PKS2_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PKS2_ARATH
• UniProt AC: Q9M9T4
• Protein Name: Protein PHYTOCHROME KINASE SUBSTRATE 2
• Gene Name: PKS2
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 442
• Subcellular Localization: Cell membrane ; Peripheral membrane protein .
• Protein Description: Acts predominantly in the phot1 pathway. Involved in the leaf positioning and also in the phot2 pathway controlling the leaf flattening. Component of the network that modulates the very low-fluence response (VLFR) branch of phyA signaling. Regulates phytochrome-mediated photomorphogenesis and hypocotyl phototropism. May act by controlling auxin homeostasis..
• Protein Sequence: MVTLTSSSSTPNVSFDFMMNNNNNSNNLYGPFSSSSTSFSYLTSKEDALTQKNLMSGITNDVLGINKKASEDLEISVFGAEKYFNGDMDSDHSPRLVSPLPDPEVPIERIFVGPKQSSKNSSETPSLRSESSWNSQSLLLQSKYVEKKKNIKKNSSCNSYFQEKDMSSNHKVSNKKSFLATLGCRCVCSNWSSVDVVDDKRRSSGLKKIKTQLSFSGDLSSEMKIHQQQQEAMLEQRKSLEIFGSPLIEKRIIQKKFPWEYSSSAKKEEHGFSVKYEEEEDGSVSDVSTDLFEIESLTGKANPFLARQGSSDPDSPDGYAPSEVSIQWSVVTASVADFSVMSECATSPVKKNRSFQIPRIPIMAKSNREIAPQRRKSSSSGLLMGCKSHKSVRVSGDSYTSMNRTPSYVPRFPVEANPTSTETRRRISSSSVSHTQSPFLYT

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
93	Phosphorylation	GDMDSDHSPRLVSPL CCCCCCCCCCCCCCC	19.39	29654922
132	Phosphorylation	PSLRSESSWNSQSLL CCCCCCCCCCHHHHH	26.65	25561503
155	Phosphorylation	KKNIKKNSSCNSYFQ HHCCCCCCCCHHHHC	45.18	25561503
156	Phosphorylation	KNIKKNSSCNSYFQE HCCCCCCCCHHHHCH	27.06	25561503
159	Phosphorylation	KKNSSCNSYFQEKDM CCCCCCHHHHCHHCC	31.48	25561503
160	Phosphorylation	KNSSCNSYFQEKDMS CCCCCHHHHCHHCCC	8.69	25561503
211	Phosphorylation	SGLKKIKTQLSFSGD CCHHHHHHCEECCCC	37.91	25561503
214	Phosphorylation	KKIKTQLSFSGDLSS HHHHHCEECCCCCCH	13.93	25561503
216	Phosphorylation	IKTQLSFSGDLSSEM HHHCEECCCCCCHHH	28.20	25561503
220	Phosphorylation	LSFSGDLSSEMKIHQ EECCCCCCHHHHHHH	29.06	22074104
221	Phosphorylation	SFSGDLSSEMKIHQQ ECCCCCCHHHHHHHH	49.35	22074104
239	Phosphorylation	AMLEQRKSLEIFGSP HHHHHHHHHHHHCCC	33.16	30291188
245	Phosphorylation	KSLEIFGSPLIEKRI HHHHHHCCCHHHHHH	13.04	30291188
261	Phosphorylation	QKKFPWEYSSSAKKE HHHCCCCCCCCCCHH	15.24	24894044
262	Phosphorylation	KKFPWEYSSSAKKEE HHCCCCCCCCCCHHH	13.29	25561503
263	Phosphorylation	KFPWEYSSSAKKEEH HCCCCCCCCCCHHHC	33.15	25561503
264	Phosphorylation	FPWEYSSSAKKEEHG CCCCCCCCCCHHHCC	37.86	25561503
354	Phosphorylation	SPVKKNRSFQIPRIP CCCCCCCCCCCCCCC	30.78	30291188
407	Phosphorylation	TSMNRTPSYVPRFPV CCCCCCCCCCCCCCC	37.84	29654922

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PKS2_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PKS2_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PKS2_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of PKS2_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-239; SER-245 ANDSER-354, AND MASS SPECTROMETRY.
PubMed: 19376835