_ARATHSR1physical
19832944
CIPKO_ARATHSOS2physical
19832944
CIPKL_ARATHCIPK21physical
21798944
CIPKA_ARATHSIP1physical
21798944
CIPKE_ARATHSR1physical
18237745
CIPK9_ARATHCIPK9physical
23109687
CIPK3_ARATHCIPK3physical
25646412
CIPK9_ARATHCIPK9physical
25646412
CIPKN_ARATHCIPK23physical
25646412
CIPKQ_ARATHAT5G21326physical
25646412
CIPKE_ARATHSR1physical
24521877
MTN1_ARATHMTN1physical
26259190
CIPKL_ARATHCIPK21physical
26198257

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNBL2_ARATH

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Related Literatures of Post-Translational Modification

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