dbPTM

KING1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KING1_ARATH
UniProt AC	Q8LBB2
Protein Name	SNF1-related protein kinase regulatory subunit gamma-1
Gene Name	KING1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	424
Subcellular Localization
Protein Description	Regulatory 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..
Protein Sequence	MATVPEIKIMRSESLGHRSDVSSPEAKLGMRVEDLWDEQKPQLSPNEKLNACFESIPVSAFPLSSDSQDIEIRSDTSLAEAVQTLSKFKVLSAPVVDVDAPEDASWIDRYIGIVEFPGIVVWLLHQLEPPSPRSPAVAASNGFSHDFTTDVLDNGDSAVTSGNFFEVLTSSELYKNTKVRDISGTFRWAPFLALQKENSFLTMLLLLSKYKMKSIPVVDLGVAKIENIITQSGVIHMLAECAGLLWFEDWGIKTLSEVGLPIMSKDHIIKIYEDEPVLQAFKLMRRKRIGGIPVIERNSEKPVGNISLRDVQFLLTAPEIYHDYRSITTKNFLVSVREHLEKCGDTSAPIMSGVIACTKNHTLKELILMLDAEKIHRIYVVDDFGNLEGLITLRDIIARLVHEPSGYFGDFFDGVMPLPENYRV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATVPEIKI ------CCCCCCEEE	19.80	-
12	Phosphorylation	PEIKIMRSESLGHRS CCEEEECCHHCCCCC	17.73	23776212
14	Phosphorylation	IKIMRSESLGHRSDV EEEECCHHCCCCCCC	40.68	19880383
19	Phosphorylation	SESLGHRSDVSSPEA CHHCCCCCCCCCHHH	36.37	23776212
22	Phosphorylation	LGHRSDVSSPEAKLG CCCCCCCCCHHHHHC	45.20	23776212
23	Phosphorylation	GHRSDVSSPEAKLGM CCCCCCCCHHHHHCC	26.97	23776212
44	Phosphorylation	DEQKPQLSPNEKLNA HCCCCCCCCCHHHHH	22.04	30291188
74	Phosphorylation	SQDIEIRSDTSLAEA CCCCEECCCCCHHHH	51.40	19880383
76	Phosphorylation	DIEIRSDTSLAEAVQ CCEECCCCCHHHHHH	27.21	20374526
77	Phosphorylation	IEIRSDTSLAEAVQT CEECCCCCHHHHHHH	30.49	19880383
134	Phosphorylation	LEPPSPRSPAVAASN CCCCCCCCCCCHHCC	22.16	23776212
140	Phosphorylation	RSPAVAASNGFSHDF CCCCCHHCCCCCCCC	27.96	23776212
144	Phosphorylation	VAASNGFSHDFTTDV CHHCCCCCCCCCCCC	24.44	23776212
148	Phosphorylation	NGFSHDFTTDVLDNG CCCCCCCCCCCCCCC	28.30	23776212
149	Phosphorylation	GFSHDFTTDVLDNGD CCCCCCCCCCCCCCC	24.89	23776212
157	Phosphorylation	DVLDNGDSAVTSGNF CCCCCCCCCCCCCCC	26.49	23776212
160	Phosphorylation	DNGDSAVTSGNFFEV CCCCCCCCCCCCEEE	30.54	23776212
161	Phosphorylation	NGDSAVTSGNFFEVL CCCCCCCCCCCEEEE	25.74	23776212
169	Phosphorylation	GNFFEVLTSSELYKN CCCEEEEECHHHHHC	35.07	23776212
170	Phosphorylation	NFFEVLTSSELYKNT CCEEEEECHHHHHCC	20.04	23776212
171	Phosphorylation	FFEVLTSSELYKNTK CEEEEECHHHHHCCC	26.78	23776212
174	Phosphorylation	VLTSSELYKNTKVRD EEECHHHHHCCCCEE	9.72	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
Oops, there are no upstream regulatory protein records of KING1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KING1_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 KING1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
KINB1_ARATH	AKINBETA1	physical	10417704
KINB2_ARATH	AT4G16360	physical	10417704

Drug and Disease Associations

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

Regulatory Network of KING1_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-12; SER-14; SER-22;SER-23 AND SER-44, AND MASS SPECTROMETRY.	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-44, AND MASSSPECTROMETRY.	19245862 [Abstract]