dbPTM

KIN10_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KIN10_ARATH
UniProt AC	Q38997
Protein Name	SNF1-related protein kinase catalytic subunit alpha KIN10
Gene Name	KIN10
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	535
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, KIN10 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. Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro..
Protein Sequence	MFKRVDEFNLVSSTIDHRIFKSRMDGSGTGSRSGVESILPNYKLGRTLGIGSFGRVKIAEHALTGHKVAIKILNRRKIKNMEMEEKVRREIKILRLFMHPHIIRLYEVIETPTDIYLVMEYVNSGELFDYIVEKGRLQEDEARNFFQQIISGVEYCHRNMVVHRDLKPENLLLDSKCNVKIADFGLSNIMRDGHFLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGTLPFDDENIPNLFKKIKGGIYTLPSHLSPGARDLIPRMLVVDPMKRVTIPEIRQHPWFQAHLPRYLAVPPPDTVQQAKKIDEEILQEVINMGFDRNHLIESLRNRTQNDGTVTYYLILDNRFRASSGYLGAEFQETMEGTPRMHPAESVASPVSHRLPGLMEYQGVGLRSQYPVERKWALGLQSRAHPREIMTEVLKALQDLNVCWKKIGHYNMKCRWVPNSSADGMLSNSMHDNNYFGDESSIIENEAAVKSPNVVKFEIQLYKTRDDKYLLDLQRVQGPQFLFLDLCAAFLAQLRVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
43	Ubiquitination	ESILPNYKLGRTLGI HHHCCCCCCCCEECC	51.62	17272265
164	Phosphorylation	HRNMVVHRDLKPENL HHCCEECCCCCHHHE	39.07	-
175	Phosphorylation	PENLLLDSKCNVKIA HHHEEECCCCCEEEE	38.79	19302419
187	Phosphorylation	KIADFGLSNIMRDGH EEEHHCHHHHHCCCC	25.37	-
198	Phosphorylation	RDGHFLKTSCGSPNY CCCCEEECCCCCCCC	31.25	30291188
199	Phosphorylation	DGHFLKTSCGSPNYA CCCEEECCCCCCCCC	18.20	27532006
202	Phosphorylation	FLKTSCGSPNYAAPE EEECCCCCCCCCCCH	17.82	24601666
205	Phosphorylation	TSCGSPNYAAPEVIS CCCCCCCCCCCHHHC	13.92	23776212
212	Phosphorylation	YAAPEVISGKLYAGP CCCCHHHCCCCCCCC	34.74	19880383
364	Phosphorylation	RFRASSGYLGAEFQE CCCCCCCCCCHHHHH	12.15	26471895
384	Phosphorylation	PRMHPAESVASPVSH CCCCCCHHCCCCHHH	25.70	23776212
387	Phosphorylation	HPAESVASPVSHRLP CCCHHCCCCHHHCCC	24.55	19880383
390	Phosphorylation	ESVASPVSHRLPGLM HHCCCCHHHCCCCCC	13.28	23776212

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
175	T	Phosphorylation	Kinase	GRIK1	Q93V58	Uniprot
175	T	Phosphorylation	Kinase	GRIK2	Q5HZ38	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	PRL1	Q42384	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
175	T	Phosphorylation	17671505
Dephosphorylated at Thr-175 by ABI1 and PP2CA.
175	T	Phosphorylation	17671505
Phosphorylated at Thr-175 in response to glucose.
175	T	Phosphorylation	17671505
Phosphorylated at Thr-175 under submergence.

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 KIN10_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNF4_ARATH	SNF4	physical	17028154
KINB2_ARATH	AT4G16360	physical	11522840
SNF4_ARATH	SNF4	physical	10929106
PRL1_ARATH	PRL1	physical	10220464
AAKG_YEAST	SNF4	physical	10220464
PSA7A_ARATH	PAD1	physical	11387208
SKP1A_ARATH	SKP1	physical	11387208
FUS3_ARATH	FUS3	physical	22026387
P2C74_ARATH	AT5G36250	physical	22449965
CDPK1_ARATH	CPK1	physical	22737156
GDU2_ARATH	GDU2	physical	22737156
PLST4_ARATH	PGLCT	physical	22737156
CNG13_ARATH	CNGC13	physical	22737156
KRP6_ARATH	KRP6	physical	23617622
KRP7_ARATH	ICK5	physical	23617622
P2C56_ARATH	ABI1	physical	24179127
P2C37_ARATH	PP2CA	physical	24179127
AI5L5_ARATH	ABF2	physical	24179127
KIN10_ARATH	KIN10	physical	24179127
SUMO3_ARATH	SUMO3	physical	20855607
SUMO1_ARATH	SUMO1	physical	20855607
KINB1_ARATH	AKINBETA1	physical	23551663
MYC2_ARATH	MYC2	physical	24890857
KAD1_ARATH	ADK	physical	24498147
KIN10_ARATH	KIN10	physical	24498147
IDD8_ARATH	NUC	physical	25929516
KIN10_ARATH	KIN10	physical	19339507

Drug and Disease Associations

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

Regulatory Network of KIN10_ARATH

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants."; Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; Mol. Cell. Proteomics 6:601-610(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-43, AND MASSSPECTROMETRY.	17272265 [Abstract]

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