PCAP1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PCAP1_ARATH
• UniProt AC: Q96262
• Protein Name: Plasma membrane-associated cation-binding protein 1
• Gene Name: PCAP1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 225
• Subcellular Localization: Cell membrane ; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, plasmodesma. Shuttles from plasma membrane to cytoplasm (e.g. colocalizes with cortical microtubules) upon calcium levels increase. Co-localizes with Turnip mosaic virus
• Protein Description: May be involved in intracellular signaling through interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs attached to the plasma membrane until Ca(2+)-CaM reaches a competitive concentration subsequent to an increase triggered by a stimulus, thus leading to PtdInsPs release and subsequent activation of InsPs-dependent signaling cascade. Interacts competitively at the N-terminus with calcium ions and CaM (in a calcium-dependent manner), and with the phosphatidylinositol phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(4,5)P(2) and PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P, PtdIns(4)P and PtdIns(5)P. Negative regulator of hypocotyl cell elongation by destabilizing cortical microtubules in a calcium-dependent manner. Binds directly to and destabilized microtubules to enhance microtubule depolymerization when cytoplasmic calcium increases. In case of Turnip mosaic virus (TuMV) infection, confers sensitivity by promoting viral cell-to-cell movement through interaction with viral P3N-PIPO..
• Protein Sequence: MGYWNSKVVPKFKKLFEKNSAKKAAAAEATKTFDESKETINKEIEEKKTELQPKVVETYEATSAEVKALVRDPKVAGLKKNSAAVQKYLEELVKIEFPGSKAVSEASSSFGAGYVAGPVTFIFEKVSVFLPEEVKTKEIPVEEVKAEEPAKTEEPAKTEGTSGEKEEIVEETKKGETPETAVVEEKKPEVEEKKEEATPAPAVVETPVKEPETTTTAPVAEPPKP

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
2	Myristoylation	------MGYWNSKVV ------CCCCCCCHH		18397324
32	Phosphorylation	AAAEATKTFDESKET HHHHHHHHHHHHHHH		22092075
58	Phosphorylation	LQPKVVETYEATSAE CCCCEEEEEECCCHH		22092075
104	Phosphorylation	FPGSKAVSEASSSFG CCCCHHHHHHHHHCC		27029354
107	Phosphorylation	SKAVSEASSSFGAGY CHHHHHHHHHCCCCC		22092075
108	Phosphorylation	KAVSEASSSFGAGYV HHHHHHHHHCCCCCC		27029354
109	Phosphorylation	AVSEASSSFGAGYVA HHHHHHHHCCCCCCC		27029354
114	Phosphorylation	SSSFGAGYVAGPVTF HHHCCCCCCCCCEEE		27029354
127	Phosphorylation	TFIFEKVSVFLPEEV EEEEEEEEECCCHHH		22092075
136	Phosphorylation	FLPEEVKTKEIPVEE CCCHHHCCCCCCHHH		23111157
152	Phosphorylation	KAEEPAKTEEPAKTE CCCCCCCCCCCCCCC		19376835
158	Phosphorylation	KTEEPAKTEGTSGEK CCCCCCCCCCCCCCH		23111157
161	Phosphorylation	EPAKTEGTSGEKEEI CCCCCCCCCCCHHHH		20374526
162	Phosphorylation	PAKTEGTSGEKEEIV CCCCCCCCCCHHHHH		27532006
172	Phosphorylation	KEEIVEETKKGETPE HHHHHHHHHCCCCCC		23111157
177	Phosphorylation	EETKKGETPETAVVE HHHHCCCCCCCEEEE		30291188
180	Phosphorylation	KKGETPETAVVEEKK HCCCCCCCEEEECCC		23776212
198	Phosphorylation	EEKKEEATPAPAVVE HHHHHHCCCCCEEEE		23776212
206	Phosphorylation	PAPAVVETPVKEPET CCCEEEECCCCCCCC		23776212
213	Phosphorylation	TPVKEPETTTTAPVA CCCCCCCCCCCCCCC		23776212
214	Phosphorylation	PVKEPETTTTAPVAE CCCCCCCCCCCCCCC		23776212
215	Phosphorylation	VKEPETTTTAPVAEP CCCCCCCCCCCCCCC		23776212
216	Phosphorylation	KEPETTTTAPVAEPP CCCCCCCCCCCCCCC		23776212

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

Oops, there are no upstream regulatory protein records of PCAP1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PCAP1_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 PCAP1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of PCAP1_ARATH !!

Drug and Disease Associations

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