CIPKN_ARATH - dbPTM
CIPKN_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CIPKN_ARATH
UniProt AC Q93VD3
Protein Name CBL-interacting serine/threonine-protein kinase 23
Gene Name CIPK23
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 482
Subcellular Localization Cell membrane
Peripheral membrane protein . Associated to the plasma membrane when associated with AKT1, CBL1 and CBL9.
Protein Description CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein leads to activation of the kinase in a calcium-dependent manner. Downstream of CBL1, CBL2, CBL3 and CBL9, regulates by phosphorylation the K(+) conductance and uptake of AKT1 in low K(+) condition, in response to calcium signaling and during the stomatal opening regulation by monitoring the turgor pressure in guard cells. In response to low nitrate concentration, phosphorylates NRT1.1, switching it from a low-affinity nitrate transporter to a high-affinity transporter. Confers tolerance to low potassium conditions. Involved in drought sensitivity and leaf transpiration..
Protein Sequence MASRTTPSRSTPSRSTPSGSSSGGRTRVGKYELGRTLGEGTFAKVKFARNVENGDNVAIKVIDKEKVLKNKMIAQIKREISTMKLIKHPNVIRMFEVMASKTKIYFVLEFVTGGELFDKISSNGRLKEDEARKYFQQLINAVDYCHSRGVYHRDLKPENLLLDANGALKVSDFGLSALPQQVREDGLLHTTCGTPNYVAPEVINNKGYDGAKADLWSCGVILFVLMAGYLPFEDSNLTSLYKKIFKAEFTCPPWFSASAKKLIKRILDPNPATRITFAEVIENEWFKKGYKAPKFENADVSLDDVDAIFDDSGESKNLVVERREEGLKTPVTMNAFELISTSQGLNLGSLFEKQMGLVKRKTRFTSKSSANEIVTKIEAAAAPMGFDVKTNNYKMKLTGEKSGRKGQLAVATEVFQVAPSLYMVEMRKSGGDTLEFHKFYKNLTTGLKDIVWKTIDEEKEEGTDGGGTNGAMANRTIAKQST
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
26PhosphorylationGSSSGGRTRVGKYEL
CCCCCCCCEEEEEEC
32.7424894044
41PhosphorylationGRTLGEGTFAKVKFA
CCCCCCCCEEEEEEE
19.0019880383
176PhosphorylationKVSDFGLSALPQQVR
EHHHCCCCCCCHHHH
28.30-
190PhosphorylationREDGLLHTTCGTPNY
HHCCCEECCCCCCCC
24.6119880383
191PhosphorylationEDGLLHTTCGTPNYV
HCCCEECCCCCCCCC
9.7419880383
194PhosphorylationLLHTTCGTPNYVAPE
CEECCCCCCCCCCHH
15.5423572148
433PhosphorylationMRKSGGDTLEFHKFY
EHHHCCCCEEHHHHH
31.3125561503

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 CIPKN_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CIPKN_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 CIPKN_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AKT1_ARATHKT1physical
16895985
AKT1_ARATHKT1physical
16814720
CNBL9_ARATHCBL9physical
16814720
CNBL1_ARATHCBL1physical
16814720
PTR7_ARATHNRT1.1physical
19766570
CNBL1_ARATHCBL1physical
21685179
CNBL9_ARATHCBL9physical
21685179
CNBL1_ARATHCBL1physical
21798944
CNBL9_ARATHCBL9physical
21798944
CNBL1_ARATHCBL1physical
22253446
ACT1_ARATHACT1physical
22253446
ACT3_ARATHACT1physical
22253446
AKT1_ARATHKT1physical
19509299
AKT1_ARATHKT1physical
17898163
CNBL1_ARATHCBL1physical
17898163
CNBL2_ARATHCBL2physical
17898163
CNBL3_ARATHCBL3physical
17898163
CNBL9_ARATHCBL9physical
17898163
P2C77_ARATHABI2physical
25943353
CNBL1_ARATHCBL1physical
25943353
CIPKN_ARATHCIPK23physical
25943353

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

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Related Literatures of Post-Translational Modification

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