KIN11_ARATH - dbPTM
KIN11_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIN11_ARATH
UniProt AC P92958
Protein Name SNF1-related protein kinase catalytic subunit alpha KIN11
Gene Name KIN11
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 512
Subcellular Localization
Protein Description Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase. In vitro, KIN11 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination. Involved in innate antiviral defenses..
Protein Sequence MDHSSNRFGNNGVESILPNYKLGKTLGIGSFGKVKIAEHVVTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRQYEVIETTSDIYVVMEYVKSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSRCNIKIADFGLSNVMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSSEARDLIPRMLIVDPVKRITIPEIRQHRWFQTHLPRYLAVSPPDTVEQAKKINEEIVQEVVNMGFDRNQVLESLRNRTQNDATVTYYLLLDNRFRVPSGYLESEFQETTDSGSNPMRTPEAGASPVGHWIPAHVDHYGLGARSQVPVDRKWALGLQSHAHPREIMNEVLKALQELNVCWKKIGHYNMKCRWVPGLADGQNTMVNNQLHFRDESSIIEDDCAMTSPTVIKFELQLYKAREEKYLLDIQRVNGPQFLFLDLCAAFLTELRVI
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
165PhosphorylationKIADFGLSNVMRDGH
EEECCCHHHHCCCCC
27.97-
176PhosphorylationRDGHFLKTSCGSPNY
CCCCEEECCCCCCCC
31.2530291188
177PhosphorylationDGHFLKTSCGSPNYA
CCCEEECCCCCCCCC
18.2027532006
180PhosphorylationFLKTSCGSPNYAAPE
EEECCCCCCCCCCCH
17.8224601666
183PhosphorylationTSCGSPNYAAPEVIS
CCCCCCCCCCCHHHC
13.9223776212
190PhosphorylationYAAPEVISGKLYAGP
CCCCHHHCCCCCCCC
34.7419880383
360PhosphorylationSGSNPMRTPEAGASP
CCCCCCCCCCCCCCC
21.1627643528
366PhosphorylationRTPEAGASPVGHWIP
CCCCCCCCCCCCCCC
21.1427643528

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
176TPhosphorylationKinaseGRIK1Q93V58
Uniprot
176TPhosphorylationKinaseGRIK2Q5HZ38
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
176TPhosphorylation

19339507
176TPhosphorylation

19339507

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 KIN11_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DSP4_ARATHSEX4physical
12148529
SNF4_ARATHSNF4physical
17028154
KINB2_ARATHAT4G16360physical
11522840
SNF4_ARATHSNF4physical
10929106
KINB1_ARATHAKINBETA1physical
10417704
KINB2_ARATHAT4G16360physical
10417704
KING1_ARATHKING1physical
10417704
PRL1_ARATHPRL1physical
10220464
AAKG_YEASTSNF4physical
10220464
PSA7A_ARATHPAD1physical
11387208
SKP1A_ARATHSKP1physical
11387208
TOE2_ARATHTOE2physical
21798944
CDKF1_ARATHCAK1ATphysical
21798944
TCP19_ARATHAT5G51910physical
21798944
GDU2_ARATHGDU2physical
22737156
PTR2_ARATHPTR2physical
22737156
CNG13_ARATHCNGC13physical
22737156
CAAT6_ARATHCAT6physical
22737156
GDU4_ARATHGDU4physical
22737156
CNG18_ARATHCNGC18physical
22737156
DNJ21_ARATHATERDJ2Aphysical
22737156
ERDL4_ARATHAT1G19450physical
22737156
Y5410_ARATHAT5G24100physical
21423366
Y2899_ARATHAT2G28990physical
21423366
IDD8_ARATHNUCphysical
25929516
SNF4_ARATHSNF4physical
8617787

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIN11_ARATH

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Related Literatures of Post-Translational Modification

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