dbPTM

STT7_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STT7_ARATH
UniProt AC	Q9S713
Protein Name	Serine/threonine-protein kinase STN7, chloroplastic
Gene Name	STN7
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	562
Subcellular Localization	Plastid, chloroplast thylakoid membrane .
Protein Description	Serine/threonine protein kinase required for state transition by phosphorylating light-harvesting complex II outer antennae (LCHII). State transition plays a central role in response to environmental changes and allows to adjust to changing light conditions via the redistribution of light excitation energy between photosystem II (PSII) and photosystem I (PSI). Phosphorylates the minor light harvesting protein LHCB4.2/CP29 and is involved in the light-dependent phosphorylation of TSP9. Acts as a key component of the long-term response (LTR) signaling pathway. Mediates phosphorylation-dependent PTAC16 subcellular localization to regulate plastid gene expression. [PubMed: 22616989]
Protein Sequence	MATISPGGAYIGTPSPFLGKKLKPFSLTSPILSFKPTVKLNSSCRAQLIDTVHNLFIGVGVGLPCTVMECGDMIYRSTLPKSNGLTITAPGVALALTALSYLWATPGVAPGFFDMFVLAFVERLFRPTFRKDDFVVGKKLGEGSFGVVYKVSLSKKRSNEEGEYVLKKATEYGAVEIWMNERVRRACGNSCADFVYGFLDKSSKKGPEYWLLWKYEGESTLAGLMQSKEFPYNVETIILGKVQDLPKGLERENKIIQTIMRQLLFALDGLHSTGIIHRDVKPQNIIFSEGSRSFKIIDLGAAADLRVGINYIPKEFLLDPRYAAPEQYIMSTQTPSAPSAPVAAALSPVLWQMNLPDRFDIYSIGLIFLQMAFPSLRSDSNLIQFNRQLKRCDYDLTAWRKLVEPRASADLRRGFELVDLDGGIGWELLTSMVRYKARQRISAKAALAHPYFDRQGLLALSVMQNLRMQYFRATQQDYSEAANWVIQLMAKNGTEKDGGFTETQLQELREKEPRKKANAQRNALASALRLQRKLVKTVTETIDEISDGRKTVWWNRWIPREE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
380	Phosphorylation	FPSLRSDSNLIQFNR CCCCCCCCCHHHHHH	34.48	25561503
494	Phosphorylation	QLMAKNGTEKDGGFT HHHHHCCCCCCCCCC	49.62	30291188
526	Phosphorylation	AQRNALASALRLQRK HHHHHHHHHHHHHHH	28.78	30291188
537	Phosphorylation	LQRKLVKTVTETIDE HHHHHHHHHHHHHHH	25.77	30291188
539	Phosphorylation	RKLVKTVTETIDEIS HHHHHHHHHHHHHHC	32.42	23111157
541	Phosphorylation	LVKTVTETIDEISDG HHHHHHHHHHHHCCC	25.10	30291188
546	Phosphorylation	TETIDEISDGRKTVW HHHHHHHCCCCCEEE	31.78	23111157
551	Phosphorylation	EISDGRKTVWWNRWI HHCCCCCEEEEECCC	21.72	30291188

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 STT7_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STT7_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 STT7_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PSAF_ARATH	PSAF	physical	24151498
PSBA_ARATH	psbA	physical	24151498

Drug and Disease Associations

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

Regulatory Network of STT7_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-526; THR-537; THR-539AND THR-541, AND IDENTIFICATION BY MASS SPECTROMETRY.	19376835 [Abstract]