dbPTM

ACA8_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ACA8_ARATH
UniProt AC	Q9LF79
Protein Name	Calcium-transporting ATPase 8, plasma membrane-type
Gene Name	ACA8
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	1074
Subcellular Localization	Cell membrane Multi-pass membrane protein.
Protein Description	This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol out of the cell..
Protein Sequence	MTSLLKSSPGRRRGGDVESGKSEHADSDSDTFYIPSKNASIERLQQWRKAALVLNASRRFRYTLDLKKEQETREMRQKIRSHAHALLAANRFMDMGRESGVEKTTGPATPAGDFGITPEQLVIMSKDHNSGALEQYGGTQGLANLLKTNPEKGISGDDDDLLKRKTIYGSNTYPRKKGKGFLRFLWDACHDLTLIILMVAAVASLALGIKTEGIKEGWYDGGSIAFAVILVIVVTAVSDYKQSLQFQNLNDEKRNIHLEVLRGGRRVEISIYDIVVGDVIPLNIGNQVPADGVLISGHSLALDESSMTGESKIVNKDANKDPFLMSGCKVADGNGSMLVTGVGVNTEWGLLMASISEDNGEETPLQVRLNGVATFIGSIGLAVAAAVLVILLTRYFTGHTKDNNGGPQFVKGKTKVGHVIDDVVKVLTVAVTIVVVAVPEGLPLAVTLTLAYSMRKMMADKALVRRLSACETMGSATTICSDKTGTLTLNQMTVVESYAGGKKTDTEQLPATITSLVVEGISQNTTGSIFVPEGGGDLEYSGSPTEKAILGWGVKLGMNFETARSQSSILHAFPFNSEKKRGGVAVKTADGEVHVHWKGASEIVLASCRSYIDEDGNVAPMTDDKASFFKNGINDMAGRTLRCVALAFRTYEAEKVPTGEELSKWVLPEDDLILLAIVGIKDPCRPGVKDSVVLCQNAGVKVRMVTGDNVQTARAIALECGILSSDADLSEPTLIEGKSFREMTDAERDKISDKISVMGRSSPNDKLLLVQSLRRQGHVVAVTGDGTNDAPALHEADIGLAMGIAGTEVAKESSDIIILDDNFASVVKVVRWGRSVYANIQKFIQFQLTVNVAALVINVVAAISSGDVPLTAVQLLWVNLIMDTLGALALATEPPTDHLMGRPPVGRKEPLITNIMWRNLLIQAIYQVSVLLTLNFRGISILGLEHEVHEHATRVKNTIIFNAFVLCQAFNEFNARKPDEKNIFKGVIKNRLFMGIIVITLVLQVIIVEFLGKFASTTKLNWKQWLICVGIGVISWPLALVGKFIPVPAAPISNKLKVLKFWGKKKNSSGEGSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MTSLLKSSPG -----CCCCCCCCCC	43.49	23820729
7	Phosphorylation	-MTSLLKSSPGRRRG -CCCCCCCCCCCCCC	41.56	23820729
8	Phosphorylation	MTSLLKSSPGRRRGG CCCCCCCCCCCCCCC	29.77	19880383
19	Phosphorylation	RRGGDVESGKSEHAD CCCCCCCCCCCCCCC	51.90	15308754
22	Phosphorylation	GDVESGKSEHADSDS CCCCCCCCCCCCCCC	37.83	27532006
27	Phosphorylation	GKSEHADSDSDTFYI CCCCCCCCCCCCEEE	39.54	30291188
29	Phosphorylation	SEHADSDSDTFYIPS CCCCCCCCCCEEECC	42.37	27532006
31	Phosphorylation	HADSDSDTFYIPSKN CCCCCCCCEEECCCC	23.45	19880383
33	Phosphorylation	DSDSDTFYIPSKNAS CCCCCCEEECCCCCC	17.64	23776212
36	Phosphorylation	SDTFYIPSKNASIER CCCEEECCCCCCHHH	29.05	23776212
40	Phosphorylation	YIPSKNASIERLQQW EECCCCCCHHHHHHH	34.08	19376835
57	Phosphorylation	AALVLNASRRFRYTL HHHHHHHHHHHHHCC	23.94	23111157
62	Phosphorylation	NASRRFRYTLDLKKE HHHHHHHHCCCCHHH	14.67	25561503
63	Phosphorylation	ASRRFRYTLDLKKEQ HHHHHHHCCCCHHHH	15.00	25561503
99	Phosphorylation	FMDMGRESGVEKTTG HHHCCHHCCCCCCCC	46.94	17317660
109	Phosphorylation	EKTTGPATPAGDFGI CCCCCCCCCCCCCCC	19.46	23111157
117	Phosphorylation	PAGDFGITPEQLVIM CCCCCCCCHHHEEEE	22.58	23111157
125	Phosphorylation	PEQLVIMSKDHNSGA HHHEEEEECCCCCCH	24.65	23111157
724	Phosphorylation	ALECGILSSDADLSE HHHHCCCCCCCCCCC	25.01	19880383
1073	Phosphorylation	KNSSGEGSL------ CCCCCCCCC------	26.97	23111157

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 ACA8_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ACA8_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 ACA8_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CALM7_ARATH	CAM7	physical	23086147

Drug and Disease Associations

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

Regulatory Network of ACA8_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-27, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis."; Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.; Mol. Cell. Proteomics 6:1711-1726(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.	17586839 [Abstract]
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-22; SER-27 ANDSER-29, AND MASS SPECTROMETRY.	15308754 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-22; SER-27;SER-29 AND THR-31, AND MASS SPECTROMETRY.	14506206 [Abstract]